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Q969X2 | MACSRPPSQCEPTSLPPGPPAGRRHLPLSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRSRRPVNLKKWSITDGYVPILGNKTLPSRCHQCVIVSSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTYRVVAHSSVFRVLRRPQEFVNRTPETVFIFWGPPSKMQKPQGSLVRVIQRAGLVFPNMEAYAVSPGRMRQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPNYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b . Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen . Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity).
Catalytic Activity: CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) = a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38068
Sequence Length: 333
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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Q92185 | MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGSKSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLSDVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSVNMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDTSLQPTS | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Can catalyze the addition of a second alpha-2,8-sialic acid to GD3 to form GT3 . Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively . Can synthesize unusual tetra- and pentasialylated lactosylceramide derivatives identified as GQ3 (II3Neu5Ac4-Gg2Cer) and GP3 (II3Neu5Ac5-Gg2Cer) in breast cancer cells .
Catalytic Activity: an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40519
Sequence Length: 356
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.8
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Q64687 | MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPCEEPSPQPTS | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 . Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively .
Catalytic Activity: an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40324
Sequence Length: 355
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.8
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Q6ZXA0 | MWGRWRGAGGRRGVAQPVIPQMKLLGGRVPLGASALGLLIVCWFYIFPGGERLPGHKEMIRQVLQFGPRWGRNRSSGDSFRKLLQDCCDPPRLFSMTKANTALGENLWYDGEFFQSLTIDNTTRSLFPQDTPIKLPLKRCSVVGNGGILKNSRCGEQIDEADFVMRCNLPPLSREYTDDVGTKTQLVTVNPSIIDKRFQNLLWSRKSFVESVSVYKQSYVYMPAFSTKRGTDPSLRVYYTLEDFGTNQTVLFANPNFLRNVGKFWKSKGVHSKRLSTGLFMVSAALSLCEEVTIYGFWPFQMDLGGRHISHHYYDNMLPLSGVHAMPEEFLQLWHLHKSGVLQMQLDQCKKDVSSKKPH | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Glycosphingolipids are required for convergence extension movements during early development . Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (By similarity). Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (By similarity).
Catalytic Activity: an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40811
Sequence Length: 359
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.8
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Q6DNG6 | MKLQGSRMWLCPRTRLPVGASALGFLILCWLYVFPGYRLPGHKEMVREVLRFGPGWRKNRTEMDSFRKLLQDCCDPPHLFSLTKVNTPLGENLWFDGEFFHSLTIDNSTRSLFPQDTPFKLPLKRCSVVGNGGILKNSRCGEQIDEADFVMRCNLPPLSREYTEDVGTRTQLVTVNPSIIDKRYQNLLWSRKSFVENLRVYQQSYVYMPAFSTKRGTDPSLRVYYTLADFGTNQTVLFANPNFLRNVGKFWKSRGIHSKRLSTGLFMVSAALSLCEEVTIYGFWPFQMDLGGRYISHHYYDNTLPLSGVHAMPEEFLQLWLLHKSGVLQMQLDQCKKDVSSQKPH | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid (By similarity). Glycosphingolipids are required for convergence extension movements during early development (By similarity). Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (By similarity). Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (By similarity).
Catalytic Activity: an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 39831
Sequence Length: 345
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.8
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Q92186 | MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSSPAVVDRSNESIKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFGTCAIVGNSGVLLNSGCGQEIDAHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHSLNGSILWIPAFMARGGKERVEWVNELILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCKQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT | Function: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42430
Sequence Length: 375
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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Q91Y57 | MLLLLLLLLLWGIKGVEGQNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLSPQSSATLSEMMMGTFVGSGVTALLFLSVCILLLAVRSYRRKPARPAVVAPHPDALKVSVSQNPLVESQADDSSEPLPSILEAAPSSTEEEIHYATLSFHEMKPMNLWGQQDTTTEYSEIKFPQRTAWP | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may 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.
PTM: Phosphorylation of Tyr-432 is required for binding to PTPN6 and PTPN11. Phosphorylation of Tyr-455 is involved in binding to PTPN6. Tyr-432 needs to be phosphorylated prior to Tyr-455.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51901
Sequence Length: 467
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: Membrane
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Q64JA4 | MLPLLLPLLWAGALALEGIFQLEVPESVTVQEGLCVFVPCTFFYPRHTFIKISLACGYWFREGDNPLRDAPVATNDPARQVREETRGRFRLLGNPREKNCSLSIRDARRRDSGSYFFRVEEAMMKYNYKDPPLSVHVTALTHRPDILIPGALKSGRPRNLVCSVPWACEQGTPPIFSWIGTSVSPLSPTTALSSVVTLIPQPQDHGSRLTCQVTLPGAGVTTTRTVRLNVSYPPQNLTLTVFQGDGTASTTLRNESSLQVLEGQSLRLVCAVDSNPPARLSWAQDNLILSPSQPNPGMLELPQMHLRNEGEFTCQARNPLGSQQVSLRLFVQRKSGPMAEVVLVAIGEAAVKILLLFLCLIILRVKSHRRKAAKAATGVEAAKVVKG | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42525
Sequence Length: 387
Subcellular Location: Membrane
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Q08ET2 | MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQVKRQGAQVTTERTVQLNVSYAPQNLAISIFFRNGTGTALRILSNGMSVPIQEGQSLFLACTVDSNPPASLSWFREGKALNPSQTSMSGTLELPNIGAREGGEFTCRVQHPLGSQHLSFILSVQRSSSSCICVTEKQQGSWPLVLTLIRGALMGAGFLLTYGLTWIYYTRCGGPQQSRAERPG | Function: Putative adhesion molecule. Sialic acid-binding paired receptor which may activate associated receptors.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43970
Sequence Length: 396
Subcellular Location: Cell membrane
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Q6ZMC9 | MEKSIWLLACLAWVLPTGSFVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHPHRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGNPRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPRIVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHGHLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGASTVALLLGALGFKALLLLGVLAARAARRRPEHLDTPDTPPRSQAQESNYENLSQMNPRSPPATMCSP | Function: Binds sialylated glycoproteins.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35653
Sequence Length: 328
Subcellular Location: Membrane
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A6NMB1 | MLLLPLLLPVLGAGSLNKDPSYSLQVQRQVPVPEGLCVIVSCNLSYPRDGWDESTAAYGYWFKGRTSPKTGAPVATNNQSREVAMSTRDRFQLTGDPGKGSCSLVIRDAQREDEAWYFFRVERGSRVRHSFLSNAFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFKKCPAPSFSWTGAALSPRRTRPSTSHFSVLSFTPSPQDHDTDLTCHVDFSRKGVSAQRTVRLRVASLELQGNVIYLEVQKGQFLRLLCAADSQPPATLSWVLQDRVLSSSHPWGPRTLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLRNGTSLRVLEGQSLRLVCVTHSSPPARLSWTWGEQTVGPSQPSDPGVLQLPRVQMEHEGEFTCHARHPLGSQRVSLSFSVHCKSGPMTGVVLVAVGEVAMKILLLCLCLILLRVRSCRRKAARAALGMEAADAVTD | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 52992
Sequence Length: 481
Subcellular Location: Membrane
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O15389 | MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPLGFLQIFLNLSVYSLPQLLGPSCSWEAEGLHCRCSFRARPAPSLCWRLEEKPLEGNSSQGSFKVNSSSAGPWANSSLILHGGLSSDLKVSCKAWNIYGSQSGSVLLLQGRSNLGTGVVPAALGGAGVMALLCICLCLIFFLIVKARRKQAAGRPEKMDDEDPIMGTITSGSRKKPWPDSPGDQASPPGDAPPLEEQKELHYASLSFSEMKSREPKDQEAPSTTEYSEIKTSK | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and 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.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60715
Sequence Length: 551
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: Membrane
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Q920G3 | MRWAWLLPLLWAGCLATDGYSLSVTGSVTVQEGLCVFVACQVQYPNSKGPVFGYWFREGANIFSGSPVATNDPQRSVLKEAQGRFYLMGKENSHNCSLDIRDAQKIDTGTYFFRLDGSVKYSFQKSMLSVLVIALTEVPNIQVTSTLVSGNSTKLLCSVPWACEQGTPPIFSWMSSALTSLGHRTTLSSELNLTPRPQDNGTNLTCQVNLPGTGVTVERTQQLSVIYAPQKMTIRVSWGDDTGTKVLQSGASLQIQEGESLSLVCMADSNPPAVLSWERPTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSIRSLLQLLGPSCSFEGQGLHCSCSSRAWPAPSLRWRLGEGVLEGNSSNGSFTVKSSSAGQWANSSLILSMEFSSNHRLSCEAWSDNRVQRATILLVSGPKVSQAGKSETSRGTVLGAIWGAGLMALLAVCLCLIFFTVKVLRKKSALKVAATKGNHLAKNPASTINSASITSSNIALGYPIQGHLNEPGSQTQKEQPPLATVPDTQKDEPELHYASLSFQGPMPPKPQNTEAMKSVYTEIKIHKC | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 61476
Sequence Length: 569
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: Membrane
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O43699 | MQGAQEASASEMLPLLLPLLWAGALAQERRFQLEGPESLTVQEGLCVLVPCRLPTTLPASYYGYGYWFLEGADVPVATNDPDEEVQEETRGRFHLLWDPRRKNCSLSIRDARRRDNAAYFFRLKSKWMKYGYTSSKLSVRVMALTHRPNISIPGTLESGHPSNLTCSVPWVCEQGTPPIFSWMSAAPTSLGPRTTQSSVLTITPRPQDHSTNLTCQVTFPGAGVTMERTIQLNVSYAPQKVAISIFQGNSAAFKILQNTSSLPVLEGQALRLLCDADGNPPAHLSWFQGFPALNATPISNTGVLELPQVGSAEEGDFTCRAQHPLGSLQISLSLFVHWKPEGRAGGVLGAVWGASITTLVFLCVCFIFRVKTRRKKAAQPVQNTDDVNPVMVSGSRGHQHQFQTGIVSDHPAEAGPISEDEQELHYAVLHFHKVQPQEPKVTDTEYSEIKIHK | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to 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.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49913
Sequence Length: 453
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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Q9Y286 | MLLLLLLPLLWGRERVEGQKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRAGNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDAGRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLEGQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEFTCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLLGAVGGAGATALVFLSFCVIFIVVRSCRKKSARPAADVGDIGMKDANTIRGSASQGNLTESWADDNPRHHGLAAHSSGEEREIQYAPLSFHKGEPQDLSGQEATNNEYSEIKIPK | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may 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. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro).
PTM: Tyrosine phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51143
Sequence Length: 467
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: Membrane
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Q9NYZ4 | MLLLLLLLPLLWGTKGMEGDRQYGDGYLLQVQELVTVQEGLCVHVPCSFSYPQDGWTDSDPVHGYWFRAGDRPYQDAPVATNNPDREVQAETQGRFQLLGDIWSNDCSLSIRDARKRDKGSYFFRLERGSMKWSYKSQLNYKTKQLSVFVTALTHRPDILILGTLESGHSRNLTCSVPWACKQGTPPMISWIGASVSSPGPTTARSSVLTLTPKPQDHGTSLTCQVTLPGTGVTTTSTVRLDVSYPPWNLTMTVFQGDATASTALGNGSSLSVLEGQSLRLVCAVNSNPPARLSWTRGSLTLCPSRSSNPGLLELPRVHVRDEGEFTCRAQNAQGSQHISLSLSLQNEGTGTSRPVSQVTLAAVGGAGATALAFLSFCIIFIIVRSCRKKSARPAAGVGDTGMEDAKAIRGSASQGPLTESWKDGNPLKKPPPAVAPSSGEEGELHYATLSFHKVKPQDPQGQEATDSEYSEIKIHKRETAETQACLRNHNPSSKEVRG | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells . Preferentially binds to alpha-2,3-linked sialic acid. Also binds to 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 . Recognizes simultaneously epitopes having a terminal N-acetylneuraminic acid (sialic acid) and an underlying 6-O-sulfated galactose. Preferentially binds to Gal-6-sulfated sialyl-Lewis X glycan epitopes .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 54042
Sequence Length: 499
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: Membrane
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P03528 | MDPRLREEVVRLIIALTSDNGASLSKGLESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLVASVSDAQLAISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQADFESRISTLERTAVTSAGAPLSIRNNRMTMGLNDGLTLSGNNLAIRLPGNTGLNIQNGGLQFRFNTDQFQIVNNNLTLKTTVFDSINSRIGATEQSYVASAVTPLRLNSSTKVLDMLIDSSTLEINSSGQLTVRSTSPNLRYPIADVSGGIGMSPNYRFRQSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHNDVVTYGAQTVAIGLSSGGAPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSFT | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis.
PTM: Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.
Sequence Mass (Da): 49095
Sequence Length: 455
Subcellular Location: Virion
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P04507 | MSDLVQLIRREILLLTGNGESANSKHEIEEIKKQIKDISADVNRISNIVDSIQGQLGGLSVRVSAIESGVSENGNRIDRLERDVSGISASVSGIDSRLSELGDRVNVAEQRIGQLDTVTDNLLERASRLETEVSAITNDLGSLNTRVTTELNDVRQTIAAIDTRLTTLETDAVTSVGQGLQKTGNSIKVIVGTGMWFDRNNVLQLFLSNQQKGLGFIDNGMVVKIDTQYFSFDSNGNITLNNNISGLPARTGSLEASRIDVVAPPLVIQSTGSTRLLRLMYEAVDFVVTNNVLTLRNRSVTPTFKFPLELNSADNSVSIHRNYRIRLGQWSGQLEYHTPSLRWNAPVTVNLMRVDDWLILSFTRFSTSGILASGKFVLNFVTGLSPGWATGSTEPSTTTNPLSTTFAAIQFINGSSRVDAFRILGVAEWNAGELEITNHGGTYTAHTNVDWAPMTIMYPCLG | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis (By similarity).
PTM: Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.
Sequence Mass (Da): 50466
Sequence Length: 462
Subcellular Location: Virion
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P04506 | MDASLITEIRKIVLQLSVSSNGSQSKEIEEIKKQVQVNVDDIRAANIKLDGLGRQIADISNSISTIESRLGEMDNRLVGISSQVTQLSNSVSQNTQSISSLGDRINAVEPRVDSLDTVTSNLTGRTSTLEADVGSLRTELAALTTRVTTEVTRLDGLINSGQNSIGELSTRLSNVETSMVTTAGRGLQKNGNTLNVIVGNGMWFNSSNQLQLDLSGQSKGVGFVGTGMVVKIDTNYFAYNSNGEITLVSQINELPSRVSTLESAKIDSVLPPLTVREASGVRTLSFGYDTSDFTIINSVLSLRSRLTLPTYRYPLELDTANNRVQVADRFGMRTGTWTGQLQYQHPQLSWRANVTLNLMKVDDWLVLSFSQMTTNSIMADGKFVINFVSGLSSGWQTGDTEPSSTIDPLSTTFAAVQFLNNGQRIDAFRIMGVSEWTDGELEIKNYGGTYTGHTQVYWAPWTIMYPCNVR | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis (By similarity).
PTM: Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.
Sequence Mass (Da): 51404
Sequence Length: 470
Subcellular Location: Virion
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Q8L607 | MVMMLKKTVKKGLIGGMSFAKDAGKINWFPGHMAAATRAIRNRLKLSDLVIEVRDARIPLSSANEDLQSQMSAKRRIIALNKKDLANPNVLNKWTRHFESSKQDCIAINAHSRSSVMKLLDLVELKLKEVIAREPTLLVMVVGVPNVGKSALINSIHQIAAARFPVQERLKRATVGPLPGVTQDIAGFKIAHRPSIYVLDSPGVLVPSIPDIETGLKLALSGSVKDSVVGEERIAQYFLAILNIRGTPLHWKYLVEGINEGPHADCIDKPSYNLKDLRHQRTKQPDSSALHYVGDMISEVQRSLYITLSEFDGDTEDENDLECLIEQQFEVLQKALKIPHKASEARLMVSKKFLTLFRTGRLGPFILDDVPETETDHPNSKRVVVL | Function: GTPase that may function in mitochondrial ribosome assembly (Probable). Involved in a variety of growth processes during vegetative development and promotes growth and cell division in the developing integuments .
Sequence Mass (Da): 42984
Sequence Length: 386
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Mitochondrion
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P93748 | MAPGGSALKEALESNSTGVDYEVKMAKVEANSKPTKSGSGSIGKFHSSNGVYELLECPVCTNLMYPPIHQCPNGHTLCSSCKLRVQNTCPTCRYELGNIRCLALEKVAESLEVPCRYQNLGCQDIFPYYSKLKHEQHCRFRSYSCPYAGSECSVTGDIPTLVDHLKDDHKVDMHDGCTFNHRYVKSNPHEVENATWMLTVFNCFGRQFCLHFEAFQLGMAPVYMAFLRFMGDENEAKKFSYSLEVGAHSRKLTWQGIPRSIRDSHRKVRDSQDGLIIPRNLALYFSGSDKEELKLRVTGRIWKEE | 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 . Mediates the proteasomal-dependent degradation of ATG6, a component of the autophagosome complex . Requires TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and subsequent regulation of autophagosome assembly . Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex . Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex .
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): 34557
Sequence Length: 305
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endosome
EC: 2.3.2.27
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Q9M2P4 | MAPGGSALKEVMESNSTGMDYEVKTAKVEVNNNKPTKPGSAGIGKYGIHSNNGVYELLECPVCTNLMYPPIHQCPNGHTLCSNCKLRVQNTCPTCRYELGNIRCLALEKVAESLEVPCRYQNLGCHDIFPYYSKLKHEQHCRFRPYTCPYAGSECSVTGDIPTLVVHLKDDHKVDMHDGCTFNHRYVKSNPHEVENATWMLTVFNCFGRQFCLHFEAFQLGMAPVYMAFLRFMGDENEAKKFSYSLEVGAHGRKLTWQGIPRSIRDSHRKVRDSQDGLIIPRNLALYFSGGDRQELKLRVTGRIWKEE | 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 . Mediates the proteasomal-dependent degradation of ATG6, a component of the autophagosome complex . Requires TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and subsequent regulation of autophagosome assembly . Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex . Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex .
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): 34993
Sequence Length: 308
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endosome
EC: 2.3.2.27
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Q9STN8 | METDSMECVSSTGNEIHQNGNGHQSYQFSSTKTHGGAAAAAVVTNIVGPTATAPATSVYELLECPVCTYSMYPPIHQCHNGHTLCSTCKVRVHNRCPTCRQELGDIRCLALEKVAESLELPCKFYNLGCPEIFPYYSKLKHESLCNFRPYSCPYAGSECGIVGDIPFLVAHLRDDHKVDMHAGSTFNHRYVKSNPREVENATWMLTVFHCFGQYFCLHFEAFQLGMGPVYMAFLRFMGDEEDARSYSYSLEVGGSGRKLTWEGTPRSIRDSHRKVRDSNDGLIIQRNMALFFSGGDRKELKLRVTGKIWKEQHSPDSGLSIPNLSSS | 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 . Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex . Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex .
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): 36574
Sequence Length: 327
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endosome
EC: 2.3.2.27
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Q8S3N1 | METDSIDSVIDDDEIHQKHQFSSTKSQGGATVVISPATSVYELLECPVCTNSMYPPIHQCHNGHTLCSTCKSRVHNRCPTCRQELGDIRCLALEKVAESLELPCKYYNLGCLGIFPYYSKLKHESQCNFRPYSCPYAGSECAAVGDITFLVAHLRDDHKVDMHTGCTFNHRYVKSNPREVENATWMLTVFQCFGQYFCLHFEAFQLGMAPVYMAFLRFMGDEDDARNYTYSLEVGGSGRKQTWEGTPRSVRDSHRKVRDSHDGLIIQRNMALFFSGGDKKELKLRVTGRIWKEQQNPDSGVCITSMCSS | 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 . Mediates the ubiquitination and proteasomal-dependent degradation of NAC021/NAC022, a transcription activator that functions downstream of the auxin signals, thereby acting as a down-regulator of auxin signals . Involved in the formation of lateral roots . Is antagonist to SINAT1, SINAT2, SINAT3 and SINAT4 by suppressing FREE1 ubiquitination and degradation mediated by SINAT1, SINAT2, SINAT3 and SINAT4, and promoting FREE1 accumulation .
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): 35037
Sequence Length: 309
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q8T3Y0 | MSVRNSRPQLSWPERVSPQRTIDTPTASGEMLTRRQSAPALVVPPEETTHVVVVKRQSPDAAAAGELVPSRRKDSVAVQSGIVATGPLDTTRSGARDDFLMALLECPVCFGYIMPPIMQCPRGHLICSTCRSKLTICPVCRVFMTNIRSLAMEKVASKLIFPCKHSHFGCRARLSYAEKTKHEEDCECRPYFCPYPDDKCSWQGPLRDVYQHLMSSHENVITMEGNDIIFLATNVNLEGALDWTMVQSCHGRHFLLSLEKINLGEDCQQYFTACRMIGSMKDAAEFVYNISLEAYNRTLRWQSKPRSIRENFSSFTNADFLVLNKHTVELFSEDGNLALNVVIRKVEERTN | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. The adapter phyl is required to direct the degradation of the two isoforms of the transcriptional repressor Tramtrack (Ttk). 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. A phyl-independent mechanism of degradation exists for isoform beta of ttk that involves motifs in the C-terminus of ttk.
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): 39645
Sequence Length: 351
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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P21461 | MSNKINPKRREPTAAAAGAGATGVATNTSTSTGSSSAGNTSSANTSSSSSSSLSSAGGGDAGMSADLTSLFECPVCFDYVLPPILQCSSGHLVCVSCRSKLTCCPTCRGPLANIRNLAMEKVASNVKFPCKHSGYGCTASLVYTEKTEHEETCECRPYLCPCPGASCKWQGPLDLVMQHLMMSHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYDGHQQFFAIVQLIGSRKEAENFVYRLELNGNRRRLTWEAMPRSIHEGVASAIHNSDCLVFDTSIAQLFADNGNLGINVTISLV | Function: E3 ubiquitin-protein ligase that is required for specification of R7 photoreceptor cell fate in the eye by mediating the ubiquitination and subsequent proteasomal degradation of Tramtrack (ttk) . 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 . Acts via the formation of a complex with ebi and phyl that ubiquitinates the transcription repressor ttk, a general inhibitor of photoreceptor differentiation, in a subset of photoreceptor cells in the eye, leading to the differentiation of cells into neurons . Also involved in external sensory organ development .
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): 33707
Sequence Length: 314
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q62231 | MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQSNMGHARSSNYSLPGLTASQPSHGLQAHQHQLQDSLLGPLTSSLVDLGS | Function: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development . Plays an important role in the development of several organs, including kidney, muscle and inner ear . Depending on context, functions as transcriptional repressor or activator . Lacks an activation domain, and requires interaction with EYA family members for transcription activation (By similarity). Mediates nuclear translocation of EYA1 and EYA2 (By similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer (By similarity). Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR . Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2 . Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex . During myogenesis, seems to act together with EYA2 and DACH2. Regulates the expression of CCNA1 (By similarity). Promotes brown adipocyte differentiation .
PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity).
Sequence Mass (Da): 32210
Sequence Length: 284
Subcellular Location: Nucleus
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Q26292 | MKLLLLLIVSASMLIESLVNADGYIKRRDGCKVACLIGNEGCDKECKAYGGSYGYCWTWGLACWCEGLPDDKTWKSETNTCGGKK | Function: Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.
Sequence Mass (Da): 9334
Sequence Length: 85
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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Q5NTH4 | MEAGVGLALQSRAAGFGGSDRRRSALYGGEGRARIGSLRVAEPAVAKAAVWARGSKPVAPLRAKKSSGGHETLHNSVDEALLLKRKSEEVLFYLNGRCIYLVGMMGSGKSTVGKIMSEVLGYSFFDSDKLVEQAVGMPSVAQIFKVHSEAFFRDNESSVLRDLSSMKRLVVATGGGAVIRPVNWKYMKKGLSVWLDVPLDALARRIAKVGTASRPLLDQPSGDPYTMAFSKLSMLAEQRGDAYANADVRVSLEEIASKQGHDDVSKLTPTDIAIESFHKIENFVIEHTVDNPVGDSQADSRAQRIQTL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 33310
Sequence Length: 308
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Plastid
EC: 2.7.1.71
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O31423 | MSYDRVKDFDLPELAVHLQPHGAVMIDRKSMFYFRLSGRGAQLAFLLSKNKNLHKTARIWEIMKKEEMSADQLKEELSAHPFTEAWTEGLLDQPLHVSGSLDSYLPISCTLQLTNACNLSCSFCYASSGKPYPEELSSEQWILVMQKLAAHGVADITLTGGEAKLIKGFKELVVVASSLFTNVNVFSNGLNWRDEEVELLSHLGNVSVQISIDGMDNTHDQLRGRKGGFKESMNTIKKLSEANIPVIVAMTINESNADEVSDVVEQCANAGAFIFRAGKTLSVGRATEGFKALDIDFEEMVQIQLREARHKWGDRLNIIDWEHEESSFTTDFCTPGYLAWYIRADGYVTPCQLEDLPLGHILEDSMADIGSPARLLQLKCEAKNCKCIGKIELSEPDLPFQKEVKAGIQE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine . The other is coordinated via 3 cysteines and maybe direct contact with the SkfA precursor (Probable).
Function: Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA . Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys . The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first reaction in SKF maturation . In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA .
Sequence Mass (Da): 45755
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 1.21.98.-
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O31425 | MNSLSLVFWSILAVVGLLLFIKFKPPTIASLLLSKDEAKEISIQFIKEFVGIDVENWDFYSVYWYDHDTVNKLHHLGILKKNRKVLYDVGLVESWRVRFVHQNQSFVVGVNANREITFFYADVPKKTLSGKFEQVSPETLKQRLMASPDGLWSRANMTGTGKKEEDFREVSTYWYIAEAGDIRLKVTVELQGGRISYIGTEQEILTDQMSKVIRDEQVESTFGVSGMLGSALAMILAILILVFMDVQTSIIFSLVLGLLIIICQSLTLKEDIQLTIVNAYDARMSVKTVSLLGILSTLLTGLLTGFVVFICSLAGNALAGDFGWKTFEQPIVQIFYGIGAGLISLGVTSLLFNLLEKKQYLRISPELSNRTVFLSGFTFRQGLNMSIQSSIGEEVIYRLLMIPVIWWMSGNILISIIVSSFLWAVMHQVTGYDPRWIRWLHLFIFGCFLGVLFIKFGFICVLVAHFIHNLVLVCMPLWQFKLQKHMHHDQPKHTSL | Function: Required for production of the bacteriocin SkfA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56292
Sequence Length: 496
Subcellular Location: Membrane
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O31427 | MQLMQVQNLSKCYRNGDGVEHLSFSIQRGEIVALLGPNGAGKTTTIRCLTGLYKPDKGDILIEGSPPGDINVQKKVALIPDQPYLYPALTAAEHIQFRARGYHPGKKDVKERVYHALKEVHLEEKANQLCGQLSRGQKQRVVLAGAIVQDALLYILDEPTVGLDIPSKQWLSNWLKTKTDQGCSAFVSTHSLEFVIETADRVILIRDGKLMQDLYVPQFEEQAEWRKEVIRLLGEWSDE | Function: Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26894
Sequence Length: 239
Subcellular Location: Cell membrane
EC: 7.3.2.3
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O31428 | MPFLIMLLFVGAIGFQVSFVSRSTTWDMSIAGWVLTGVFILYTAFGLFSNRLPSQMADIIWLYGTATSFSKVVYSVLFFSVTWKALLWIISAIFGDVLIVLLSGDHINLLGRSIIFVGLFFIAEVWLMSVSCARTVKKMKRVYVLVFLLMLGIYSICLYRFFFLQHSSGIWESIARFISGVGLVFDTLSPLYVVVFIGIITVSFMTIAFTSRQVEMKESLVKEAEFWEEFQERQFGSGQIIQKPKTTWWGLQGLNGIWSFLWLELLLFKKYLFFHSIHTVMLSGVFYVVIFMYPEWFYLLFFLIVSAVMLSSYYSGIVRHSQSGTLHLFPGALWKKIIILELTNTVWLYILYCVSITFMAVGNLVYWYIYGLGIYIWFMTIRLFAFTHTNRNDIKLSLPQYYKSFFMALGLSGICLYVIHLLTADWYTLVVVVCIGSLSWCLFYRFR | Function: Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for the translocation of bacteriocin SkfA across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51817
Sequence Length: 447
Subcellular Location: Cell membrane
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Q753L2 | MAVDTTTVAVALAVVLPVSIAVLIALVFWCKTQRRFKREEQDDEKNRGYDDEVVTFREMRASSGTLGPDGTPPTACAEGSGSSEGSESEKDPSPTPAPAGRAARTYMPAYRRRLNRSLSRQQSRADEMTTNSSAASYDTQHAQNAQLSVFEQMVPVLQVDNSSPFANPRDAAFERGSRHSSESLMKSLKNQDFGSYPKRRPSAANTANLAVYNGSVSSFSSRVPSSTTLNCMGDESFYAYEGSVLPRTGRDLPEVKQDVYMLKNNYDVTNNEEITEEDQYENEFTNYSENKREFIDSLRPKAERMSN | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 34105
Sequence Length: 307
Subcellular Location: Cell membrane
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Q6FLL2 | MTGTVSTAVGCAVGIPVGVGVIVACLFWIRMQRRLKEEDIIDQELNRAVYDESGFVSFNNIDTLKAEPNGHPSSEDTNEVMHSSDIDDNGDDDDEDHNARRNNTYAAQDKNNGKYVPAYRRQINKHNSILQQQRKSRNLVNTMGHSIESLSMDDHSQANGKSRQVSVYDQMVPVLDDANRDSSSPFPTNDKDTSDKKSNLFQSHDVSANTSTSFFETRSNDNLIKNLNSHDFGSYYPRRPSTSNLNHSQGSLHTRNSSMLSLGKIENAENVFATPKSENILKHPHPLEHESSSISNETNNVTDNTIDGESASKSSKTYQLKNNYDIQNTSEIAEEDQYENEFTNYSENKRAYIDGLRPKM | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 40439
Sequence Length: 360
Subcellular Location: Cell membrane
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C5DH21 | MTDGLGVSVGCAVGIPCGVAVLVAVIFWYYMQRKFKKEIEDDEESMSGDGTISFTNLHSMRVPDNPEKDLPVSHVVGGSTSSDNTTTAQNVATAGQMEAQQSQPSKKPKNTYMPAYRKRLNSSLSTLQHQDEQRSPTDSSSTSLDTKNQNGRAHSTVLDQMIPVLAQDDNAAAASSEFSLTHERTSSNDNLIKNLHNHDFGSYPKRRSSGNLTGMISGNVSSASVHTRTSSVHSGKKNNENVFDTPNSQKFHEAVAPSEEDAESKGMRSYYMLKNNYDVENASQIAEEDQYENEFTNYSESKREFINSLRPKKN | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 34636
Sequence Length: 314
Subcellular Location: Cell membrane
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A7TSZ6 | MVASNSVAVGCAVGIPVGVGLIIAGCFWLRLQRRFKREDEQDADLQRAVFDEDAYINFESMPTLRNNNNNDEDNNDDKRIKKIEENGNENTIPINDNKEQRKSKYFVPAYRRKINALSVRYDGQQNIEMQGFGANSSKVSLDSSNAPPKRVISVYDQMVPFVDGDKNSVIQNTELLESNDSVGNDSTRPSSQANLISNLNSNDFGSYYPRKESFSSINIPHLNTSSPSFTTRPSSVNSMIRPNSTDNIFDTPRKSNSDIVSINKDQVNRTGSPVKGTVISENMGYKLKNNYNIENSNEIAEEDQYENEFTNYSQNKKEFIDSLRPK | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 36744
Sequence Length: 326
Subcellular Location: Cell membrane
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B3LRH5 | MTASTSVAVGCAVGIPVGVGIIIAVCFWFNLQKRYKREEQDDRELERAIYDESGFVSFDNFGPLRDSKDEAALASSELKNPDHTSGSSEGSAHPEEKDGKSRDQEKPLGKKNSKYYVPAYRRKINLLQVRNNNYGNNARQKSVVDLPSINNSSNVSLSSSQRHITKRQISVYDQMVPVISDEGPKFFADPSSDTNTSNDQNKASMIELKHNTRQSSNENLIRKLQNQDFGSYYPRRASSSFLNGNISNASFHTRNSSITSVNKRDALEDVFATPKSAAQSQLPNTFDKDNEGIDADHSVKDSRSAITDKDKNIYKLQNNYDVGNIGEIAEEDQYENEFTNYSQSKREFIESLRPK | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 39839
Sequence Length: 355
Subcellular Location: Cell membrane
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C5DSG3 | MGDVSIAVGCAVGLPVGLSFLLAIVFWIRMQRRYKKEDARDCELENIIRDESGFISFDNLGTWQETQQEKKDVYVNDESVESSGIQGSSSSEQLQQPNETHQNKHQSKHYMPAYRRNLNAYRIRQLPTGINVDNNGSNLSLDSTQNMRKRPNLHQETVYDQMIPVLANTEPKLFSEDNNEQDTAATIQQNQQNNEKVIMKNLRNNDFGSYPRGTQSATSLSRSNSNSNTNTNTNVSRSSLHTRSSSVMSAVKGTTSYDNVFDTPKSATAASLVDVKVSNNNNNNNKQPVYSLKNNYDIKNTSEIQEEDQYENEFTNYSESKRTFIDSLRPKPGI | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 37761
Sequence Length: 334
Subcellular Location: Cell membrane
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P32900 | MYHTHMHESLISVTSTVSVSDASYAYARLTRRDDSDSSSSSASSTKNSKSAECTGSKQQCQLPTDSSHSTSVTVGVAVAVPVGVIIIVLAVILCIVYRRSKKEAEEDNDPDFEGDSEFLPTMKDYSPGINHLYSSDSQQDFMEKTLQQPPSDPFVGSMHSSKYNVRSATPPAIGRSWYVDPFQLPQESNDSNSLRDFAMRVQEDGLGGYKVAAESRNASQTSLHPDNFSNCTPIRASSRFQESESFRSHGSPIHNNQLSRGSATEGANKQFTFPNEDNDSSSVSEEAEVLNESNESASNDAFEFELDNSSEKTHERNLRFGKDDDNYELQDIREAEHMNDRSSSKSQDDDYYVSLLSPNEEEDIKRMKSIYQVYLDRAKTMKKEEDKADNANDISQEENRVDNIVQNPLPSIKINNNDNIDNNEVPEAKHLVKEALPLNNTNLAEYGPEMAQSQKQYPVQDTLTVNDTEAAPSNRIASSIYSEAIQPLNYQDQYQQQEQSPVYNGHTQYPGNGYSGNPQQQGYTAQFVQNPQWYGVPTPQQQQHNHPQTLETIGELPTPAYLAQSASSHSLTSFKRPNKQQLLQLQTARLNGTALNPVDHPEMFYSPTNDAYYAPQQQGQYMKFNENGAVPSPYQLRQSVVMTNPSDLTAKPSYKPAGSFRSVSATNSRNNSLTTQNNIYLQQQQQQLYNSRVSGILEETDVVQPPSVGGILPHSGSQDDLRKQLGSSHNYTVN | Function: May be involved in the polarity establishment process. Suppresses the lethality of KEX2-GAS1 double null mutant when overexpressed.
PTM: Phosphorylated by CDC28.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81849
Sequence Length: 734
Subcellular Location: Membrane
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J9VSG5 | MATTNAQIYQQSQMPIPMPTPSLNPNINSAPTPGPNAMSVYEDCQSPLDTSVSGMYPGDRGSRVVSQPAPLLDQSHLRPGNQANLLSHDRTIELYRENAKKTNDPELIFEFSAFMIDAAKAMIPPEQEKDTNPSPALIKQMEKREEIIKEATSLLKRLADRGFPDAQYFLADCYANGIGTARGKQDFDRAFPLFILAAKHGHPDACYRAGTCCEHGWGCRRDSAKAVSFYKKAAVGLHPGAMYRLGTAELNGALGFPRRPKEGVKWLKRSAEHATEEFPHALHELALLHERGIENVVFVDNDYAAELLAQSAELGYAPSAFKLGECYEYGKMGCPVDPALSIHYYNISAQQDHKDACFALTAWYLVGSPGVLPQSDTEAYLWAKKAAELGLAKAQYAVGYFTETGIGIEANPQAALTWYKQAAEGGDKRAAKRLATGSRSSALDRRLEMEALKEEKRLGAANLAQRSGSGSGASGKDGKDGCLIM | Function: Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall . Chitin produced by CHS3 is deacetylated to chitosan, which helps to maintain cell wall integrity, anchor melanin, and offers an advantage during infection, as chitosan is less readily detected by host immunosurveillance .
Location Topology: Lipid-anchor
Sequence Mass (Da): 52855
Sequence Length: 485
Subcellular Location: Cell membrane
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P34226 | MASSPQVHPYKKHLMQSQHINFDNRGLQFQNSSLKVGQDFSDNKENRENRDNEDFSTADLPKRSANQPLINEHLRAASVPLLSNDIGNSQEEDFVPVPPPQLHLNNSNNTSLSSLGSTPTNSPSPGALRQTNSSTSLTKEQIKKRTRSVDLSHMYLLNGSSDTQLTATNESVADLSHQMISRYLGGKNNTSLVPRLKTIEMYRQNVKKSKDPEVLFQYAQYMLQTALTIESSNALVQDSDKEGNVSQSDLKLQFLKEAQSYLKKLSIKGYSDAQYLLADGYSSGAFGKIENKEAFVLFQAAAKHGHIESAYRASHCLEEGLGTTRDSRKSVNFLKFAASRNHPSAMYKLGLYSFYGRMGLPTDVNTKLNGVKWLSRAAARANELTAAAPYELAKIYHEGFLDVVIPDEKYAMELYIQAASLGHVPSATLLAQIYETGNDTVGQDTSLSVHYYTQAALKGDSVAMLGLCAWYLLGAEPAFEKDENEAFQWALRAANAGLPKAQFTLGYFYEHGKGCDRNMEYAWKWYEKAAGNEDKRAINKLRSRDGGLASIGKKQHKKNKSISTLNLFSTVDSQTSNVGSNSRVSSKSETFFTGNPKRDREPQGLQINMNSNTNRNGIKTGSDTSIRKSSSSAKGMSREVAEQSMAAKQEVSLSNMGSSNMIRKDFPAVKTESKKPTSLKNKKDKQGKKKKDCVIM | Function: Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall.
PTM: Farnesylation is required for chitin synthase CHS3 activity but is not required for SKT5 membrane association.
Location Topology: Lipid-anchor
Sequence Mass (Da): 77066
Sequence Length: 696
Subcellular Location: Cell membrane
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Q9SU40 | MDLFKILLLVFFVNISFCFAADPYSFYNFEVSYITASPLGVPQQVIAINGKFPGPTINVTTNENLVVNVRNKLDEGLLLHWNGIQQRRVSWQDGVLGTNCPIPPKWNWTYEFQVKDQIGSFFYFPSLHFQRASGGFGSFVVNPRAIIPVPFSTPDGDITVTIGDWYIRNHTALRKALDDGKDLGMPDGVLINGKGPYRYNDTLVADGIDFETITVHPGKTYRLRVSNVGISTSLNFRIQGHNLVLAESEGSYTVQQNYTSLDIHVGQSYSFLVTMDQNASSDYYIVASARVVNETIWRRVTGVGILKYTNSKGKAKGQLPPGPQDEFDKTFSMNQARSIRWNVSASGARPNPQGSFKYGSINVTDVYVLRNMPPVTISGKRRTTLNGISFKNPSTPIRLADKLKVKDVYKLDFPKRPLTGPAKVATSIINGTYRGFMEVVLQNNDTKMQSYHMSGYAFFVVGMDYGEWTENSRGTYNKWDGIARSTIQVYPGAWSAILISLDNPGAWNLRTENLDSWYLGQETYVRVVNPDENNKTEFGHPDNVLYCGALSKLQKPQKVSSSASKSIGFTSLSMVVMALVMMMMLQH | Function: May be a monocopper oxidase of unknown specificity. Involved in directional growth processes, possibly by participating in cell wall expansion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 65638
Sequence Length: 587
Subcellular Location: Secreted
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Q03656 | MGSSINYPGFVTKSAHLADTSTDASISCEEATSSQEAKKNFFQRDYNMMKKAPAPTKSKLSLALQTSKSSSSANGTVQEDTSSKTEDFSTKSIKKKPDSGVESHVSIQSDSGPQSDSDLDSDSSISSCDERNEESLKDYRPGGYHPAFKGEPYKDARYILVRKLGWGHFSTVWLAKDMVNNTHVAMKIVRGDKVYTEAAEDEIKLLQRVNDADNTKEDSMGANHILKLLDHFNHKGPNGVHVVMVFEVLGENLLALIKKYEHRGIPLIYVKQISKQLLLGLDYMHRRCGIIHTDIKPENVLMEIGDVEGIVQMVEALDKQKREAKRLQRHVSRSSDITANDSSDEKWAECQTSMPCGSSSNSKSRSIEKDLSKRCFRRPRRHTIITGSQPLPSPISSSNFFEMRAHFCGSSHNSFSSVSGNRNIPSSINNNSINNGIGIKNSNNSFLNSVPHSVTRMFINEDSNDNNNNDNSKNKNNNNNNSNNNNNEDIMNTPLHEEQLADSLSTFDISNISQSSDTNGPYISNTMDSNSNVSTDINSPENLIQIKIADLGNACWYDEHYTNSIQTREYRSPEVLLGAPWGCGADIWSTACLIFELITGDFLFEPDEGHSYTKDDDHIAQIIELLGELPSYLLRNGKYTRTFFNSRGLLRNISKLKFWPLEDVLTEKYKFSKDEAKEISDFLSPMLQLDPRKRADAGGLVNHPWLKDTLGMEEIRVPDRELYGSGSDIPGWFEEVRDHKRH | Function: Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 83238
Sequence Length: 742
EC: 2.7.11.1
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Q9VIH7 | MPYHRGGDASSQADKLSGIVEESDLYEGFAPHVETSEIKTLDFYNLPKQTGKEPALRSYTEIQQLLQQGKKRDVKNILRENSWPINSPIRAQLWPMLCGQHQTKQQMLDGFYWEMVHQVFGTTELSEKPIMLPAFVDATHCLPYHLTSTGRAVADRIVNVLGYDCPDITYSPVLYPITSILLHFMSEEEAYICLAGLVGSKEKVFINQTKLQHEVTWKTVMQIAKKHTKSATSYFQRICPGLKLERIFMDWCWWILAGLPFQHLVRIMDCYFHEGIKVLYRVALVILNLFHKECQSNNEWSPDNIKNDIGNALIKFCKKIPVSPAKLLHAAFSIRGLSTQYISRIFIKTEMLLKSRSVLTSGSKQLIKSRSSDNLPTSQSQVNIQMMSHTLTIREHFGLPGTKNFIKTWTDRQFLFTLWSWLPVRITMYQPVLLYTTEEHGCSLTTFYVRVEQHEPTLLMIKTCNNEVFGAYCSSRWFERNVKDDKGQRQAYFGTGETFLFSLYPERAKYPWVGIEGDKDLGHSSELFMAADSKMITIGGGEGQAIWMDENIRFGKTDSCKTFNNPPLCPSGDFEIRVLEVYGFVGI | Function: GTPase-activating protein (GAP) for Rab35 which regulates synaptic vesicle (SV) protein recycling and turnover at the neuromuscular junction boutons and possibly ventral nerve cord via endosomal trafficking . Inhibits Rab35-mediated endosomal sorting which traffics old or dysfunctional SV proteins through a degradative endolysosomal route that involves the ESCRT pathway and the HOPS complex members dor, vps39 and rab7 . This function is essential for preventing excessive degradation and turnover of vesicles from the readily releasable pool which leads to increased neurotransmission and eventually neurodegeneration . Preferentially binds phosphoinositides phosphorylated at the D5 position of the inositol ring, such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) . Binding to phosphoinositides and thus membrane-association, is required for its function in regulating the turnover of synaptic-vesicle proteins . It is therefore likely that it is recruited to vesicle membranes with high phosphoinositide content and thereby selectively prevents endolysosomal degradation of these vesicles .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67328
Sequence Length: 587
Domain: The Rab-GAP TBC domain is essential for phosphoinositide binding.
Subcellular Location: Cytoplasmic vesicle
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Q00497 | MEARVSQSLQLSSWINSDKVVRKPSGLLRFSEKWNEKPRHRVVVSCHLQPRKAAHSDRRVQLKVSCSPQNVQASVLESGCFSASIDEIETLKNKAEEVEEYLDGRCVYLVGMMGCGKTTVGRILAETLGYSFFDCDRLIEQAVGGITVAEIFELRGESFFRDNETEVLHKLSLMHRLVVSTGGGAVVRPINWRHMHKGISVWLDVPLEALAKRITTEGTKSRPLLHEESGDVYDTTLKRLTTLMETRGENYANASARVSLENIALKREKDVCHITPAEITLEVLIQIENFLKTQKSVVVL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 33720
Sequence Length: 300
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Plastid
EC: 2.7.1.71
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A2ZLU6 | MAGDRAEEEEGEAPPPEARAAAAVERVAAAVEAVAAGAGAGAGEYRNAYRRQLLALSRRIRLLGPFVEELRERRRGEGEGEEEERALAPLADALEAALALLRLGREGSRISLVLERDSVMKKFQGVILQLEQALCDIPYNELDISDEVREQVELVHAQLKRAKERIDMPDDEFYNDLLSVYDKNYDPSAELAILGRLSEKLHLMTITDLTQESLALHEMVASGGGQDPGEHIERMSMLLKKIKDFVQTQNPDMGPPMASRVLDSNGDSRPITIPDEFRCPISLELMKDPVIVSTGQTYERACIEKWIASGHHTCPTTQQKMSTSALTPNYVLRSLISQWCETNGMEPPKRSTQPNKPTPACSSSERANIDALLSKLCSPDTEEQRSAAAELRLLAKRNANNRICIAEAGAIPLLLSLLSSSDLRTQEHAVTALLNLSIHEDNKASIISSGAVPSIVHVLKNGSMEARENAAATLFSLSVIDEYKVTIGGMGAIPALVVLLGEGSQRGKKDAAAALFNLCIYQGNKGRAIRAGLVPLIMGLVTNPTGALMDEAMAILSILSSHPEGKAAIGAAEPVPVLVEMIGSGTPRNRENAAAVMLHLCSGEHHLVHLARAQECGIMVPLRELALNGTDRGKRKAVQLLERMSRFLVQQQEEQESQSQASAQVPPQATPEQVPENDIPEQLDSPASQYPMVV | Function: Defense related protein that negatively regulates programmed cell death. In vitro, possesses E3 ubiquitin ligase activity.
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): 75300
Sequence Length: 694
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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P35829 | MKKNLRIVSAAAAALLAVAPVAASAVSTVSAATTINASSSAINTNTNAKYDVDVTPSVSAVAANTANNTPAIAGNLTGTISASYNGKTYTANLKADTENATITAAGSTTAVKPAELAAGVAYTVTVNDVSFNFGSENAGKTVTLGSANSNVKFTGTNSDNQTETNVSTLKVKLDQNGVASLTNVSIANVYAINTTDNSNVNFYDVTSGATVTNGAVSVNADNQGQVNVANVVAAINSKYFAAQYADKKLNTRTANTEDAIKAALKDQKIDVNSVGYFKAPHTFTVNVKATSNTNGKSATLPVVVTVPNVAEPTVASVSKRIMHNAYYYDKDAKRVGTDSVKRYNSVSVLPNTTTINGKTYYQVVENGKAVDKYINAANIDGTKRTLKHNAYVYASSKKRANKVVLKKGEVVTTYGASYTFKNGQKYYKIGDNTDKTYVKVANFR | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 46570
Sequence Length: 444
Subcellular Location: Secreted
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P38059 | MKKNLRIVSAAAAALLAVAPIAATAMPVNAATTINADSAINANTNAKYDVDVTPSISAIAAVAKSDTMPAIPGSLTGSISASYNGKSYTANLPKDSGNATITDSNNNTVKPAELEADKAYTVTVPDVSFNFGSENAGKEITIGSANPNVTFTEKTGDQPASTVKVTLDQDGVAKLSSVQIKNVYAIDTTYNSNVNFYDVTTGATVTTGAVSIDADNQGQLNITSVVAAINSKYFAAQYDKKQLTNVTFDTETAVKDALKAQKIEVSSVGYFKAPHTFTVNVKATSNKNGKSATLPVTVTVPNVADPVVPSQSKTIMHNAYFYDKDAKRVGTDKVTRYNTVTVAMNTTKLANGISYYEVIENGKATGKYINADNIDGTKRTLKHNAYVYKTSKKRANKVVLKKGTEVTTYGGSYKFKNGQRYYKIGANTEKTYVKVANFE | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 46688
Sequence Length: 439
Subcellular Location: Secreted
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Q05044 | MQSSLKKSLYLGLAALSFAGVAAVSTTASAKSYATAGAYSTLKTDAATRNVEATGTNALYTKPGTVKGAKVVASKATMAKLASSKKSADYFRAYGVKTTNRGSVYYRVVTMDGKYRGYVYGGKSDTAFAGGIKSAETTTKADMPARTTGFYLTDTSKNTLWTAPKYTQYKASKVSLYGVAKDTKFTVDQAATKTREGSLYYHVTATNGSGISGWIYAGKGFSTTATGTQVLGGLSTDKSVTATNDNSVKIVYRTTDGTQVGSNTWVTSTDGTKAGSKVSDKAADQTALEAYINANKPSGYTVTNPNAADATYGNTVYATVSQAATSKVALKVSGTPVTTALTTADANDKVAANDTTANGSSVAGSTVYAAGTKLAQLTTDLTGEKGQVVTLTAIDTDLEDATFTGTTTYYSDLGKAYHYTYTYNKDSAASSNASTQFGSNVTGTLTATLVMGKSTATANGTTWFN | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 48159
Sequence Length: 465
Subcellular Location: Secreted
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P22258 | MKNLKKLIAVVSTFALVFSAMAVGFAATTPFTDVKDDAPYASAVARLYALNITNGVGDPKFGVDQPVTRAQMITFVNRMLGYEDLAEMAKSEKSAFKDVPQNHWAVGQINLAYKLGLAQGVGNGKFDPNSELRYAQALAFVLRALGFKDLDWPYGYLAKAQDLGLVHGLNLAYNGVIKRGDLALILDRALEVPMVKYVDGKEVLGEPLISKVATKAEYTVIATNAQDRSVEEGKVAVLDKDGKLTTINAGLVDFSEYLGKKVIVYSERFGDPVYVAEGDNDVVSFTEGQDSVGTTVYKNDDNKTAIKVDDNAYVLYNGYLTKVSKVTVKEGAEVTIINNNYLIVNGSYDNSTIVYNDVQSGDKYLNRDSNYELKGTVTVTGAVSKVTDIKANDYIYYGKQYDVNGNVVGTVIYVVRNQVTGTVTEKSVSGSTYKASIDNVSYTVADNNVWNQLEPGKKVTVILNKDNVIVGISSTTTTTAVNYAIFKEKSDPFTAWFAKVKLILPDAAEKVFDAVYSDVYDKVNLAEGTIVTYTVDANGKLNDIQRANDQPFSSASYKADAKVLTEGSTTYYITDNTVLLNNTSDGYKALKLTDLKDATNLNVKIVADNYNVAKVVVFNNASFVSTTTSTVYAYVTGTADVYVNGSTFTRLTVLENGQTKTYDANAQLATNYTHKAVVLTLTNAKIANIALPTVASGVKLTNIDQANLRITDTTNKGYLLDPNFIVVDTNGNLKGLSDITKDTGVNLYTNDVGKVFVIEIVQ | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated; contains 8% carbohydrates, which correspond to about 40 to 50 sugar molecules per monomer. O-linked glycans consist of Glc, GalNAc and GlcNAc.
Sequence Mass (Da): 82785
Sequence Length: 762
Subcellular Location: Secreted
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O14216 | MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS | Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
PTM: Phosphorylated by cdc2 at the onset of S-phase.
Sequence Mass (Da): 38685
Sequence Length: 337
Subcellular Location: Cytoplasm
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P34252 | MYSFELDKLKIELKTWEHDFIDKNKREPTRDDIKSLRTVRQMYKQYSTLKKKQSLQRQKVDTQESVELPAHKKDHDEVVEIGPTPQVYGKAISIFDMNLSPIKPIYMTFTNNIDVNNDNSKTISNESSPRKTILLKSSPADRTLVAEPISSVKRQLNFQMLNASSTRTPTSSPCKNRNGKLVEIKKCSPTINPPLESGKPSGYYGPNSPLKLDEENIHLNISLNSSTKRRLQIAYPSLQKTPSKDQADISTSFSPSPLIRRPLTKSLIELAREHTEIVKEFGVLQEEDIEEEEEGEEGENGYDEKNHEDDFGLEDELIRPKVVKDIFQEDDDNDDSQAREDTFIRKRPKRRKVIRRLRDNDPETETAGFERDVHKELVKLKRRKVAEFLGSTSQISDTEFEHDPEASSGVVSSEQKPTAKRKGRKKYNLVSNNFRRLKLPKKNRFSNGRWGRR | Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks.
PTM: Phosphorylated by CDC28 at the onset of S-phase. This phosphorylation, specifically phosphorylation of Thr-84 promotes interaction with DPB11 leading to DNA replication. Dephosphorylated by CDC14.
Sequence Mass (Da): 52272
Sequence Length: 453
Subcellular Location: Nucleus
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Q09761 | MNNDHASKKSFCIKAPSNWEKSYLEVWPLVTVPRQCICLRWCISKEYHEFTCSSLQFIVIRPAGTSVLLGRVKSSKANQLVGIEHVEGSRYALIFLSEKLDFKSLKVIANHQLTKSSKSLSNVSNKPLGDQLFRSNSLMSPSLLKKELHRIQSDASQANERESQAPHSFVTHDLISSSKDGNSLTHEFANDSVTEMVQDYTPSCSRDVKSLLDHLYNSYFYQLLMTKTPVVFYVKQMVGKTRQLAVEVHNHVEEKALVDELLKFLDNLKSVDDRKSRLLQCFESHLNYKAWHLEFENEAHQYEIKGYRLWLQNILNRENCQITKLDFEREFSQLKLKEYEIRVLLYFEILYLFLKWDPEYARRRANDNSLLDSRDSGKRKSRKKNAKTLNPFETAQLKLEFTFDGLCIRRTIEQNATERSEDLLLKFCKETIVPYYSSKFPRITRNLLEKCNGLDLLPERSHKHRHSAPPRSKLISSKSEAGRALPGNTSGASISNTSSPHSEASISKDYEILKRRRSNSGVHSLTRSDSSFNGFERDTRRRSSDIARIKNREINLPSSSLSKQRNSMHDISTNFPRRNLSFTEKLTMASLQGQSEESVQPKTTSSLSRSKTLSILEGSVSKRSEPSMDSILVQATPRKSSSVITELPDTPIKMNSLDKASACTVENHIVTESPAHKSNKAQLFVCVPTTPVKKKSASP | Function: Required for loading and maintenance of stable association of cdc45 with chromatin during initiation and elongation of DNA replication. Also involved in temporal regulation of origin firing. Plays a role in meiosis.
PTM: Phosphorylated.
Sequence Mass (Da): 79815
Sequence Length: 699
Subcellular Location: Nucleus
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A6XIG6 | MSEQAVEVSPKCLGPQHHINPLRFVMPPGSWDTHFHVFGPTTKYPYSETRKYTPPDSPFEEYVKLMLALGIERGVCVHPNIHGPDNSVTLDAVERSEGRFLAIVKIAPDVTLPQLKEMKKKGACGVRFAFNPEHGSGELDTALFDRVVQWCGELDWCVNLHFASNAIHSLAERLSQLTIPTLIDHFGRVHPTKGVDQPDFKTLVDLMRLPHMWVKLTGADRISRNSPSYQDVVPLARTLVDVAPDRVIWGTDWPHSGYFDVKRMPNDGDLTNLLLDFAPSEEQRRRILVDNPSRLFGQVAKGA | Function: Involved in the degradation of 4-sulfocatechol which is a central intermediate in the degradation of substituted sulfonated benzenes. Catalyzes the hydrolytical desulfonation of 4-sulfomuconolactone to yield maleylacetate.
Catalytic Activity: 4-sulfomuconolactone + H2O = 2 H(+) + maleylacetate + sulfite
Sequence Mass (Da): 34092
Sequence Length: 303
EC: 3.1.1.92
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Q8IYM2 | MNISVDLETNYAELVLDVGRVTLGENSRKKMKDCKLRKKQNESVSRAMCALLNSGGGVIKAEIENEDYSYTKDGIGLDLENSFSNILLFVPEYLDFMQNGNYFLIFVKSWSLNTSGLRITTLSSNLYKRDITSAKVMNATAALEFLKDMKKTRGRLYLRPELLAKRPCVDIQEENNMKALAGVFFDRTELDRKEKLTFTESTHVEIKNFSTEKLLQRIKEILPQYVSAFANTDGGYLFIGLNEDKEIIGFKAEMSDLDDLEREIEKSIRKMPVHHFCMEKKKINYSCKFLGVYDKGSLCGYVCALRVERFCCAVFAKEPDSWHVKDNRVMQLTRKEWIQFMVEAEPKFSSSYEEVISQINTSLPAPHSWPLLEWQRQRHHCPGLSGRITYTPENLCRKLFLQHEGLKQLICEEMDSVRKGSLIFSRSWSVDLGLQENHKVLCDALLISQDSPPVLYTFHMVQDEEFKGYSTQTALTLKQKLAKIGGYTKKVCVMTKIFYLSPEGMTSCQYDLRSQVIYPESYYFTRRKYLLKALFKALKRLKSLRDQFSFAENLYQIIGIDCFQKNDKKMFKSCRRLT | Function: Ribonuclease which is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling . May play a role in cell differentiation .
PTM: Phosphorylation at Ser-368 and Ser-573 negatively regulates the ribonuclease activity . Dephosphorylation is induced by the interaction with PDE3A and stimulates the rRNA ribonuclease activity .
Sequence Mass (Da): 66972
Sequence Length: 578
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q5U311 | MEIHPSLVVEPSYPDLIIHAGEVTLGEKDRNKMDSKKKRLEKARITEAACALLNSGGGVIVMQMSNKSEHPVEMGLDLETSLRELIPSSDLQAFIETKQQGDLFYIFVKSWSCSPKDGSTKPRICSLSSSLYCRSLTSKLPLDSKETFEFLERKKTCVKGSLTDGKGPPAKIPRLMYQNDLESNPAFEIFQSERLEYGQRLPFSESASIEFKQFSTRRAHEYIKSVIPEYISAFANTQGGYLLFGVDDESKRVLGCPKDNVDRDSLKAVVNEAISKLPVFHFCSSKEKVSYKTRVIDVFKEGNLYGYLCVIKVERFCCAVFSEAPISWMADKENGVYSLNTEKWVRMMVDIGPEAASSKQSSLDDLSKDFECQLSLSNSPPHCRPVYSKKGLEHKGDLQKRLFQVSADCFKYTPESLWRELCSQHERLENLISQQMCSFSCGLLILSRSWAVDLNLEGKQGVICDALLIAENSPPTLYTILEEQDELGQDYCTRTAFTLKQKLVNTGGYTGRVCVMTKVLCLSSQNNIETNGNSVSLIDYPRSYNLANIQEMEDLLQALVIVLLNFSSFLSDQLGCEILNLLTVQQYEILSKSLHKTRKLFVHGMPGSGKTIIAMKIMEKIKNTFHCERDSILYICENQLLRDFIRAKNVCRAVTRKTFMTPNFEVEKIQHIIVDEAQNFRTENGDWYMKAKRITQRMKTCPQIFWIFLDYFQTSHQKESGLPDFLHQYPKEELTKVVRNADKIAEFLQKISEKIRSNPPPIIPRESLNMVCEFNWSQGVSGTCKLLTSLGLEQMARYVAERCYFFLKNGYSAQDIAVLFSTEDEKDNNEDMFLREIRNRTSQIDDAYHLYMFDSIRRFSGLERSIVFGIDPRTAEKSIFHNLMLCLASRARKHLYILSKVPNPFNF | Cofactor: Can also use Mn(2+).
Function: Endoribonuclease that cleaves tRNAs and rRNAs . Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem . Does not act on tRNA(Sec) .
Sequence Mass (Da): 103655
Sequence Length: 907
Domain: Shows a pseudo-dimeric U-pillow-shaped architecture of the SLFN13 N'-domain that may clamp base-paired RNAs.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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P0C7P3 | MESLKTDTEMPYPEVIVDVGRVIFGEENRKKMTNSCLKRSENSRIIRAICALLNSGGGVIKAEIDDKTYSYQCHGLGQDLETSFQKLLPSGSQKYLDYMQQGHNLLIFVKSWSPDVFSLPLRICSLRSNLYRRDVTSAINLSASSALELLREKGFRAQRGRPRVKKLHPQQVLNRCIQEEEDMRILASEFFKKDKLMYKEKLNFTESTHVEFKRFTTKKVIPRIKEMLPHYVSAFANTQGGYVLIGVDDKSKEVVGCKWEKVNPDLLKKEIENCIEKLPTFHFCCEKPKVNFTTKILNVYQKDVLDGYVCVIQVEPFCCVVFAEAPDSWIMKDNSVTRLTAEQWVVMMLDTQSAPPSLVTDYNSCLISSASSARKSPGYPIKVHKFKEALQRHLFPVTQEEVQFKPESLCKKLFSDHKELEGLMKTLIHPCSQGIVIFSRSWAGDVGFRKEQNVLCDALLIAVNSPVVLYTILIDPNWPGGLEYARNTAHQLKQKLQTVGGYTGKVCIIPRLIHLSSTQSRPGEIPLRYPRSYRLADEEEMEDLLQALVVVSLSSRSLLSDQMGCEFFNLLIMEQSQLLSESLQKTRELFIYCFPGVRKTALAIKIMEKIKDLFHCKPKEILYVCESDSLKDFVTQQTTCQAVTRKTFMQGEFLKIKHIVMDETENFCSKYGNWYMKAKNITHPKAKGTGSENLHHGILWLFLDPFQIHHADVNGLPPPSAQFPRKTITSGIHCALEIAKVMKEEMKRIKENPPSNMSPDTLALFSETAYEEATCAQALPGVCETKTNLTTEQIANYVARKCHSLFQCGYLPKDIAILCRRGEDRGRYRLALLKAMELIETHRPSEVVFSPATGVWGSHIVLDSIQQFSGLERTVVFGLSPECDQSEEFHKLCFASRAIKHLYLLYEKRAAY | Cofactor: C-terminally truncated SLFN14 endoribonuclease requires manganese and magnesium for its endoribonuclease activity.
Function: Shows no ribosome-associated and endoribonuclease activities.
Sequence Mass (Da): 103907
Sequence Length: 912
Subcellular Location: Nucleus
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Q8W127 | MKREYQDGGGSGGGGDEMGSSRDKMMVSSSEAGEGEEVDELLAALGYKVRASDMADVAQKLEQLEMAMGMGGPAPDDGFATHLATDTVHYNPTDLSSWVESMLSELNAPPPPLPPAPPQLNASTSSTVTGGGGYFDLPPSVDSSSSTYALRPIISPPVAPADLSADSVRDPKRMRTGGSSTSSSSSSSSSLGGGAARSSVVEAAPPVAAAAAAPALPVVVVDTQEAGIRLVHALLACAEAVQQENLSAAEALVKQIPLLAASQGGAMRKVAAYFGEALARRVFRFRPQPDSSLLDAAFADLLHAHFYESCPYLKFAHFTANQAILEAFAGCRRVHVVDFGIKQGMQWPALLQALALRPGGPPSFRLTGVGPPQPDETDALQQVGWKLAQFAHTIRVDFQYRGLVAATLADLEPFMLQPEGEEDPNEEPEVIAVNSVFEMHRLLAQPGALEKVLGTVRAVRPRIVTVVEQEANHNSGSFLDRFTESLHYYSTMFDSLEGGSSGGPSEVSSGGAAPAAAAGTDQVMSEVYLGRQICNVVACEGTERTERHETLGQWRNRLGNAGFETVHLGSNAYKQASTLLALFAGGDGYKVEEKEGCLTLGWHTRPLIATSAWRLAAP | Function: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Acts as a negative regulator of GAMYB gene expression.
PTM: Phosphorylated.
Sequence Mass (Da): 65206
Sequence Length: 618
Domain: The DELLA motif is required for its GA-induced degradation.
Subcellular Location: Nucleus
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Q0V640 | MPASPLPALSPPASPRRNTSGASALGSRKADIPPDAIRGFATVGSLVRSEHFAQHFDDDIAGKDQEQSRKKSPEDVGNIAATKKKPGKRAATTSTADGEAKPKPKPRARKPKAADEEAVIIDPELRLPAAKVSPFFAAEGAPAAIEPSDEPVVDVPKLTKAGKPRKPRAKKENVGGEEAVPKPKRTRVTKPKAAKAKAGGKSQEEACVESAHFRKSEDTGDETVAGVLATRKSATTENVGSGEASIWDVPQSPKPKKKRAPKKPPPDPVINNLELDEAVSRRRDWTPPRDTAIPSPFTDSVGKENKQIEPDADNGGFTHMISNFAYAQALPAQVASTVADSATGTMAATKRRRIELLDVPGNQTTSRNSSPEKGKAPKKKPRTITDIATEQYQHRAAQLDQSDVASDFFQSHTAVTKVPLNDASLPNGDAPTKKPPRKRSTSKPASEKEKVGSKARSKKASTKAAAKPKHIAEKLLSPGSALMRMNKQDILFGTSSQLALEEPPTLVRQLQHALKESEVEADLSSNGMIAPPPRWPKLDKVVGKRSLWDASSRDVEGGMLEHMEDVYIPEFDRTQDFPLLMDGTNDQPDGAPPSFADIDDFEPAPPVIISSDGPTPPPTTSRTSQRKANDEPDHVMEGPVFEDIDDFDFQPPPSNQNVEFQDSFADDDEILHTSVQSSTHPPPRLRPPATSDPMNGSSKKPRGCPAKSQSAIATSGSPAVAKEPKRTKGKEVKSAPAPPTTPAKGSGRFIDIDEILDSDDEALQALSPTPPRIHNFENSQPLPLYSVSPTRAKKPKADSSVDSKIVPVHIIPTAHLEWLNLKNSIFPSITSHIRSLPSTRDPSKPSWHEKILMYDPIVLEDFTAYLNAKTSLRTWRRATKIQSKAWNKAQKSIGAQEIGVVEGGGNVLAVEKELEAWQVQSWCESMSVCCIWGEGRGKGGVRKGFY | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 102257
Sequence Length: 946
Subcellular Location: Nucleus
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A5DIU9 | MSNDVYFESIHMQSNYEEFETQAQERENISKISTSLSKFRKMSPKSTRSFKVKSAPLTNRKARNRIKSINAHVSAQYKVSNGQQNDDILDFFLKRKHNISSILEGVEDLENRNIVSNDTPQPSDNTGNYSSQLFTQEEWFQILRRIKLRFPKLSARTRKSLKYVTTKLEHLKNINSDDDSPQLWTQAASLPEEGLVNEDMKWLYELDDEQMDIGSSFCNVDEDSDQKLFVLTLSQAMGEREKSEPDVEIISDSSPEPTQLLNDGIIEEEHEVDEEEEDNENEEKSEKQLASSPTQISSDDTQEQLTNRAEISSYEASSLFPNTLETQKQPVKSTIQKQASVVVPDYPKISNVKDEEIILSSSPTRDNEIFQTPRKYSVESVRSSPSSRSGRLGRLMVSPLKLLSPDRLDASQSVYSTARSSPTKQKRVRGREVNEKIVRKRFKTSRVEVAGNFHLKASDDLKIVSTVDKVNGSEVEDSEDDDHSVSIIEITHEVNDEELKAVDEEVTGEAEDGPSIIQVPSSPGNENLQEDLTSMQTSIASVTQEVPSNYTATQMRQALRSLDFPPERSKEGMASSLTRAASIAGTSVSSLLTPDAPYEEVKNQIYSAISESVKKDQLWHERVLSYEPIVLEEFKQWLGELDKDLKFDVTFLQQYCDHMGITTTIGTTTGTTAGTNTTTTD | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 76784
Sequence Length: 681
Subcellular Location: Nucleus
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A3GGG8 | MVDSESQNDFANDGDNDSYFVSTQFESKQEEIMEKELQKLQTGQTVSQLLRFRSGISGLTSVTPKPVKVSRPGLRKTGSRKSKKNQSMSAMVKERFKTDKYAYFSGDQRKIDEFLRRLEGSEDIENMAMSTSGKDGSCLFTRDEWICIVQSIKLRFPELSTTKKKSLSAITRQINKQEKENEDENSIWSQARSLPSLELTDEDLKWLYDLDDEQMANRTITSSMTEVDGNDDHSPFVMTLSQTTPSQLSHIKESDSLYSQETNVQTTEPADHQSGHMQRCHSQTAEGKTQSKILEIEIVSDSEEEIESLIRNTEPDSSEDVYGANEVSSHQVPAVDALASFQSFPFAADMIPRNNVRDKEHESLHISSSIRSSPAQSLTQSQVPSSIDSIIEPPCESPRKMSPIRDTQPEPVITSPFKTPTKKSKELLSKYSSPVKNSIHNNMGSPVAMMVPRSSESAKHVEEIIVSSDEESVYSTAKSVFPSAQIVISEVEDEDEEFYEIVSSIPEKHKPTAAAKKRKLLQTSRYEVVSNFNINDYDDDQRGFKLRKLETKPIIIDSDNEIADSEEDEKNLSIIEITREVEAEESEHDTEYLINLGKQVEGNSKMNTSVLQVPSSPSSITFGRTDILKELEAFSNSDLDTDRTINSNTSKNSNAIKSGTNQTIDFTLLSTKELQERFKKWELKPVQGRQRMVSVLSEVSKLFTNSFNDPVPETRQGFEGTVYGSLNRLVGSNQYWHEKIISFEPLRVSELRDWICTKGYELEEDFLMRYCDDNGYCCTRQP | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 88506
Sequence Length: 782
Subcellular Location: Nucleus
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Q9P6M0 | MSAEEYIEVSSSPDIFTDDDDMITIEPELNKNPKDCNSKRKRSVTECCEIRLITSKCDFESTQQLVHHNCTGHKVHEHNLNAVDEEDFDTENLPLLFSSFSDNESDILEPDLNTRVAEDNDVLLSRYSKIKNSASCRNTFEHSAYHSNREEISSSGFYYHRKPQLFEKSLEKLGNKSIEANRSPLIKELCESANSTENVCFSVSTVDEIQQRHPSAGHSIDSTCQSNSFLEGDSATHKKKKTDNIKEFTSCEFNDRSRTLLNYAGYMDTNKNADNEAKSLKEKLENFPVEKLRAIAESYGFKSSDSKATLIKIVESCLDAIDSRSQSKKLGKETPHDYLITSTKTVLEFDDIVTQTHRAISQVVKQAKDNSVWIKILTYSAIDVEEFQLWLKRKNLNVSLDLIKSWCDKYGVLMKGSWH | Function: Regulatory 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. Has Holliday junction resolvase activity in vitro. Slx4 is required for efficient processing of DNA substrates.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 47765
Sequence Length: 419
Subcellular Location: Nucleus
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A7F2D1 | MATTDVFIISSSPPRRLVSHIASSPPLPSLDKMVNGKKASNLRQGSSVAPIPTGATIFASASTLLRESSSGSLQGFDNARSFVTSAVQDENDLKKSAKPKAPRKTAPKKEDGTVEKVAKASRKTVKKKDKDVSGDFVDELVGEAAEIIAEKKPRKPRAKKGDNAEGKSGSVAEATVEKKPRKSRAKKAVDATGEDLKEKVPRKSRAKKTDVEAGIETVPKEKAVRKPRAKNSDLDSNLQSKMVKGRVTKSAVNASNTHKVETSKADTGNKHFAPNPIVEDIVADEGFGLVEAIRRRTNWTPPKSTKVPIDLEDSPEAQESDTSKGFAELLGSFGYSSYQADSIEKRISSGVSNGAAATRKRKLIEMVTTNIPREPGSKTTKEKAVKKKARTLTDLATSAYATAEDDDNLLDAPTPLLQYFPHAAPEGSTNNGFKIPPKPRSKSPMKRVQKSKTGSAEEPILLSPESAMKQVSNQDFVFGTSSQLAREDSPSLLRDLHDAMQASNELDDYDDPFVSPPTKIAERGKAVVAAKRNLWSIAARDNHGDLMDVETIDLAHTPVAKPDRIMLSQKPSSLVTPGKDDWFDIDEIEDNRPPSTQVPLRETGPIERSINFQLLDSPTQPKNTSKDSSKVFPQKKGTKSLVDKSTTPKKVDASKMPDYESFTTPQLTREIQKYKFKQIKSRKRMIDLLIQCYESQNRPALGVLQGNIPIITQNSLEKSKDVADSSTQVKPTIPSPRRGRAKKVTTSTASLPKSKAKSKMTDTVAFLEMDSDTPLSKIRTPQKSRKGKQPLEDIFDSDHPITPSPPRRSDSQIRKISKALELSPDNNQDDEAQQAQLFTHIYTAITKAPPSQDPFNPSWHEKILLYDPIILEDLASWLNTGALSKVGWDEEVAPLEVKKWCESKSICCLWKENQGGGARSRY | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 101156
Sequence Length: 922
Subcellular Location: Nucleus
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B8MED8 | MTSRLDHTIVIPSSPEQNWARSVSPCTPTRLFGLPPMSISPPSLPSPSRLFEEIGLGQQKNPPSPKSPFSSAAGKTATSKAITENPSRNESSSKRGRPGSSEAKTAGSRKNSKSQETRNKILTGRVAKPTTVSKAKATAASKSKDTSVVKAKAGTKKSKPASQNKKDKLAEEAEAEAKEVADAEGLNLEEALKRRSDWTPPKALSLVSIDEDTPSQGSGTKLSFGDVLRDYHYNRENSSCEPAQPSKEGNPTKRRRLELVEFEVLQERKPIQQKQIKDAVKTRKTKSKPKKQLNTITARVTARYEQIGELEDLFVYNEESSCETSECLKKPTKPKKETAGKQKEPEYIILSPDAATKSLNDQNFLFGTCSQLERDDSPTFFEETQTAIQLSECLTFKKTASTITTASSAMSIATRFTGKKSHWSEAARDFNGAVVQPEIIDMTDSPTVSVALSRLSEVKHDAPKMASLVSSQSVSATNSLVPKDVVTASKPAADVQLASSGPEPNKTELAAGPFRKTASRLPEMPNFNGYTDSELKNQVLSYGFSLRAVRGRKKMIELLDKCWQSKHGNTATAAIVETSSSAAINETVSVSAARHSDTQVSDKLPTRKKKTTPSRLEPKTTSRAGKKKVSEKPLAGKADKPVEKAASPIPASTYNMVDEIEDSEEEIIPSPTRIQIQRQSSSRQTTPAISCLPLGTKSKRSLKSTKSSTYDEATLLELQSSITKAIHLQTRPRRSLGGSSYSPQLTWHEKILLYEPIILEDFAAWLNTEGFALACEDREVGVALVRTWCESRGICCTFRP | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 87385
Sequence Length: 800
Subcellular Location: Nucleus
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C4JJE8 | MSFLNSSRRRTRSPSPGQIFAPSATPIVIDSSPSVPSASSILDSLLGEFSEARDPYTVEAGPTGRSSDHLFSSPGVLTQSPGRENVPPRPSERTKDAHGKDRFLVSTERNGRSPFRGNPYRSAEIHSPKGRLKAPTKEGGTRKTKKFSSSNRTLTGRSTKFLAKTASKPTQSSKVPSEIPAAKLDSLQWEDGELRLELATTRRGSWTPIKDTSIDIVDPTRNLSPSNVSAAGSQKFSSMLSDYGFTKGSTLTMENELRREVPTTKRRLELLQGTANDIFSEGDFSRPPEKSVVNPNGTHSRRSRKTTSTTITSLSTAQYGHQDSRQMSNLADFFPSGEAVERPSGAIKKLKTSKSGTKKKGVKKAKEAPLFKVASIEDALKSLEDQVCLFGTSSQLERVSSDEEPQMANFNLNAQFPRKNSRPQKTRSPCSNPKTSKSLWYASSRGYDDIEFVDMIDSSNPKTLESVEASTFVTPIDSSPMHSQVASQMVFENPCDVSHVLTKIPQTGPKDPIENPVCPEIQIRHSGNVKTQSTSGQSIPSFRGLTTAQLAQKVASFGFKPLRSREKMISLLEKCWESQQQTHIPAMLPASHTALPDSVTRAEQMSKRDTIKSRDIRASKSRSNSNHIPGLVSSTSQNTGYAAKSPDCIRGSSKSNDIGTTQGSPLLTTQSVIVIPDSDDSDNDNNPTGGAYSYPSLASNTPSSSTRTMASESLLSVRTRYEANVGEEQGSNDINQQITKAIRAQPRLVAINGVKRPTWLEKILMYDPIVLDDLTVWLNTEGLDQIGEDSEVSGTTVREWCESKGICCTWKKKRHVAP | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 89414
Sequence Length: 818
Subcellular Location: Nucleus
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A7TEM0 | MDFRQAQRNLELIEEVAKNSQDSDEPIIDEDDLKEGKVEEEGEGTQIPSMPFSDDDDSDNNSKDTFKETPLELVDKEEAIEDKAPNDDEPVVSVEEKIATQEPEPEEQIFMNTQIQGQLDDIEQEDNLRSKLSNFKYASEESSSVQVIKRSNERKLKSKKITKPKLTKTSKRTKTNSNPSTQQTLDEIKISRSENILKLLSGKHGKVKDMINHQRNVEKKVKLVKNKNSNIITYDTYNSEEWLRIMKLILEKFPSANDMEVKQVYHYIYGEEQEQEYDNLWEASQIPLASMREEAYNEDNQIDRKIPNIPNSTQTRVEVMSLSQVMDDVSIIEESKKTTIDSEREMHIYEVPDSTDDEDSRIIRVISGSDEVASIVAESEFSTETESTSTQFFTADGNMVDGVIDLTQGSFKAVTKLFSPLKVDTLLSINKNKEKVQVAVTRTSTRFSNLGSGPVGLEETPRLAPDEAATPPTVISRSPQSTRTPQATRLPNPNITVMYEVNKCELQSSNSYQSRSSEDIRIVNQYDIDVRDSQDEYDSATEKCLIEFAVTNSATPSVQPEDVMNVISSQSVQKLRQDLKTIGLKPVRTKAKMIEALMAASQVLDTDNVDQEQTREALYDQLTSMIKQIPELVSKISRFEPITMEELVLQLIEVNPFADHIDESTIKEWADIQGITLRNN | Function: Regulatory 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.
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 77170
Sequence Length: 680
Subcellular Location: Nucleus
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B3LT96 | MELQRAQRNLKFLQNEDYVNVTDQTNLNGESQNAYSLGMETQVPEMQFSLSSDDDSIGTQVKSVTAQKSPMTQETTKNDTERNKDVDKSCNPVSTSHPDLGGSNIEENIFINTQIQSRLDDAEEETNLKLKLEKFKYSFKSSNADDTHSNANVTAKRRPAIRKANSKLKTKPKTKRDPKIIKNITDFNINNYERSRTASLLKQLSGKHKKVLDIIKTQNEGNSDKPPRARNNKGEKATFDTYSEQEWKDIMKLLLQKFPQSEETDLNEVQKFLYGSEKSSNSLDNQESSQQRLWTASQLPPELPDEAIQPEQEERIRDTQSAVNFLSLSQVMDDKSEIMKDEESIIISRGDSTSSQEYGNGLEPQQPVGNVVGEDIELAVGTRINAFSLTDYKACKPMSVEVSRRCENSTDNDYDNISIVSDTTDETSTLFPLDQYRYVFIENDERPPLATDTIGSTQFFTPNTSPLDGIIDLTQESFKAVRSLISPLKVENNKTGVTSQASNQVQVPATRTPTIIPQKNLTTTLKTEEEKNNIGSSIRVKLLQESVVKLNPKLVKHNFYRVEANDSEEEETEFDDQFCIADIQLVDSSKISTKDSTQNPTTSNDIIDTSAASSIASPEKFCEIMMSQSMKELRQSLKTVGLKPMRTKVEIIQSLQTASQILSTANPDNKGEHGGVANFSKIEIFDHLTELIEAFPDFLERIYTFEPIPLNELIEKLFSAEPFVSQIDEMTIREWADVQGICLRNDKK | Function: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component 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. Interacts with the structure-specific RAD1-RAD10 endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail removal (NHTR) during repair of double-strand breaks by single-strand annealing. SLX4 also promotes recovery from DNA-alkylation-induced replisome stalling during DNA replication by facilitating the error-free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10, but probably RTT107.
PTM: Phosphorylated by ATR (MEC1) and ATM (TEL1) upon DNA damage. This appears to be required for the function with the RAD1-RAD10 endonuclease.
Sequence Mass (Da): 84362
Sequence Length: 748
Subcellular Location: Nucleus
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C5DY61 | MDFHRANRNLQLVESGVSDGRNPESFSLDETQVPVSSGFSSDSDKDQQEQIFINTQVQGRLDEAEEADKVRANLGQFRYDSQDSAISPKHKSAIQRPSARTTKRSSSSQRRKAPTKAQSLLKQLSGKHAKVQDMIKYQQKLDSLAGSQQRAKSKGKTTKTKKQQEKRYDTYNANEWQHIYNLLLEKFPHTRPSEVEDVYQYLYGDESEDQPLWNESQRPIEPESQDLGFLPPPPADKQRVSVLSLSQVMDDKHSREPDEDIIVPDSTDEEYIVIPIPSSPQPLRPPLATKPPLLTKPPLKKVESDAGTPKTAHSPSDGVIDLTNGSFKVVKSLISPLKEETAQVQVPATRMPTLGTTPNLAPTKEQPLRYRLHRSQLESFSAVEGLIVCSPGPSQDDVPVPDTESEDSAAEDHCMVELQPSILASRTPSPSVQSDWNSQSAQQLRQSMKSLGLKTSRSKRQMLHSLQQASQVLEIDTGGQENQRQEIHDYLTSLVQSSPVLLEKVYTFQPIASKELLTKLTEANPFVDVIDEYTIREWADYQGICLTTS | Function: Regulatory 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 (By similarity).
PTM: Phosphorylated in response to DNA damage.
Sequence Mass (Da): 61482
Sequence Length: 549
Subcellular Location: Nucleus
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P32828 | MHSDTNGRTKSNNSPSDNNPNETVILIDSDKEEDASIREANLPVRLYPDRRVGRRRDALNRFVRSDSRSRNSQRTHITASSERPDFQANNDDITIIREVGRFFGDDGPIDPSAHYVDLDQEPGSETLETPRTIQVDNTNGYLNDNGNNNESDDGLTIVEERTTRPRVTLNLPGGERLEVTATTTDIPIRRSFEFQEDLGASRRQLLRRSATRARNLFVDRSDENDEDWTDDTHNLPEAIQRARRESRMRMSRRIAERQRRVQQQRVSSDENISTSIRLQSIRERIQSYTPDIRSAFHRAESLHEFRSILQNVAPITLQECEEELMALFTEFRNQLLQNWAIDRVRNTQEEALRLHREALERQERTAGRVFHRGTLRESITNYLNFNGEDGFLSRLWSGPALSDADEERHTQNIIDMIQEREERERDVVMKNLMNKTRAQQEEFEARAASLPEGYSASFDTTPKMKLDITKNGKEETIIVTDDDLAKTLEDIPVCCLCGAELGVGIPDDFTGISQKDRGVSFEGLVSKYKFHCPYQTLARPSMLDRDLSKRTFIASCGHAFCGRCFARIDNAKKKSKMPKKKLAQLKGSAHPDNYGPKLCPADSCKKLIRSRGRLKEVYF | Function: Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation . The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2, and mediates the proteolytic down-regulation of sumoylated proteins . The STUbL complex SLX5/SLX8 is involved in ubiquitin-mediated degradation of histone variant CSE4, preventing mislocalization to euchromatin . The complex plays an essential role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis . The complex is involved in proteolysis of spindle positioning protein KAR9 and ensures correct spindle function by regulating levels of microtubule-associated proteins . During replication, the complex helps prevent DNA lesions via recombination and has a role in localizing the DNA damage protein DCD2 . The complex especially ubiquitinates the nuclease YEN1 and prevents persistent accumulation of a fraction of YEN1 associated with sites of activity in late G2/M and helps maintain the balance between pro- and anti-crossover pathways during homologous recombination . It is also involved in ubiquitin-mediated degradation of DNA repair proteins RAD52 and RAD57 . Along with SIR2, promotes silencing of genes at telomeric or ribosomal DNA (rDNA) loci . Finally, the complex is recruited to distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots) by the sumoylated transcription factor-like protein EUC1 where it ubiquitinates EUC1 and presumably other targets .
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): 71071
Sequence Length: 619
Domain: The region between Ser-201 and Leu-335 is required recruitment of SLX5 to ub-hotspots via interacion with EUC1.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P87176 | MPPAHKRDTNVRNLSAPYNIPSQSARVAAGNAAINRRRSSPVENSPGNGFPVSEDATDYPSGTTSENESLPLNRAPRSLREVASELAQEETLPVETSDLNIDVESEVFDLEDINFQNDADDINQRFTYNNHPASVENSLTNVNSIHAQPTTISDMIDLTDETSYDPRKQKFEQGKNPSTTNAEIEKEEPSKKQVVPSSQRLADYKCVICLDSPENLSCTPCGHIFCNFCILSALGTTAATQKCPVCRRKVHPNKVICLEMMLGSQKKKS | Function: Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Acts as a critical suppressor of gross chromosomal rearrangements (GCRs) during normal cell cycle progression. Involved in stabilizing, restarting or resolving transiently stalled replication forks. Prevents accumulation of DNA damage during cell cycle progression (By similarity).
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): 29656
Sequence Length: 269
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P40072 | MARRPDNQNPEGENLRIKRVRLESVRQNDEEEENEVSRTQNIVTDNRHDSPEAVVEIIGERALENTSEEDGDDDLSLFRALEEDPGSDHNTSNNDSGNHDRETMHTEEPEASSGNNITLTNNVEELHTMDVLSQTANTPSASPMLDAAPPTTKPGTNSKEQTVDLTADAIDLDAEEQQVLQISDDDFQEETKEAPKEYGAAKDYRCPICFEPPETALMTLCGHVFCCPCLFQMVNSSRTCRQFGHCALCRSKVYLKDVRLIILRKKQVKKKVKS | Function: Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation . The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2, and mediates the proteolytic down-regulation of sumoylated proteins . The STUbL complex SLX5/SLX8 is involved in ubiquitin-mediated degradation of histone variant CSE4, preventing mislocalization to euchromatin . The complex plays an essential role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis . The complex is involved in proteolysis of spindle positioning protein KAR9 and ensures correct spindle function by regulating levels of microtubule-associated proteins . During replication, the complex helps to prevent DNA lesions via recombination and has a role in localizing the DNA damage protein DCD2 . The complex especially ubiquitinates the nuclease YEN1 and prevents persistent accumulation of a fraction of YEN1 associated with sites of activity in late G2/M and helps maintain the balance between pro- and anti-crossover pathways during homologous recombination . It is also involved in ubiquitin-mediated degradation of DNA repair proteins RAD52 and RAD57 . Finally, the complex is recruited to distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots) by the sumoylated transcription factor-like protein EUC1 where it ubiquitinates EUC1 and presumably other targets .
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): 30764
Sequence Length: 274
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q9UHJ3 | MNGEQQLDADAGSGMEEVELSWEDYLEETGSTAVPYGSFKHVDTRLQNGFAPGMKLEVAVRTDPETYWVATVITTCEQLLLLRYDGYGEDRRADFWCDIRKADLYPIGWCEQNKKTLEAPEGIRDKVSDWDEFLRQTLIGACSPPVPLLEGLRNGRNPLDLIAPGSRLECQAFQDSLSTWIVTVVENIGGRLKLRYEGLESSDNYEHWLYYLDPFLHHVGWAAQQGYELQPPSAIRHLKNEAEWQEILAKVKEEEEEPLPSYLFKDKQVIGIHTFSVNMKLEAVDPWSPFGISPATVVKVFDEKYFLVEMDDLRPENHARRSFVCHADSPGIFPVQWSLKNGLHISPPPGYPSQDFDWADYLKQCGAEAAPQRCFPPLISEHEFKENMKLEAVNPILPEEVCVATITAVRGSYLWLQLEGSKKPIPECIVSVESMDIFPLGWCETNGHPLSTPRRARVYKQRKIAVVQPEKQVPSSRTVHEGLRNQELNSTESVMINGKYCCPKIYFNHRCFSGPYLNKGRIAELPQCVGPGNCVLVLREVLTLLINAAYKPSRVLRELQLDKDSVWHGCGEVLKAKYKGKSYRATVEIVKTADRVTEFCRQTCIKLECCPNLFGPRMVLDKCSENCSVLTKTKYTHYYGKKKNKRIGRPPGGHSNLACALKKASKRRKRRKNVFVHKKKRSSASVDNTPAGSPQGSGGEDEDDPDEGDDDSLSEGSTSEQQDELQEESEMSEKKSCSSSPTQSEISTSLPPDRQRRKRELRTFSFSDDENKPPSPKEIRIEVAERLHLDSNPLKWSVADVVRFIRSTDCAPLARIFLDQEIDGQALLLLTLPTVQECMDLKLGPAIKLCHHIERIKFAFYEQFAN | Function: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis.
Sequence Mass (Da): 98141
Sequence Length: 866
Domain: The MBT repeats mediate binding to histones tails; however, in contrast to other MBT repeats, does not bind specific histone lysine modifications. The MBT repeats lack the conserved Asp and aromatic cage at conserved positions .
Subcellular Location: Nucleus
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Q9MA17 | MEIGSSSTVAGGGQLSVPPGFRFHPTEEELLYYYLKKKVSYEPIDLDVIREVDLNKLEPWELKEKCRIGSGPQNEWYFFSHKDKKYPTGTRTNRATAAGFWKATGRDKSIHLNSSKKIGLRKTLVFYTGRAPHGQKTEWIMHEYRLDDSENEIQEDGWVVCRVFKKKNHFRGFHQEQEQDHHHHHQYISTNNDHDHHHHIDSNSNNHSPLILHPLDHHHHHHHIGRQIHMPLHEFANTLSHGSMHLPQLFSPDSAAAAAAAAASAQPFVSPINTTDIECSQNLLRLTSNNNYGGDWSFLDKLLTTGNMNQQQQQQVQNHQAKCFGDLSNNDNNDQADHLGNNNGGSSSSPVNQRFPFHYLGNDANLLKFPK | Function: Transcription regulator. Together with BRN1 and BRN2, regulates cellular maturation of root cap. Represses stem cell-like divisions in the root cap daughter cells, and thus promotes daughter cell fate. Inhibits expression of its positive regulator FEZ in a feedback loop for controlled switches in cell division plane. Promotes the expression of genes involved in secondary cell walls (SCW) biosynthesis.
Sequence Mass (Da): 42382
Sequence Length: 371
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain.
Subcellular Location: Nucleus
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C0NUU1 | MTPLLRTICAILCILIAVPLTFACPTKAGVSKQANKRPTYAIAHMVLDRKGLKDAIKNGANSVEIDIAAYKEGWWADHDIRGRSWGDSLEDMFKAVAKESKNIAFVWLDLKTPDMCSGATCNKDVLDPSKCKPKDKCSMNSLQELAQKILNPAGVRILYGFFGAGATDSAGFNYIQGNLKAGEAVCLSGEVENVLNVYKKKGRGVKPQQRVMDYGYTQLETGFGNCKEKGYNTCAGLRNGAKARDKGDVKRVFGWTSRVGDGERVGQLLDKAHVDGIIYGFAITRYYDHEDSRAAARDITQRVQKSDDRYMATGADKPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane destabilization and host cell penetration, but also pulmonary inflammation and cutaneous lesions.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 35095
Sequence Length: 319
Domain: The SMD-tail motif is highly conserved and may be responsible for structural stabilization.
Subcellular Location: Secreted
EC: 3.1.4.41
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D4AZV8 | MVSLLRLCSFLLAAGSILVQGSPIIAPSIPPCEPPSNFTGPSNFTSRPGNGASPFWLIAHRVLTKDGVKAALGHGANALEMDITGWWSGWFGDHDGLLTSAGDTVSDLFDEIASRRTQGDPVSFVWLDLKNPDFNKNGVNIVSLMILCREKLEKVGVRVLYGFYSSQTNGPSFKFVKQVMNENEAIGIDGKFETVEKDFEEKGIPLQKRVFSSGLFNPDFNFGNCEVHSSGVCAQLREGKESHEFSKVFGWTVSSYTRKDHVYKMMEVGVDGLIYGFVASHYYDHADIRHTLSTIRGWLEEHKDTHRLATVDDNPWSSMSKKGSSKSSWVKGEVPSIAH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane destabilization and host cell penetration, but also pulmonary inflammation and cutaneous lesions.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 37485
Sequence Length: 339
Domain: The SMD-tail motif is highly conserved and may be responsible for structural stabilization.
Subcellular Location: Secreted
EC: 3.1.4.41
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B8NQ51 | MQSISVLICVLLALSILNFTVASLTQRPIYAIAHRVLRNEAVTAALSHGANALEVDLTAWYFGWWADHDGKLFSAGSTARDLFKFIAQKQWTKDYNISFVWLDIKNPDFCRKGRPCSIEALRDLAREILEPAGIRVLYGFFETAESRGFKVIRDGLNSNEAVVLSGETSTILHLYNISGAGIPVKQMVMDFGDSWLRKGVDIYPELRYGSWKRDHGKLGKVFSWTSAQGDTEMVRYLLREAGIDGLIYGYQTDEYNDKSGPKSALKDIVDFVEAHSDTHRMATEDDAPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane destabilization and host cell penetration, but also pulmonary inflammation and cutaneous lesions.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 32525
Sequence Length: 289
Domain: The SMD-tail motif is highly conserved and may be responsible for structural stabilization.
Subcellular Location: Secreted
EC: 3.1.4.41
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J3K844 | MVSLSLLLCSALAGLLHVASCIDVPDQAPLTVDECKCKPTSPKPVYAIAHRVLTEEGIQAAIAHGANAIEIDMTAWKSGWWADHDGLPTSGNVTAKAMFREVARLREDGAHLSFVWLDIKNPDWAISGRSSVAYLRKLAREYLEPAGVRVLYGFSNPRNSWGFKEIRNFLNANESVSVWMDSGDAKKIYAGVGRSIPVAQRVVDNGLFSLFWKPYIFDDLRRSSEARDCCTVGKAFGWTILAGQDRYVDKLLGYSGVDGLIYGTMASAYEDSEDTRAAAALISNWIKNHPDTHRVPTQDDKPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane destabilization and host cell penetration, but also pulmonary inflammation and cutaneous lesions.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 33481
Sequence Length: 303
Domain: The SMD-tail motif is highly conserved and may be responsible for structural stabilization.
Subcellular Location: Secreted
EC: 3.1.4.41
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C4JUE5 | MLLSSLISLALLSSQVVADPAWAPPDKGLKPEVARLLPPFLRYRRPIYAIAHRVVTVGGIKDAISHGANAFEVDMCADSIGEGWWANHDCTNGRKAGDSARKIFETFAAERKRGKTVTFVWLDFKNPDACVKNQGCSIEAIQQLCRDILEKQGIRVLYGFYKAEDSRAFKTIRNNLNDREAISLNGATTKVLKLFEGTAPKVSKHQRVMDYGDTYLDKGFGDCTEKDWYTCTELRQGADLRRKGKLGKVFAWTSTVNQGRLVDQLLGKAHVDGIIYGFKLTDYYDHADSRAAANDIISWVKRRRALYYMATNDNNPWIDIHKLFLYLLSWFSCILLLMMNEWTCPQDGA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane destabilization and host cell penetration, but also pulmonary inflammation and cutaneous lesions.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 39447
Sequence Length: 349
Domain: The SMD-tail motif is highly conserved and may be responsible for structural stabilization.
Subcellular Location: Secreted
EC: 3.1.4.41
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P38925 | MVNVGPSHAAVAVDASEARKRNISEEVFELRDKKDSTVVIEGEAPVRTFTSSSSNHEREDTYVSKRQVMRDIFAKYLKFIGPGLMVSVAYIDPGNYSTAVDAGASNQFSLLCIILLSNFIAIFLQCLCIKLGSVTGLDLSRACREYLPRWLNWTLYFFAECAVIATDIAEVIGTAIALNILIKVPLPAGVAITVVDVFLIMFTYKPGASSIRFIRIFECFVAVLVVGVCICFAIELAYIPKSTSVKQVFRGFVPSAQMFDHNGIYTAISILGATVMPHSLFLGSALVQPRLLDYDVKHGNYTVSEEQDKVKKSKSTEEIMEEKYFNYRPTNAAIKYCMKYSMVELSITLFTLALFVNCAILVVAGSTLYNSPEADGADLFTIHELLSRNLAPAAGTIFMLALLLSGQSAGVVCTMSGQIVSEGHINWKLQPWQRRLATRCISIIPCLVISICIGREALSKALNASQVVLSIVLPFLVAPLIFFTCKKSIMKTEITVDHTEEDSHNHQNNNDRSAGSVIEQDGSSGMEIENGKDVKIVYMANNWIITVIAIIVWLFLSLLNVYAIVQLGMSHGDIS | Function: High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63264
Sequence Length: 575
Subcellular Location: Cell membrane
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P38778 | MTSQEYEPIQWSDESQTNNDSVNDAYADVNTTHESRRRTTLQPNSTSQSMIGTLRKYARFIGPGLMVSVSYMDPGNYSTAVAAGSAHRYKLLFSVLVSNFMAAFWQYLCARLGAVTGLDLAQNCKKHLPFGLNITLYILAEMAIIATDLAEVVGTAISLNILFHIPLALGVILTVVDVLIVLLAYKPNGSMKGIRIFEAFVSLLVVLTVVCFTVELFYAKLGPAKEIFSGFLPSKAVFEGDGLYLSLAILGATVMPHSLYLGSGVVQPRLREYDIKNGHYLPDANDMDNNHDNYRPSYEAISETLHFTITELLISLFTVALFVNCAILIVSGATLYGSTQNAEEADLFSIYNLLCSTLSKGAGTVFVLALLFSGQSAGIVCTLSGQMVSEGFLNWTVSPALRRSATRAVAITPCLILVLVAGRSGLSGALNASQVVLSLLLPFVSAPLLYFTSSKKIMRVQLNRTKELSRTTDKKPVADRTEDDETIELEEMGIGSSSQERSLVSPAPEYKDMSNGMIVTVLAIIVWLIISGLNFYMLLGFTTGKEVHL | Function: High-affinity manganese transporter involved in mobilizing manganese from vesicular stores iin conditions of low manganese ion concentrations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59768
Sequence Length: 549
Subcellular Location: Vacuole membrane
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Q12078 | MRSYMQILQKFAKFIGPGILVSVAYMDPGNYATSVSGGAQYKYTLLFSIFISNIFAVLLQCLCVKLGTITGYDLAENCRHNLPKKLNYTLYLFAEVAIIATDLAEVVGTAIALQILFKIPLTWGVLLTVLDVLVILMFYTPNGQSLKKVRVFEFGVGILVIGTCICFVLELFKVSIPDKAELFKGFLPSNIIFKEQQALYISLGILGATVMPHSLYLGSSIVKPRLHDYDLKKYGKVNARPSLSAIKYTLNYAYAELIISLFLIATFVNSAILIVAGATLSGQPEAEDADLLSIYKLLVHYISPAAGLIFALAMLCSGQSAGIICTLAGQIVSEGFLQWSLPPWATRLCTRLIAIVPCLFVTLTMGEKGISDILNFSQVVLSLILPIVSAPLIYFTANRKLMVVHDENGVVRAPADVNAIADETTPLNSKHSKIVDFTNSRLLTYTSVFVWALIGSLNCYLVISYLLGADIHF | Function: Has a role in controlling the cellular iron ion levels. Mobilizes vacuolar stores of iron in conditions of low iron levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51775
Sequence Length: 473
Subcellular Location: Vacuole membrane
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B0R061 | MSFFNLDRFRFQRDNAVGIHRKSPDGSNSDKENKQAHQRKADGQFPSGKTSRQVLEDVSSDDEVVRMGKDSASDLQQHINKDMEDKIIKLLEIFPQKSKKDLLEVIENTSTLDGAVAHCLMIYGDEDSGGRKDKGGRSDDDDQPKKKRKIQRSDSSESEDEDSEDEESEEPSREKQEALLKKLKRKLPDIEKEVLRDILKEHDWDYENALGSLLVFSSTDTSSPENQKSKQKSKSSHSKEKTDKITQRPSGSSSLSRWLTAASSHVPEVSSMSALKTQKSALSKSTSKNSSFKRKRGDEMPLNDVSASEDEDEIDSDVDSMSDDQDSEDEDSISGTLQDKIIQFLQDASLDELALISGCSIKKAQKIISLRPFNTWKDVKEQFFKDNGLSIDLVHGCKVVLKERQVVLDLMGRCEKIAQKMTKDVTQVIEAGMGSIKQPKVLNSNLKLQAYQLIGLKWLILLHQHKLSGILADEMGLGKTIQAIAFLAHLYEKGIKGPHLITVPSSTLDNWVRELGLWCPSLKVLIYYGSVEDRKYLRQDILTGLIDFNIIVSTYNLTIGNDHDRSLFRKLKLKYAVFDEGHMLKNMNSLRYRHLMTINAEHRLLLTGTPLQNNLLELMSLLNFIMPSMFSSSTSQISKMFSTRSSEEESSFHKDRIAQARLIMKPFILRRVKSEVLKELPPKMEKIEMCPMSDAQHKLYDILFKRLKKTPNGDKRELCNVMMQLRKMANHPLLHRQYYTSDKLAAMSKAMLKEPTHYDADPALIQEDMEVMSDFELHNLCREYSSISGFQLEKALILDSGKFALLTKTLAKLKEKGDRVVLFSQFTMMLDIVEILLKHLDHQYVRLDGSTPMAERIGLIDKYNTNPEIFVFLLSTRAGGQGINLASANTVILHDIDCNPFNDKQAEDRCHRMGQTRTVQVIKLISKDSIEDCMLRVGQEKLKLEQDMTTDEGEDGAITEQMAELLKVSLGL | Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 110346
Sequence Length: 972
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q9U3D4 | MSVTVEVADEETHDVPLVEQVRTTPDQNVDVKVQENNVVTTKIGPKLETIPAAKMQDDNGDEEKAENSEGAAAEKVEKQHDDDGVVVHEETDGVASSRSSHHDKQKPGETKKSGDGKMDDDDIITTARSSSRRICGSAASSSDSETADDAPLLPDEGPSHAVRLEMPGDKPASPHDRFPKTPLKTLVAFLMLVVAAAGNTITLSWIHERYPLTPPLPDIVFELIPKIPWGLRLCENLMIGSFVSLLVLILFHRHRWIVLRRLCFIGSILYGMRCITMMVTPVPKADEDFECSPRFGENATFSLIVMRGVWSMFGLGLNLFDNQKVVLCGDYIYSGHTLVLVVSALFIGEYSPRRFYILHWLSWLVCSVGVIFLVLSHGHYTIDVILSYFACTRVFWAYHTQAAHPSIRLSVQNHQAKEFWFPLLRWFEGDIRRPVPRRFDCPISYSQVCNAFRRVRPRGRNGAARPAFE | Function: Sphingomyelin synthases (SM synthase or SMS) synthesize the sphingolipid sphingomyelin (SM) through transfer of the phosphatidyl head group of 1,2-diacyl-sn-glycero-3-phosphocholine (phosphatidylcholine, PC) on to the primary hydroxyl of ceramide (N-acylsphingoid base), yielding 1,2-diacyl-sn-glycerol (diacylglycerol, DAG) as a side product. Functions as a bidirectional lipid cholinephosphotransferases capable of converting PC and ceramide to SM and DAG and vice versa depending on the respective levels of ceramide and DAG as phosphocholine acceptors, respectively.
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): 52642
Sequence Length: 469
Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.7.8.27
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Q7T3T4 | MSGRMKEVVSWSPEEVTNWLMENAVPEYCEPLKSFTGQDLINLTEEDFKKTPLSRVSSDSGQQLLHMIETLKMAHHIEAHKNGHVNGHIHVSVNNTAHENGFSSKTKLNGVPNGYKKEMIKIPMPEPERLQYPMEWGKTFLAFIYALFCFIFTTVTISVVHERVPPKEVQPPLPDAFFDRFDRVQWAFSICEINGMILVGLWLVQWLLLKYKSIISRRFFCIVCTLYLYRCITMYVTTLPVPGMHFKCSPKLFGDWESHLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVILTLTYLFIKEYSPRRLWWYHWLCWTLSMVGMFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQTNLLARVWWYKPFQYFEKNVQGIVPRSYHWPFPWPVLHRGRQVKYSRLVNDT | Function: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and specifically recognizes the choline head group on the substrate, requiring two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Major form in macrophages. Required for cell growth in certain cell types. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide (By similarity).
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): 49014
Sequence Length: 417
Subcellular Location: Golgi apparatus membrane
EC: 2.7.8.27
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Q86VZ5 | MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSSDNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKEMIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFFDHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTTLPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT | Function: Major sphingomyelin synthase at the Golgi apparatus . Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction depends on the levels of CER and DAG in Golgi membranes . Does not use free phosphorylcholine or CDP-choline as donor . Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting . Plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1 .
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): 48617
Sequence Length: 413
Pathway: Sphingolipid metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.7.8.27
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Q20735 | MTNSSEFTDVLQSRDPCVSNGIVINIDPIDPEPTPIRKEFTCEDTFHHEHHGNSEGFKTLTAFLCLMLSAFLNFFLLTVIHDVVPRQPLPDLTFMIIPQQRWAWSVGDVLSTVSSVVAFTIIFLHHQRWIVLRRTFLLGAIMYGLRAVILGVTFLPPSFHNRDEICQPQVNRTAMYGMEIATRFLTYVITLGLTSGQDKILCGDLMFSGHTVVLTIMYFVQLQYTPRGLVILRYIAAPITFLGIAALVVSGGHYTMDVLIAYWLTSHVFWSYHQIFEMRKDDRPQAPLSRLWWFWLCYWFESDVADGKLVNKWNWPLEGPQRMHTIMNRINYKLQ | Function: Sphingomyelin synthases (SM synthase or SMS) synthesize the sphingolipid sphingomyelin (SM) through transfer of the phosphatidyl head group of 1,2-diacyl-sn-glycero-3-phosphocholine (phosphatidylcholine, PC) on to the primary hydroxyl of ceramide (N-acylsphingoid base), yielding 1,2-diacyl-sn-glycerol (diacylglycerol, DAG) as a side product. Functions as a bidirectional lipid cholinephosphotransferases capable of converting PC and ceramide to SM and DAG and vice versa depending on the respective levels of ceramide and DAG as phosphocholine acceptors, respectively.
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): 38737
Sequence Length: 335
Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
EC: 2.7.8.27
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Q7ZXV5 | MGQPEGLERFDSPGKGRGLKATRSFALGELLFTCPAYTYVLTDTERGNHCDFCFARKEGLSKCGKCKQAFYCNVDCQKGDWPMHKLECSAMCSYGQNWCPSETVRLTARILAKQKTQTERTPSETFLSVKEFESHLSKLDNEKKELIESDIAALHRFYSKNLHYTDNAALVFLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNIIVTFKGTVAEIRAVQEIHAGDEVFTSYIDLLYPTEDRNDRLMDSYFFTCDCRECSTKQKDPAKLEIRKLSDPPSHQTVKDMIKYARNIVEEFRRAKHYKTPSELLEMCELSLDKMGSVFVDSNVYMLHMMYQAMGVCLYLQEWDGALKYGEKIIKPYSKHYPAYSLNVASMWLKLGRLYMGLEKTTIGTKALKKALAIMQIAHGPDHHYIAEIKKELEL | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 49119
Sequence Length: 430
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q5RGL7 | MMKAEGIPGIEQFASPGKGRGLRVSRAYGVGELLFSCPAYSYVLSVGERGLICEQCFTRKKGLAKCGKCKKAFYCNANCQKKNWPMHKLECQAMCAFGENWRPSETVRLVARIIARLKAQKERSPSEILLLLGEMEAHLEDMDNEKREMTEAHIAGLHQFYSKHLDFPDHQALLTLFSQVHCNGFTVEDEELSNLGLAIFPDIALLNHSCSPNVIVTYRGINAEVRAVKDISPGQEIYTSYIDLLYPTADRLERLRDMYYFSCDCKECTTKSMDVVKMSVRKRSDEIGEKEIKDMVRYARNSMENFRRAKQDKSPTELLEMCELSIDKMSTVFDDSNVYILHMMYQAMGICLFTEDYEGAVRYGEKVIKPFTVLYPAYSMNVASMFLKLGRLYIALDRKLAGIDAFQKALTIMEVVHGKDHTYVTELKQEMRDF | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 49630
Sequence Length: 434
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q8NB12 | MTIGRMENVEVFTAEGKGRGLKATKEFWAADIIFAERAYSAVVFDSLVNFVCHTCFKRQEKLHRCGQCKFAHYCDRTCQKDAWLNHKNECSAIKRYGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKDLRVDVDTFLQYWPPQSQQFSMQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGNHEAVKSMFHTQMRIELRALGKISEGEELTVSYIDFLNVSEERKRQLKKQYYFDCTCEHCQKKLKDDLFLGVKDNPKPSQEVVKEMIQFSKDTLEKIDKARSEGLYHEVVKLCRECLEKQEPVFADTNIYMLRMLSIVSEVLSYLQAFEEASFYARRMVDGYMKLYHPNNAQLGMAVMRAGLTNWHAGNIEVGHGMICKAYAILLVTHGPSHPITKDLEAMRVQTEMELRMFRQNEFMYYKMREAALNNQPMQVMAEPSNEPSPALFHKKQ | Function: Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 56617
Sequence Length: 490
Domain: The SET domain is split between the S-sequence (residues 1-49) and the core SET domain (residues 181-258), however the two segments still come together to form a conserved SET domain fold.
Subcellular Location: Cytoplasm
EC: 2.1.1.354
|
E1C5V0 | MRSEAVPQPGGLERFASPGKGRGLRALRRYAVGELLFSCPAYTAVLTVSERGSHCDGCFARKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECAAMCAFGQNWNPSETVRLTARILAKQKIHPERTQSEKLLAVKEFESHLDKLDNEKRELIQNDIAALHHFYSKHMEYPDNAALVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVKEIEPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCDCRECTMKEKDKEKLKIRKLNDPPSAEAVRDMIKYARNVIEEFRRAKHYKPPSELLEICELSLDKMGAVFEDSNVYMLHMMYQAMGVCLYVQDWEGALRYGQKIIRPYSKHYPSYSLNVASMWLKLGRLYMALENRPAGDKALKKAIAIMEVAHGKDHPYISEIKKELEDH | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 49947
Sequence Length: 436
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q9NRG4 | MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 49688
Sequence Length: 433
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9H7B4 | MEPLKVEKFATAKRGNGLRAVTPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLMRCSQCRVAKYCSAKCQKKAWPDHKRECKCLKSCKPRYPPDSVRLLGRVVFKLMDGAPSESEKLYSFYDLESNINKLTEDKKEGLRQLVMTFQHFMREEIQDASQLPPAFDLFEAFAKVICNSFTICNAEMQEVGVGLYPSISLLNHSCDPNCSIVFNGPHLLLRAVRDIEVGEELTICYLDMLMTSEERRKQLRDQYCFECDCFRCQTQDKDADMLTGDEQVWKEVQESLKKIEELKAHWKWEQVLAMCQAIISSNSERLPDINIYQLKVLDCAMDACINLGLLEEALFYGTRTMEPYRIFFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMRVTHGREHSLIEDLILLLEECDANIRAS | Function: Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation . Also methylates 'Lys-5' of histone H4 . Plays an important role in transcriptional activation as a member of an RNA polymerase complex . Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences .
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 49097
Sequence Length: 428
Subcellular Location: Cytoplasm
EC: 2.1.1.354
|
Q5F3V0 | MALPVEEWRRSAARCWAALEPALRERLAAAPLGEALRMGCGLFGPEEAALQRLCRRARTGKEPAAARFYREEGNRQFGRCCYRDAVRLYSQAAAHEPPRSPEVALCFANRSAALFHLGHFEVCLEDIARAESHGYPDRLLPKVLLRKAECLLRLGRLQDATDTLTAVENKMAVDGIMTSPIHRMLLKKLSQLKTEIHEGSCPEPAREADGDVQRESEIWEENGSISGASSSLSLNFSTERGRHLVASQDILPGQNLLKEKAFVSVLCPGEGDSLLLQDSSETVWDTRVTNADLYCHHCLKQLLASIPCCGCSYAKYCSQNCADVAWEQYHRTECPLGALLLTLGVFFHVALRTVLLAGFSEVSRLVEWSRDDSNKDLCNAEAGGEHPSEALDTRAGRKVIPGCNDNGQYQSSYQAVFNLLPHVEKHSPEHKFLCMLSIVAICKKLQETGLEAAVLNGESSTTGSEQKTCGKTSDELSPELMIMAEAMLRHVLQLQCNAQAITVMQELESGDGAVVNKKPVRLATAFFPVLSLLNHSCSPNISVSFSGTAATVRASQPIPSGQEIFHCYGEEMLCCSSEACAFSVSRERLSQRLLDLQQQMEKALELLRDSKADEAIKMLLKCQIDARNFLSPEHLLMGELEDHLAQVYATLGKWQEAARHLGRSIQLVEMHHGPSSVEMGHELFKLAQILFNGFAVSEALSTIQRAEEILSVHCGPQSTQIQELQEMKTCLLELPRSILQRT | Function: Plays a critical role in cardiac development. Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1.
Sequence Mass (Da): 82027
Sequence Length: 742
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q08C84 | MDLPCQDWVCHVEQKWAELRSEETERFSLLTDIDAIFNYGLSLICPEDLNILSRISEKFSVKKSPETASEFRQQGNLSFKVKDYPAAVLHYSKGVCHADKNTDELSLCYANRSAALFYQGLYQACLEDIRRSLEAGYPSHLQDKLQTRQTACQNQLRKAEKPNIPHTDHQLSPCQKTVNSTGHLSDGVSVYFSSDKGRHMLVMENKPAGEVVLEDEAYCSVLIPANIFNTGTNKAVETFGTEDRHCHHCLSQSLSFVPCPKCSYARYCGESCQKDAWDQWHQWECPVGADLLAIGVLGHLALRVVLKAGQTEVQMGIKNTKDHVTTYKNDSPVQLSLGGDCGKSLDHTDCFHGSSYMGIYSLLPHVAQHSPASRFLMAITMAVIYGKLQGGPPPNKWMSFKDEGVKASWQPEMSMLGATALRHMMQLRCNAQAITAVRVKEESGMAVQSSSEIRIATAIFPVLSLLNHSCSPNTSISFTTGFQPDPHNQLGCSEGHFDHPKGSRSGVTVTVRASKDLTAGQEILHCYGPHRSRMEVKERQRLLLEQYFFQCVCQACQRDLSEGSPNAKEHTAPGMKCVKCGKPLQSHTDGYTCSWSSCGHQISSADVQNRLQGFQLLLDEAVHLMEQDRLNEALHILQSAFSQANSILTETHPFQGELADALARLYASTGEWSLAASHLKRSLVAIQAQFGEDSIELGRQLFKLAQLHFNGRDGVASLSVIPRARRLLSLHCSPRCEELQELSEMEHCLQGLL | Function: Plays a critical role in cardiac development . Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1 .
Sequence Mass (Da): 83677
Sequence Length: 753
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q8IYR2 | MDLPVDEWKSYLLQKWASLPTSVQVTISTAETLRDIFLHSSSLLQPEDELFLKRLSKGYLVGKDSDAPLFYREEGNKKFQEKDYTGAAVLYSKGVSHSRPNTEDMSLCHANRSAALFHLGQYETCLKDINRAQTHGYPERLQPKIMLRKAECLVALGRLQEASQTISDLERNFTATPALADVLPQTLQRNLHRLKMKMQEKDSLTESFPAALAKTLEDAALREENEQLSNASSSIGLCVDPLKGRCLVATKDILPGELLVQEDAFVSVLNPGELPPPHHGLDSKWDTRVTNGDLYCHRCLKHTLATVPCDGCSYAKYCSQECLQQAWELYHRTECPLGGLLLTLGVFCHIALRLTLLVGFEDVRKIITKLCDKISNKDICLPESNNQVKTLNYGLGESEKNGNIVETPIPGCDINGKYENNYNAVFNLLPHTENHSPEHKFLCALCVSALCRQLEAASLQAIPTERIVNSSQLKAAVTPELCPDVTIWGVAMLRHMLQLQCNAQAMTTIQHTGPKGSIVTDSRQVRLATGIFPVISLLNHSCSPNTSVSFISTVATIRASQRIRKGQEILHCYGPHKSRMGVAERQQKLRSQYFFDCACPACQTEAHRMAAGPRWEAFCCNSCGAPMQGDDVLRCGSRSCAESAVSRDHLVSRLQDLQQQVRVAQKLLRDGELERAVQRLSGCQRDAESFLWAEHAVVGEIADGLARACAALGDWQKSATHLQRSLYVVEVRHGPSSVEMGHELFKLAQIFFNGFAVPEALSTIQKAEEVLSLHCGPWDDEIQELQKMKSCLLDLPPTPVGPAL | Function: Plays a critical role in cardiac development . Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1 (By similarity).
Sequence Mass (Da): 89225
Sequence Length: 804
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q12483 | MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEFRSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELEKVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILGYSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL | Function: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26954
Sequence Length: 233
Subcellular Location: Cytoplasm
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O43759 | MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPTGPDPAGMGGTYQQPANTFDTEPQGYQSQGY | Function: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25456
Sequence Length: 233
Subcellular Location: Cytoplasmic vesicle
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P46950 | MTKSVGDEESQYIEDPSFAAAAAFTGGRDGVSYSNQRFAEGSGHSSDLAKSLEDYRPPDEKPSSLSSVGEGGANEEEKGGNDGGPLARIQTGLFSPRLRNHRKKILSKFVLNNFFIACVCVSLISIYWGACYGTDRYFFKVKNIVVLQDAPSNTSVQSISAIIPSLLASVPGTWHIYNATSFHRKFGTTNSTEIDRKIVDLIYDERYWLALNVKPNATDTLYNSLISQDANSEFNSSIFFESVFESGRDPSSVKSTILPLMQQLEVRLQKYYVKEYLPSLMSNITSNDRDLNINMENWAIAGQLLFTYNDYRPFADRILMAPLQVGLIYCILLTVLQLSLYGKLHGEMARVLKPKHILIYRLLISWATYFLLSIGFCTVSAIFRIDFTPAFGRGGFVVYWMSTWLVMMAVGGANENVLSLVIAYCPPYLSIWLMTWIILNISASFYPMVLNNEFYRYGYIMPIHNAVDIYKVIFLNLTKRKMGRNYGILVAWVALNTSLMPFCMKFAGKKMQKNAMQAAEAAVAAATQRASRPAEANTDKNNNPPGN | Function: May function as a N-methyl-N'nitro-N-nitrosoguanidine (MNNG) export permease.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61293
Sequence Length: 547
Subcellular Location: Membrane
|
O43760 | MESGAYGAAKAGGSFDLRRFLTQPQVVARAVCLVFALIVFSCIYGEGYSNAHESKQMYCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAYFPQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAVTNPKDVLVGADSVRAAITFSFFSIFSWGVLASLAYQRYKAGVDDFIQNYVDPTPDPNTAYASYPGASVDNYQQPPFTQNAETTEGYQPPPVY | Function: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.
PTM: May be tyrosine phosphorylated by Src.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24810
Sequence Length: 224
Subcellular Location: Cytoplasmic vesicle membrane
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