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Q5AVI2 | MAALRASNLLGDPFALATSSIAMLGWLIAFIASIAADVQDPYPSFQWWAIAYSFCCNVGVIVVFLTDTGLTYGVAVVGYLAASLVMNSISANSMFNSKSTSSFQAAGAGFILLCMVNIVWTFYFGSAPQAKHRGFIDSFALNKENQGSYGANRPMSSAYGARPETTTSRPQMYTSAQLNGFETSSPVSGYHGGAPGETRSPSQARFTSLGGPNASNPDTVGEIPPPTEYPYKAKAIYKYEANPEDANEIGFEKGEELEVSDVSGRWWQARKANGETGIAPSNYLILL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30709
Sequence Length: 287
Subcellular Location: Cell membrane
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E1BDF2 | MAPPAGGTAAGSDPGSAAVLLAVHVAVRPLGAGLDVAAQPRRLQLSADPERPGRFRLEMLGAGPGAVILEWPLESVSYTVRGPCQHELQPPPGGPGTLSLHFANPQEAQRWAALVRDATVEGQNGSDSLPPALGPETRPVSPPSPLEVPTPKAPKPKVDLPWSPGDLMEKEELAGRLTRAVEGGDEKGAAQAAAILAQRHVALRVQLQEAYFPPGPIRLQVTVEDAASSAHVSLQVHPHCTIRALQEQVFSEFGFPPAVQRWVIGRCLCVPEHSLAFYGVQRDGDPAFLYLLSAPREAPGRSPQRPQKVDGELGRLFPQSLGLPPTPQPTSSSLPSPLQPGWPCPSCTFINAPSRPGCEMCSTQRPCAWDPLPTASIQQLPKVTRREDGPSLPGPRSLDPLLNLSGNLC | Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Sequence Mass (Da): 43394
Sequence Length: 409
Domain: The Ubiquitin-like domain is required for the interaction with RNF31.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q9H0F6 | MAPPAGGAAAAASDLGSAAVLLAVHAAVRPLGAGPDAEAQLRRLQLSADPERPGRFRLELLGAGPGAVNLEWPLESVSYTIRGPTQHELQPPPGGPGTLSLHFLNPQEAQRWAVLVRGATVEGQNGSKSNSPPALGPEACPVSLPSPPEASTLKGPPPEADLPRSPGNLTEREELAGSLARAIAGGDEKGAAQVAAVLAQHRVALSVQLQEACFPPGPIRLQVTLEDAASAASAASSAHVALQVHPHCTVAALQEQVFSELGFPPAVQRWVIGRCLCVPERSLASYGVRQDGDPAFLYLLSAPREAPATGPSPQHPQKMDGELGRLFPPSLGLPPGPQPAASSLPSPLQPSWSCPSCTFINAPDRPGCEMCSTQRPCTWDPLAAAST | Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation . LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways . Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation . LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex . The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria . LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin . The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation . Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis .
Sequence Mass (Da): 39949
Sequence Length: 387
Domain: The Ubiquitin-like domain is required for the interaction with RNF31.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q91WA6 | MSPPAGGAAVAADPASPVVLLAVHAAVRPLGAGQDAEAQPRKLQLIADPERPGRFRLGLLGTEPGAVSLEWPLEAICYTVRGPNQHELQPPPGGPGTFSVHFLDPEEAQQWAALVRDATAEGQNGSGSPAPAPAPAMCPISPPCSSMAQIPKATQPEVDLPQSSGNFKKEELATRLSQAIAGGDEKAAAQVAAVLAQHHVALNVQLMEAWFPPGPIRLQVTVEDATSVLSSSSSAHVSLKIHPHCSIAALQDQVFSEFGFPPAVQRWVIGRCLCMPERSLASYGVSQDGDPAFLYLLSAPREVSGQSLQNSKMDRKLGLFPQSLGLPHDLQPSSSSLPSPSQPGWSCPSCTFINASNRPGCEMCSTQRPCAWDPLAAAST | Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation . LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways . Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation . LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity).
Sequence Mass (Da): 39852
Sequence Length: 380
Domain: The Ubiquitin-like domain is required for the interaction with RNF31.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q59VX8 | MSRFDYRNTSKNTSVVDPDHSSPIINYRKDAKKGIKFTFMVVGESGTGKTTFINSLLNKKVLNHRYEKLSPTVGDTKTLMFTSAKSVALPNTSILTKNEFNPRTINEEPGIALTETHIEIIDDDNQKLLLNIIDTPGFGENLNNELCFIEIENYLKQQFDLVLAEETRIKRNPRFVDTRVHVMLYFITPTGHGLREIDIQCMKRLSKYVNIIPVIGKADSFTLNELQHFKQQIRIDIQKFNVPTFQFDNSLNDYDEDEDYDLIQECKFLTNLQPFAVVTSEDVFEVRESTTSTKGNNDKPKIIRARKYPWGLVDINDTRYSDFPILKSVLLGSHLQDLKDLTHDFLYETYRTERLTKVTGNGQAFDDEENEDAEFHDTVEHQLNDSNRGVGGDDNNNNNNNNNNASTIPSMSNLAQLTTSTNEHDASHIDNNSITSTSSSIKKSTSMLIDDHPSSSPKLKNISSFTSSTSTVSLEGGEKEGGHHDRGANSTSTNNNNNNNAFKRLSIGPQRNQLRQISETVPYVLRHERILERQQKLEEMEQASARELANRAALLEKKAAQLKAKEKALRQLELNRQKQEESATSSLHRKDSDISGSVQSGGVDDGKSESTNNNNNNRNGYGYGHGHGHGQSHEYDNSEYHHDDSTPNYETSRLQKDETLTDLHSIVSNH | Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. SEP7 is required to convert hyphal septin rings into the hyphal-specific state and is necessary for CDC10 turnover during hyphal growth.
PTM: Phosphorylated by GIN4 which stabilizes the GIN4-SEP7 interaction.
Sequence Mass (Da): 75795
Sequence Length: 670
Subcellular Location: Bud neck
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Q07657 | MSTASTPPINLFRRKKEHKRGITYTMLLCGPAGTGKTAFANNLLETKIFPHKYQYGKSNASISSNPEVKVIAPTKVVSFNSKNGIPSYVSEFDPMRANLEPGITITSTSLELGGNKDQGKPEMNEDDTVFFNLIMTHGIGENLDDSLCSEEVMSYLEQQFDIVLAEETRIKRNPRFEDTRVHVALYFIEPTGHGLREVDVELMKSISKYTNVLPIITRADSFTKEELTQFRKNIMFDVERYNVPIYKFEVDPEDDDLESMEENQALASLQPFAIITSDTRDSEGRYVREYPWGIISIDDDKISDLKVLKNVLFGSHLQEFKDTTQNLLYENYRSEKLSSVANAEEIGPNSTKRQSNAPSLSNFASLISTGQFNSSQTLANNLRADTPRNQVSGNFKENEYEDNGEHDSAENEQEMSPVRQLGREIKQENENLIRSIKTESSPKFLNSPDLPERTKLRNISETVPYVLRHERILARQQKLEELEAQSAKELQKRIQELERKAHELKLREKLINQNKLNGSSSSINSLQQSTRSQIKKNDTYTDLASIASGRD | Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck . This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck . The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle . Many proteins bind asymmetrically to the septin collar . The septin assembly is regulated by protein kinases GIN4 and/or CLA4 . May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage . Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation . CDCd11 with SHS1 11 are involved in the recruitment of BNI5 and thereby ensure efficient localization at the bud neck of MYO1, the type II myosin of the actomyosin contractile ring .
PTM: Phosphorylated by GIN4 and CLA4. Phosphorylation state is essential for septin ring dynamics during telophase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62630
Sequence Length: 551
Domain: The C-terminal extension (CTE) that contains a coiled coil is important for the recruitment of BNI5 and subsequent localization at the bud neck of MYO1.
Subcellular Location: Membrane
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A2RV66 | MEFIVLLTVCALLGLSCGQHGEYCHGWTDSYGIWRPGFQCPERYDPPEATFCCGSCGLKYCCSTVESRLDQGLCPNEEDLRDGVPSIELPPTVPTYFPFLLVGSIFVSFVILGSLVGLCCCKCLKPEDDTQVSGPAPIQSRLLDQDPSTDTSRHSSSSSASMPRPPIGARPQNLCSLGAENINLYMNMPPTFPMMGCPQNAQFMHPGTAGPSFMQPPFINYAVPAEHAIIMAPAPYIDARNCYGQTSNIYCQVPQQNDQTVCSGSPSKC | Function: Required for head formation during gastrulation. Functions as an inhibitor for the caudalizing signals wnt and fgf, does not inhibit bmp, activin and nodal signaling in head formation process. Induces retention of fzd8 in the endoplasmic reticulum and inhibits trafficking of fzd8 to the cell surface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29184
Sequence Length: 269
Subcellular Location: Endoplasmic reticulum
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D3ZEH5 | MIAWRLPLCVLLVAAVESHLGALGPKNVSQKDAEFERTYADDVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGLYQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVNRVDNFVLRTGELFTFNTTAAQPQYFKYEFPDGVDSVIVKVTSKKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFVEDEPVDQGHRQKTLSVLVSQAVTSEAYVGGMLFCLGIFLSFYLLTVLLACWENWRQRKKTLLVAIDRACPESGHPRVLADSFPGSAPYEGYNYGSFENGSGSTDGLVESTGSGDLSYSYQDRSFDPVGARPRLDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLCVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLYALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSVIHIISTLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYTDRMVLLVMGNIINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVLLTLDDDLDTVQRDKIYVF | Function: Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. Involved in the uptake of single-stranded oligonucleotides by living cells, a process called gymnosis (By similarity). In vitro, mediates the uptake of linear DNA more efficiently than that of circular DNA, but exhibits similar uptake efficacy toward RNA and DNA. Binds long double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than 100 bp (By similarity).
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94527
Sequence Length: 832
Subcellular Location: Lysosome membrane
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Q38674 | MSDSMSYAVLVAATLFLGIGLQIAWLFFSNFIKRKRLESRISEVSIAIGKNAKNPENEAYVLNYLKEKFSPERFENRITDALGLIISVIHIPLSLLITVWYFAMIAGRIFGFMNIEPVVLWVPMILQLLLSIAIFIFSVFIKIVFGRYPGEANGFNKEFIKTIK | Function: Probably blocks the subsequent transfer of the phage DNA across the inner membrane into the cytoplasm. By this means, P22 excludes superinfection by the phages of the same family and also against DNA coming from oter phages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18701
Sequence Length: 164
Subcellular Location: Host cell inner membrane
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P38396 | MNNSWWQELMRFFLQGMTLKQLIHMLIILIVLIIVMPVSVKEWINLHNPEILPHYWMYYILLFCVSYVLNGVVNSVYHAVTERIEASTAQRRKDREEKVVRDLFDSLTLGERAYLAFAVAANNQLKTEKGSPEAISLLKKGIITRLPSAIGYPDIDRFIIPEKYFNECYMRFAGKSDILMNELIVQDEQLKK | Function: Has a role in the prevention of superinfection by phages that are insensitive to repression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22443
Sequence Length: 192
Subcellular Location: Host membrane
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P03762 | MMSIEMDPLVILGRVFSNEPLERTMYMIVIWVGLLLLSPDNWPEYVNERIGIPHVWHVFVFALAFSLAINVHRLSAIASARYKRFKLRKRIKMQNDKVRSVIQNLTEEQSMVLCAALNEGRKYVVTSKQFPYISELIELGVLNKTFSRWNGKHILFPIEDIYWTELVASYDPYNIEIKPRPISK | Function: Has a role in the prevention of superinfection by phages that are insensitive to repression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21557
Sequence Length: 184
Subcellular Location: Host membrane
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O74446 | MSNRIGPQRSTKTAAKLRLLPSTEEFDDFRRQDTGREVYSQIPQIEGSTAKRDAEHLGKRHREFLPRVTAYCTCDTFRVDLLFKFFQSRRSSHKTRPKQFDECIYSPYSYNNEETTDLLPDTLESSRGTLNRESSQESLQSIFEESGLDRNQPLFREVFCFTYGVVVLWGYTIDEEHRFLRELGRFEIEKLKIEDMEVEEFNYYITTLYQPRIFNDFIALRDASNYMIRLSISHAIAQSVKISLFEELVNETIDATKDTPQMIAETGRVNLKREEIMMAVGQLFILRININLQGSVLDSPELMWTEPQLEPIYTAARSYLEINQRVALLNQRVEVIGDLLSMLKEQITHTHDESLEWIVVILMGLLVLIALFSIVVDWKLFQ | Function: Required for sporulation where it is believed to have a role in meiotic nuclear division.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44642
Sequence Length: 382
Subcellular Location: Nucleus membrane
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P38262 | MSITSEELNYLIWRYCQEMGHEVSALALQDETRVLEFDEKYKEHIPLGTLVNLVQRGILYTESELMVDSKGDISALNEHHLSEDFNLVQALQIDKEKFPEISSEGRFTLETNSESNKAGEDGASTVERETQEDDTNSIDSSDDLDGFVKILKEIVKLDNIVSSTWNPLDESILAYGEKNSVARLARIVETDQEGKKYWKLTIIAELRHPFALSASSGKTTNQVTCLAWSHDGNSIVTGVENGELRLWNKTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFELKETGGSSINAENHSGDGSLGVDVEWVDDDKFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDKVISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKYAVAFMDGQVNVYDLKKLNSKSRSLYGNRDGILNPLPIPLYASYQSSQDNDYIFDLSWNCAGNKISVAYSLQEGSVVAI | Function: Antagonizes telomeric silencing in yeast. May recruit SIR4 to non-telomeric sites or repression.
Sequence Mass (Da): 59161
Sequence Length: 535
Domain: The LisH domain mediates tetramerization and interaction with SNT1.
Subcellular Location: Nucleus
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Q8IN35 | MMAASGRIRKRKHKSHTSGDVPSTTTSVPMPIPTMAPGKMVAETMEEAAALAGDYNNFTHNFVDLQNLLSFNELNGTSGSGGTAVSSLGSSSAIKLNNSAITDTLLGTVLTTATATVAPAASSLLATLAATTTASARGSLAGKSLAIADATSSTYYSNLLNLSPATTSLISAAAATKSYNDSALRWEQLDGSVDFGFDPLYRHSLAMSMVYCVAYIVVFLVGLIGNSFVIAVVLRAPRMRTVTNYFIVNLAIADILVIVFCLPATLIGNIFVPWMLGWLMCKFVPYIQGVSVAASVYSLIAVSLDRFIAIWWPLKQMTKRRARIMIIGIWVIALVTTIPWLLFFDLVPAEEVFSDALVSAYSQPQFLCQEVWPPGTDGNLYFLLANLVACYLLPMSLITLCYVLIWIKVSTRSIPGESKDAQMDRMQQKSKVKVIKMLVAVVILFVLSWLPLYVIFARIKFGSDISQEEFEILKKVMPVAQWLGSSNSCINPILYSVNKKYRRGFAAIIKSRSCCGRLRYYDNVAIASSTTSTRKSSHYHQNSSRKSPSSKGNAVSYIYEHNSLRRHNMMLKQDSNLSQQMLLKQDSHGSRQFLIKQESSCSDASGIRRPLCQQDSNGSKVSLSKQDSIVSYMEARRSAGHGLNDTLVDRDSVSMDVGRRQGATPSSLLDKRQKFVKQDSVISFVDQRPEQRRHQLVKQDSVISFADQRRGLLHKQDSLMANRTGDAPTHHVSILKKTDSQLSYGSSTSPRRNADLYE | Function: Receptor for the neuropeptide SIFamide . Modulates sexual behavior by playing a role in male sex discrimination . Also involved in promoting sleep .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83442
Sequence Length: 758
Subcellular Location: Cell membrane
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Q56061 | MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFAERAPTRERLTEIFFELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKSHPQMTAMIKRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYTELRKGHLDGWKAQEKATYLAAKIQSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDPSTSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and formation of Salmonella-induced filaments (Sifs), which are filamentous structures containing lysosomal membrane glycoproteins within epithelial cells. Sif formation is concomitant with intracellular bacterial replication.
Sequence Mass (Da): 38498
Sequence Length: 336
Domain: Domains throughout the protein, and not only the N-terminus, are required for secretion and translocation. Both N- and C-terminal domains are also required for formation of tubules.
Subcellular Location: Secreted
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Q96LC7 | MLLPLLLSSLLGGSQAMDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSNGAFLGIGITALLFLCLALIIMKILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules . Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (By similarity). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells . Plays a role in the control of autoimmunity (By similarity). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (By similarity).
PTM: Phosphorylation of Tyr-667 is involved in binding to PTPN6.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76592
Sequence Length: 697
Domain: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Subcellular Location: Cell membrane
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Q80ZE3 | MSLLLFLLSFLLDGPQGQMESYFLQVQRIVKAQEGLCIFVPCSFSSPEGKWLNRSPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARGRFQLLGDISKKNCSLLIKDVQWGDSTNYFFRMERGFERFSFKEEFRLQVEALTQKPDIFIPEVLEPGEPVTVVCLFSWTFNQCPAPSFSWMGDAVSFQESRPHTSNYSVLSFIPGLQHHDTELTCQLDFSRMSTQRTVRLRVAYAPRSLAISIFHDNVSVPDLHENPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSVLYPPQDLRVTVSQANRTVLEILRNAISLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIPIQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVHYPPQMSSPSCSWEAKGLHCNCSSRAWPAPSLRWRLGEGLLEGNSSNASFTVTFSSLGPWVNSSLSLLQELGPSLWLSCESWNTHGAQTTSVLLLPDKDSATAFSKGAVLGFGITALLALCLIVVIVKTLQKKGTQEEPSRPKLSRGSTILDYINVVPKTRSLARNWKAEPDAPSRSSPLDTHFPKPKKKQKDPHFTYPGCPDPTSSSQVPVSENNPEELHYAALNFSRLRLQETQDPQDTYSDYTEVRVH | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid . The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (By similarity). Involved in negative regulation of B-cell antigen receptor signaling and specifically acts on B1 cells to inhibit Ca(2+) signaling, cellular expansion and antibody secretion . The inhibition of B cell activation is dependent on PTPN6/SHP-1 . In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 . In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (By similarity). Plays a role in the control of autoimmunity . During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification .
PTM: Phosphorylation of Tyr-659 is involved in binding to PTPN6.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76884
Sequence Length: 688
Domain: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Subcellular Location: Cell membrane
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Q60670 | MVIMSEFSAVPSGTGQGQQKPLRVGFYDVERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPNIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARQKFWQILSAVEYCHNHHIVHRDLKTENLLLDSNMDIKLADFGFGNFYKPGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDVWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCETLIRRMLVVDPAKRITIAQIRQHRWMQADPTLLQQDDPAFDMQGYTSNLGDYNEQVLGIMQALGIDRQRTIESLQNSSYNHFAAIYYLLLERLKEHRSAQPSSRPTPAPTRQPQLRSSDLSSLEVPQEILPCDPFRPSLLCPQPQALAQSVLQAEIDCDLHSSLQPLLFPLDTNCSGVFRHRSISPSSLLDTAISEEARQGPSLEEEQEVQEPLPGSTGRRHTLAEVSTHFSPLNPPCIIVSSSATASPSEGTSSDSCLPFSASEGPAGLGSGLATPGLLGTSSPVRLASPFLGSQSATPVLQTQAGLGTAVLPPVSFQEGRRASDTSLTQGLKAFRQQLRKNARTKGFLGLNKIKGLARQVCQSSVRTPRGGMSTFHTPAPSSGLQGCTTSNREGRSLLEEVLHQQRLLQLQHHSSTAAASSGCQQGPQLSPVPYVLAPCDSLLVSGIPLLPTPLLQAGMSPVASAAHLLDTHLHISAGPVALPTGPLPQCLTRLSPGCDPAGLPQGDCEMEDLTSGQRGTFVLVQ | Function: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1.
PTM: Phosphorylated at Thr-182 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39, leading to its activation. Phosphorylation at Thr-182 promotes autophosphorylation at Ser-186, which is required for sustained activity. Autophosphorylation at Ser-186 is maintained by sequential phosphorylation at Thr-182 by GSK3-beta. GSK3-beta cannot initiate phosphorylation at Thr-182, it can only maintain it. Phosphorylation at Ser-577 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 85115
Sequence Length: 779
Domain: The RK-rich region determines the subcellular location.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9IA88 | MVIMSEDASVPAPSAAQPRPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDPSNLEKIYREVQIMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDHLTSNGHLSESEARKKFWQILSAVEYCHSHHIVHRDLKTENLLLDANMNIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPHLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPYFMSEDCETLIRRMLVVDPTKRITISQIKQHKWMQADPSLRQQQSLSFSMQNYNSNLGDYNEQVLGIMQTLGIDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRSSQLSSRPATGRQQRPRSSEISNAEMPQDSLTSETLRSSLLYQQPQSLIQPSLQAEMDCDMNNPLQPVFFPVDPNFNGLFRNRSISPSSLLETTISEEVRQEKELEDEIKAYDHPIRIPSNTSRRHTLAEVTTHFYQHAPPCIVISSSASPTEGTSSDSCLTSSSNDSSVALSSCLAGQVMTGSPATARMTSAFLASQSDAPVLQVQGCMGGASLLPVSFQEGRRASDTSLTQGLKAFRQQLRKNARAKGFLGLNKIKGFARQVCQSSSSRAARSAMSPFQHAQPNTCIYSSSGSSREGRNLLEEVLQQQRMLQLQHHQLLQPACPQTSQTSATNGLPPSDSAGTCKASNSLLLSELQRENSFELAFGGNSQLLQPHFFGVSVSPVSSAAHLLDTHLYISSNVSPVGTTFSQQQSFSAQSPSYDAVTLQHGDCEMEDLTSNQLGKFVLVK | Function: Phosphorylates IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing the CREB-specific coactivators, CRTC1-3 (By similarity).
PTM: Phosphorylated at Thr-181 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 88866
Sequence Length: 798
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q8CFH6 | MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRTTKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKVVHRDLKAENLLLDNNMNIKIADFGFGNFFKTGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLSIAQIKEHKWMLIEVPVQRPILYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTVESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRLDGRQRRPSTIAEQTVAKAQTVGLPVTLHPPNVRLMRSTLLPQASNVEAFSFPTSSCQAEAAFMEEECVDTPKVNGCLLDPVPPVLVRKGCQSLPSSMMETSIDEGLETEGEAEEDPSQAFEAFQATRSGQRRHTLSEVTNQLVVMPGAGKMFSMSDNPSLESVDSEYDMGSAQRDLNFLEDSPSLKDIMLANQPSPRMTSPFISLRPANPAMQALSSQKREAHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQMGSNADPTLTSTAPQLQDLSSSCPQEEISQQQESVSSLSASMHPQLSPQQSLETQYLQHRLQKPNLLPKAQSPCPVYCKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPGPSQQLALPHQETPLTSQQPPSFSLTQALSPVLEPSSEQMQFSSFLSQYPEMQLQPLPSTPGPRAPPPLPSQLQQHQQPPPPPPPPPPQQPGAAPTSLQFSYQTCELPSTTSSVPNYPASCHYPVDGAQQSNLTGADCPRSSGLQDTASSYDPLALSELPGLFDCEMVEAVDPQHNGVVSCLARET | Function: Serine/threonine-protein kinase that plays a role in many biological processes such as fatty acid oxidation, autophagy, immune response or glucose metabolism . Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction . Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators . Phosphorylates EP300 and thus inhibits its histone acetyltransferase activity. In turn, regulates the DNA-binding ability of several transcription factors such as PPARA or MLXIPL (By similarity). Also plays a role in thymic T-cell development .
PTM: Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (By similarity). Phosphorylated at Thr-484 in response to insulin in adipocytes (By similarity). Phosphorylation at Ser-358, Thr-484 and/or Ser-587 following cAMP signaling is required for 14-3-3 interaction and thus inactivation .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 104198
Sequence Length: 931
Domain: The RK-rich region is required for cAMP responsiveness.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q84K34 | MARFSVCGGDDGEGPSNNNHQSRKRQRLPSIDENEEDAETSDAGSSGEEDEDETQNQGMRPESEDRGSTSDDSDREVVIEERRFGKFVNSQSSSSSKDSPLSVTLLDPDVLDCPICCEPLKIPIFQCDNGHLACTLCCTKVRNRCPSCTLPIGYVRCRAMEKVIEASRVSCLNAKYGCKESTSYGNRFSHEQVCVFTPCSCPILDCHYTGYYKDLNNHVRAEHKDDLISFVWNTRLTISLDLNKKTTILQEENDGHVIVVQVFRALHAVYVSVSCIAPLTPGVGRLSCRLAKITVDSLLKQGFMVKNIQKVTNEHPEDGFMLIPSYLFSGNDNLNLQIWIGHGRIFVHS | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 38924
Sequence Length: 349
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q9FM14 | MEDSNSHPQNQTSKRKSSHPQKKQRMENETRSAKLLDLDVLDCPVCFEPLTIPTFQCDDGHIVCNFCFAKVSNKCPGPGCDLPIGNKRCFAMERVLESAFVPCQNTEFGCTKSVSYEKVSSHEKECNYSQCSCPNLECNYTGSYNIIYGHFMRRHLYNSTIVSSKWGYSTVDVLINIKEKVSVLWESRQKLLFVVQCFKERHGVYVTVRRIAPPASEFKKFSYRLSYSIDGHNVTYESPEVKRLLEVNSQIPDDSFMFVPNCLLHGFLIKPANEVQQVTIAQETVMEDPPTSLFKNSVPIREDQIQNAITNSIR | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 35880
Sequence Length: 314
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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P59941 | MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLMWQSSSVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFENARPSKTHMALVQLERMGFLSFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECPKCKTQYVRDTVVGTMGLKATGRLCTVAKTRGLRACRGELRDTILDWEDSLPDRDLMLADEASRTADLSVTLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRQADLRIHGYVDEVMCRLMKHLGLEIPAWDGPCVLDKALPPLPRPVALKAEPPVHLNGAVHVSYKSKPNSPILHRPPKRVKTEAAPS | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging . Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (By similarity). Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B . Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing . Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac . SIRT6 participation to DSB repair is probably involved in extension of life span . Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (By similarity). Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (By similarity). Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage . Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac . Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism . Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes . Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect . Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (By similarity). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 . Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA . Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 . Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 . The defatty-acylase activity is specifically involved in regulation of protein secretion . Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (By similarity). Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 . Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription .
PTM: Acetylated at Lys-33 (By similarity). Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites (By similarity).
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass (Da): 36920
Sequence Length: 334
Domain: The C-terminal disordered region mediates non-specific DNA-binding.
Subcellular Location: Nucleus
EC: 2.3.1.-
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Q9VAQ1 | MEKDLGEEKDQDQEQNTEMEPKQEMDVAQSYITRAKMNPAKKDNEKRRRKDAMRRVSMILRKCDSMRTTEDRQFLEKHPDMVKTTKKRKERVEIYKERVVEREDAPHVIEAKVEQLANIISQAKHLVCYTGAGISTAALIPDYRGSQGIWTLLQKGQDIGEHDLSSANPTYTHMALYELHRRRLLHHVVSQNCDGLHLRSGLPRNSLSEIHGNMYVEVCKNCRPNSVYWRQFDTTEMTARYCHKTHRLCHRCSEPLYDTIVHFGERGNVKWPLNWAGATANAQRADVILCLGSSLKVLKKYTWLWQMDRPARQRAKICVVNLQWTPKDAIASIKINGKCDQVMAQLMHLLHIPVPVYTKEKDPIFAHASLLMPEELHTLTQPLLKNADEEEAFTTTTEETQDSTISSESCSFNYSDLPIGKGPRIRTPIKNGRRVKTNLELRQKFKTLNGQDEEIKVEHVKTNGEVKTEKDLITLESSIKIETEVKLEKLECSDTNFQQELKLLELLPKLEPLSLKEETEETPSNGFPELPKLVAIQKTHAECLSAVPTESRLKPLQLPPLVPIGAPLSTPFVEPKLVLPPASQSSSIQIKSEGDGDSSTENDNEEEEESELAQMDLLRQNNDEELLRQLPTWYDAKYAYSGLHSILIPPPADLNIWNSQVVPNFAMNRSAASCFFCFDRYAELECQFYRRWNLSQRKHKKRARSGRFVVCECCPTSDDDDDYDENISLAHIAAAETAKRRQQLSTSFPRKLARTQAGWYGKGYKKGRKRR | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass (Da): 88469
Sequence Length: 771
EC: 2.3.1.286
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Q9NRC8 | MAAGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESADLVTELQGRSRRREGLKRRQEEVCDDPEELRGKVRELASAVRNAKYLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRSVSAADLSEAEPTLTHMSITRLHEQKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCVPNREYVRVFDVTERTALHRHQTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASRADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMAELGLEIPAYSRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context . Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac) . In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression . H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor . Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells . Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes . Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 . Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex . Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region . In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription . Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis . Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex . Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65 . Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation . Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B) . Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II . Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL . Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51 . Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases . In addition to protein deacetylase activity, also acts as protein-lysine deacylase . Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes . Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair . Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ) (By similarity). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina . Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability . Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity).
PTM: Phosphorylated during mitosis.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass (Da): 44898
Sequence Length: 400
Subcellular Location: Nucleus
EC: 2.3.1.286
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B2RZ55 | MAAGGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESEDLVTELQGRSRRREGLKRRQEEVCDDPEELRRKVRELAGAVRSARHLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRPVSAADLSEAEPTLTHMSITQLHKHKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCIPNREYVRVFDVTERTALHRHLTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASKADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMDELGLEIPVYNRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEPPPGDQSAPLASATPILGGWFGRGCAKRAKRKKAA | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context. Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes. Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53. Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex. Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region. In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription. Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis. Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex. Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65. Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation. Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II. Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (By similarity). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51. Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases. In addition to protein deacetylase activity, also acts as protein-lysine deacylase (By similarity). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (By similarity). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina. Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (By similarity). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity).
PTM: Phosphorylated during mitosis.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass (Da): 45113
Sequence Length: 402
Subcellular Location: Nucleus
EC: 2.3.1.286
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O00241 | MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTCAHRDDVVLTCQVEHDGQQAVSKSYALEISAHQKEHGSDITHEAALAPTAPLLVALLLGPKLLLVVGVSAIYICWKQKA | Function: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP .
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43211
Sequence Length: 398
Subcellular Location: Cell membrane
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P0A238 | MTIAMLLTLHLICVALSVSLFVARYWWRYCGHALAAARWTRIVPPVIDTLLLLSGIGLIVKTHILPFTESGSWLTEKLFGVIIYIVLGFIALDYRQARSQQARFIAFPLALVVLYIIIKLATTKIPLLG | Function: Required for maximal expression of sirC, not required to invade host cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14467
Sequence Length: 129
Subcellular Location: Cell inner membrane
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Q84JH7 | MTTQSQFLVNLSYGGLASQSNLRANNRVSPSSCQITRTNRSWALPVSFKVEKFQLQRGRRRRGSPCFGESEGLVKNGIGDADGIIIVDHGSRRRESNLMLEEFVKMFKEKTGYPIVEPAHMELAEPSIKDAFSLCVQQGAKRVVVSPFFLFPGRHWHTDIPSLTADAAKEFSGISYLITAPLGPHNLLLDVVNDRIQHCLSHVEGDADECLVCAGTNKCKLYNSS | Cofactor: Binds 2 [4Fe-4S] clusters per dimer. The [4Fe-4S] cluster quickly oxidizes to a [2Fe-2S] form in the presence of oxygen.
Function: Chelates iron to the siroheme precursor. Catalyzes the last step of the siroheme biosynthesis. Unlike its counterparts in bacteria, contains an [Fe-S] cluster which is not involved directly in the enzymatic reaction, but may play regulatory role in iron, sulfur and tetrapyrrole metabolism . The [Fe-S] cluster is required for normal plant growth .
Catalytic Activity: 2 H(+) + siroheme = Fe(2+) + sirohydrochlorin
Sequence Mass (Da): 24925
Sequence Length: 225
Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
Subcellular Location: Plastid
EC: 4.99.1.4
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Q86WV1 | MQAAALPEEIRWLLEDAEEFLAEGLRNENLSAVARDHRDHILRGFQQIKARYYWDFQPQGGDIGQDSSDDNHSGTLGLSLTSDAPFLSDYQDEGMEDIVKGAQELDNVIKQGYLEKKSKDHSFFGSEWQKRWCVVSRGLFYYYANEKSKQPKGTFLIKGYGVRMAPHLRRDSKKESCFELTSQDRRSYEFTATSPAEARDWVDQISFLLKDLSSLTIPYEEDEEEEEKEETYDDIDGFDSPSCGSQCRPTILPGSVGIKEPTEEKEEEDIYEVLPDEEHDLEEDESGTRRKGVDYASYYQGLWDCHGDQPDELSFQRGDLIRILSKEYNMYGWWVGELNSLVGIVPKEYLTTAFEVEER | Function: Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-271 is required for GRB2 interaction. Phosphorylation by FYN on Tyr-295 abolishes interaction with FYB1. Tyr-232 is dephosphorylated by PTPRC (Probable).
Sequence Mass (Da): 41432
Sequence Length: 359
Domain: The SH3 domain interacts with FYB1.
Subcellular Location: Cytoplasm
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Q3UUV5 | MQAVALPEEICWLLEDTEDFLAEGLQNENLSPGAQDQRAHILRGFQQIKSRYCWDFQPQGGDLGQDGSDDNLSGTHGPPLTSEASFWSDYQDEGIEDILRGAQELDSVIKQGYLEKKSKDHSFFGSEWQKRWCVISRGLFLYYANEKSKQPKGTFLIKGYSVRMAPHLRKDSKKESCFELISQDRRSYEFTASSPAEARDWVDQISFLLKDLSSLTIPFEEEEEEEEEEEKEEEEMYNDVDGFDSPRSGSQCRAMALPEPTEKEEDIYEVLPDDDDLEEDTCGAHRRRVDYADYYQGLWDCHGDQPDELSFQRGDLIRILSKEYNMYGWWVGELNSVIGIVPKDYLTTAFEMEGI | Function: Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway (By similarity). Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells .
PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-268 is required for GRB2 interaction (By similarity). Phosphorylation by FYN on Tyr-291 abolishes interaction with FYB1. Tyr-237 is dephosphorylated by PTPRC (By similarity).
Sequence Mass (Da): 40962
Sequence Length: 355
Domain: The SH3 domain interacts with FYB1.
Subcellular Location: Cytoplasm
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Q1KKW7 | MEAVDLLANVSVTGLLLFWGDCEFFVSEILYDENLSENAQETRKVLLNNFRVVHVRNPQEFPFPSDYKEEDGSDDNRSSSLGRSAQSDDASLASDNQDDGIPEYFGDIPPVAAQDIVNVLKQGYLEKKRKDHSFFGSEWQKRWCVLNNLVFYYFGSDKDKQQKGSFYISDYSVQLVTNLRKDSRKTSCFEFFAPGRRPFQFTAGSPQEAKEWVDQIKIVLRDLSSTVIPVDDEEEEEEEEETYDDIEGEGGPPLPQPLSGTWGRGGDTGAADEEDEDIYEVLPEESPDSADGSMERNNKPEYANYYQGLWDCSADEPDELPFQRGDLIYIISKEYNIYGWWVGELNGAVGIVPKDFLHPAYIL | Function: Positively regulates T-cell receptor signaling. Required for optimal conjugation between T-cells and antigen-presenting cells (By similarity).
PTM: Phosphorylated on tyrosines.
Sequence Mass (Da): 41279
Sequence Length: 363
Subcellular Location: Cytoplasm
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Q6DII7 | MQGYDIPRDVISLLKDAETYLAECLQNEKLSGRAREQRDEILHSFGQIRNRYGVEFALKGGEAAFTHTGQDDYDDIHNASYAPSQASDEVSVASDYVENDSEVEEELDKIFKQGYLERRKKDHGFFGSEWQKRWCVLTTRAFLYYSSEKGKQPKNGFLIKDSLAQMMPYIRKDSRRDSCFEVVTPNQQVFQFTAASPSDARDWVEQIQFLVKDTQSTIIPYEDDEETYDDIESTESSPVVGLTNDSENSLQEDDVYESIPGDEETEESEDENYEMKPGEPVIFYGDYYQGLWNCFSDNSDELSFERGDLIHILSKEYHAYGWWVGELDGIVGIVPKDYLTLAFDL | Function: Positively regulates T-cell receptor signaling. Required for optimal conjugation between T-cells and antigen-presenting cells (By similarity).
PTM: Phosphorylated on tyrosines.
Sequence Mass (Da): 39737
Sequence Length: 345
Subcellular Location: Cytoplasm
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Q12505 | MLSDCLLNNFRITAQIGSGAYGLVFHVVDILTSREYAVKTVFKSSSMDEFYNKNGLNNNSQVARTTLLQTQLYHFFKSFQKKLFLPSVDLDSILQLTENELNRLPHYREIAFQLRVQSHGNIVKIHQVLESSIATFIVMDYYDRDLFTSIVDDKHFVNHGILIKKVFLQLCSALDHCHRLGIYHCDIKPENVLLDRNDNAYLCDFGLSTKSKYLAPNVCVGSSYYMAPERILYCLNTTTNGIHVDECCSSLPTDTGDIWSLGIILINLTCIRNPWLKAHQKEDNTFQHFANDNNVLKKILPISDELFTVLTKILQLNPYTRIDMKTLMSEVSSLTSFTREGPLSQVPILSSEVYMTHIIRNENLFLSDLSHFSADQEQQQQQQQQQQQVQEQEQEQKQEQIQNQEQAQQQQEEEDAEPESDIPSTYNSDGSMEKYEYTNNHNNSTFLTSSMDSTPYQSDIDDVSASKDCKFQQDTLRNRLLCLQMNFSTLTDGPNEKWLPDY | Function: May have a role in glucose regulation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 57844
Sequence Length: 502
EC: 2.7.11.1
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Q92581 | MARRGWRRAPLRRGVGSSPRARRLMRPLWLLLAVGVFDWAGASDGGGGEARAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYMLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTALVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFVAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPENERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTEPATSSAPRRFMGNSSEDALDRELAFGDHELVIRGTRLVLPMDDSEPPLNLLDNTRHGPA | Function: Endosomal Na(+), K(+)/H(+) antiporter . Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo . Plays a critical role during neurodevelopment by regulating synaptic development and plasticity (By similarity). Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH . Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane (By similarity).
PTM: Ubiquitinated (in vitro).
Location Topology: Multi-pass membrane protein
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Sequence Mass (Da): 77917
Sequence Length: 701
Subcellular Location: Endosome membrane
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Q96T83 | MEPGDAARPGSGRATGAPPPRLLLLPLLLGWGLRVAAAASASSSGAAAEDSSAMEELATEKEAEESHRQDSVSLLTFILLLTLTILTIWLFKHRRVRFLHETGLAMIYGLIVGVILRYGTPATSGRDKSLSCTQEDRAFSTLLVNVSGKFFEYTLKGEISPGKINSVEQNDMLRKVTFDPEVFFNILLPPIIFHAGYSLKKRHFFRNLGSILAYAFLGTAVSCFIIGNLMYGVVKLMKIMGQLSDKFYYTDCLFFGAIISATDPVTVLAIFNELHADVDLYALLFGESVLNDAVAIVLSSSIVAYQPAGLNTHAFDAAAFFKSVGIFLGIFSGSFTMGAVTGVNANVTKFTKLHCFPLLETALFFLMSWSTFLLAEACGFTGVVAVLFCGITQAHYTYNNLSVESRSRTKQLFEVLHFLAENFIFSYMGLALFTFQKHVFSPIFIIGAFVAIFLGRAAHIYPLSFFLNLGRRHKIGWNFQHMMMFSGLRGAMAFALAIRDTASYARQMMFTTTLLIVFFTVWIIGGGTTPMLSWLNIRVGVEEPSEEDQNEHHWQYFRVGVDPDQDPPPNNDSFQVLQGDGPDSARGNRTKQESAWIFRLWYSFDHNYLKPILTHSGPPLTTTLPAWCGLLARCLTSPQVYDNQEPLREEDSDFILTEGDLTLTYGDSTVTANGSSSSHTASTSLEGSRRTKSSSEEVLERDLGMGDQKVSSRGTRLVFPLEDNA | Function: Golgi Na(+), K(+)/(H+) antiporter. Mediates the electoneutral influx of Na(+) or K(+) in exchange for H(+). May contribute to the regulation of Golgi apparatus volume and pH.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Sequence Mass (Da): 80131
Sequence Length: 725
Subcellular Location: Golgi apparatus
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Q5ZJ75 | MAEFANASHEVINVTLGTTLAATTKLVMPTPAKPILPVQTGVQAQQEEQSSGMTIFFSLLVLAICIILVHLLIKYRLHFLPESVAVVSLGIIMGAFIKIIEAQKLANWKEEEMFRPNMFFLLLLPPIIFESGYSLHKGNFFQNIGSITLFSVFGTAISAFIVGGGIYFLGQADVIYKLNMTDSFAFGSLISAVDPVATIAIFNALNVDPVLNMLVFGESILNDAVSIVLTNTAEGLTRENMSDVSGWQTFLQALGYFLKMFFGSAALGTLTGLISALVLKHIDLRKTPSLEFGMMIIFAYLPYGLAEGISLSGIMAILFSGIVMSHYTHHNLSPVTQILMQQTLRTVAFMCETCVFAFLGLSIFSFPHKFEMSFVIWCIVLVLFGRAVNIFPLSYLLNFFRDHKITPKMMFIMWFSGLRGAIPYALSLHLGLEPIEKRQLIGTTTIIIVLFTVLLLGGGTMPLIRLIGIEDSKARKRNKKDVNLSKTEKMGNTIESEHLSELTEGEYEAQYIKRQDLKGFMWLDAKYLNPFFTRRLTQEDLHHGRIQMKTLTNKWYEEVRQGPSGSEDDEQELL | Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64133
Sequence Length: 574
Subcellular Location: Golgi apparatus membrane
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Q9Y2E8 | MGEKMAEEERFPNTTHEGFNVTLHTTLVVTTKLVLPTPGKPILPVQTGEQAQQEEQSSGMTIFFSLLVLAICIILVHLLIRYRLHFLPESVAVVSLGILMGAVIKIIEFKKLANWKEEEMFRPNMFFLLLLPPIIFESGYSLHKGNFFQNIGSITLFAVFGTAISAFVVGGGIYFLGQADVISKLNMTDSFAFGSLISAVDPVATIAIFNALHVDPVLNMLVFGESILNDAVSIVLTNTAEGLTRKNMSDVSGWQTFLQALDYFLKMFFGSAALGTLTGLISALVLKHIDLRKTPSLEFGMMIIFAYLPYGLAEGISLSGIMAILFSGIVMSHYTHHNLSPVTQILMQQTLRTVAFLCETCVFAFLGLSIFSFPHKFEISFVIWCIVLVLFGRAVNIFPLSYLLNFFRDHKITPKMMFIMWFSGLRGAIPYALSLHLDLEPMEKRQLIGTTTIVIVLFTILLLGGSTMPLIRLMDIEDAKAHRRNKKDVNLSKTEKMGNTVESEHLSELTEEEYEAHYIRRQDLKGFVWLDAKYLNPFFTRRLTQEDLHHGRIQMKTLTNKWYEEVRQGPSGSEDDEQELL | Function: Na(+)/H(+) antiporter. Mediates the electoneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry . Acts as an Na(+)/H(+) exchanger in the trans-Golgi. Contributes to the regulation of pH regulation of Golgi apparatus, and consequently, in protein trafficking and endosomal morphology . In germ cells, plays a crucial role in acrosome biogenesis and sperm development, probably by playing a role in the fusion of the Golgi-derived vesicles that form the acrosomal cap (By similarity). Can also be active at the cell surface of specialized cells. In the small intestine, at the cell membrane, plays a major physiological role in transepithelial absorption of Na(+) and regulates intracellular pH homeostasis of intestinal epithelial cells . Acts as an important regulator of mucosal integrity in the intestine and in the stomach, could mediate the pH fluctuation necessary for mucin exocytosis or assist membrane trafficking of other proteins (By similarity). Plays a role in photoreceptor survival and in the maintenance of intracellular pH homeostasis in retinal pigment epithelium (RPE cells) (By similarity).
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65422
Sequence Length: 581
Subcellular Location: Golgi apparatus membrane
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Q8IVB4 | MERQSRVMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCVKLTFSPSTLLVNITDQVYEYKYKREISQHNINPHQGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMIHAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAIITALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSSDSKIRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKQKIPWNFQHMMMFSGLRGAIAFALAIRNTESQPKQMMFTTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDENLKEDPSSQHQEANNLDKNMTKAESARLFRMWYSFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDVECIVNQDELAINYQEQASSPCSPPARLGLDQKASPQTPGKENIYEGDLGLGGYELKLEQTLGQSQLN | Function: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+) (Probable). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, e.g., endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters . Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain . Regulates synaptic transmission by regulating the luminal pH of axonal endosomes (By similarity). Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages (By similarity). Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity).
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72565
Sequence Length: 645
Subcellular Location: Late endosome membrane
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Q49UX4 | MRKKIIATVIGTSALAAVTWTNADAATTYKVKSGDSLWSIANKYNMSVAKLKSLNNLTSNVIFPNQSLKVSGSTSSSTSSNTSTGSTYTVKSGDTLSGIAAKYGTTYQKIMSLNGLSNFNIYPGQKLKVSGAASSSSSNTSGNTSSGSTTTYTVKSGDSLSAIAAKYGTTYQKIMSLNGLTNFNIYPGQKLKVSGKASTGGSGSSSTGSAGYKTPVFNHSNLYDWGQCTWHVFNKRAQIGKGISTYWWNANNWDTAAAADGYTIDRKATVGSILQSDMGYYGHVAFVESVNANGSITISEMNYSASPGIVTYRTIPASQVSSYVYIH | Function: Peptidoglycan hydrolase involved in the splitting of the septum during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 34491
Sequence Length: 327
Subcellular Location: Secreted
EC: 3.5.1.28
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Q8ZQQ2 | MFNITNIQSTARHQSISNEASTEVPLKEEIWNKISAFFSSEHQVEAQNCIAYLCHPPETASPEEIKSKFECLRMLAFPAYADNIQYSRGGADQYCILSENSQEILSIVFNTEGYTVEGGGKSVTYTRVTESEQASSASGSKDAVNYELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLKILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPPELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENLPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNPFSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLHQAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDTQNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISCEDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIFRLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTTMTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALWGPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELEDLRIADDSDAERTTEVQMDAERAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYWR | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death.
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 86872
Sequence Length: 765
Domain: The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins.
Subcellular Location: Secreted
EC: 2.3.2.27
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Q4E4I4 | MVLMGPHSALRLLPLKTQAIRFVLLLLLSVLILAVALLVTNARMPDPKVVRPLPDIGFEVFPKVGWLEHLTDVCIFILNFLSLLVVFKLYLLHRQNEGLDELQPFSCCPLIGKIIFGVWDSGRQSGIEKRDAHLIAWIRYFTTYFIVLLFRAIVVVMTSYPATDNHCQNPMKITNPVKNVIMTLVTFGSGSIHCGDLMFSGHTVSITLSLLVQWIYGSMLHWVFRPASVLLVLLSFYSIIASRSHYTDDILVSFYITVTTFLVLRHSPDGAPWQLQLLIGWWPCCVSNEETEDSDRNPTFVAVEVFLPHGDYQCAERISEEKTTVGPACGNFGHW | Function: Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37851
Sequence Length: 335
Subcellular Location: Membrane
EC: 2.7.8.-
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Q05047 | MEMDMDTIRKAIAATIFALVMAWAWRVLDWAWFTPKRIEKRLRQQGFRGNPYRFLVGDVKESGKMHQEALSKPMEFNNDIVPRLMPHINHTINTYGRNSFTWMGRIPRIHVMEPELIKEVLTHSSKYQKNFDVHNPLVKFLLTGVGSFEGAKWSKHRRIISPAFTLEKLKSMLPAFAICYHDMLTKWEKIAEKQGSHEVDIFPTFDVLTSDVISKVAFGSTYEEGGKIFRLLKELMDLTIDCMRDVYIPGWSYLPTKRNKRMKEINKEITDMLRFIINKRMKALKAGEPGEDDLLGVLLESNIQEIQKQGNKKDGGMSINDVIEECKLFYFAGQETTGVLLTWTTILLSKHPEWQERAREEVLQAFGKNKPEFERLNHLKYVSMILYEVLRLYPPVIDLTKIVHKDTKLGSYTIPAGTQVMLPTVMLHREKSIWGEDAMEFNPMRFVDGVANATKNNVTYLPFSWGPRVCLGQNFALLQAKLGLAMILQRFKFDVAPSYVHAPFTILTVQPQFGSHVIYKKLES | Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. secologanin) biosynthesis pathway. Catalyzes the conversion of loganin into secologanin . Catalyzes the conversion of secologanin into secoxyloganin .
Catalytic Activity: loganin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + secologanin
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60558
Sequence Length: 524
Pathway: Alkaloid biosynthesis; secologanin biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.19.62
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B3A0M2 | MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNIHTIAWIRFITSYALLLLFRSAVIVMTSLPAPDDLCQDPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWWPCCGANSREVTEDSQPVMVAFKSEELDEMNGVLEGRQKKHGGVGDGESLMFKCGAYV | Function: Bifunctional sphingomyelin (SM)/ethanolamine phosphorylceramide (EPC) synthase with minimal inositol phosphorylceramide (IPC) synthase activity . Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors . SM is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphoryl headgroup from a 1,2-diacyl-sn-glycero-3-phosphocholine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) with release of 1,2-diacyl-sn-glycerol . Also catalyzes the reverse reaction, production of ceramide from sphingomyelin . EPC is synthesized by transferring phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF . The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40900
Sequence Length: 365
Subcellular Location: Golgi apparatus membrane
EC: 2.7.8.-
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Q0UAL6 | MSEALKIESRPIPAFYCCYLLRSKNRKSYYIGSTPNPARRLGQHNGSSKGGAKRTSMQGKRPWEMTCIVTGFPSKFAALQFEWAWQNTHATRHIDKDVRDARAEELQKGKKKATSPGRRRKRPPMSLEARLKNLHHLLSVDSFCRWPLNLRFFAPDVFVQWERHTTKMTTTLRKSITIQLTPAEIPKLASDVSTELQTHFIPEVIRAIPVAYEDCKQYIEKSRRVLEDDQRLGCGVCKNPADMSSSLILVCPIEACQTVSHLSCLSNKFLTEGGELETLVPLEGTCPGCRSCIKWATMIKELSLRTNGEEELKLLFKPKRKRKSDNPAESDAADGQALEQEDEELDETWMEDMSQDEEPSPVKKSR | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 41673
Sequence Length: 366
Subcellular Location: Nucleus
EC: 3.1.-.-
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A5DFX7 | MAPTQIFVSPEFYGVYILQSEPSPRSFYIGSTPDPIRRLRQHNGDLKQGAFRTRRTSRRPWKMIAITHNFPSRVAALQFEHALQHPKTSRHMAGGGGSVTATAETAKSAPVAGKSDATSPAKNRRNAAPVARSGRTHLRNVARLLESPYFSRMGLKVTIFDPSLFDMDLLPAQLQSFAAFSGARTAACSDYFSVAKKAALTTAHCCLCSDAIDYVPEMLPESIKDVLLVLPLIAVCPSCAVICHLRCLAASWYQSSEINAALIPSDVSCSQCGAQTSWRLVADMATKLRQYALSS | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 32138
Sequence Length: 295
Subcellular Location: Nucleus
EC: 3.1.-.-
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A3LZG5 | MPRRPSTGTQSDTPALHVVPSFYGVYLLQSEPKPSSFYIGSTPDPPRRLRQHNGDLKAGGAYRTKRAGFRPWRMLLVVYDFPSKVSALQFEHSFQHCHETRHIKQEERISKNKLSGRTLHHKVANVALLLRSSYFRHLPLKVLVFEEAVYNSFMNNKFVTCSHVDLLNTNFNEYFSVMEKDLDSTVDSWKTRHTNENEIWSMAKEAVILGSPRCALCLEPIEQVPETSSPISKRSDLQRYLQSESLPLVTMCYNPQCRDVFHLSCLGHRFTNSDGFQSLIPATVNRCCSCNAKLEWRTLAKIATKLRYYVLKDSLQLPSQVLENDDNYESQNVNDS | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 38610
Sequence Length: 336
Subcellular Location: Nucleus
EC: 3.1.-.-
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B2WM34 | MTDGLKIDSRPLPAFYCCYLLRSKNRKAFYIGSTPNPARRLGQHNGSSKGGAKRTSMQGKRPWEMTCIVTGFPSRFAALQFEWAWQNTHATRHIERDVREARKDELEKGRKNASPVKRSRPPMSLEARLKNLHHLLGVGSFSRWPLHVRFFAPDVFSQWEKHISKMNTSLRKSITIRLTPAELPKLAPDVSSEMRTHFIPEVIRAIPVAYEDIKPYVEKSMSTLRDGKTRDCGVCKKDVNVDRSLVLICPNETCCSVSHMSCLSQRFLAEEANKEAFIPIEGTCPSCHSPIKWSDMIKELSLRMRGEDELKTLFKTKRKKKQVDTTEDDTDEYPDIDDLNADLDEDLDETWMENVNEEDDKPRS | Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 41819
Sequence Length: 364
Subcellular Location: Nucleus
EC: 3.1.-.-
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B6JY16 | MFYCCYLLVSEKAASRSVYIGSTPDPARRLRQHNGEIKGGAYKTKRSRPWKVACFVHGFPTKIAALQFEWVWQHPQSTRHDDLRQHSRVVSVKRQTLLSCVRALGVMLCCEAWSRWGLRVAIFDDAVHRLWLKERLPSNCIQLCSFDDVESLRLADYGGDAGWLDTQRKKRAQLSVQAQCSICVRAILLPCFFLCCPFPDCRMIAHSTCLAASFLQEAQDDEHILPISGTCARCKRLLSWKLLVQASLSPSDEDNGAVGDTGESDDNNERESS | Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 30842
Sequence Length: 273
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q9P7M3 | MDLCNFYCCYLLKSNRTQSSGAVYIGSTPDPPRRLRQHNGEIVGGASKTKHGRPWSISCLVYGFPNKVSALKFEWNWQNLGISRYTKDCDFRSKKQKTIMYCLKGLKHLVDSDTWRRWPLNITFLNKTAFSKWNQLGKTYGNINVYFDEEWLNGFHEKVIQKTYDHKLCLRKTISEPVKCNLCYECIESDELRANCPFTDCNSINHLTCLASSFLTEECQVLPIEGMCTKCKRVLRWREFLSTVFTTSLETDERDFESENRIEIIDLELEK | Cofactor: Divalent cation. Mg(2+) is preferred. Has Holliday junction resolvase activity solely in the presence of Mn(2+).
Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.
Sequence Mass (Da): 31701
Sequence Length: 271
Subcellular Location: Nucleus
EC: 3.1.-.-
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B8MDD1 | MTTTVSEEAVLTKPIPAFYCCYLLRSAKRPSALYIGSTPDPARRLEQHNGFAKGGAKRTERNTLRPWEMVAIVEGFPSRTGALQFEWSWQHVHTTRHIGAVETDQLNRKRKNPPTDKGSGIWTSTPKVLGNLHQLLRSTYFGTWPLTVRFLSSEAHNHWQRWIERADGLLPDTIRVKLDFRAEGASVLDSNLPANDMTHIDATYGGIQEHLAKSTSLLGDNTNSLSCEVCQQQLSTQTEIIVVCSHRRCHAVFHVNCISQLFLEDEGSSGLVPILGECPACRQEVTWVELMKELSMRLHGGKNATKLLKGERKDKANTQGTKSSKGGKKPAKTGDYTLDGDYEDLDEDWMNAVNVEPSSEDGDRNAANVKGSTGRVEIVIDDSEEDGFD | Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 43280
Sequence Length: 389
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q57XV5 | MDTRFHCVYLLTSLDPQCEGAHYIGYTVNPIRRLRQHNGELVNGARRTKRNGRPWLLLMCVSGFGEDRIALKFEWCWQNPSKSTRLKSHVSQLRCVHKLTHAVGVLLLLLRTELFSRLQLTLHIFDREHFDKVISQLLSALPTMEPLVETSLLRVESTTIEQFQTQYMNDGQWGAAVDYGAYFMRAPPGANVDVSKPIVGGQDNTLRCGVMHNNLCEEEVIRQHVKERTLLESGHYPCSLCSLPLRAPYFLRCSRTPFCRLRAHIVCLAMWFIYDSSQRGGDPLVKDAGPAEVAENSNDAACQVNENCYSLSGCGPVVGGIFNHDAYTDRRDDNSPPSPPCPLPTQSSQADASLAATSLPLVPRAPCDCPLCDEELQWSALVYDLKRRVAVEKRRAERERREAMDAEFAQRFQRLQSESNKKSTARERGALEGVRRKRRRRGEVAAKLTQQTAVRHEPTSGASGDRAHSAPPAPSCGGFDEIPANVTNPTAPLHADVLQVTEFNVDEWLNH | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 57341
Sequence Length: 511
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q4PDF6 | MPSSVTKHTIPPFYACYFLRSLSTPGTTYIGSTPAPPRRKRQHNGHLTQGAYKTSRARPWEMECIVYGFSSKIAALQFEWAWAKPHLSRHLKFLTTEHSVDGTPKNTSDWAGMSLFPSTSLTPGQTRWGRPKKRMARPPSSPNARLLAMRALLRSEPFCGWGLKLAFFTEWSWLAYQRLDACDPGLVAKSALSTLQNRYSRSGKPLHALYPVAVCDFSGVDGKREPLVHVSEPYRLDAGVAEHPVKKRQTSSRQKPHTEETSAWPETLPRSANLKGLDACMQDFATFPIPQPAAPNTDLTKKSKRAKKLSDKARPSALEDHDAENGVDDDDTEVEVVATDAANGSDLALSRPLYRMRFDDLNMEESEWKRFAESIAANVGASRSTTQAMSEFLHTCVQRHIAAQDARTANTALPAPTSLCSLCSIPIDLSQQLDFVLCPNPHASTLPLISSSSTASHETISECRETGCDSIFHLSCLARSFLEQQLGDQKATASSASTVLPTHGTCPCHRGEHKEPTMWADVVRAMYRRHERFERLIQFLIRSGRSLEQHLHPPLEVEMTVKGSKIKERVKASVKATEDAQVDIGDQRQVISGTTSRTKAALTRKRRQPTTSSVNAIQVDPLARNGSKIDGDGAGKDTKKNTTQKAKSNETSEVIDLT | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 72798
Sequence Length: 658
Subcellular Location: Nucleus
EC: 3.1.-.-
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A7TTE6 | MMNSSQFSDSQTTSLHRIPTFYCCYLLQSINKKQSFYIGSTPNPVRRLRQHNGNLSNGGAYRTKREGTRPWEMVLVVYGFTSKIAALQFEHAWQHGYKTHYIPMDDRIMKNANSGRTVHHKLGLVRQLLANVYFRHMNLKVHFFSMPILDVWNLNKFNIKMGSNEISVDVSQVSQETKTNLEQASDDDDDNGACSRDERNLQLVTELYDNTVTKENEIKEIIKDILVLGERNCNLCGQCYDYTSEDDTMKMHIFICPNSTCHYEAHLNCLYEKFIEEESGIDSKNILLPNFCMCPGCLDEMSWSDFVKISTMIKNSFSN | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 36874
Sequence Length: 319
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q0IH86 | MVVEVEGFYGVYLLFCTNPKYKGRIYIGFTVNPERRIQQHNGGKHKGGAWKTSGRGPWDMVLIVHGFPNDIAALRFEWAWQHPHVSRRLTHVPRKTKKQSSFDFHLLVLCHMLRVAPWNRLPLTLRWLRQEYRRELPLLLQPPLHMPLAFGQVRARPIPKGEKEKGRLGENRAEETEQEVILLGDAVVQRCRVCYERVQDKDDSLHCFHPGCTLTAHIMCLAKLFLLNEPQNLIPVEGLCPSCGHSLLWGDLIRHRNGCYGDLEEISSSQAHWGDELHRCSD | Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 32576
Sequence Length: 282
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q6C0W7 | MTHQYPPFYGVYLLQSTKKPLSCYVGSTPNPFRRIRQHNGDLKAGGAWRTKRAHLRPWSMVLIVNGFPSKISALKFEHALQHPNMTRLITTKDIKRKVPQKARALGTHLAFIRLLVRCSYFRRMHLRITFFRSHAHEAWEKNDYDVGSLPPQFQVETDYPSDEAEAPPSTVGSGELDINNRSIEEYLQKCRDAVSNDKQLTCYLSEKTLNISEGNVALCHNCDGAFDVAELAERFLNEEIPEELPFTTPSRHIIPIGGDCPSCLARMEWSNVIKGVLAMRPVLEDNKE | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Sequence Mass (Da): 32838
Sequence Length: 288
Subcellular Location: Nucleus
EC: 3.1.-.-
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P38324 | MSQKIQQHQFPDFYCCYLLQSINKRQSFYVGSTPNPVRRLRQHNGKLAVGGAYRTKRDGSRPWEMIMIVRGFPSKIAALQFEHAWQHGYQTHYIAEKDRVVKHKAGGRTLHHKVALMKLLLKHEFFQRMNLIVEVFNIKAWEVWKQDKFFIERDRFPINIQINENALEEPKEKTVDVLMDHSDENLKVVEAVYTKVIENERNIFETFEKKLTTGVVRCEICEKEIDYTSEEQNLKPFVALCNNKDCGCVNHLKCLHRYFLDDEQLMVGRRNLIPRGGKCPKCDMFCDWTTLVKFSTRMKLAHGK | Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro.
Sequence Mass (Da): 35857
Sequence Length: 304
Subcellular Location: Nucleus
EC: 3.1.-.-
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P84022 | MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS | Function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
PTM: Phosphorylated on serine and threonine residues. Enhanced phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle dependent manner and inhibits both the transcriptional activity and antiproliferative functions of SMAD3. This phosphorylation is inhibited by flavopiridol. Maximum phosphorylation at the G(1)/S junction. Also phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1 and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is required for interaction with SMAD4, nuclear location and transactivational activity, and appears to be a prerequisite for the TGF-beta mediated phosphorylation in the linker region. Dephosphorylated in the C-terminal SXS motif by PPM1A. This dephosphorylation disrupts the interaction with SMAD4, promotes nuclear export and terminates TGF-beta-mediated signaling. Phosphorylation at Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Phosphorylated by PDPK1.
Sequence Mass (Da): 48081
Sequence Length: 425
Domain: The MH1 domain is required for DNA binding. Also binds zinc ions which are necessary for the DNA binding.
Subcellular Location: Cytoplasm
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Q13485 | MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD | Function: In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling . Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
PTM: Phosphorylated by PDPK1.
Sequence Mass (Da): 60439
Sequence Length: 552
Domain: The MH1 domain is required for DNA binding.
Subcellular Location: Cytoplasm
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P97471 | MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPAESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPVVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD | Function: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression . Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions . In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8.
PTM: Phosphorylated by PDPK1.
Sequence Mass (Da): 60342
Sequence Length: 551
Domain: The MH1 domain is required for DNA binding.
Subcellular Location: Cytoplasm
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P97454 | MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHNEFNPQHSLLVQFRNLSHNEPHMPQNATFPDSFHQPNNAPFPLSPNSPYPPSPASSTYPNSPASSGPGSPFQLPADTPPPAYMPPDDQMAPDNSQPMDTSSNMIPQTMPSISSRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKSRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSSCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS | Function: Transcriptional regulator that plays a role in various cellular processes including embryonic development, cell differentiation, angiogenesis and tissue homeostasis . Upon BMP ligand binding to their receptors at the cell surface, is phosphorylated by activated type I BMP receptors (BMPRIs) and associates with SMAD4 to form an heteromeric complex which translocates into the nucleus acting as transcription factor. In turn, the hetero-trimeric complex recognizes cis-regulatory elements containing Smad Binding Elements (SBEs) to modulate the outcome of the signaling network . Non-phosphorylated SMAD5 has a cytoplasmic role in energy metabolism regulation by promoting mitochondrial respiration and glycolysis in response to cytoplasmic pH changes. Mechanistically, interacts with hexokinase 1/HK1 and thereby accelerates glycolysis.
PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.
Sequence Mass (Da): 52172
Sequence Length: 465
Subcellular Location: Cytoplasm
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O43541 | MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLQHAPEPDAADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNPR | Function: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta . Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes . Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding . Binds to regulatory elements in target promoter regions .
PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX.
Sequence Mass (Da): 53497
Sequence Length: 496
Subcellular Location: Nucleus
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O35182 | MFRSKRSGLVRRLWRSRVVPDREEGSGGGGGVDEDGSLGSRAEPAPRAREGGGCSRSEVRSVAPRRPRDAVGPRGAAIAGRRRRTGGLPRPVSESGAGAGGSPLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFTAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLLQHADAAHGPYDPHSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR | Function: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (By similarity). Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes . Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions (By similarity).
PTM: Monoubiquitinated at Lys-174 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte differentiation (By similarity). Ubiquitinated by WWP1 . Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling .
Sequence Mass (Da): 53714
Sequence Length: 495
Subcellular Location: Nucleus
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O15105 | MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR | Function: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access . Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (By similarity). Phosphorylated by PDPK1.
Sequence Mass (Da): 46426
Sequence Length: 426
Subcellular Location: Nucleus
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P61278 | MLSCRLQCALAALSIVLALGCVTGAPSDPRLRQFLQKSLAAAAGKQELAKYFLAELLSEPNQTENDALEPEDLSQAAEQDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC | Function: Inhibits the secretion of pituitary hormones, including that of growth hormone/somatotropin (GH1), PRL, ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-stimulated secretion of GH1 and LH; the inhibition of ghrelin-stimulated secretion of GH1 can be further increased by neuronostatin.
PTM: C-terminal amidation of the neuronostatin peptide is required for its biological activity, including for the regulation of mean arterial pressure.
Sequence Mass (Da): 12736
Sequence Length: 116
Subcellular Location: Secreted
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Q9LM02 | MDLASNLGGKIDKSDVLTAVEKYEQYHVFHGGNEEERKANYTDMVNKYYDLATSFYEYGWGESFHFAQRWKGESLRESIKRHEHFLALQLGIQPGQKVLDVGCGIGGPLREIARFSNSVVTGLNNNEYQITRGKELNRLAGVDKTCNFVKADFMKMPFPENSFDAVYAIEATCHAPDAYGCYKEIYRVLKPGQCFAAYEWCMTDAFDPDNAEHQKIKGEIEIGDGLPDIRLTTKCLEALKQAGFEVIWEKDLAKDSPVPWYLPLDKNHFSLSSFRLTAVGRFITKNMVKILEYIRLAPQGSQRVSNFLEQAAEGLVDGGRREIFTPMYFFLARKPE | Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of cycloartenol to form 24-methylene cycloartenol.
Catalytic Activity: cycloartenol + S-adenosyl-L-methionine = 24-methylenecycloartanol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38268
Sequence Length: 336
Pathway: Steroid biosynthesis; sterol biosynthesis.
EC: 2.1.1.41
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Q54I98 | MNTQQRAMEGDLSRIVAISRKEKDAVSRNDKVDDTLNGYKELFKGNDDKAIQARKNNYTHMVNTFYDLATDFYEFGWGQSFHFATRHKYESFEASIARHEMYMAHQLGLFPGMKVIDIGCGVGGPMRTIARFSGANVVGLNNNEYQIQRGKRLNESAGLSHLCSFIKADFMHVPVEDNTYDCAYQIEATCHAPDLVGLYKEVFRIVKPGGLFGGYEWIMTNKFNPEDPVEVNIKKQIELGNGLPDLVKPAEIINAAKAAGFEVITAFDVAETSELPWYLPLSSGVSITGFLHTGVGRYLTGKFTQLLEIVKLAPAGSYNTNVWLQNAATFLVQGGEKQIFSPMFFLLCRKPSTD | Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of cycloartenol to form 24-methylene cycloartenol.
Catalytic Activity: S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39559
Sequence Length: 354
Pathway: Steroid biosynthesis; sterol biosynthesis.
EC: 2.1.1.41
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Q39227 | MDSLTLFFTGALVAVGIYWFLCVLGPAERKGKRAVDLSGGSISAEKVQDNYKQYWSFFRRPKEIETAEKVPDFVDTFYNLVTDIYEWGWGQSFHFSPSIPGKSHKDATRLHEEMAVDLIQVKPGQKILDVGCGVGGPMRAIASHSRANVVGITINEYQVNRARLHNKKAGLDALCEVVCGNFLQMPFDDNSFDGAYSIEATCHAPKLEEVYAEIYRVLKPGSMYVSYEWVTTEKFKAEDDEHVEVIQGIERGDALPGLRAYVDIAETAKKVGFEIVKEKDLASPPAEPWWTRLKMGRLAYWRNHIVVQILSAVGVAPKGTVDVHEMLFKTADYLTRGGETGIFSPMHMILCRKPESPEESS | Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the methylene group of 24-methylene lophenol to form 24-ethylidene lophenol.
Catalytic Activity: 24-methylidenelophenol + S-adenosyl-L-methionine = (Z)-24-ethylidenelophenol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40450
Sequence Length: 361
Pathway: Steroid biosynthesis; sterol biosynthesis.
EC: 2.1.1.143
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Q94JS4 | MDSVALYCTAGLIAGAVYWFICVLGPAERKGKRASDLSGGSISAEKVKDNYNQYWSFFRKPKEIESAEKVPDFVDTFYNLVTDIYEWGWGQSFHFSPHVPGKSDKDATRIHEEMAVDLIKVKPGQKILDAGCGVGGPMRAIAAHSKAQVTGITINEYQVQRAKLHNKKAGLDSLCNVVCGNFLKMPFDENTFDGAYSIEATCHAPKLEEVYSEIFRVMKPGSLFVSYEWVTTEKYRDDDEEHKDVIQGIERGDALPGLRSYADIAVTAKKVGFEVVKEKDLAKPPSKPWWNRLKMGRIAYWRNHVVVVILSAIGVAPKGTVDVHKMLFKTADYLTRGGETGIFSPMHMILCRKPEKASE | Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the methylene group of 24-methylene lophenol to form 24-ethylidene lophenol.
Catalytic Activity: 24-methylidenelophenol + S-adenosyl-L-methionine = (Z)-24-ethylidenelophenol + H(+) + S-adenosyl-L-homocysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40124
Sequence Length: 359
Pathway: Steroid biosynthesis; sterol biosynthesis.
Subcellular Location: Membrane
EC: 2.1.1.143
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O43623 | MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLYESYSMPVIPQPEILSSGAYSPITVWTTAAPFHAQLPNGLSPLSGYSSSLGRVSPPPPSDTSSKDHSGSESPISDEEERLQSKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQSRKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH | Function: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis.
PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation.
Sequence Mass (Da): 29986
Sequence Length: 268
Domain: Repression activity depends on the C-terminal DNA-binding zinc fingers and on the N-terminal repression domain.
Subcellular Location: Nucleus
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O08954 | MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLCESYPMPVIPKPEILTSGAYSPITVWTSAVPFHSPLPSGLSPLTGYSSSLGRVSPLPSSDTSSKDHSGSESPISDEEERLQPKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQARKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH | Function: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells. Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis (By similarity).
PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation.
Sequence Mass (Da): 29936
Sequence Length: 268
Domain: Repression activity depends on the C-terminal DNA-binding zinc fingers and on the N-terminal repression domain.
Subcellular Location: Nucleus
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Q3KNW1 | MPRSFLVKTHSSHRVPNYRRLETQREINGACSACGGLVVPLLPRDKEAPSVPGDLPQPWDRSSAVACISLPLLPRIEEALGASGLDALEVSEVDPRASRAAIVPLKDSLNHLNLPPLLVLPTRWSPTLGPDRHGAPEKLLGAERMPRAPGGFECFHCHKPYHTLAGLARHRQLHCHLQVGRVFTCKYCDKEYTSLGALKMHIRTHTLPCTCKICGKAFSRPWLLQGHVRTHTGEKPYACSHCSRAFADRSNLRAHLQTHSDAKKYRCRRCTKTFSRMSLLARHEESGCCPGP | Function: Seems to inhibit myoblast differentiation. Transcriptional repressor of E-box-dependent transactivation of downstream myogenic bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-CAGGTG-3' and 5'-CACCTG-3' (By similarity).
Sequence Mass (Da): 32474
Sequence Length: 292
Domain: Binds E-box via C2H2-type zinc finger domain.
Subcellular Location: Nucleus
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Q9QY31 | MPRSFLVKTHSSHRVPNYGKLETLREANGSCSACKELAGSRHLPDEEAPCNPSDPLQPWDSTSAVACISLPLLPNHRETLGVSGPEPQETSWVGPRAAQAPSVTLKDSFTLPPLLVLPTRWPPILGPDGALNEHLRAEGTSRVPGSFECIHCHRPYHTLAGLARHQQLHCHLPTGRAFTCRYCDKEYASLGALKMHIRTHTLPCICKVCGKAFSRPWLLQGHIRTHTGEKPYTCSHCSRAFADRSNLRAHLQTHVGTKKYRCAVCPKAFSRMSLLARHEEAGCCPGP | Function: Seems to inhibit myoblast differentiation. Transcriptional repressor of E-box-dependent transactivation of downstream myogenic bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-CAGGTG-3' and 5'-CACCTG-3'.
Sequence Mass (Da): 31636
Sequence Length: 287
Domain: Binds E-box via C2H2-type zinc finger domain.
Subcellular Location: Nucleus
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Q41358 | MRLVAKLLYLAVLAICGLGIHGALTHPRVTPPVYPSVSFNLTGADTYEPFLRALQEKVILGNHTAFDLPVLNPESQVSDSNRFVLVPLTNPSGDTVTLAIDVVNLYVVAFSSNGKSYFFSGSTAVQRDNLFVDTTQEELNFTGNYTSLERQVGFGRVYIPLGPKSLDQAISSLRTYTLTAGDTKPLARGLLVVIQMVSEAARFRYIELRIRTSITDASEFTPDLLMLSMENNWSSMSSEIQQAQPGGIFAGVVQLRDERNNSIEVTNFRRLFELTYIAVLLYGCAPVTSSSYSNNAIDAQIIKMPVFRGGEYEKVCSVVEVTRRISGWDGLCVDVRYGHYIDGNPVQLRPCGNECNQLWTFRTDGTIRWLGKCLTASSSVMIYDCNTVPPEATKWVVSIDGTITNPHSGLVLTAPQAAEGTALSLENNIHAARQGWTVGDVEPLVTFIVGYKQMCLRENGENNFVWLEDCVLNRVQQEWALYGDGTIRVNSNRSLCVTSEDHEPSDLIVILKCEGSGNQRWVFNTNGTISNPNAKLLMDVAQRDVSLRKIILYRPTGNPNQQWITTTHPA | Function: Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin . Behaves as a type-2 ribosome-inactivating protein . Strongly inhibits mammalian but not plant ribosomes . The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA (Probable). The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity) (Probable). Involved in plant defense against insects (By similarity).
PTM: The precursor is processed in two chains, A and B, that are linked by a disulfide bond . A small truncated form corresponding roughly to the second ricin B-type lectin domain of the B chain, TrSNAI, can also be produced .
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 63102
Sequence Length: 570
Domain: The B-chain consists of six tandemly repeated subdomains. Only subdomains 1-alpha and 2-gamma possess a functional carbohydrate-binding site.
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P0CI51 | MNHLILIVAMCLMVIGVQCLKDGYLYDDVDCKFSCWDNEYCRKLCKSKKAVGGYCWRWRFSCYCTGLPDNEKTEGTYKCGQGRFLMGKDK | Function: Binds voltage-independently at site-3 of voltage-gated sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.
Sequence Mass (Da): 10446
Sequence Length: 90
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q948Z4 | MKLFLLTLLLVTLVITPSLIQTTMAGSSFCDSKCKLRCSKAGLADRCLKYCGICCEECKCVPSGTYGNKHECPCYRDKKNSKGKSKCP | Function: Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria.
PTM: Six disulfide bonds may be present.
Sequence Mass (Da): 9664
Sequence Length: 88
Subcellular Location: Secreted
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Q93X17 | MAISKALFASLLLSLLLLEQVQSIQTDQVTSNAISEAAYSYKKIDCGGACAARCRLSSRPRLCNRACGTCCARCNCVPPGTSGNTETCPCYASLTTHGNKRKCP | Function: Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria.
PTM: Six disulfide bonds may be present.
Sequence Mass (Da): 11038
Sequence Length: 104
Subcellular Location: Secreted
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P05049 | MIILWSLIVHLQLTCLHLILQTPNLEALDALEIINYQTTKYTIPEVWKEQPVATIGEDVDDQDTEDEESYLKFGDDAEVRTSVSEGLHEGAFCRRSFDGRSGYCILAYQCLHVIREYRVHGTRIDICTHRNNVPVICCPLADKHVLAQRISATKCQEYNAAARRLHLTDTGRTFSGKQCVPSVPLIVGGTPTRHGLFPHMAALGWTQGSGSKDQDIKWGCGGALVSELYVLTAAHCATSGSKPPDMVRLGARQLNETSATQQDIKILIIVLHPKYRSSAYYHDIALLKLTRRVKFSEQVRPACLWQLPELQIPTVVAAGWGRTEFLGAKSNALRQVDLDVVPQMTCKQIYRKERRLPRGIIEGQFCAGYLPGGRDTCQGDSGGPIHALLPEYNCVAFVVGITSFGKFCAAPNAPGVYTRLYSYLDWIEKIAFKQH | Function: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo.
Sequence Mass (Da): 48458
Sequence Length: 435
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9VQF9 | MDSDSTVTSLEENTENFCTNPTRDILAEGITNLFKPTIERLDERVASTIQLQAELRGQLDALAAQLRDIEKAQSQIPEFADKVKELLNVKHKVTVISNVLVTSQERLTGLHKLIEKEQRRRQALLDSALSTNIS | Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis . May participate in the coupling of lysosomes to microtubule plus-end-directed kinesin motor (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15056
Sequence Length: 134
Subcellular Location: Membrane
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O95295 | MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK | Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells . As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor .
PTM: Phosphorylated by CSNK1D/CK1 (By similarity). Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14874
Sequence Length: 136
Subcellular Location: Membrane
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E0W3E3 | MKTAEKLGIIGTTISIFGIGFGWGVFPWLIRMQIGRVSLSPGSETREFWEKIPFPIDFKIHIFNITNHVEVQNEGKIPNLQEIGPYYYKEWKEKSEMIDYENDDSITFFMKNTWFDNKEKTLPLTGDEMVIIPNPILVGLITAAEREKKGVLPMINKAIPILFNKPDSVFLKIKVYDLLFGGIIFNCTTKDFSASAVCAVLKKEAPFLETVSRSVFKFSILNQKNGTEEPLKLQIKRGIKDYTEVGKVIGANGKNKLTNWRGRPCNNLEGTDGTIFPSDISEHQDIWSFNLELCRSIPAKFVRKSEYKGIPAFRYNVTIGDTSTDPSLKCLCINDTFCWKKGAMELLKCSGLPVVATLPHFYDSHEDFLNGVKGLSPNEENHSIFFDIEPMTGTPLYAKKRIQFSFPLGKINKIDLTKNLPDTLLPFLWVEESIELPDYLIDKLNSELFRILQFLDVIKWVITLFGAGVVSGGVGLYYKEKNSLPITPTSSATSKKIDNPTDKTTTHELGHTNFGYIN | Function: Plays an olfactory role that is not restricted to pheromone sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58606
Sequence Length: 518
Subcellular Location: Cell membrane
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E2IHA6 | MKLPKHLKFAAGAGGAFLFGILFGWVMFPAILKGQLKKEMALSKKTDVRKMWETIPFALNFKVYLYNYTNPEEVQKGGVPIIKEVGPYHFDEWKEKVEIEDHEEDDTITYKKRDTFYFNQEKSGPGLTGEEVITMPHVFMLAMATVVSREKPAMMNMIGKAINGIFDNPADVFIRVKALDIMFRGTMINCARTEFAPKAVCTALKKEAVNGLVMEPNNQFRFSLFGSRNGTIDPHVVTVKRGIKNVMDVGQVVAIDGKPQQDVWRDHCNEYQGTDGTVFPPFLTEHDRLQSFSGDLCRSFKPWYQKKSFYRGITTHRYIANIGDFANDPELNCFCDGPCPPKGLMDLMKCMKAPMYASMPHFLDSDPELLKNVKGLNPDVNEHGIEIDFEPISGTPMVANQRVQFNMQLLKHDKVELLNNLPDTIVPLFWIDEGLALNKTFVNMLKFQLFYPKKAVGVIKWLLVTFGGFGLIGCTIYHYKDRIMSFASSPGSAAVTKVKPEEVEQKDVSVIGQPQEPAKINM | Function: Plays an olfactory role that is not restricted to pheromone sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59030
Sequence Length: 522
Subcellular Location: Cell membrane
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D2A0H5 | MRLPVKIAIGCAIGLVVIIVFGFIAFPKMIKGKVKSMINLNKGSEIRQMFVKVPFALDFKIYMFNVTNPMDVQKGALPVLKEVGPFCFEEWKEKVDLDDNDDEDVMFYNPKDTFYKANGPGCLDGSQMITMAHPLILGMVNTVVRTKPGAISLISKAINSIYGNPDSIFMTASAMDILFDGVVIKCGVKDFAGKAVCSQLKEAPDLRHVDENDLAFSFIGPKNATPGKRFKVLRGVKESHDVGRILEYDNKKEMEVWPTKECNQYKGTDGTVFPPYLTKEEGLASYAPDLCRSLVAVYSGDTKYDGIPVRIYTATLGDMSKNADEKCYCPTPDTCLKKGMMDLFKCAGVPVYVSLPHFYESDESYVKGVVGLNPNKKDHGIQILFESTTGGPVKAAKRLQFNMPLEPNPKLPIFANLPNTVLPLFWVEEGVALNNTFTKPLKDLFKIMKIVKIAKWLIMLGCLGGLGAAGYLYFSKKGEANITPVHKVKPAENGVSTLGGEVNHAMSDNEIEKY | Function: Plays an olfactory role that is not restricted to pheromone sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56760
Sequence Length: 514
Subcellular Location: Cell membrane
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C3U0S3 | MMVMNTELRQDTPQFKRWEAVPQPLDFKVYIFNVTNPYEVQMGRRPRVVEVGPYVYFQYRHKDNIRFSRDRSKVHFSQQQMYVFDAESSYPLTENDQLTVLNMHMNSILQIIDTQAKETITNFRSDVNNTLEKIPVVRVIKRIIEKTTPIQSILQLAEDETYDSLRLINAELNRIFGRPDSMFLRTTPREFLFEGVPFCVNVIGIAKAICKEIEKRNTKTIRVQPDGSMKFSFFNHKNMTNDGTYTINTGIKEPALTQMIEYWNGRNTLDRWINQSAGSSSKCNKIVGTDGSGYPPFREGVERMTIFSSDICRTVDIKYVGPSSYEGIPALRFETDSHFLNEIGPEYGNDCYCVNRIPKAIVKNNGCLYKGALDLSTCFDAPVVLTHPHMMGAAQEYTSLIDGLYPDPEKHQIFVDVEPLTGTPLNGGKRVQFNMFLRRIDSIRLTDRLQTTLFPVLWIEEGIALNEDMVKLIDDSLMKVLTLLDIVQWVMIGSGLLLAIIMPIVYFIKRRPSSGSITPTLTTTTSTVSISDGGGLGGNPQK | Function: Plays an olfactory role that is not restricted to pheromone sensitivity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61707
Sequence Length: 542
Subcellular Location: Cell membrane
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E1JI63 | MIHWSLIVSALGVCVAVLGGYCGWILFPNMVHKKVEQSVVIQDGSEQFKRFVNLPQPLNFKVYIFNVTNSDRIQQGAIPIVEEIGPYVYKQFRQKKVKHFSRDGSKISYVQNVHFDFDAVASAPYTQDDRIVALNMHMNAFLQVFEREITDIFQGFANRLNSRLNQTPGVRVLKRLMERIRGKRKSVLQISENDPGLALLLVHLNANLKAVFNDPRSMFVSTSVREYLFDGVRFCINPQGIAKAICNQIKESGSKTIREKSDGSLAFSFFGHKNGSGHEVYEVHTGKGDPMRVLEIQKLDDSHNLQVWLNASSEGETSVCNQINGTDASAYPPFRQRGDSMYIFSADICRSVQLFYQTDIQYQGIPGYRYSIGENFINDIGPEHDNECFCVDKLANVIKRKNGCLYAGALDLTTCLDAPVILTLPHMLGASNEYRKMIRGLKPDAKKHQTFVDVQSLTGTPLQGGKRVQFNMFLKSINRIGITENLPTVLMPAIWVEEGIQLNGEMVAFFKKKLINTLKTLNIVHWATLCGGIGVAVACLIYYIYQRGRVVEPPVK | Function: Plays an olfactory role that is not restricted to pheromone sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62634
Sequence Length: 556
Subcellular Location: Cell membrane
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B2RFN2 | MLGKHSKIFFGVSLIFLVIAIVLASWGFQKIVNKQIQKNVQLANDSKMFERWVKLPMPLDFKVYVFNVTNVEEVNQGGKPILQEIGPYVYKQYREKTILGYGDNDTIKYMLKKHFEFDPEASGSLTEDDELTVVHFSYLAALLTVHDMMPSLVTVVNKALEQLFPSLEDAFLRVKVRDLFFDGIYLSCDGDNSALGLVCGKIRAEMPPTMRKAEGSNGFYFSMFSHMNRSESGPYEMIRGRDNVYELGNIVSYKGQENMPMWGDKYCGQINGSDSSIFPPIKEDDVPKKIYTFEPDICRSVYADLVDKRELFNISTYYYEISETAFAAKSANPNNRCFCKKNWSANHDGCLLMGLLNLTPCQGAPAIASLPHFYLGSEELLDYFQSGVQPDKEKHNTYVYIDPVTGVVLSGVKRLQFNIEMRQINNIPQLKSVPTGLFPMLWLEEGATIPESIQQELRDSHKLLGYVEVAKWFLLTIAIISVIASAVAVARANALLSWPRNSNSVSFILGPSVTQVNKGN | Function: Plays an olfactory role that is not restricted to pheromone sensitivity (By similarity). May play a role in the elimination of lipophilic components from the sensillum lymph.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58629
Sequence Length: 520
Subcellular Location: Cell membrane
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Q17Q87 | MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLTPNGPEVHS | Function: Plays a role in the toxic effects of organotins. Plays a role in endosomal maturation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9396
Sequence Length: 87
Subcellular Location: Mitochondrion outer membrane
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O75324 | MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG | Function: Plays a role in the toxic effects of organotins . Plays a role in endosomal maturation .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9497
Sequence Length: 88
Subcellular Location: Mitochondrion outer membrane
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P61807 | MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTANSPEVHG | Function: Plays a role in the toxic effects of organotins (By similarity). Plays a role in endosomal maturation .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9501
Sequence Length: 88
Subcellular Location: Mitochondrion outer membrane
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Q8MP06 | MFRKFVIMLVLSLLVAAGISQASSASRVCIIGAGYSGLATARYLQDYGLNYTIFEATPNIGGTWRYDPRVGTDEDGIPIYSSNYKNLRVNSPVDLMTYHGYEFQEGTRSFISGNCFYKYMKSFVRHFGLMENIQVRSLVTWVQRTEDKWNLTYMKTDTRKNYTEECDFVVVASGEFSTPKIPHIKGQEEYKGKTMHSHDYKEAESFRGQRVLVIGAGPSGLDVVMQLSNITSKLVHSQHILKSWHIFNQPDFPGNFISKPNVKHFTANGAVFEDDTVEEFDMVIYCTGFYYNHPFLSTLSSGITATENYVMPLYQQVVNINQPTMTFVGICKPFFAKLLDQQAHYSAKLAAGHFKLPSQDKMLRHWLEHVQMLREAQFKITDVNSVGPNVDEYFKALHKEAGVPLLPPVYASVFVFSGKTLLEDLQNYREYDYRIISDTQFKKKYNPREEVCPYDD | Function: NADPH-dependent monooxygenase that detoxifies senecionine and similar plant alkaloids that are ingested by the larvae. Is active towards a narrow range of related substrates with highest activity towards senecionine, followed by seneciphylline, retrorsine, monocrotaline, senecivernine, axillarine and axillaridine.
Catalytic Activity: NADPH + O2 + senecionine = H2O + NADP(+) + senecionine N-oxide
Sequence Mass (Da): 52232
Sequence Length: 456
Subcellular Location: Secreted
EC: 1.14.13.101
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Q03144 | MHKTHSTMSGKSMKVIGVLALQGAFLEHTNHLKRCLAENDYGIKIEIKTVKTPEDLAQCDALIIPGGESTSMSLIAQRTGLYPCLYEFVHNPEKVVWGTCAGLIFLSAQLENESALVKTLGVLKVDVRRNAFGRQAQSFTQKCDFSNFIPGCDNFPATFIRAPVIERILDPIAVKSLYELPVNGKDVVVAATQNHNILVTSFHPELADSDTRFHDWFIRQFVSN | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 24907
Sequence Length: 224
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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O15079 | MAMSLPGSRRTSAGSRRRTSPPVSVRDAYGTSSLSSSSNSGSYKGSDSSPTPRRSMKYTLCSDNHGIKPPTPEQYLTPLQQKEVCIRHLKARLKDTQDRLQDRDTEIDDLKTQLSRMQEDWIEEECHRVEAQLALKEARKEIKQLKQVIDTVKNNLIDKDKGLQKYFVDINIQNKKLETLLHSMEVAQNGMAKEDGTGESAGGSPARSLTRSSTYTKLSDPAVCGDRQPGDPSSGSAEDGADSGFAAADDTLSRTDALEASSLLSSGVDCGTEETSLHSSFGLGPRFPASNTYEKLLCGMEAGVQASCMQERAIQTDFVQYQPDLDTILEKVTQAQVCGTDPESGDRCPELDAHPSGPRDPNSAVVVTVGDELEAPEPITRGPTPQRPGANPNPGQSVSVVCPMEEEEEAAVAEKEPKSYWSRHYIVDLLAVVVPAVPTVAWLCRSQRRQGQPIYNISSLLRGCCTVALHSIRRISCRSLSQPSPSPAGGGSQL | Function: Inhibits SNARE complex formation by absorbing free syntaxin-1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53537
Sequence Length: 494
Subcellular Location: Membrane
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Q80U23 | MAMSLQGSRRASAGSRRRTSPPVSVRDAYGTSSLSSSSNSGSCKGSDSSPTPRRSMKYTLCSDNHGIKPPTPEQYLTPLQQKEVCIRHLKARLKDTQDRLQDRDTEIDDLKTQLSRMQEDWIEEECHRVEAQLALKEARKEIRQLKQVIDTVKNNLIDKDKGLQKYFVDINIQNKKLETLLHSMEVAQNGVAKEEGTGESAGGSPARSLTRSSTYTKLSDPAVCGDRQPGDPSNTSAEDGADSGYVAADDTLSRTDALEASSLLSSGVDCGLEEASLHSSFNLGPRFPASNTYEKLLCGMEAGVQVSCMQERAIQTDFVQYQPDLNTILEKVGQAQVCGSVLKDRHSELDPHPSGPRDPDSAVVVTVGDELEAPEPITCGPATHRPAVNSNPGLPVSVVCPVEEEEEEAAAATTTEKEPKSYWSRHYIVDLLAVVVPAVPTVAWLCRSQRRQGQPIYNISSLLRGCCTVALHSIRRISCRSLGQPSSSTAGGSQL | Function: Inhibits SNARE complex formation by absorbing free syntaxin-1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53753
Sequence Length: 495
Subcellular Location: Membrane
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Q8WVK2 | MGRSRSRSPRRERRRSRSTSRERERRRRERSRSRERDRRRSRSRSPHRRRSRSPRRHRSTSPSPSRLKERRDEEKKETKETKSKERQITEEDLEGKTEEEIEMMKLMGFASFDSTKGKKVDGSVNAYAINVSQKRKYRQYMNRKGGFNRPLDFIA | Function: May play a role in mRNA splicing.
PTM: Phosphorylated in vitro by snRNP-associated protein kinase.
Sequence Mass (Da): 18860
Sequence Length: 155
Subcellular Location: Nucleus
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Q4WWS3 | MQAVPESRQQTFEEIYGPPENFLEIEVRNPQTHGTSRNMYTSYEIVCRTNIPAFKLKHSVVRRRYSDFEYFRDILERESTRVTIPPLPGKVFTNRFSDDVIEHRREGLQRFLQIVAGHPLLQTGSKVLASFIQDPNWDRNAW | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16755
Sequence Length: 142
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q5A748 | MSKPFQPISDVINTSPKNKSQSFNEIYGEPENFLEIEVKNPLTHGYGSNLFTDYEIVCRTNIPAFKKRESRIRRRYSDFVAFRKILEQETTRVIIPPLPGKIFLNSNKFNDLNIEKRRQGLEKFLIVVSGHPLLQTGSKSLIEFIQNEKWDPKQIIY | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18362
Sequence Length: 157
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q6FT03 | MSGKREFKSFGSTEETMFSQHHKIPSTSEMYAEPENFLEIEVRNPKTHVPNGVDQRGMYTDYEIICRTNLPNFHKRASRVRRRYSDFEFFRKCLLKEISMLNNPRVVVPHLPGKIYLSNRFSDEVIEERRQGLNRWMQIVAGHPLLQSGSKTLIRFIEDDKFVG | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19339
Sequence Length: 164
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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P0CR61 | MARMAGRPQTFDEMYSVPESFLEIEIRNPMTHGIGRKMYTDYEIVCMTNIPAFKLRHSAVRRRYSDFEAFRDILERESTRVNIPPLPGKVRVFTNRFSDEVIEQRREGLQRFLEIVAGHPLLQTGSKVLCAFLQDPAWDKSQWI | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16894
Sequence Length: 144
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q4I1H6 | MASDQDNSGLDAPGSQFHRPILQSMPDTRQQSFDEIYGPPENFLEIEVRNPRTHGMGRHMYTDYEILCRTNIPAFKLRQSSVRRRYSDFEYFRDILERESARVTIPPLPGKVFTNRFSDDVIEGRRAGLEKFLKIVVGHPLLQTGSKVLAAFVQDPNWDRNAW | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18885
Sequence Length: 163
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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O60493 | MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA | Function: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway . Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes . Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (By similarity). In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs .
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10 (By similarity).
Sequence Mass (Da): 18762
Sequence Length: 162
Domain: The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Location: Early endosome
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