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stringlengths 6
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stringlengths 11
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stringlengths 108
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P29346 | MTISINEYSDLNNLAFGLGQDVSQDLKELVKVASIFMPDSKIHKWLIDTRLEEVVTDLNLRYELKSVITNTPISVTWKQLTGTRTKREANSLVQAVFPGQCSRLAIVDWAAKNYVSVAVAFGLLKFHRADKTFTISEIGIQAVKLYDSEELAELDKFLYERLLEYPYAAWLIRLLGNQPSKQFSKFDLGEHFGFIDELGFETAPIEIFLNGLAQAEIDGDKTAAQKIKSNFESTSDKYMRWLAGVLVTAGLATSTTKKVTHTYKNRKFELTLGTVYQITAKGLTALKEVNGKSRYPRSRKRVMWEFLATKDKEAIAKKTSRSLMLKHLTEKKNPIQAEVIATLINTDYPTLEITPEEVIDDCIGLNRIGIEILIDGDKLTLNDKLFDFEIPVQKDVVLEKSDIEKFKNQLRTELTNIDHSYLKGIDIASKKKTSNVENTEFEAISTKIFTDELGFSGKHLGGSNKPDGLLWDDDCAIILDSKAYSEGFPLTASHTDAMGRYLRQFTERKEEIKPTWWDIAPEHLDNTYFAYVSGSFSGNYKEQLQKFRQDTNHLGGALEFVKLLLLANNYKTQKMSKKEVKKSILDYNISYEEYAPLLAEIE | Function: An S subtype restriction enzyme that recognizes the double-stranded sequences 5'-GGATG-3' and 3'-CATCC-5' and cleaves respectively 15 bases after G-1 and 14 bases before C-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 68392
Sequence Length: 602
EC: 3.1.21.4
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P34880 | MQRLSPGEFKTLISKERKSHFITPFALVYKTFCDLGYDQKNSDYFLNNPSEYIIAMRKNCWKEFEPFEKEFTTRMLSYLIDEERIKDMSPYDAIRDFTMEYPTHIYDLALSNTQSRRSRAGKEFESILELLMMGAGIPVDVQGAIGKSFFQKNQIGKLVDLVMPGVVQYTSNKRNTMLISAKTTLRERWQEVPEEVNRTGIREMYLATLDDSFSEETINILYEANVVVVTTIENKNFKYKNNNRVLTFEDMLQSAMELSRKWNNVSYTDSEKEEIQRSILKQIEKYSDFPYVVNYYRNRLSALFD | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CCNGG-3' and cleaves before C-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 35939
Sequence Length: 305
EC: 3.1.21.4
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Q9SR34 | MENIKNPKNADDCSDSISKNSHQGVDDSLNQSRSYVCSFCIRGFSNAQALGGHMNIHRRDRAKLRQKLMEDNKDDVVAESDASEVVSLDLNEQQQQQGEALTCDDHDQYVDNDISPKQKLEFWVQESKLDTNDHGKVTEASIDGSSSSHHRDIEVLDLELRLGQSVVKKKTT | Function: Activation factor which mediates telomerase activity and potentiates responses to auxin through the regulation of BT2. Binds in vitro to the DNA sequence 5'-GACAGTGTTAC-3' of the BT2 promoter.
Sequence Mass (Da): 19331
Sequence Length: 172
Domain: Contains a slightly degenerated ERF-associated amphiphilic repression (EAR) motif, which may be involved in the activity of transcriptional repression.
Subcellular Location: Nucleus
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P34070 | DSGSSRDPGASSGGC | Function: Tremerogen A-I is produced by the a mating-type cells and induces formation of conjugation tubes in a mating-type cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 1339
Sequence Length: 15
Subcellular Location: Cell membrane
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P0CF14 | KKVYSFLKLKGCLPRNRFCNALSGPRCCSGLRCKELSIWASKCL | Function: Insect active toxin causing rapid but reversible paralysis in crickets. No activity shown in mammals. Does not show effect on mammalian voltage-gated calcium channels (By similarity).
Sequence Mass (Da): 4979
Sequence Length: 44
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9NYW7 | MLESHLIIYFLLAVIQFLLGIFTNGIIVVVNGIDLIKHRKMAPLDLLLSCLAVSRIFLQLFIFYVNVIVIFFIEFIMCSANCAILLFINELELWLATWLGVFYCAKVASVRHPLFIWLKMRISKLVPWMILGSLLYVSMICVFHSKYAGFMVPYFLRKFFSQNATIQKEDTLAIQIFSFVAEFSVPLLIFLFAVLLLIFSLGRHTRQMRNTVAGSRVPGRGAPISALLSILSFLILYFSHCMIKVFLSSLKFHIRRFIFLFFILVIGIYPSGHSLILILGNPKLKQNAKKFLLHSKCCQ | Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34333
Sequence Length: 299
Subcellular Location: Membrane
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Q9NYW6 | MMGLTEGVFLILSGTQFTLGILVNCFIELVNGSSWFKTKRMSLSDFIITTLALLRIILLCIILTDSFLIEFSPNTHDSGIIMQIIDVSWTFTNHLSIWLATCLGVLYCLKIASFSHPTFLWLKWRVSRVMVWMLLGALLLSCGSTASLINEFKLYSVFRGIEATRNVTEHFRKKRSEYYLIHVLGTLWYLPPLIVSLASYSLLIFSLGRHTRQMLQNGTSSRDPTTEAHKRAIRIILSFFFLFLLYFLAFLIASFGNFLPKTKMAKMIGEVMTMFYPAGHSFILILGNSKLKQTFVVMLRCESGHLKPGSKGPIFS | Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35915
Sequence Length: 316
Subcellular Location: Membrane
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Q7TQA7 | MFGFIEGVFLVLTITEFILGNLVNGFIVSINSSYWFKSKKISLSNFIITSLALFRIFLLWIIFIDSLIIVFSYQTHDSGIMMQLIDVFWTFTNHFSIWLISCLSVFYCLKIASFSHPSFLWLKWRASRVVVGMLWGALLLSCVSTMSLMNEFKIYSALTRSKDTPNMTEYIRLKRQEYNLMHVLGNLWKIPSLIVSLVAYLLLLLSLGKHTQQMQQYSIDSRDQSAEAHKRAMRIISSFLLFFLFYFLSFMILSSSRFLPETRIARIIGVVISMSYLVGDSFILIVCNNKLKHTFVAMLPCECGHLKPGSKGPSAS | Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36289
Sequence Length: 316
Subcellular Location: Membrane
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Q9U8X3 | MKLQNTLILIGCLFLMGAMIGDAYSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY | Function: Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC(50)=4.2 ug/ml)) and fungi (C.albicans (IC(50)=3.0 ug/ml) and P.pastoris (IC(50)=0.5 ug/ml)) than Gram-negative bacteria (E.coli (IC(50)=25 ug/ml)) . Binds to chitin (8.4 uM are required to obtain 50% of binding) . Does not cause hemolysis on sheep erythrocytes . Has no blocking activity on the P-type calcium channel . Has also been shown to weakly inhibit Kv1.2/KCNA2 voltage-gated potassium channels and TRPV1 receptors .
Sequence Mass (Da): 7511
Sequence Length: 67
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q05B45 | MHPPPPGPLGDCLRDWEELQQDFHGIQETHRLYRLKLEELTKLQNSCTSSITRQKKRLQELALVLRKCKPSLPSEAEEAARELENQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLGNFFTTLRVVHQKFHNQLHGSKKE | Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40730
Sequence Length: 343
Subcellular Location: Cell membrane
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A3KNK1 | MLFNPTGLTECLQEWEDLEKDYQQIQDTHRHYKHKLEEVSKLQESCSSSIARQRKKLKDLSESLEECKGAVNPEDVNKIDDIQESIKERPNVFFEMEAFLPKKNGLYLSLVLGNVNVTLLNKQSKFAYKDEYEKFKLYLTVLLLFFSFTCRFLVSYRVVDALFNFLLVWYYCTLTIRESILINNGSKIKGWWVFQHYVSTFLSGVMLTWPDGELYQMFRNQFLSYSMYINFVQFFQYYYQSGCLYRLRALGERHNMDLTVEGFQSWMWRGLTFLLPFLFLGHFFQLYNGITLFQMTQLPEWKEWQVLMCGSTFLVLFMGNFFTTLGVVYHKYMDQDKAKGL | Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40684
Sequence Length: 341
Subcellular Location: Cell membrane
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Q9BXJ8 | MQPPPPGPLGDCLRDWEDLQQDFQNIQETHRLYRLKLEELTKLQNNCTSSITRQKKRLQELALALKKCKPSLPAEAEGAAQELENQMKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLAQDPQCKEWQVLMCGFPFLLLFLGNFFTTLRVVHHKFHSQRHGSKKD | Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli (By similarity). May also be required for efficient adipogenesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40610
Sequence Length: 343
Subcellular Location: Cell membrane
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Q8C1E7 | MQSPPPDPLGDCLRNWEDLQQDFQGIQETHRLYRLKLEELTKLQANCTNSITRQKKRLQELALVLKKCRPSLPSESMEAAQELENQMKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILIVISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLGNFFTTLRVVHQKFHSQQHGNKKD | Function: Ion channel involved in sensing mechanical pain . Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli . May also be required for efficient adipogenesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40751
Sequence Length: 343
Subcellular Location: Cell membrane
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P0C1Z8 | YVSCLFRGARCRVYSGRSCCFGYYCRRDFPGSIFGTCSRRNF | Function: Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC(50) is 7.4 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.1 ug/ml)) than Gram-negative bacteria (E.coli no inhibition at 100 ug/ml). Binds to chitin (4.3 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel.
Sequence Mass (Da): 4919
Sequence Length: 42
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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O75410 | MAFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFSSDSEGNFETPEAETPIRSPFKESCDPSLGLAGPGAKSQESQEADEQLVAEVVEKCSSKTCSKPSENEVPQQAIDSHSVKNFREEPEHDFSKISIVRPFSIETKDSTDISAVLGTKAAHGCVTAVSGKALPSSPPDALQDEAMTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITSGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGEPEEDLEYFECSNVPVSTINHAFSSSEAGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD | Function: Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways . Might promote the nuclear localization of the receptors . Likely involved in the processes that promote cell division prior to the formation of differentiated tissues.
PTM: Isoform 1 is heavily phosphorylated; isoform 6 is not.
Location Topology: Lipid-anchor
Sequence Mass (Da): 87794
Sequence Length: 805
Subcellular Location: Cytoplasm
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Q9PTG8 | MSLQIINDENAGNDITAEKFDLLLNPQTTGRPSILRPSQKDNLPPKPALKSTKVTFQTPMRDPQTLRIMTPSVANKPENVFLLEDCTQALEQLHLSLPSSCGPNPVEINVSVSNNQPDSEELPVRTTGAYSIDFDNFDDINPFKSKTQMLNSPIKADLPSLTENIETTTPVVPADEASKQMVSLNLSAANLDSPVTVQFSSESGSIGVSEKTALDDTLPLSESGIKDLQGLNASSNNIEEPVPLDKDICSNNEKDDATMADSTCEGTSDAHTSSNNIEEPVTLDKDICSSNEKDNAAVADSTCEGTSDAQSPLPIPKSSYSFDPDQFDMMNPFKTGGSKLQNSPAGKKQTPPSADLNTAKTEPVKLEFNFGDGDVSERKPPPKKLGKRPLLKTAAKKPSPKPEIASEKQEQQTAKPSEDEAIVPKASYKFDWEKFDDPNFNPFGCGGSKISSSPKGQKIANEQPSACTQGSKPEAECTASDMAPAENADEKDHGEIEPSQDSGAAEDRSQAEDQSVALSKVEVPHEQTTDCSPVENETQPEVSLINEEPSQKEVEHTSSDMTPPEINGTDSEFKLATEADFLLAADMDFKPASEIFSEGFRQPVEIDYLENFGTNSFKESVLRKQSLYLKFDPLLRESPKKSAAGINLLPSVPLKCSSDLFGAIPEANFPLIPSIENEEKPKGLDLLGTFTVADTALLIVDAPSSVAVPNPFLSTSDAIVEMLKYSQKDMDAAIEAVRLEVQEKDLEVLEWKTKHEKLYLEYVEMGKIIAEFEGTITQILEDSQRQKETAKLELNKVLQEKQQVQVDLNSMETSFSELFKRLEKQKEALEGYRKNEEALKKCVEDYLVRIKKEEQRYQALKAHAEEKLNRANEEIAHVRSKAKSEATALQATLRKEQMKIQSLERSLEQKSKENDELTKICDDFILKMEKI | Function: Maternal RNA in oocytes remains in a dormant state as masking outcompetes eif4g to bind eif4e, thereby preventing translation. During oocyte maturation this complex dissolves and eif4g binds eif4e to allow translation of maternal RNAs . Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome (By similarity). Involved in microtubule assembly during M-phase. Involved in spindle pole assembly by recruiting and regulating ckap5 at the spindle pole leading to microtubule elongation .
PTM: Phosphorylation by aurka is required for localization to mitotic centrosomes.
Sequence Mass (Da): 102541
Sequence Length: 931
Subcellular Location: Cytoplasm
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P09758 | MARGPGLAPPPLRLPLLLLVLAAVTGHTAAQDNCTCPTNKMTVCSPDGPGGRCQCRALGSGMAVDCSTLTSKCLLLKARMSAPKNARTLVRPSEHALVDNDGLYDPDCDPEGRFKARQCNQTSVCWCVNSVGVRRTDKGDLSLRCDELVRTHHILIDLRHRPTAGAFNHSDLDAELRRLFRERYRLHPKFVAAVHYEQPTIQIELRQNTSQKAAGDVDIGDAAYYFERDIKGESLFQGRGGLDLRVRGEPLQVERTLIYYLDEIPPKFSMKRLTAGLIAVIVVVVVALVAGMAVLVITNRRKSGKYKKVEIKELGELRKEPSL | Function: May function as a growth factor receptor.
PTM: The N-terminus is blocked.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35709
Sequence Length: 323
Subcellular Location: Membrane
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Q8BGV3 | MARGLDLAPLLLLLLAMATRFCTAQSNCTCPTNKMTVCDTNGPGGVCQCRAMGSQVLVDCSTLTSKCLLLKARMSARKSGRSLVMPSEHAILDNDGLYDPECDDKGRFKARQCNQTSVCWCVNSVGVRRTDKGDQSLRCDEVVRTHHILIELRHRPTDRAFNHSDLDSELRRLFQERYKLHPSFLSAVHYEEPTIQIELRQNASQKGLRDVDIADAAYYFERDIKGESLFMGRRGLDVQVRGEPLHVERTLIYYLDEKPPQFSMKRLTAGVIAVIAVVSVAVVAGVVVLVVTKRRKSGKYKKVELKELGEMRSEPSL | Function: May function as a growth factor receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35574
Sequence Length: 317
Subcellular Location: Membrane
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Q27272 | MSAEKSDKAKISAQIKHVPKDAQVIMSILKELNVQEYEPRVVNQLLEFTFRYVTCILDDAKVYANHARKKTIDLDDVRLATEVTLDKSFTGPLERHVLAKVADVRNSMPLPPIKPHCGLRLPPDRYCLTGVNYKLRATNQPKKMTKSAVEGRPLKTVVKPVSSANGPKRPHSVVAKQQVVTIPKPVIKFTTTTTTKTVGSSGGSGGGGGQEVKSESTGAGGDLKMEVDSDAAAVGSIAGASGSGAGSASGGGGGGGSSGVGVAVKREREEEEFEFVTN | Function: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.
Sequence Mass (Da): 29314
Sequence Length: 278
Domain: The C-terminus is important for mediating interaction with e(y)2.
Subcellular Location: Nucleus
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P53228 | MSEPSEKKQKVATSSLEQLKKAGTHVVADSGDFEAISKYEPQDSTTNPSLILAASKLEKYARFIDAAVEYGRKHGKTDHEKIENAMDKILVEFGTQILKVVPGRVSTEVDARLSFDKKATVKKALHIIKLYKDAGVPKERVLIKIASTWEGIQAARELEVKHGIHCNMTLLFSFTQAVACAEANVTLISPFVGRIMDFYKALSGKDYTAETDPGVLSVKKIYSYYKRHGYATEVMAASFRNLDELKALAGIDNMTLPLNLLEQLYESTDPIENKLNSESAKEEGVEKVSFINDEPHFRYVLNEDQMATEKLSDGIRKFSADIEALYKLVEEKM | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 37254
Sequence Length: 333
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
EC: 2.2.1.2
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Q8ZN83 | MNQLDGIKQFTTVVADSGDIESIRHYQPQDATTNPSLLLKAAGLEQYGHLIEDAIAWGKKHGGTQEQQVAAASDKLAVNFGAEILKSIPGRVSTEVDARLSFDKEKSIEKARHLVDLYQQQGVDKSRILIKLAATWEGIRAAGQLEKEGINCNLTLLFSFAQARACAEAGVYLISPFVGRIYDWYQARSPLEPYVVEEDPGVKSVRNIYDYFKQHRYETIVMGASFRRTEQILALTGCDRLTISPNLLKELKEKEEPVIRKLVPSSQMFHRPTPMTEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 35592
Sequence Length: 316
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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Q8FLD1 | MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAVDQEKLEKMIGDLL | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 35205
Sequence Length: 317
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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Q1CZW4 | MKFFIDSADVEEIRKAHAMGCVDGVTTNPSLLAKVGRGLEETIREICSIVDGPISAECVSMEADELIKEGRSLAKIHDNVVVKIPMGVEGMKATKALTAEGIRTNVTLCFSANQALLCAKAGATYVSPFVGRLDDISQDGMELISHILEIYRNYEHFNTQVLVASVRNPVHVLQAARLGADVATLPYNVITQLANHPLTDAGIKKFLADWEKVPKAAKPPAAK | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 24082
Sequence Length: 223
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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Q5F6E9 | MTILSDVKALGQQIWLDNLSRSLVQSGELAQMLKQGVCGVTSNPAIFQKAFAGDALYADEVAALKRQNLSPKQRYETMAVADVRAACDVCLAEHESTGGKTGFVSLEVSPELAKDAQGTVEEARRLHAAIARKNAMIKVPATDAGIDALETLVSDGISVNLTLLFSRAQTLKAYAAYARGIAKRLAAGQSVAHIQVVASFFISRVDSALDATLPDRLKGKTAIALAKAAYQDWEQYFTAPEFAALEAQGANRVQLLWASTGVKNPAYPDTLYVDSLIGVHTVNTVPDATLKAFIDHGTAKATLTESADEARARLAEIAALGIDVETLAARLQEDGLKQFEEAFEKLLAPLV | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 37502
Sequence Length: 351
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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A9A413 | MKIFLDTANLESIKKFNDMGLLDGITTNPSLMSKEKGNPKDAMEEITKIIKGDVSLEVVSTDFSGMVDEGKRLRQYGDNVVVKVPMTPDGLKACKSLSSEGIPVNVTLVFSPNQALLAAKSGAKYVSPFIGRLDDIGQDGMNLIQDIKDIFKNYPHLKTEILVASVRHPMHVVEAAKIGADVVTLPPGVLDKMLQHPLTKIGLENFLKDWEKVKAENPDIKI | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 24341
Sequence Length: 222
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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Q8D1X3 | MNQLDYIKKFTNVVIDSGNIKYIKKYSPKDVTTNPSLILRESKSKHYYPLLMDAISYAKKKGGNLNSYIINANDKLLVNIGREILKIIDGRISIEIDVRLSFSYLDLIIRAKKIISLYNSYGIENNRILIKIAATWEGIQAAKFLEKSGINCNLTLIFSLVQAIACAESNVYLISPFVGRVNDWYIKNFKLNKNSKIDPGVKLVYKIFYFYQKYGYKTFVMGASFRNIDQIISIIGCDAITISPDFVNKLNNLKLKKIKNFIRVNLESKIKKNKLLEKEFRWKFNQNFMAVEKLSEGIRLFLRDQKKIDSFFLKKFKSG | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 36964
Sequence Length: 319
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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P45791 | MKKQSGFTLIELMIVVAIVAILAAIALPAYQTYTKKAKFTEVVSATGTYKSALEVCFQTVGSLLNCTNGTNGVPPAAGASGLVTSVAVSGNTASAATITATGDATTFGATSNVYIMTAAGSNGQIIWTAPASGSTCAGAGFC | Function: Major component of the type IV (TAP) pilus . Aeromonas hydrophila possesses two distinct families of type IV pili: the bundle-forming pilus (Bfp) and the type IV pilus (Tap) .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14069
Sequence Length: 142
Subcellular Location: Membrane
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P45793 | MATLTQKQNAPKKVFAFRWSGVNRKGQKVSGELQADSINTVKAELRKQGVNVTKVSKKSQGLFSKGGAKIKPMDIAIVSRQITTMLSAGVPLVQSLQIIARSHEKASMRELMGQIAADVETGTPMSEALRRHPRHFDALYCDLVEAGEQSGALETIYDRIATYREKSEALKSKIKKAMFYPAMVILVAIVVTSILLLFVIPQFEDIFKSFGAELPIFTQFVIGISRFMQHWWYVIFGGTAFAIFLYVRAWRASQKVKDNTDKFILTIPVVGMILHKAAMARFARTLSTTFSAGIPLVDALISAAGASGNYVYRTAVMAIRNEVVAGMQINVAMRTVDLFPDMVIQMVMIGEESGAIDDMLSKVATIFEQEVDDLVDGLTSLLEPLIMVVLGVLVGGMVVAMYLPIFKLGDLVG | Function: Involved in the translocation of the type IV pilin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45386
Sequence Length: 413
Subcellular Location: Cell inner membrane
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A2BIE7 | MADSVAAGLGDENETENEDKEREKRLFSGVKKMEKQAAASDVTETLGFYERKAKCKDRKTNVSDLSLVRFISAELTRGYFLEHNEAKYTERRERVYTCLRIPKELEKLMIFGYFLCLDVFLYVFTLLPLRVLLALVRLLTLPCCGLSGSRILQPAQVCDVLKGFIMVLCYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYTLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDVVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVSRRMGFIPLPLALLLIRVVTSSVKIQGSLSIVCVLLFYLGMITLKVLNSIVLLGKSCMYVKEANMEEKLFQNPPSAAPSRVSSRAHRTKHTREPPGDPAEEGMSASVTTQPTQQDECPAPQIPTSESDQFLTTPDESEEKSLIQDDSELKHRAPKKDLLEIDRFTICGNRID | Function: Plays a role in primary cilia formation . Involved in cartilage and bone development . May play a role in the differentiation of cranial neural crest cells . May act as a downstream effector of hoxc8 during development (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64778
Sequence Length: 567
Subcellular Location: Cytoplasm
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Q6NXT6 | MAGVGDAAAPGEGGGGGVDGPQRDGRGEAEQPGGSGGQGPPPAPQLTETLGFYESDRRRERRRGRTELSLLRFLSAELTRGYFLEHNEAKYTERRERVYTCLRIPRELEKLMVFGIFLCLDAFLYVFTLLPLRVFLALFRLLTLPCYGLRDRRLLQPAQVCDILKGVILVICYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYVLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDIVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVARRMGFIPLPLAVLLIRVVTSSIKVQGILSYACVILFYFGLISLKVLNSIVLLGKSCQYVKEAKMEEKLSNPPATCTPGKPSSKSQNKCKPSQGLSTEENLSASITKQPIHQKENIIPLLVTSNSDQFLTTPDGDEKDITQDNSELKHRSSKKDLLEIDRFTICGNRID | Function: Plays a role in primary cilia formation . May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64260
Sequence Length: 567
Subcellular Location: Cytoplasm
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A0A0F7GFI5 | MTVSNKTQTALVGSPDGAIILSDTAPLPPSQLEDEQVAVAVQAVSLNPVDTKMAGDYHTPGAISGCEFAGVVTAVGPGAASEWGLGPGDRVSAAIMGMNPLRPSIGAFAQHSVAPAHCLLKMRDDWGFAQAAGLGNSWYTVAWALFHVMGLPAGPELEPLHTKHPPPAREPRISIDNPAPNGGGGKRTTVLVSGGSSSTGTCAIQLLKLAGFDVVATSSARNFDLVRSYGADAVFDHSSPSVAADIKAHTRNGLRLALDCITTPDTTRLCYGAIGRTGGRYVSLDPYSEVVAASRAVVRADWVLGPELMGEDVGWPAPHGRKGNPEAKAFCKVWNRTLQGLLDRGAIRTHPQRVRDTGLRGVLEGLDDIREKRVSGEKLVYTLQV | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of the tetramic acids Sch210971 and Sch210972, potential anti-HIV fungal natural product that contain a decalin core . The PKS module of tasS together with the enoylreductase tasC catalyze the formation of the polyketide unit which is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the condensation domain of the tasS NRPS module . One unique structural feature of Sch210971 and Sch210972 is the tetramic acid motif proposed to be derived from the non-proteinogenic amino acid HMG, by a Dieckmann-type condensation catalyzed by the reductase domain of tasS . The aldolase tasA catalyzes the aldol condensation of 2 molecules of pyruvic acid to yield the intermediate 4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then be stereoselectively transaminated, may be by tasG, to form HMG . The Diels-Alderase tas3 then uses the Dieckmann product of tasS as substrate and catalyzes the Diels-Alder cycloaddition to form the decalin ring of Sch210971 and Sch210972 .
Catalytic Activity: (2S,4S)-4-hydroxy-4-methylglutamate + ATP + 11 H(+) + 8 malonyl-CoA + 8 NADPH + 3 S-adenosyl-L-methionine = (2S)-3-[(2S)-3,5-dioxo-4-[(2E,4R,6R,8E,10E,12E)-4,6,12-trimethyltetradeca-2,8,10,12-tetraenoyl]pyrrolidin-2-yl]-2-hydroxy-2-methylpropanoate + AMP + 8 CO2 + 8 CoA + diphosphate + 6 H2O + 8 NADP(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 40464
Sequence Length: 385
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A0F7CUE9 | MFFDSVTNGPEDVMYQVKAACDSDNDPSKIDLGVGTYRNEDGDYHELDVLKEIATVQTISGTGAIHIGAMFLARSATDVLPHVYVGTPTWGNYQPLLRLAGLEMRTYNHYLSQTGRVDFASVLSAIRTTPRGSTFILQGCCHNPTAADFSREQWDIVVAEMESHGHLPFFDIAYQGLGEGVDEDVYGVRLCADKGMEMVVCQSFAKNFGLYGERCGALHVVCTSDDVAARVKDQLRCLIRWEFSSSPAYGARLVNLVLSDARAEEQCLLPLSKTQCQELQNKFRIYAVPNGRITMSGLSQGNIDYAARAIDAVVRSGLEAREPTG | Function: Aminotransferase; part of the gene cluster that mediates the biosynthesis of the tetramic acids Sch210971 and Sch210972, potential anti-HIV fungal natural product that contain a decalin core . The PKS module of tasS together with the enoylreductase tasC catalyze the formation of the polyketide unit which is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the condensation domain of the tasS NRPS module . One unique structural feature of Sch210971 and Sch210972 is the tetramic acid motif proposed to be derived from the non-proteinogenic amino acid HMG, by a Dieckmann-type condensation catalyzed by the reductase domain of tasS . The aldolase tasA catalyzes the aldol condensation of 2 molecules of pyruvic acid to yield the intermediate 4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then be stereoselectively transaminated, may be by tasG, to form HMG . The Diels-Alderase tas3 then uses the Dieckmann product of tasS as substrate and catalyzes the Diels-Alder cycloaddition to form the decalin ring of Sch210971 and Sch210972 .
Sequence Mass (Da): 35713
Sequence Length: 325
Pathway: Secondary metabolite biosynthesis.
EC: 2.6.1.-
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A0A0F7CUE8 | MRSMSLWMLIGPVTGIATWASLRYAATTTTSSTAAASTRMGLAPVIALSHGGGPLPLLGDPGHKSIIHSLSHRIPKILSLNDPDRRPRAIILITAHWSTAAPTISGAANPDLIYDYYGFPPETYELKYPARGDPGIAAEAAAAFRAEGLGDVVVDPGRGWDHGVFVPMTLVRPEADIPIVQMSVLASEDPTSHLRMGRALRALRAENIAIVGSGFASFHNLRAMMAMRSSAGSRNPEGARIQAISREWNSALTDVVDKNPWQGLEGWRSLPGADLMHPPRGGEHFMPLIACAGAAHEEEKVRWYTDEYLGVDIYTYYWGGSDVE | Cofactor: Binds 1 zinc ion per subunit.
Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of the tetramic acids Sch210971 and Sch210972, potential anti-HIV fungal natural product that contain a decalin core . The PKS module of tasS together with the enoylreductase tasC catalyze the formation of the polyketide unit which is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the condensation domain of the tasS NRPS module . One unique structural feature of Sch210971 and Sch210972 is the tetramic acid motif proposed to be derived from the non-proteinogenic amino acid HMG, by a Dieckmann-type condensation catalyzed by the reductase domain of tasS . The aldolase tasA catalyzes the aldol condensation of 2 molecules of pyruvic acid to yield the intermediate 4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then be stereoselectively transaminated, may be by tasG, to form HMG . The Diels-Alderase tas3 then uses the Dieckmann product of tasS as substrate and catalyzes the Diels-Alder cycloaddition to form the decalin ring of Sch210971 and Sch210972 .
Sequence Mass (Da): 35021
Sequence Length: 324
EC: 1.-.-.-
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A0A0F7GG06 | MDDQKGPLPPYTPTATAPPPASMRQRRPPGRRRALRRSRTVRVLALACLAFVVLAQWKQLWRGERKAPPYLSVDKLNDNLETCRKLRVRPQDPAGPGRSKNDRYLDGGGKPTLIRNALIWTGEPVPGTSDEDARAGVGWAWWLGDVLVERGLITKVDNKMPASEVPEDAIIYDAEGRRLTSGIVDMHSHAGVSPLPGLNGNDDTNEASDNITPWARSIDGLFPLDPQIQVIKSGGVTSSLILPGSANNIGGEAFLIKHAVGRHDGRPELSAASMLADPDRTWRYMKMACGENAKRVHGSRTTRPVTRMGESYDFRRAFERASQLVRRQDDWCDRAGEVGVGSMDEYLPEDLEWEALGAALRGQVHVNAHCYTVNDLEAMVDHSNEFEFPIRAFHHAHQAHLVPEILNRTWGGRPPALAIFADNMYYKAEAYIGTPSAGKMLYDQGLTPIYVSDNPVLNAQHVVLEAAKGFHYGLPYHAALASVTTAPADTLGMGQRLGKIKAGFDADIVVWDSDPLGVGAAPVQVWIDGTAQFDDPVVLSKPHARAEKDTVVVPDAPPPVVVEEPVEVADVLFRGVTRVLLDEHDVSAEDGASLNVAIRGGRISCIGECADEFRVAIDAGVGVVTLGNGHLHKTFVGVGGTLGLNEIDGESKTGNGKNPKTFTRAVDGLLLGGKKLRAAHHAGVTRAISAPRFKGGGNTHHGTSVGIVTSARTSLDAGAIFGNGDVAVHYTLDLSVRGGDDESYSAAFGSLREKLIRAGVHGGKEKEVGAEEVGAEEEEEEEEKAFLRRVLASEMVLALTINSADGIATALRIKDEVDKKQQKQQQQQQQQQQQQHGTSSGIRMAIIGGAEAYLVAEHLAAANVGVILSPLQSYGETWDARRALPGAPLTNGTNIDRLLDAGVKVGIGLKEDWEVRDLALAAGTAYENGGGRLTGRQALDLVGRNVLEILGVEEEEETPGATMGESGHFVVLLIINMFCGL | Function: Amidohydrolase; part of the gene cluster that mediates the biosynthesis of the tetramic acids Sch210971 and Sch210972, potential anti-HIV fungal natural product that contain a decalin core . The PKS module of tasS together with the enoylreductase tasC catalyze the formation of the polyketide unit which is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the condensation domain of the tasS NRPS module . One unique structural feature of Sch210971 and Sch210972 is the tetramic acid motif proposed to be derived from the non-proteinogenic amino acid HMG, by a Dieckmann-type condensation catalyzed by the reductase domain of tasS . The aldolase tasA catalyzes the aldol condensation of 2 molecules of pyruvic acid to yield the intermediate 4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then be stereoselectively transaminated, may be by tasG, to form HMG . The Diels-Alderase tas3 then uses the Dieckmann product of tasS as substrate and catalyzes the Diels-Alder cycloaddition to form the decalin ring of Sch210971 and Sch210972 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 105554
Sequence Length: 981
Subcellular Location: Membrane
EC: 3.5.4.-
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Q32LD7 | MLSEGYLSGLAYRNDIQWSYPSSNEQVAEEKEEEMEATAAASLSYSSVDETQVQNLYVSCKSSGKVISSVYSRESQHSRNPRITVLQTNPNPVYESPNLAAVELYRDTSRETYLVPPSCKSICKNYNDLQIAGGQVMAINSATTDFPSEGSFQYGPLLKSSEIPLSMEDSMFTQPSDLPPTPIQRYSSYWRITSIKEKNSLQMQKPISNAVLNEYLEQKLVELYKQYFMDTGFHDSSPTQILASELIMTNVDQISIQVSIEKNLEISKARDIVINRLLQYGSTEISTQSLHISQYSNVNP | Function: Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9. Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons. Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes.
PTM: The phosphorylated pLxIS motif constitutes an IRF5-binding motif, leading to recruitment of the transcription factor IRF5 to induce type-I interferons and other cytokines.
Sequence Mass (Da): 33758
Sequence Length: 300
Domain: The pLxIS motif constitutes an IRF5-binding motif: following phosphorylation, the phosphorylated pLxIS motif of TASL recruits IRF5.
Subcellular Location: Lysosome membrane
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Q9HAI6 | MLSEGYLSGLEYWNDIHWSCASYNEQVAGEKEEETNSVATLSYSSVDETQVRSLYVSCKSSGKFISSVHSRESQHSRSQRVTVLQTNPNPVFESPNLAAVEICRDASRETYLVPSSCKSICKNYNDLQIAGGQVMAINSVTTDFPSESSFEYGPLLKSSEIPLPMEDSISTQPSDFPQKPIQRYSSYWRITSIKEKSSLQMQNPISNAVLNEYLEQKVVELYKQYIMDTVFHDSSPTQILASELIMTSVDQISLQVSREKNLETSKARDIVFSRLLQLMSTEITEISTPSLHISQYSNVNP | Function: Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 . Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons . Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes .
PTM: The phosphorylated pLxIS motif constitutes an IRF5-binding motif, leading to recruitment of the transcription factor IRF5 to induce type-I interferons and other cytokines.
Sequence Mass (Da): 33894
Sequence Length: 301
Domain: The pLxIS motif constitutes an IRF5-binding motif: following phosphorylation, the phosphorylated pLxIS motif of TASL recruits IRF5.
Subcellular Location: Lysosome membrane
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Q9D3J9 | MLSEGYLSGLTYWNDIHWNCASYNEPVAGDQGKETSSVAALSYSSVDETQVQSLYVSCKSSGKFISSVHARASQHSRSQSRTVLQANSNPVFESPTLAAVGICRDVIRETYLVPPSCKSICKNYNDLHIAGGQVMAINSVMANFPSESSFEDGPLLKSSEISLSMEDSTSTQLTELPLKPIQRYSSYWRITSIKEKSSLQMQKPISNAVLNEYLEQKVVELYKQYIMDTVFHDSSPTQILASEFIMTNVDQISLQVSKEKNLDTSKVKDIVISHLLQLVSSEISTPSLHISQYSNITP | Function: Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9. Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons. Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes.
PTM: The phosphorylated pLxIS motif constitutes an IRF5-binding motif, leading to recruitment of the transcription factor IRF5 to induce type-I interferons and other cytokines.
Sequence Mass (Da): 33057
Sequence Length: 298
Domain: The pLxIS motif constitutes an IRF5-binding motif: following phosphorylation, the phosphorylated pLxIS motif of TASL recruits IRF5.
Subcellular Location: Lysosome membrane
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Q9P6N7 | MSNGLVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDSESGLTASVACCNCCRHPSEACLYILNKRKVMSQHGLVPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWKEILYQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFDNKSHSSTCAVATSGTGEHISNTCFACRSSQLLVSEDNVVSSLNKLINDFHEHPSATLYSDLQVGIIFAKVETSNSHNKRIIFGLAHSSPDMVFGFMKGDHSKPTTEISRKGSKRSSVQLYAERL | PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).
Sequence Mass (Da): 36833
Sequence Length: 345
Subcellular Location: Cytoplasm
EC: 3.4.25.-
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A8F2N4 | MGMSVSHLLIVLLIIFVLFGAGKLPQVMSDLAKGLKAFKDGMKDDGSDNDKNK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5708
Sequence Length: 53
Subcellular Location: Cell inner membrane
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A5UZ79 | MPQLGMGELLIILIIVLLLFGASRITGVASALGGSIKAFRKAVRDDDVPASKSEPAESTDKKVETNV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7039
Sequence Length: 67
Subcellular Location: Cell membrane
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Q1AUL2 | MIPANFGGTELIILLVIILLLFGAKRIPELARGLGTGVREFRKGTSGAYEELEEKKGEEEKDEGGKKEAEASGRGEEEQQARAAGEAGRKQG | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9872
Sequence Length: 92
Subcellular Location: Cell membrane
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A1AVW1 | MMPGPFELIVILVIVLLLFGGKRLKNVGSDLGNAIKGFKKSMQKEPADQINTKDNIVEAKTTKESTK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7345
Sequence Length: 67
Subcellular Location: Cell inner membrane
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Q21FP8 | MGLGGISIWQLLIVLVIVLLLFGTKRLKGLGGDLGGAIKGFKKAMSDDEAAKQEAEEAEQKKVAAEEAAAAKTAEQKEKTEAK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8741
Sequence Length: 83
Subcellular Location: Cell inner membrane
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A4FBZ2 | MGLPGGWELVLIVGVLVLLFGATKLPQMARSLGQSARVFKAEARGMKEDEEAAKREKQAKSEPQQLTAGESSAPTVASPVEETQRNDSKK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9666
Sequence Length: 90
Subcellular Location: Cell membrane
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A8M2B2 | MGALKPWHIAVLVVVLILLFGAKRLPDAARSLGRSLRIIKAETKSLHDDDRDLAEKANAQAGYQPLPPQVQQEPYPQQTPYQAPPQQQPVVDPVQRARDS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11113
Sequence Length: 100
Subcellular Location: Cell membrane
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P0A2H4 | MGGISIWQLLIVAVIVVLLFGTKKLGSIGSDLGASIKGFKKAMSDDDAKQDKTSQDADFTAKSIADKQGEAKKEDAKSQDKEQV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8944
Sequence Length: 84
Subcellular Location: Cell inner membrane
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Q4ZZG9 | MFGISFSELLLVGLVALLVLGPERLPGAARTAGLWIGRLKRSFNAIKQEVEREIGADEIRRQLHNEHILSMEDEARKMFAPNQPSENSPEPANPPPAPAAAEAASPVHNQAAHHEIGPAQPAAPKTELSLEKTAKPADAGTPVPAPPAHDSSLPPRAP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16764
Sequence Length: 158
Subcellular Location: Cell inner membrane
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Q4FQ60 | MFDIGFSELLLFGVIALIVLGPEKLPQAARTAGQWYAKIRRTVSTLQSEIEAELDLAETRQLMQKELAKIRQTEAEMRREMAEMRGSIKEFEHSQSQNLKTSDKAASPANQANNDSAIQNNNEPATFSYAYGQSNNLTDSQQLSNQDITSINSDAVTDSSTIKQPAQPLITKPWENMWFRLGAYDKARRLPAVPYLPNYKADILLNSSFDSSFDSPLNTQASVNQQESE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25642
Sequence Length: 229
Subcellular Location: Cell inner membrane
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A1SRS0 | MFDIGFWELVLISVIGLVVLGPERLPHAIRSVMHWITTAKNMANSVKTEVTQELKLHEINENMIKASKQGLSDLDPELQKSIDEMKETAEQLSRPYKKDIDDIKTSLDKNPSGTTQQENSILDSSKTTPPRQDKNE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15388
Sequence Length: 136
Subcellular Location: Cell inner membrane
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Q2K969 | MFDIGWTELLVIAVVLIVVVGPKDLPPMLRAFGKMTQRARKVAGEFRAQFDEALREAELDDVRQTISDAQKLNPVSSLREAMNPLRQMGNEIKADLQKATAVTENKTEVPSAAMSAPTPSMSLPETPPVVPTPAPAPEPAAVAAETVAAKPKAPRKPRAKAADKAAFAIAAPVENPPAEKPKRTTAARKPAAPKTPVQTKKKKDEA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21995
Sequence Length: 206
Subcellular Location: Cell inner membrane
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Q1MHM4 | MFDIGWTELLVIAVVLIVVVGPKDLPPMLRAFGKMTQRARKVAGDFRAQFDEALREAELDDVRQTISDAQKLNPVNSLREAMNPLRQMGNEIKADLQKATTVTENKTEVPPDAVAAPTPSMSLPETPPLVATPAPSEPVAAAVVQADTVAAKPKAVRKPRGKIADKVDAAAAVAVPVEKPKRTTAVRKPATLKKPAQTKKDEA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21753
Sequence Length: 203
Subcellular Location: Cell inner membrane
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Q92Q24 | MLDIGWTELVVIAIVLIIVVGPKDLPPMLRAFGRMTSKMRGMASDFRRQFDEALREADLDDVRKTISDAQSLNPTAALRDAMNPLRQLGNEIKSDLQKATTPDRPPASATPEPLVEPVNTDAVGETAAKATEKVAAAAVSSASRQMDRAADVPKASEPKPAPKPRAQSKKPGTSVTKKAAGETAPKKSPARKAPGEAPAANKSKTRAASRKKGDA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22754
Sequence Length: 215
Subcellular Location: Cell inner membrane
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Q214X1 | MFDIGWSELLVIGVVALIAIGPKELPGVLRMVGQWMGKARKMASEFQGQFNEAMREAEMADLKKSFDDIKATANTFSRDNIMTSLQKDVDAAMTIDKIEHIDTSPVEPTTPEPPTAETLLEAETHAASISAATAVTEVGEPLAITQEIHPALPSPEPAAAIAIAPIKDAKAS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18351
Sequence Length: 172
Subcellular Location: Cell inner membrane
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Q2RTH3 | MFDLSWSEIALVGVVALIVIGPKDLPNVLRTAGKWVRKIRSLGSEFQRQMDDVMRETGAEDVRRQVTTLARTDVGRKIDQAIDPDGKLAASLSSVPPPSPAGPFGTSPAAPPSLPPQAPAQPVPPATGAAPPSPSAGPDRRTDGSLPPQD | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15674
Sequence Length: 150
Subcellular Location: Cell inner membrane
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Q163T8 | MFDLGWTEMLVIGIVALIVIGPKDLPVMFRTIGQFVGKAKGMAREFSRAMNDAAADSGVNDVTKSLKAAVNPVNTAMDSVKSAASDLGKFDPESETGKLAADKAERAQNAKKIQAATARAAADRKLKEAQEAQARASELEAAVTPPEKNET | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15962
Sequence Length: 151
Subcellular Location: Cell inner membrane
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Q5LQ14 | MFDLGWSELLVIGVVALIVVGPKDLPVLFRNVGRWVGKARGLAREFSRAMNDAADEAGVKDISKGLKAATNPVDAALDGVRKAATDFKTDLDPTKYNPDSETGKLAAERAEQAKKIQAATARVAAERRLREATAELEKAKDAEAALKPGPET | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16242
Sequence Length: 152
Subcellular Location: Cell inner membrane
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Q1GFN7 | MFDLGWTELLVIGVVALIVVGPKDLPKLFRNVGRFVGKARGMAREFSRAMEDAADEAGVSDIQKTFKTATNPMGSAMDSVKQATRDLTDSIDPTKFDPESETGKLAADRAENAKKIQAATARAAADRMAREAAEAAAKAEEAEAALSATPASTASSDSETKA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17036
Sequence Length: 162
Subcellular Location: Cell inner membrane
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Q21FP7 | MFDIGFLELAVIAVIGLIVIGPERLPEAVRSGATWMAKIRKMMRDTRAEIEVQIGADEIRRELHNEQVMKSLEALKVTKDDIQQHILDADRKMMLEQEAEEAKLQTPVSRRVAGDDPTLGTDDNVFTDPSYAHPPEEPSKVEADTSAETPQANNQDQQPTTKTEPANDR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18904
Sequence Length: 169
Subcellular Location: Cell inner membrane
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Q75005 | MEPVDPNLEPWNHPGSQPKTACNQCYCKKCSYHCLVCFLTKA | Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA.
Sequence Mass (Da): 4786
Sequence Length: 42
Domain: The transactivation domain mediates the interaction with CCNT1, GCN5L2, and MDM2.
Subcellular Location: Host nucleus
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P04608 | MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE | Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1.
Sequence Mass (Da): 9837
Sequence Length: 86
Domain: The cell attachment site mediates the interaction with ITGAV/ITGB3 and ITGA5/ITGB1 integrins, leading to vascular cell migration and invasion. This interaction also provides endothelial cells with the adhesion signal they require to grow in response to mitogens.
Subcellular Location: Host nucleus
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P12508 | EAETATKSCSGRQANQVSLPKQPASQPRGDPTGPKESKKKVETETETDPVN | Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B. In this purpose, it activates EIF2AK2/PKR which, in turns, may phosphorylate and target to degradation the inhibitor IkappaB-alpha which normally retains NF-kappa-B in the cytoplasm of unstimulated cells. Through its interaction with TBP, Tat may be involved in transcription initiation as well. Interacts with the cellular capping enzyme RNGTT to mediate co-transcriptional capping of viral mRNAs. Tat protein exerts as well a positive feedback on the translation of its cognate mRNA. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs (By similarity).
PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat.
Sequence Mass (Da): 5439
Sequence Length: 51
Domain: The transactivation domain mediates the interaction with CCNT1, GCN5L2, and MDM2.
Subcellular Location: Host nucleus
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P20879 | MEPVDPSLEPWKHPGSQPKTACTNCYCKKCCLHCQVCFTTKGLGISYGRKKRRQRRRPPQDSQTHQVSLPKQPSSQQRGDPTGPKESKKKVERETETDPDN | Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1.
Sequence Mass (Da): 11508
Sequence Length: 101
Domain: The cell attachment site mediates the interaction with ITGAV/ITGB3 and ITGA5/ITGB1 integrins, leading to vascular cell migration and invasion. This interaction also provides endothelial cells with the adhesion signal they require to grow in response to mitogens.
Subcellular Location: Host nucleus
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P86234 | AVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRLSVDYGKKNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKLDHKFDLMYAK | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 22006
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P09734 | MREVISINVGQAGCQIGNACWELYSLEHGIKEDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRTGRFKELFHPEQLINGKEDAANNYARGHYTVGREIVDEVEERIRKMADQCDGLQGFLFTHSLGGGTGSGLGSLLLENLSYEYGKKSKLEFAVYPAPQLSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDICKRNLGISRPSFSNLNGLIAQVISSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYAPILSKKRATHESNSVSEITNACFEPGNQMVKCDPTKGKYMANCLLYRGDVVTRDVQRAVEQVKNKKTVQMVDWCPTGFKIGICYEPPSVIPSSELANVDRAVCMLSNTTAIADAWKRIDQKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGADSYAEEF | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49694
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P68366 | MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group . Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold . Glutamylation is also involved in cilia motility (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49924
Sequence Length: 448
Domain: The MREC motif may be critical for tubulin autoregulation.
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q9H853 | MRHQQTERQDPSQPLSRQHGTYRQIFHPEQLITGKEDAANNYAWGHYTIGKEFIDLLLDRIRKLADQCTGLQGFLVFHSLGRGTGSDVTSFLMEWLSVNYGKKSKLGFSIYPAPQVSTAMVQPYNSILTTHTTLEHSDCAFMVDNKAIYDICHCNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVSYLTSTSPWPPMHQSSLQKRYTTSSCWWQRLPMPALSLPTRW | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Glutamylation is also involved in cilia motility (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 27551
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P09643 | ADACSGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICCRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISSERAYHEQLSVAEITSSCFEPNNQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRNIQFVDWCPTGVKVGINYQPPTVVPGGDLAQVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVSEGMEEGEFAEAREDLAALEKDYEEVGTDSFEDENDEE | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 35936
Sequence Length: 322
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P06606 | MREVVSIQIGQCGIQIGNACWELYLLEHGINLDGSLKTKEELTASGSSASVGHDTSANDARTFFTETGNGKQVPRSIFVDLEPTVIDDVRNGCMRELYHPEQLISGKEDAANNYARGRYSIGKEVIDRVTSRLQKIAEQCDSLQGFLIFHSLGGGTGSGFTSLLVERLSTDYSKKCKLDFAVYPSPKVSTAVVEPYNALLTTHSTMDHSDCVFMVDNEAIYDICNNSLGVDRPAYRNLNRLIAQIVSSTTASLRFSGSMNVDLNEFQTNLVPFPRIHFPLVAYAPLMSAERSAHEQHAITTLTNACFESSNMMVKCDPRAGKFMACCMLYRGDVVPKDVNAAVSAIKSKRHIQFVDWCPTGFKIGINYEKPAFVPDGDLAKTSRACCMLSNTTAISVAFSNLSYKFDLMFKKRAFVHWYVGEGMEEGEFTEARENIAVLERDFEEVGLDNAEEGGDEDFDEF | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 51181
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P33626 | MRECISIHIGQAGIQVGNACWELYCLEHGIQADGQMPGDKTIGGGDAEFDEGEDGDEGDEY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 6532
Sequence Length: 61
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q02245 | MREIISIHIGQAGIQVGNACWELYCLEHGIEHDGTMPSDSSVGVAHDAFNTFFSETGSGKHVPRAIFVDLEPTVIDEVRTGSYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVPEITNAVFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTVQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGADDEGDEGDDY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49625
Sequence Length: 450
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q8IZP1 | MDVVEVAGSWWAQEREDIIMKYEKGHRAGLPEDKGPKPFRSYNNNVDHLGIVHETELPPLTAREAKQIRREISRKSKWVDMLGDWEKYKSSRKLIDRAYKGMPMNIRGPMWSVLLNTEEMKLKNPGRYQIMKEKGKRSSEHIQRIDRDVSGTLRKHIFFRDRYGTKQRELLHILLAYEEYNPEVGYCRDLSHIAALFLLYLPEEDAFWALVQLLASERHSLQGFHSPNGGTVQGLQDQQEHVVATSQPKTMGHQDKKDLCGQCSPLGCLIRILIDGISLGLTLRLWDVYLVEGEQALMPITRIAFKVQQKRLTKTSRCGPWARFCNRFVDTWARDEDTVLKHLRASMKKLTRKKGDLPPPAKPEQGSSASRPVPASRGGKTLCKGDRQAPPGPPARFPRPIWSASPPRAPRSSTPCPGGAVREDTYPVGTQGVPSPALAQGGPQGSWRFLQWNSMPRLPTDLDVEGPWFRHYDFRQSCWVRAISQEDQLAPCWQAEHPAERVRSAFAAPSTDSDQGTPFRARDEQQCAPTSGPCLCGLHLESSQFPPGF | Function: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11.
PTM: Ubiquitinated by a CUL7-based E3 ligase, which leads to proteasomal degradation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 62187
Sequence Length: 549
Subcellular Location: Cell membrane
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Q9SEZ9 | MKQTDGRERKAYLSLLYFAVILLPVFLLGCYLYNEKQLRVGQFQEFNTHNLQEHITPLQQSKEDKDKKTDLVPLEFCDVFTGKWVLDNVTHPLYKEDECEFLSEWVACTRNGRPDSKYQKWRWQPQDCSLPRFDSKLLLEKLRGKKLMFIGDSIHYNQWQSMVCMVQSVIPSGKKTLKHTAQMSIFNIEEYNATISFYWAPFLVESNADPPDKRDGKTDPVIIPNSISKHGENWKDADYLIFNTYIWWTRHSTIKVLKQESFNKGDSKEYNEIGIYIVYKQVLSTWTKWLEQNINPSQTSIFFSSMSPTHIRSSDWGFNEGSKCEKETEPILNMSKPINVGTNRRLYEIALNATKSTKVPIHFLNITTMSEYRKDGHTSFYGSINGKLMTPEQKLDPRTFADCYHWCLPGLPDSWNELLSLYIIYKI | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50013
Sequence Length: 427
Subcellular Location: Membrane
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Q1PFD9 | MSIQTTADSRMIQSIFQVVLVSLLVLGSVRWILDELKSKESRISKLYGFRQKEAVFVTKEDQLDESCNVFEGQWVWDNVSYPLYTEKSCPYLVKQTTCQRNGRPDSYYQNWRWKPSSCDLPRFNALKLLDVLRNKRLMFIGDSVQRSTFESMVCMVQSVIPEKKKSFHRIPPMKIFKAEEYNASIEYYWAPFIVESISDHATNHTVHKRLVKLDAIEKHSKSWEGVDVLVFESYVWWMHQPKINATYGDTSEVREYNVTTAYKMALETWAKWFKTKINSEKQKVFFTSMSPTHLWSWEWNPGSDGTCYDELYPIDKRSYWGTGSNQEIMKIVGDVLSRVGENVTFLNITQLSEYRKDGHTTVYGERRGKLLTKEQRADPKNYGDCIHWCLPGVPDTWNEILYAYLLRSHRNFF | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48589
Sequence Length: 413
Subcellular Location: Membrane
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Q9SRL3 | MTTALFSPSNRRKRRLTHFFFTVLAFILLAAFIYGHDFISFSRRSLHSPTIVHQSAIVVVVDEPPPPPPTSPPPPSPPPPSPPPPSPPPPSPPPPAFAVGKTPEGCDVFKGNWVKDWSTRPLYRESECPYIQPQLTCRTHGRPDSDYQSWRWRPDSCSLPSFNATVMLESLRGKKMMFVGDSLNRGMYVSLICLLHSQIPENSKSMDTFGSLTVFSLKDYNATIEFYWAPFLLESNSDNATVHRVSDRIVRKGSINKHGRHWRGADIVVFNTYLWWRTGFKMKILEGSFKDEKKRIVEMESEDAYRMALKTMVKWVKKNMDPLKTRVFFATMSPTHYKGEDWGGEQGKNCYNQTTPIQDMNHWPSDCSKTLMKVIGEELDQRAEFPVTVLNITQLSGYRKDAHTSIYKKQWSPLTKEQLANPASYSDCIHWCLPGLQDTWNELFFAKLFYP | Function: Probable xylan acetyltransferase that plays a role in xylan acetylation and normal deposition of secondary cell walls . Required for 2-O-monoacetylation, 3-O-monoacetylation and 2,3-O-diacetylation of xylosyl residues in xylan . Required for the formation of 3-O-acetylated, 2-O-glucoronic acid-substituted xylosyl residues . May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51708
Sequence Length: 451
Subcellular Location: Golgi apparatus membrane
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F4IH21 | MKPSSPISLTSSSIARKARFSPYLFTLLAFILFVSVLYGEDFMCIFGQLEPNFVLPPSRTPEKNKKSEKLAFAIGKTEESCDVFSGKWVRDEVSRPLYEEWECPYIQPQLTCQEHGRPDKDYQFWRWQPNHCDLPSFNASLMLETLRGKRMMYVGDSLNRGMFVSMICLLHRLIPEDQKSIKTNGSLTVFTAKEYNATIEFYWAPFLLESNSDDAIVHRISDRVVRKGSINKHGRHWKGVDIIIFNTYLWWMTGLKMNILQGSFDDKEKNIVEVSTEDAYRMGMKSMLRWVKNNMDRKKTRVFFTSMSPTHAKGIDWGGEPGQNCYNQTTLIEDPSYWGSDCRKSIMKVIGEVFGRSKTPITLLNITQMSNYRKDAHTSIYKKQWSPLTAEQLENPTSYADCVHWCLPGLQDTWNELLFAKLFYT | Function: Probable xylan acetyltransferase that plays a role in xylan acetylation and normal deposition of secondary cell walls . Required for 2-O-monoacetylation, 3-O-monoacetylation and 2,3-O-diacetylation of xylosyl residues in xylan . Required for the formation of 3-O-acetylated, 2-O-glucoronic acid-substituted xylosyl residues . May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49319
Sequence Length: 425
Subcellular Location: Golgi apparatus membrane
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O80919 | MAKRQLLMLGIRTSFHTIAAVLVAGLIFTAVFLSRNSLPKENPQSHGVTDRGGDSGRECNLFEGKWVFDNVSYPLYKEEDCKFMSDQLACEKFGRKDLSYKFWRWQPHTCDLPRFNGTKLLERLRNKRMVYVGDSLNRGQWVSMVCMVSSVITNPKAMYMHNNGSNLITFKALEYNATIDYYWAPLLVESNSDDPTNHRFPDRIVRIQSIEKHARHWTNSDIIVFNSYLWWRMPHIKSLWGSFEKLDGIYKEVEMVRVYEMALQTLSQWLEVHVNPNITKLFFMSMSPTHERAEEWGGILNQNCYGEASLIDKEGYTGRGSDPKMMRVLENVLDGLKNRGLNMQMINITQLSEYRKEGHPSIYRKQWGTVKENEISNPSSNADCIHWCLPGVPDVWNELLYAYILDHHSS | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47657
Sequence Length: 410
Subcellular Location: Golgi apparatus membrane
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Q8RXQ1 | MSQRWSRKKSRLPLAGLLFILVVTFMILFNERSIQQIHHHAASHTQNLREPSTFDFVKPNVPRINYLGAHEVLDRFSKCNSTKEYSGKKIGWVDPFEDHPGQVTKEEQKCDVFSGKWVFDNSSSYPLHKESQCPYMSDQLACQKHGRKDLEYQHWRWQPHACNLKRWNAIEMWEKLRGKRLMFVGDSLNRGQWISMVCLLQSVIPRDKQSMSPNAHLTIFRAEDYNATVEFLWAPLLVESNSDDPVNHRLSERIIRPDSVLKHASKWQHADILIFNTYLWWRQDSVKLRWSSEEKGSCEEVKSAEGMEMAMDSWGDWVANNVDPNKKRVFFVTMSPTHQWSREWNPGSEGNCYGEKKPIEEESYWGSGSDIPTMRMVKRVLERLGPKVSVINITQLSEYRKDGHPSVYRKFWEPLNEDRLKNPASYSDCTHWCVPGVPDVWNQLLFHFL | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52689
Sequence Length: 449
Subcellular Location: Membrane
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Q940H3 | MATSETRVLFLSLCLILGKVVLSQFDELWLVGDDDPLNALQTRRERREERCDYSVGKWTFDETYPLYDSSCPYLSSALSCQRNGRPDSYYQKWRWIPKACSLPRFDALKFLGKMRGKRIMLVGDSMMRNQWESLVCLVQSVLPTHRKKLTYNGPTMSFHSLDFETSIEFCWAPLLVELKRGVDRKRVLHLDSIEDNARYWRGVDVLVFDSAHWWTHSQRWSSWDYYMDGNKIFKAMDPMVAYERGLTTWAKWVEINLDPSKTKVIFRTVSPRESGQMCYNQKHPLPSLSSSTKPHVPQQSRVLNKVLRTMKYRVYLYDITTMSAYRRDGHPSVFKRAMHEEEKHHRIAGPSSDCSHWCLPGVPDIWNEMLSSIILTNAV | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44371
Sequence Length: 379
Subcellular Location: Membrane
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O22960 | MGFKLNSLFLLLSLLILTILSGADQALAYVKKPHVSQRNKTALAAVAGRGGGKEMLKGRKQTSGCNLFQGRWVFDASYPFYDSSTCPFIDGEFDCLKFGRPDKQFLKYSWQPDSCTVPRFDGEAFLKKWRGKRVMFVGDSLSLNMWESLACMIHSSVPNTKTTFLKRTPLSSLTFQEYDVTLFLYRTPYLVDISKESVGRVLNLGAIEDGADAWKNMDLLVFNSWHWWTHTGVQSQGWDFIRDGSSLMRDMDRLDAFNKGLTTWGQWVDQNVNVSQTRVFFQGISPTHYMGREWNEPRKTCNGQMQPLTGSTYPGGSLPAASIVSRVLSTMRTPVYLLDITTLSQLRKDAHPSTYGGDGGTDCSHWCLPGLPDTWNQLLYAALSM | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43354
Sequence Length: 385
Subcellular Location: Membrane
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Q9SIN2 | MGFTSRGNPSFLFFFFFFLCLSTVSAYINSTSSNNDEVRRELASGRCNWFRGNWVYDVKYPLYDPYKCPFIDPQFNCKKYGRPDNAYLKYRWQPSSCSLPRFNGLYFLRRMRGKKIMFVGDSLSTNMWQSLACLIHSWVPNTRYTLIRQKGLASLTFEEYGVTLLLYRTQFLVDLNVEKVGRVLKLDSIKQGNMWRGMDVLIFNSWHWWTHTEHIQPWDYMEDGNRLYKDMNRLVAFYKGMTTWARWVNAYVDPSKTKVFFNGVSPTHYEGKDWGEPMNSCRSQTQPFYGRKYPGGTPMAWVILNKVMRRLKKPVHWLDITGLSQLRKDAHPSAFSGNHPGNDCSHWCLPGLPDTWNLLFYSTLFSS | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43166
Sequence Length: 367
Subcellular Location: Membrane
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Q8LED3 | MSFLIPNRGVGGTKIPLSIIVLVLCGFMFFILLYTERISLLSSSSSSSSSFFKLKSCPRKDVSSKPKEKIRKERSEILEVLDDRFEFDPEECNVAAGKWVYNSSIEPLYTDRSCPYIDRQFSCMKNGQPETDYLRWEWQPDDCTIPRFSPKLAMNKLRGKRLLFVGDSLQRSQWESFVCLVESIIPEGEKSMKRSQKYFVFKAKEYNATIEFYWAPYIVESNTDIPVISDPKKRIVKVDSVKDRAKFWEGADILVFNTYVWWMSGLRMKALWGSFGNGESGAEALDTQVAYRLGLKTWANWVDSTVDPNKTRVFFTTMSPTHTRSADWGKPNGTKCFNETKPIKDKKFWGTGSNKQMMKVVSSVIKHMTTHVTVINITQLSEYRIDAHTSVYTETGGKILTAEQRADPMHHADCIHWCLPGLPDTWNRILLAHL | Function: Involved in secondary cell wall cellulose deposition. Required for normal stem development . May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49829
Sequence Length: 434
Subcellular Location: Golgi apparatus membrane
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Q67XC4 | MGLCFQLNLASLSLILFSSFPGLLAQSQQHFLGQNNTSLLSGGRCNLARGKWVYDSSYPLYSAFSCPFIDSEFNCQKAGRPDTNYQHFRWQPFSCPLPRFDGANFMRRMRGKKIMMVGDSLSLNMFESLACLLHASLPNAKYSLRRSQPLTSLTFQDYGVTINLYRTQFLVDVVQEKAGRVLVLDSIKQADAWLGMDVLIFNSWHWWTHTSGLQPWDYMREGNQLYKDMNRLVAYYKGLNTWARWINNNIVPSRTQVFFQGVSPVHYDGREWNEPLKSCNGQTQPFMGQRYPGGLPLGWVVVNKVLSRIRKPVHLLDLTTLSEYRKDAHPSLYNGISKDLDCSHWCLPGLPDTWNLLLYSSLTS | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41768
Sequence Length: 364
Subcellular Location: Membrane
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F4IWA8 | MGSKDNAISNDSALVLSLLLLLLLPLLHEAAEGCDMFTGRWVKDDSYPLYNSSTCPFIRHEFSCQRNGRPDLDYSTFRWQPLSCKLARFNGLQFLKKNKGKKIMFVGDSLSLNQWQSLACMLHSSVPNSTYTLTTQGSISTYTFKEYGLELKLDRNVYLVDIVREKIGRVLKLDSINDGKNWVEMDTLIFNTWHWWSRRGPAQPWDLIQIGTNVTKDMDRVAAFEIALGTWGKWVDTVLNTKKTRVFFQGISPSHYKGVLWGEPAAKSCVGQKEPLLGTKYPGGLPAEVGVLKRALGKISKPVTLLDITMLSLLRKDAHPSVYGLGGRNSSGDCSHWCLSGVPDTWNEILYNYMVE | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40111
Sequence Length: 356
Subcellular Location: Membrane
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Q9ZV89 | MNFHQVLFLLLLIFLVDLSDYGVLADKTNDGYKNATKCNIYQGRWIYDNSSNPLYGTSTCPFIGLDCQKFGRPDKNYLHYRWQPTGCDIPRFNGRDFLTRFKGKKILFVGDSLSNNMWVSLSCMLHAAVPNAKYTFQLNKGLSTFTIPEYGISVNFLKNGFLVDLVSDKTRGLILKLDSISRGNQWLGSDVAIFNTFHWWSHTGRAKTWDYFQTGDKIVKEMNRMEAFKIALTTWSKWIDHNIDPSKTRVFYQGVSPVHLNGGEWGKPGKTCLGETVPVQGPSYPGRPNEGEAIVKSVIGRMAKPVELLDVTAMTEMRKDGHPSIYAGGGDRLNDCSHWCLPGVPDAWNQLLYTALLSH | Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40568
Sequence Length: 359
Subcellular Location: Membrane
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Q9JKD8 | MGIVEPGCGDMLTGTEPMPSDEGRGPGADQQHRFFYPEPGAQDPTDRRAGSSLGTPYSGGALVPAAPGRFLGSFAYPPRAQVAGFPGPGEFFPPPAGAEGYPPVDGYPAPDPRAGLYPGPREDYALPAGLEVSGKLRVALSNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACSASNTHVFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYASVDTSVPSPPGPNCQLLGGDPFSPLLSNQYPVPSRFYPDLPGQPKDMISQPYWLGTPREHSYEAEFRAVSMKPTLLPSAPGPTVPYYRGQDVLAPGAGWPVAPQYPPKMSPAGWFRPMRTLPMDPGLGSSEEQGSSPSLWPEVTSLQPEPSDSGLGEGDTKRRRISPYPSSGDSSSPAGAPSPFDKETEGQFYNYFPN | Function: Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs. Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN-gamma and the chemokine receptor CXCR3. Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation . Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells . Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC . Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2 . Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN- stimulated genes . Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program .
PTM: Phosphorylations at Ser-52, Tyr-76, Ser-224 and Ser-508 are regulated by mTORC1 . Phosphorylation at Tyr-525 is essential for its interaction GATA3 . Phosphorylation at Tyr-219, Tyr-265 and Tyr-304 enhances its transcriptional activator activity . Phosphorylation at Thr-302 is required for its interaction with NFATC2 .
Sequence Mass (Da): 57852
Sequence Length: 530
Subcellular Location: Nucleus
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Q9IBC8 | MRDPAFPGAAMAYHPFHAPRAADFPMSAFLAAAQPSFFPALTLPPAALGKPLSDASLAGAAEAGLHLSALGHHHQAAHLRSLKSLEPEEEVEDDPKVNLEAKELWDQFHKIGTEMVITKSGRRMFPPFKVRVSGLDKKAKYILLMDIVAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMAKPVAFHKLKLTNNISDKHGFTILNSMHKYQPRFHIVRANDILKLPYSTFRTYVFPETDFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLSLPSLRMYEEQCKADRDGAESDASSCDPAPGRDSLHSPLSAEPSPLRLHRNNREEKFGADSDQELDRREIRSARSHSPVGHRSPPSSPRLEDRGKDKSTPEKKSDSPESRKDGSDSLFSSIRSLEKDKAESRRKEDSKSDPECGSLSKETFAPLMVQTDSPPHLSASHLQSLALSGLHGQQFFNPLNAGQPLFIHPGQFTMGPGAFSAMGMGHLLASMTGAGALDNGSLSSVQGATGAANPFPFHFSQHMLASQGIPMPAFGGLFPYPYTYMAAAAAAASAMPATSAATTMPRNPFLSSTRPRLRFNPYQIPVGIPPSTNLLTTGLPGSLNPGSESSKPGSSRESSPIPDTPVPKRSHSNSLSPKASMKDSINELQNIQRLVSGLESQREISPGRETPK | Function: Transcription factor which acts as a transcriptional repressor (By similarity). May also function as a transcriptional activator (By similarity). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (By similarity).
Sequence Mass (Da): 75225
Sequence Length: 688
Domain: Repression domain 1 (RD1) is involved in transcriptional repression.
Subcellular Location: Nucleus
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Q19691 | MAFNPFALGRPDLLLPFMGAGVGGPGAGGPPPNLFFSMLQAGFPPGPVGSPPEDDGVTDDPKVELDERELWQQFSQCGTEMVITKSGRRIFPAYRVKISGLDKKSQYFVMMDLVPADEHRYKFNNSRWMIAGKADPEMPKTLYIHPDSPSTGEHWMSKGANFHKLKLTNNISDKHGYTILNSMHKYQPRLHVVRCADRHNLMYSTFRTFVFRETEFIAVTAYQNEKVTELKIENNPFAKGFRDAGAGKREKKRQLHRMNGDATQSPPGKTASLPTHSPHPSESNSEDDEPTLKKCKPEPSQTPTTSSLSTSTTPTLSAHHPLRSPQFCIPPPIDMMYQNMPMDLLAHWQMATLFPQFSMALNSPAAAASLLSKHLAKASSECKVEATSEDSEEAEKPEVKKEQKSVTPPKKGGFDVLDLLSKP | Function: Involved in the transcriptional regulation of genes required for the development of pharyngeal muscles derived from the ABa lineage . Acts as a transcriptional repressor and binds to T-box binding sites in its own promoter to negatively autoregulate its own expression in neurons, seam cells and the gut in order to restrict its expression to certain tissues . May function together with the nfya-1-NF-Y complex to repress its own expression . Plays a role in neural fate specification in the hermaphrodite-specific neuron (HSN)/PHB neuron lineage, acting in concert with homeobox protein egl-5 and the asymmetric cell division protein ham-1.
PTM: Sumoylated.
Sequence Mass (Da): 46997
Sequence Length: 423
Subcellular Location: Nucleus
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Q60707 | MREPALAASAMAYHPFHAPRPADFPMSAFLAAAQPSFFPALALPPGALGKPLPDPGLAGAAAAAAAAAAAAEAGLHVSALGPHPPAAHLRSLKSLEPEDEVEDDPKVTLEAKELWDQFHKLGTEMVITKSGRRMFPPFKVRVSGLDKKAKYILLMDIVAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMAKPVAFHKLKLTNNISDKHGFTILNSMHKYQPRFHIVRANDILKLPYSTFRTYVFPETDFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLPTLRLYEEHCKPERDGAESDASSCDPPPAREPPPSPSAAPSPLRLHRARAEEKPGAADSDPEPERTGEERSAAPLGRSPSRDASPARLTEPERSRERRSPERCSKEPTEGGGDGPFSLRSLEKERPEARRKDEGRKDVGEGKEPSLAPLVVQTDSASPLGAGHLPGLAFSSHLHGQQFFGPLGAGQPLFLHPGQFAMGPGAFSAMGMGHLLASVAGGSGSSGGAGPGTAAGLDAGGLGPAASAASTAAPFPFHLSQHMLASQGIPMPTFGGLFPYPYTYMAAAAAAASALPATSAAAAAAAAAGSLSRSPFLGSARPRLRFSPYQIPVTIPPSTSLLTTGLAAEGSKGGNSREPSPLPELALRKVGGPSRGALSPSGSAKEAASELQSIQRLVSGLESQRALSPGRESPK | Function: Transcription factor which acts as a transcriptional repressor . May also function as a transcriptional activator . Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes . Required for cardiac atrioventricular canal formation . May cooperate with NKX2.5 to negatively modulate expression of NPPA/ANF in the atrioventricular canal . May play a role as a positive regulator of TGFB2 expression, perhaps acting in concert with GATA4 in the developing outflow tract myocardium . Plays a role in limb pattern formation . Acts as a transcriptional repressor of ADAM10 gene expression, perhaps in concert with histone deacetylase HDAC1 as cofactor . Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX3 . Required, together with TBX3, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling . Involved in modulating early inner ear development, acting independently of, and also redundantly with TBX3, in different subregions of the developing ear . Acts as a negative regulator of PML function in cellular senescence (By similarity). Acts as a negative regulator of expression of CDKN1A/p21, IL33 and CCN4; repression of CDKN1A is enhanced in response to UV-induced stress, perhaps as a result of phosphorylation by p38 MAPK . Negatively modulates expression of CDKN2A/p19ARF and CDH1/E-cadherin (By similarity). Plays a role in induction of the epithelial-mesenchymal transition (EMT) (By similarity). Plays a role in melanocyte proliferation, perhaps via regulation of cyclin CCND1 . Involved in melanogenesis, acting via negative modulation of expression of DHICA oxidase/TYRP1 and P protein/OCA2 . Involved in regulating retinal pigment epithelium (RPE) cell proliferation, perhaps via negatively modulating transcription of the transcription factor CEBPD .
PTM: Phosphorylated . May be phosphorylated by p38 MAPK in response to UV irradiation stress .
Sequence Mass (Da): 75081
Sequence Length: 711
Domain: Repression domain 1 (RD1) is involved in transcriptional repression (By similarity). RD1 is necessary for its interaction with PML (By similarity).
Subcellular Location: Nucleus
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O74428 | MERPSLSRRTSSSTVSTDGEGVYSRSTKERKRNFIVNSRLKRGGGHVRVNRSGRLGSVTMRPSALTRAHSQNPNSSLVNNSSAVSHLTKQRSLNDLHELNGPKHVAKNGLIPLTQRKPNCVWDDAPVDNDSTAGNLDSDSALPTPSVTTNEAADSSRASSPVTRVVAVHDNKKKIINSNISNAPPFNNTDVQASARPPAAGQDDSAADASTTKSSPVHNEVMAEPLPHSNNREVTQATNQPKWQIHSGSDIASEPPTLSRGNSLSLLANRKVPSTNVKKSQAELYDLGSSTSRTQQKLLIQRASSKFDIVEDDMDTNPSKRFSNPHTKHIMDLVRTQYRNVLRTRELIPEFLEKIRSSYSNNQNFDSQNAFNTSAAGTAGTREETISNGQNGIVASAETSKKDDGVQSASLNASMSARSHARQRSIHVPKTRKDTDYESIHQKLLQLWSQG | Function: Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Tor2 is essential for growth. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2.
PTM: Either Thr-10, Ser-11, Ser-12, Ser-13 or Thr-14 and Ser-214 or Ser-215 and Ser-247 or Ser-249 are phosphorylated as well.
Sequence Mass (Da): 49212
Sequence Length: 451
Subcellular Location: Cytoplasm
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Q08921 | MVHRGRTLKSDTDVTSLNASTVSHQSKPFRQFSTRSRAKSNASFKGLRRVLTHDGTLDNDYFNKHNVSQKCKSSDALFRKRTISGLNMTALTRVKSNQGKRSASFHSPVHNTLLSPKNSSHSNTGTAGFGLKPRRSKSTQSVLSLRDAQESKKSESTTDEEVECFSEDNIEDGKVNNDKVIAEHVMPEEKKNVQQLNQNELQSPDSIDEQEEDKSGTDGKENHRAVSLPLPHLSSNNYFGESSHSIEHQKDGETSPSSIETKLNATSVINEEGQSKVTKEADIDDLSSHSQNLRASLVKAGDNISEAPYDKEKKILDVGNTLAAHKSNQKPSHSDEQFDQEDHIDAPRSNSSRKSDSSFMSLRRQSSKQHKLLNEEEDLIKPDDISSAGTKDIEGHSLLENYAPNMILSQSTGVERRFENSSSIQNSLGNEIHDSGEHMASGDTFNELDDGKLRKSKKNGGRSQLGQNIPNSQSTFPTIANIGSKDNNVPQHNFSTSISSLTNNLRRAAPESFHGSRMNNIFHKKGNQNLLLRSNDLNKNSAAPASPLSNEHITSSTNSGSDANRQSNSGAKFNSFAQFLKSDGIDAESRTQRKLWLQRENSIMDLSSQNDGSDSIFMAGNIDAKREFERISHEYSNVKRFYNPLDEALLRVQPIITGNANNIRKKSHNDAQSIAHSSSDTDHKDEDDLLFTNYDKKFDDLYPHLASAKIQAVLSGIWKSESYLFNKDVNPINKNRTTSTNHSVGHTASQNARNLLRGPMGSSTTLHHQRVINSLQPTTRAVNRRMENVGYMHTQPQQR | Function: Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 88845
Sequence Length: 799
Subcellular Location: Cell membrane
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Q8WWU5 | MPDVKESVPPKYPGDSEGRSCKPETSGPPQEDKSGSEDPPPFLSVTGLTETVNEVSKLSNKIGMNCDYYMEEKVLPPSSLEGKVKETVHNAFWDHLKEQLSATPPDFSCALELLKEIKEILLSLLLPRQNRLRIEIEEALDMDLLKQEAEHGALKVLYLSKYVLNMMALLCAPVRDEAVQKLENITDPVWLLRGIFQVLGRMKMDMVNYTIQSLQPHLQEHSIQYERAKFQELLNKQPSLLNHTTKWLTQAAGDLTMSPPTCPDTSDSSSVAGPSPNEAANNPEPLSPTMVLCQGFLNLLLWDLENEEFPETLLMDRTRLQELKSQLHQLTVMASVLLVASSFSGSVLFGSPQFVDKLKRITKSLLEDFHSRPEEAILTVSEQVSQEIHQSLKNMGLVALSSDNTASLMGQLQNIAKKENCVCSVIDQRIHLFLKCCLVLGVQRSLLDLPGGLTLIEAELAELGQKFVNLTHHNQQVFGPYYTEILKTLISPAQALETKVESV | Function: Plays a role in the process of sperm capacitation and acrosome reactions. Probable receptor for the putative fertilization-promoting peptide (FPP) at the sperm membrane that may modulate the activity of the adenylyl cyclase cAMP pathway.
PTM: Constitutively phosphorylated on serine, threonine and tyrosine residues within the head and tail regions of noncapacitated spermatozoa. Phosphorylation on tyrosine residues increases upon sperm capacitation within the acrosomal region in a protein kinase A (PKA)-dependent signaling pathway.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56141
Sequence Length: 503
Subcellular Location: Membrane
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Q01755 | MPDVKERAARKEPGAAESASRESRGGNTRESASSARGTDRVGSTVARARPPSPQGPRRGAVKTAPRGPVGHGGLRTGPTSRCPQPSARAKLPSVTRGAPLPPSPGKGHLGGTPSSHRLGMTERVHDASKLDCQLEERSLSSSSLKGKVKDTMPSDFWEHLNEQLSAVPPDFSCALELLKEIKEILLSLLLPRQSRLKNEIEEALDMEFLQQQADRGDLNVSYLSKYILNMMVLLCAPIRDEAVQRLENISDPVRLLRGIFQVLGQMKMDMVNYTIQSLQPQLQEHSVQFERAQFQERLNKEPRLLNHTTKWLTQAATQLIAPSASSSDLQDCSSSAGPSPSDVAVPEPLSPAMVLSQGFLNLLTWDPENEEFPETLVADRPRLQELESQQSQLTILASVLLVASSFSDSGLFSSPQFVDKLKQITKSLVEDFNSRPEEVMQSVSEQVVEEVHQGLESMGLAALSSENTASLVGQLQNIAKKENCVRSVIDQRIHLFLKCCFVLGVQRSLLDLPGGLTLIEAELAELGQKFVSLTHHNQQVFAPYYTEILKTLISPAQTLATKGGSL | Function: Plays a role in the process of sperm capacitation and acrosome reactions . Probable receptor for the putative fertilization-promoting peptide (FPP) at the sperm membrane that may modulate the activity of the adenylyl cyclase cAMP pathway .
PTM: Constitutively phosphorylated on serine, threonine and tyrosine residues within the head and tail regions of noncapacitated spermatozoa . Phosphorylation on tyrosine residues increases upon sperm capacitation within the acrosomal region in a protein kinase A (PKA)-dependent signaling pathway .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61970
Sequence Length: 566
Subcellular Location: Membrane
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Q93Z00 | MQKPTSSILNVIMDGGDSVGGGGGDDHHRHLHHHHRPTFPFQLLGKHDPDDNHQQQPSPSSSSSLFSLHQHQQLSQSQPQSQSQKSQPQTTQKELLQTQEESAVVAAKKPPLKRASTKDRHTKVDGRGRRIRMPALCAARVFQLTRELGHKSDGETIEWLLQQAEPSVIAATGTGTIPANFTSLNISLRSSGSSMSLPSHFRSAASTFSPNNIFSPAMLQQQQQQQRGGGVGFHHPHLQGRAPTSSLFPGIDNFTPTTSFLNFHNPTKQEGDQDSEELNSEKKRRIQTTSDLHQQQQQHQHDQIGGYTLQSSNSGSTATAAAAQQIPGNFWMVAAAAAAGGGGGNNNQTGGLMTASIGTGGGGGEPVWTFPSINTAAAALYRSGVSGVPSGAVSSGLHFMNFAAPMAFLTGQQQLATTSNHEINEDSNNNEGGRSDGGGDHHNTQRHHHHQQQHHHNILSGLNQYGRQVSGDSQASGSLGGGDEEDQQD | Function: Transcription factor involved the regulation of plant development. Together with TCP15, modulates plant stature by promoting cell division in young internodes. Represses cell proliferation in leaf and floral tissues . Together with TCP15, acts downstream of gibberellin (GA), and the stratification pathways that promote seed germination. Involved in the control of cell proliferation at the root apical meristem (RAM) by regulating the activity of CYCB1-1 . Involved in the regulation of seed germination. May regulate the activation of embryonic growth potential during seed germination . Acts together with SPY to promote cytokinin responses that affect leaf shape and trichome development in flowers . Transcription factor involved in the regulation of endoreduplication. Represses endoreduplication by activating the gene expression of the key cell-cycle regulators RBR1 and CYCA2-3 . Regulates the expression of the defense gene pathogenesis-related protein 2 (PR2) in antagonism to SRFR1, a negative regulator of effector-triggered immunity . Involved in positive regulation of plant defense. Represses jasmonate (JA) response to promote disease resistance. Regulates the plant immune system by transcriptionally repressing a subset of JA-responsive genes .
PTM: Ubiquitinated (Probable). Targeted for degradation by the SCF(COI1) E3 ubiquitin ligase-proteasome pathway during jasmonate signaling in response to Pseudomonas syringae infection and the secreted type III effector HopBB1 .
Sequence Mass (Da): 52300
Sequence Length: 489
Subcellular Location: Nucleus
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P51563 | MRSSAIIALLIVGLDAMGLGLIMPVLPTLLRELVPAEQVAGHYGALLSLYALMQVVFAPMLGQLSDSYGRRPVLLASLAGAAVDYTIMASAPVLWVLYIGRLVSGVTGATGAVAASTIADSTGEGSRARWFGYMGACYGAGMIAGPALGGMLGGISAHAPFIAAALLNGFAFLLACIFLKETHHSHGGTGKPVRIKPFVLLRLDDALRGLGALFAVFFIIQLIGQVPAALWVIYGEDRFQWNTATVGLSLAAFGATHAIFQAFVTGPLSSRLGERRTLLFGMAADGTGFVLLAFATQGWMVFPILLLLAAGGVGMPALQAMLSNNVSSNKQGALQGTLTSLTNLSSIAGPLGFTALYSATAGAWNGWVWIVGAILYLICLPILRRPFATSLVI | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40913
Sequence Length: 393
Subcellular Location: Cell inner membrane
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P51564 | MNKSIIIILLITVLDAIGIGLIMPVLPTLLNEFVSENSLATHYGVLLALYATMQVIFAPILGRLSDKYGRKPILLFSLLGAALDYLLMAFSTTLWMLYIGRIIAGITGATGAVCASAMSDVTPAKNRTRYFGFLGGVFGVGLIIGPMLGGLLGDISAHMPFIFAAISHSILLILSLLFFRETQKREALVANRTPENQTASNTVTVFFKKSLYFWLATYFIIQLIGQIPATIWVLFTQYRFDWNTTSIGMSLAVLGVLHIFFQAIVAGKLAQKWGEKTTIMISMSIDMMGCLLLAWIGHVWVILPALICLAAGGMGQPALQGYLSKSVDDNAQGKLQGTLVSLTNITGIIGPLLFAFIYSYSVAYWDGLLWLMGAILYAMLLITAYFHQRKTTPKAVISTP | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43672
Sequence Length: 400
Subcellular Location: Cell inner membrane
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O07776 | MADETTMRAGRGPGRACGRVSGVRILVVEDEPKMTALLARALTEEGHTVDTVADGRHAVAAVDGGDYDAVVLDVMLPGIDGFEVCARLRRQRVWTPVLMLTARGAVTDRIAGLDGGADDYLTKPFNLDELFARLRALSRRGPIPRPPTLEAGDLRLDPSEHRVWRADTEIRLSHKEFTLLEALIRRPGIVHTRAQLLERCWDAAYEARSNIVDVYIRYLRDKIDRPFGVTSLETIRGAGYRLRKDGGRHALPR | Function: Member of the three-protein two-component system HK1/HK2/TcrA.
PTM: Phosphorylated by HK2.
Sequence Mass (Da): 28170
Sequence Length: 253
Subcellular Location: Cytoplasm
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P23054 | MNTSYSQSTLRHNQVLIWLCVLSFFSVLNEMVLNVSLPDIANEFNKLPASANWVNTAFMLTFSIGTALYGKLSDQLGIKNLLLFGIMVNGLGSIIGFVGHSFFPILILARFIQGIGAAAFPALVMVVVARYIPKENRGKAFGLIGSLVAMGEGVGPAIGGMVAHYIHWSYLLLIPTATIITVPFLIKLLKKEERIRGHIDMAGIILMSAGIVFFMLFTTSYRFSFLIISILAFFIFVQHIRKAQDPFVDPELGKNVFFVIGTLCGGLIFGTVAGFVSMVPYMMKDVHHLSTAAIGSGIIFPGTMSVIIFGYIGGLLVDRKGSLYVLTIGSALLSSGFLIAAFFIDAAPWIMTIIVIFVFGGLSFTKTVISTVVSSSLKEKEAGAGMSLLNFTSFLSEGTGIAIVGGLLSIGFLDHRLLPIDVDHSTYLYSNMLILFAGIIVICWLVILNVYKRSRRHG | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49756
Sequence Length: 458
Subcellular Location: Cell membrane
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O69730 | MRRADGQPVTVLVVDDEPVLAEMVSMALRYEGWNITTAGDGSSAIAAARRQRPDVVVLDVMLPDMSGLDVLHKLRSENPGLPVLLLTAKDAVEDRIAGLTAGGDDYVTKPFSIEEVVLRLRALLRRTGVTTVDSGAQLVVGDLVLDEDSHEVMRAGEPVSLTSTEFELLRFMMHNSKRVLSKAQILDRVWSYDFGGRSNIVELYISYLRKKIDNGREPMIHTLRGAGYVLKPAR | Function: Member of the two-component regulatory system TcrY/TcrX.
PTM: Phosphorylated by TcrY.
Sequence Mass (Da): 25844
Sequence Length: 234
Subcellular Location: Cytoplasm
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O69729 | MGITAATEMALRRHLVAQLDNQLGGTSYRSVLMYPEKMPRPPWRHETHNYIRSGPGPRFLDAPGQPAGMVAAVVSDGTTVAAGYLTGSGSRAALTSTGRSQLERIAGSRTPLTLDLDGLGRYRVLAAPSRNGHDVIVTGLSMGNVDATMLQMLIIFGIVTVIALVAATTAGIVIIKRALAPLRRVAQTASEVVDLPLDRGEVKLPVRVPEPDANPSTEVGQLGSALNRMLDHIAAALSARQASETCVRQFVADASHELRTPLAAIRGYTELTQRIGDDPEAVAHAMSRVASETERITRLVEDLLLLARLDSGRPLERGPVDMSRLAVDAVSDAHVAGPDHQWALDLPPEPVVIPGDAARLHQVVTNLLANARVHTGPGTIVTTRLSTGPTHVVLQVIDNGPGIPAALQSEVFERFARGDTSRSRQAGSTGLGLAIVSAVVKAHNGTITVSSSPGYTEFAVRLPLDGWQPLESSPR | Function: Member of the two-component regulatory system TcrY/TcrX. Activates TcrX by phosphorylation.
PTM: Autophosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 50344
Sequence Length: 475
Subcellular Location: Cell membrane
EC: 2.7.13.3
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A1JIM8 | MHIDNAITTTIETKTWRKSDTTWTLGLFGTAIGAGVLFFPIRAGFGGLIPILIMLVLAYPIAFLCHRALARLCLSGSNCSGNITETVEEHFGKTGGVVITFLYFFAICPLLWIYGVTITNTFMTFWENQLQLAPLNRGVVALALLLLMAVVIYFGKDLMVKVMSFLVFPFIACLVLISLSLIPYWNASVIEQVDLSQISLLGHDGILVTVWLGISIMVFSFNFSPIVSSFVVSKREEYEPEFGREYTEKKCSQIISRASILMVAVVMFFAFSCLFTLSPQNMAEAKAQNIPVLSYLANHFSSMAGSRSTFSITLEYAASLIALVAIFKSFFGHYLGTLEGLNGLVIKFGYKGDKTKISSGKLNLISMFFIMGSTWLVAYINPNILDLIEAMGAPIIASLLCLLPMYAIHKLPSLARFRGRPENYFVTIVGLLTIFNIVYKLL | Function: Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system).
Catalytic Activity: H(+)(in) + L-threonine(in) = H(+)(out) + L-threonine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48950
Sequence Length: 442
Subcellular Location: Cell inner membrane
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