wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized esterase/lipase C417.12 (EC 3.1.-.-) (O94493)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Enhancer of rudimentary homolog 1
Sequence:
MYESPIILGSKPCTLNIPGMGVLHGLTVLDENGKEKCHRFTGIRYAKPPVGKLRWRRPVTLEDGYDYSGDYNQFKTICPQPFYNNRKNQVRNPDFKYDEDCLFLNIWVPAGEKPAEGWPVLYFIHGGWLQVGNPLHYRQCDPQDLQADGSPAKFILVSPGHRLNLFGFLAGKELLEEDPKSSNFGFWDQRLGLEWTYKHIESFGGNKENIAVGGISAGSYSALFQLIYETYHPEANQIIKRALLLSNGLSVQPKSVEESQIQFNELAQKFGIPLELSSAEKLEKLRAIPFQDLADNILNLRLHTFRAVTDGDFVNPNTFKDIYDGTFGKRIRDSGRELIIGEVNNEHSIYANTNPPKSKEDLFNQVNNYYPEKVTKALLELYPKVPDMEDEKEYLAAIKALFGSIVSDMQVYASTRVLINGLVKGGVPLEKIYRYRIAFRGKFFDKYEPPESLVPHAGDLGLWFYNVVDGILPEEIPIYKAWLKSYGEWMSTGKTDWGTTKTEEYRLLDADGTIKVVDDEKWDWGLKVGRTVAGVFGLN
Protein: P-type Cu(+) transporter (EC 7.2.2.8) (G5ED40)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
Sequence:
MAEKPKIRRAIVSIEGMTCHACVNNIQDTVGSKDGIVKIVVSLEQKQGTVDYNSEKWNGESVAESIDDMGFDCKLITDQEIAAVEPQKASTTKLSISPLKTVDLSDGKVELQLNGVKYSKEGSSDHLEKCTFAVEGMTCASCVQYIERNISKIEGVHSIVVALIAAKAEVIYDGRVTSSDAIREHMTGELGYKATLLDSMGANPNYSKIRLIIGNLSTESDANRIESHVLSKSGIDSCNVSIATSMALVEFSPQVIGPRDIINVVESLGFTADLATRDDQMKRLDHSDDVKKWRNTFFIALIFGVPVMIIMIIFHWILRTPMHPDKQTPIFTPALSLDNFLLLCLCTPVQIFGGRYFYVASWKAIKHGNANMDVLIMLSTTIAYTYSIVVLLLAIIFKWPSSPMTFFDVPPMLIVFIALGRMLEHKAKGKTSEALSKLMSLQAKEATLVTMDSEGRLTSEKGINIELVQRNDLIKVVPGAKVPVDGVVVDGKSSVDESFITGESMPVVKKPGSTVIGGSVNQKGVLIVKATHVGNDSTLSQIVRLVEEAQTNRAPIQQLADKIAGYFVPFVIVLSLFTLGVWIYIEYNSARNANLPPGLRFEEALKIAFEAAITVLAIACPCSLGLATPTAVMVGTGVGAANGILIKGGEPLESVHKVTTIVFDKTGTITEGRPRVVQIASFVNPSTMSLKLITFLSGATEALSEHPIGNAVAAFAKQLLNEPTWPNTSRFHVSAGHGVTCRIDSIRQSFSSLALSGSTCEIPRLPDGQTITIPGTEVNLLQVSSKEVSQPNPDTANIVIGTERMMERHGIPVSEVVKMTLSEEQRKGHISVICAINAEVVAVISIADQVKKEASLAIYTLREMGLRVVLLTGDNSKTAESTAKQVGIDEVFAEVLPNQKQQKIKQLKGYKNKVAMVGDGVNDSPALAEANVGIAIAAGSDVAIESAGIVLVRNDLVDVVGAIKLSKMTTRRIRLNFLFAIIYNAIGIPIAAGVFRPFGFMLQPWMAAAAMALSSVSVVSSSLLLKNFRKPTIANLYTTSFKRHQKFLESGSFQVQVHRGLDDSAVFRGAASSKLSILSSKVGSLLGSTTSIVSSGSSKKQRLLDNVGSDLEDLIV
Protein: Protein argonaute 7 (OsAGO7) (Protein SHOOT ORGANIZATION 2) (Protein SHOOTLESS 4) (Q75HC2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). Regulates shoot apical meristem (SAM) initiation and maintenance and leaf polarization through the trans-acting siRNAS (ta-siRNAs) pathway which probably modulates the expression of the ARF2, ARF3, ARF4, ARF14 and ARF15 genes.
Interaction partners:
- Endoribonuclease Dicer homolog 4
- Endoribonuclease Dicer homolog 1
- Endoribonuclease Dicer homolog 3b
- Endoribonuclease Dicer homolog 3a
- Endoribonuclease Dicer homolog 2a
- DNA-directed RNA polymerase subunit
- Os02g0152700 protein
- DNA-directed RNA polymerase subunit
- Endoribonuclease Dicer homolog 2b
- Os03g0121901 protein
Sequence:
MEGEREGVVAKNEDNAGGGGGGLGTGGNGGGGGGGSANGRRRWRGGGSSGYRQHPIIQAYPALLPLPINGATGHAHINGAVSLPLPLPPPVLLYLQPPPPPPLLPLLPKVAAATFYGKPPKAADAAPRGSMWKHRPSKKPPPHAITAALLPLPRDGKALQEKIFFANERKTSEKEVNHVDTHEKFTVAPLDNAIARRPDMGGVEGAEIPLSANHFLVQFDPGQKIFHYNVDISPRPSKETARMIKKKLVEENPSVLSGSQPAFDGRKNLYSPVRFQEDRVEFFVSLPVALARCSVVKEDTGHMLDKQKLKTFKVNVRLVSKLCGEDLNKYLNEDKDGIPLPQDYLHALDVVLREGAMESSILVGRSLYARSMGEARDIGGGAVGLRGFFQRLRPTKQGLALNVDLSLSAFHESTGIISYLQKRCDFLKDLPQKKTRALAEEEHREVEKALKNIRVFVCHRETNQRYHVHSLTKETTENLKFRDRSGKDLMVVDYFKEHYNHDIQFRNLPCLQIGRSKPCYVPMELCVVCEGQKFLGKLSDEQTSKILKMGCERPSERKGIIKGVVKGAFHARSDTYADQFSLQVSKHMTKLSGRVLLPPKLKLGSSGRIKDITPDRFDRQWSFLDSHVAEGSKIKSWALISFGGTPEQHFCITKFVNQLSNRCEQLGILLNKKTIISPIFERIQLLNNVGILEGKLKKIQEAASGNLQLLICVMERRHQGYADLKRIAETSIGVVTQCCLYSNLSKLTSQFLTNLALKINAKLGGCNIALYSSFPCQIPRIFLSEEPVMFMGADVTHPHPLDDSSPSVVAVVASMNWPSANKYISRMRSQTHRKEIIEQLDVMAGELLEEFLKEVGKLPSRIIFFRDGVSETQFYKVLKEEMHAVRTTCSRYPGYKPLITFIVVQKRHHTRLFHRERNGSSSHYSDQNIPPGTVVDTVITHPREFDFYLCSHWGTKGTSRPTHYHVLWDENNFRSDEVQQLIHNLCYTFARCTRPVSLVPPAYYAHLAAYRGRLYLERSDTTMYRVSPLQTVPLPKLRDNVKRLMFYC
Protein: Endo-1,4-beta-xylanase B (Xylanase B) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase B) (Endo-1,4-beta-xylanase G1) (Xylanase G1) (Endo-1,4-beta-xylanase II) (Xylanase II) (P55330)
Organism: Aspergillus niger
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MLTKNLLLCFAAAKAALAVPHDSVAQRSDALHMLSERSTPSSTGENNGFYYSFWTDGGGDVTYTNGDAGAYTVEWSNVGNFVGGKGWNPGSAQDITYSGTFTPSGNGYLSVYGWTTDPLIEYYIVESYGDYNPGSGGTYKGTVTSDGSVYDIYTATRTNAASIQGTATFTQYWSVRQNKRVGGTVTTSNHFNAWAKLGMNLGTHNYQIVATEGYQSSGSSSITVQ
Protein: Peroxidase 28 (Atperox P28) (EC 1.11.1.7) (ATP39) (Q9SS67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- GDSL esterase/lipase At1g74460
- GDSL esterase/lipase At1g28650
- GDSL esterase/lipase At5g45960
- GDSL esterase/lipase At5g37690
- GDSL esterase/lipase At2g30310
- GDSL esterase/lipase At2g19050
- GDSL esterase/lipase At2g23540
- GDSL esterase/lipase At4g26790
- CASP-like protein 1A1
- Cytochrome b561 and DOMON domain-containing protein At4g17280
Sequence:
MKIATFSVLLLLLFIFPVALAQLKFKFYSESCPNAETIVENLVRQQFARDPSITAALTRMHFHDCFVQGCDASLLIDPTTSQLSEKNAGPNFSVRGFELIDEIKTALEAQCPSTVSCSDIVTLATRDAVFLGGGPSYVVPTGRRDGFVSNPEDANEILPPPFISVEGMLSFFGNKGMNVFDSVALLGAHTVGIASCGNFVDRVTNFQGTGLPDPSMDPTLAGRLRNTCAVPGGFAALDQSMPVTPVSFDNLFFGQIRERKGILLIDQLIASDPATSGVVLQYASNNELFKRQFAIAMVKMGAVDVLTGSAGEIRTNCRAFN
Protein: Large ribosomal subunit protein uL5B (60S ribosomal protein L11-B) (L16) (RP39) (YL22) (Q3E757)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}.
Interaction partners:
- Large ribosomal subunit protein uL2A
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL11A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
Sequence:
MSTKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK
Protein: Cecropin-like peptide 1 (CLP1) (L7VIN3)
Organism: Hermetia illucens (Black soldier fly)
Function: Antimicrobial peptide active against Gram-negative bacteria E.coli KCCM 11234 (MIC<=1.03 uM), E.aerogenes KCCM 12177 (MIC<=2.07 uM) and P.aeruginosa KCCM 11328 (MIC<=2.07 uM). Not active against various Gram-positive bacteria at concentrations up to 4.14 uM.
Subcellular location: Secreted {ECO:0000269|Ref.1}.
Interaction partners:
Sequence:
MNFTKLFVVFAVVLVAFAGQSEAGWRKRVFKPVEKFGQRVRDAGVQGIAIAQQGANVLATARGGPPQQG
Protein: Histone deacetylase (EC 3.5.1.98) (F1LM64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
- Histone deacetylase 4
- Calcium/calmodulin-dependent protein kinase type IV
- Histone deacetylase 2
- Nuclear receptor corepressor 2
- Catenin beta-1
- Myocyte-specific enhancer factor 2C
- Forkhead box O3
- Myocyte-specific enhancer factor 2D
- Myc proto-oncogene protein
- Probable ATP-dependent RNA helicase DDX20
Sequence:
MLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESKASGRFLDPTTPWPQLQAPSSAVPCPVGAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLLGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGTGPGVSSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGSTLTGKFMSTSSIPGCLLGVALEGDTSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQMQLGKQEALLGEGDEEEDEEDCIQVKDEDGESGPDEGADLEESSAGYKKLFADAQQLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGSMKSPTDHPTVVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSINAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTGEKEEAETVSAMALLSMGAEQAQAAATQEHSPRPAEEPMEQEPAL
Protein: Lipophorin receptor 2, isoform C (A8JRC4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MATTCMPHFTEYFQTTTQSELTTNESANSRSSSSSSGCREPSKTSGFFYSASTHYQSKVQQLISFSFTSSFHLLFITCILSISKFCNAAAVNAAHVTAATPTASEIMHNLSGSALLERLKASTLGPTLDQLKHLAPAAANSISPGTGSGMGIGMGHFGSSINSVLNGNPLKFLNVSGKIGTPLDISLGLSNYCDEKQFQCSTGECIPIRFVCDGSSDCPDHSDERLEECKFTESTCSQEQFRCGNGKCIPRRWVCDRENDCADGSDESTSQCRSHTCSPEEFACKSGEGECIPLSWMCDQNKDCRDGSDEAQCNRTCRSDEFTCGNGRCIQNRFKCDDDDDCGDGSDEKNCGEKAKCGSNFFACKSGPCIPNQWVCDGDSDCRNGEDEMQNCTVSLLNFCQAGEFQCSDRITCLHKSWVCDGEADCPDGEDESQSNCLKVSCRPDQFQCNDQSCIAGHLTCNGKRDCADGSDEIMCDISATPRTCNATTEFDCGGGLCIPNAKVCNRRKDCPNGEDEPAGKCGINECSSKNGGCMHQCVNLEVGYRCECHDGYKLGADQHTCVDIDECETPGICSQVCVNEIGAFKCECEAGYMRLLKNHTRCKASEGHASLLLARRHDIRKIALDRPEMTSIVNSTKAATALDFVFRTGMIFWSDVATQSIYKAPIDEGNDRTVVLTKSSVTSDGLAVDWIYNHVYFTDTHKCTIELTNFEGSMGKVLVKDSLDIPRSIALDPIEGWMYWSDWGASPRIERAGMDGTHRTAIITYDVKWPNGITLDLVQKRLYWVDGKLNTISSSNYDGSQRHQVLYSGEYLRHPFSITTFEDYVYWTDWDKQAVFKANKFNGMDVEPVTATHMLEHPMVVHVYHPYRQPDGVNHCQSVNGHCSHLCLPAPRINERSPRISCACPTGLKLMPDGLMCVEDLETKTGNNRTDTSNQVHKSDAESENDYVEIALHVIASLAGTALVASVIYVVYRRCTRAVNSMNFENPVYHKTTEDHFSLEKNGTPHIYAAANDEEAVNPLFKSGTECV
Protein: Protein lin-28 homolog A (Lin-28A) (Q803L0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism. Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (By similarity). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Suppressor of microRNA (miRNA) biogenesis, including that of let-7. Binds specific target miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in their terminal loop, and recruits uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation (By similarity). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y3}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q8K3Y3}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8K3Y3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8K3Y3}. Note=Predominantly cytoplasmic. In the cytoplasm, localizes to peri-endoplasmic reticulum regions and may be bound to the cytosolic surface of rough endoplasmic reticulum (ER) on which ER-associated mRNAs are translated. Shuttle from the nucleus to the cytoplasm requires RNA-binding. {ECO:0000250|UniProtKB:Q8K3Y3}.
Interaction partners:
- POU domain, class 5, transcription factor 1
- Terminal uridylyl transferase 4.
- Uncharacterized protein.
- Kruppel-like factor 4.
- Biklf
- Uncharacterized protein.
- Transcription factor Sox-2
- Transcriptional regulator Myc-A
- E3 ubiquitin-protein ligase TRIM71
- Achaete-scute homolog 1a
Sequence:
MPPANPHLNHTGGCTKTEEEEAASSEEDSGSFHGSGVCKWFNVRMGFGFLSMTHREGICLDSPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKRSSKGLESLQVTGPGGAPCVGSEKKPKGTQKRRSKGDRCFNCGGPNHHAKECQLPPQPKKCHFCQSISHMVANCPIKAQQLSPGSQGKSTTSTGEEEDMSHTPLLPESTD
Protein: FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) (Augmenter of liver regeneration) (Q63042)
Organism: Rattus norvegicus (Rat)
Function: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. May have a function in liver regeneration and spermatogenesis.
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P55789}. Mitochondrion {ECO:0000250|UniProtKB:P55789}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
Sequence:
MAAPSEPAGFPRGSRFSFLPGGAHSEMTDDLVTDARGRGARHRKDNAPAAAPAPKGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRNTWAFLHTLAAYYPDMPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIDRSQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD
Protein: Tumor protein p73 (D4AA88)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.
Interaction partners:
- Transcriptional coactivator YAP1
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase Mdm2
- WW domain containing transcription regulator 1
- Tumor protein 63
- Tumor protein p53 binding protein, 2
- Protein phosphatase 1, regulatory subunit 13 like
- E3 ubiquitin-protein ligase
- Protein phosphatase 1, regulatory subunit 13B
- TP53-binding protein 1
Sequence:
MSSPRQLDAYATALPLQATGPPAPLPKSTDPSRAQVQPRMSNGVGEMAQSSSSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGNSEATGSEESNMDVFHLQGMTSSVMAQFNLLSSAMDQMGSRAAPASPYTPEHAASAPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDIVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILVIITLETRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESTTKNGAASKRAFKQSPPAIPALGTNVKKRRHGDEDMFYMHVRGRENFEILMKVKESLELMELVPQPLVDSYRQQQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGVNKLPSVNQLVGQPPPHSSAAGPNLGSMGSGILNSHSHSMPANGEMNGGHSSQTMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKIPDQYRMTIWRGLQDLKQSHDCGQQLLRSSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGAGGVTGPDEWADFGFDLPDCKSRKQPIKEEFTETESH
Protein: Bcl-2-like protein 2 (Bcl2-L-2) (Apoptosis regulator Bcl-W) (c98) (P70345)
Organism: Mus musculus (Mouse)
Function: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.
Subcellular location: Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Bcl-2-like protein 11
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-modifying factor
- Bcl-2-interacting killer
- Induced myeloid leukemia cell differentiation protein Mcl-1 homolog
- Beclin-1
- Activator of apoptosis harakiri
- Bcl-2-binding component 3
- Bcl-2 homologous antagonist/killer
- Caspase-9
Sequence:
MATPASTPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQDWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK
Protein: Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain] (Q60928)
Organism: Mus musculus (Mouse)
Function: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4 (By similarity). Indirectly regulates multiple aspects of skeletal biology.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
Interaction partners:
- Glutathione synthetase
- Glutamate--cysteine ligase catalytic subunit
- Glutathione reductase, mitochondrial
- Glutathione hydrolase 6
- 5-oxoprolinase
- Gamma-glutamylcyclotransferase
- Glutamate--cysteine ligase regulatory subunit
- Aminopeptidase N
- Cytosol aminopeptidase
- Glutathione hydrolase 7
Sequence:
MKNRFLVLGLVAVVLVFVIIGLCIWLPYTSGKPDHVYSRAAVATDAKRCSEIGRDILQEGGSVVDAAIASLLCMGLMNAHSMGIGGGLFFTIYNSTTGKVEVINAREVAPRLANTTMFNNSKDSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARHGFPVGKGLAIALDKKRDVIEKTPALCEVFCRQGKVLQEGETVTMPKLADTLQILAQEGAKAFYNGSLTAQIVKDIQEAGGIMTVEDLNNYRAELIEHPMSIGLGDATLYVPSAPLSGPVLILILNILKGYNFSPKSVATPEQKALTYHRIVEAFRFAYAKRTMLGDPKFVDVSQVIRNMSSEFYATQLRARITDETTHPAAYYEPEFYLQDDGGTAHLSAVSEDGSAVAATSTINLYFGSKVLSRVSGILFNDEMDDFSSPNFINQFRVAPSPANFIKPGKQPLSSMCPSIILDKDGQVRMVVGASGGTQITTSVALAIINSLWFGYDVKRAVEEPRLHNQLLPNTTTVEKDIDQVVTAGLKIRHHHTEVTPTFIAVVQAVVRASGGWAAASDSRKGGEPAGY
Protein: U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) (P09234)
Organism: Homo sapiens (Human)
Function: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153, ECO:0000269|PubMed:2136774}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated proteins B and B'
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein F
Sequence:
MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLIDKTTAAFQQGKIPPTPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGPPMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPTRPGMTRPDR
Protein: Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B (EC 2.4.1.-) (EC 2.4.1.155) (Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase B) (GlcNAc-T Vb) (GNT-Vb) (Mannoside acetylglucosaminyltransferase 5B) (N-acetylglucosaminyl-transferase Vb) (N-acetylglucosaminyltransferase IX) (GNT-IX) (Q765H6)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAc-beta1,2-Man-alpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan (By similarity). Also acts on the GlcNAc-beta1,2-Man-alpha1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan. Plays an active role in modulating integrin and laminin-dependent adhesion and migration of neuronal cells via its activity in the O-mannosyl glycan pathway.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16413118}; Single-pass type II membrane protein {ECO:0000269|PubMed:16413118}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
- Beta-1,4-galactosyltransferase 3
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Sequence:
MITVNPDGKIMVRRCLVTLRPFRLFVLGIGFFTLCFLMTSLGGQFSARRLGDSPFTIRTEVPGSPESRGALRKMSDLLELMVKRMDMLARLENSSELHRTASVAHLAADRLTPGASLIERIQAIAQNVSDIAVKVDQILRHSLILHSKVSEGRRDQCEAPSDPKFPDCSGKVEWMRARWTSDPCYAFFGVDGTECSFLIYLSEVEWFCPPLPWRNQTAARTAPKSLPRVQAVFRSNLSHLLELMGSGKESLIFMKKRTRRFTAQWTKAAKYLAQKLGDIRRDQKQILVHIGFLTEESGDVFSPRVLKGGPLGEMVQWADILAALYVLGHSLRITVSLKELQSNLGVPPGRGNCPLTVPLPFDLIYTDYHGLQQMKQHMGLSFKKYRCRIRVIDTFGTEPAYNHEEYATLHGYRTNWGYWNLNPKQFMTMFPHTPDNSFMGFVSEELNETEKQLIKDGKASNMAVVYGKEASIWKLQGKEKFLAVLNKYMEIHGTVYYESQRPPEVPAFVKNHGLLPQPEFQQLLRKAKLFIGFGFPYEGPAPLEAIANGCIFLQSRFSPPHSSLNHEFFRGKPTSREVFSQHPYAENFIGKPHVWTVDYNNSDEFETAIKAIMNTQVDPYLPYEYTCAGMLERINAYIQHQDFCVGPSPLPPGASTAQSPFVLAPNATHLEWAQNISSVPGAWPPTHSLRAWLAAPGRACTDACLDHGLICEPSFFPFLNSQNSFLKLQVPCDSTEWEMHHLYPAFAQPGQECYLQKEPLLFSCAGASTKYQRLCPCRDFRKGQVALCQGCL