wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor GATA-4 (GATA-binding factor 4) (I3LUZ9)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Homeobox protein Nkx-2.5
- T-box transcription factor 5.
- Nuclear factor of activated T cells 4.
- Myocyte-specific enhancer factor 2C
- Serum response factor
- Nuclear factor of activated T-cells, cytoplasmic 1
- Nuclear factor of activated T cells 3.
- Ras homolog family member A
- Nuclear factor of activated T-cells, cytoplasmic 1
- Cingulin
Sequence:
MYQSLAMAANHGPPPGPYEAGGPGPFMHSAGAASSPVYVPTPRVPSSVLGLSYLQGGGGGAAAGAASGGSSSAAPSGAGPGTQQGSPGWSQAGAEGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYSSGGGAAGAGLAGREQYGRAGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPAARHPNLVDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTSAGPSGSESLPPTTSASSNSSSVATSSSEEMRPIKTEPGLSAHYGHGSSLSQTFSVSAMSGHGPSIHPVLSALKLSPQGYASSVSQSPQASSKQDPWNSLALADSHGDIITA
Protein: Glutamine synthetase cytosolic isozyme 2 (EC 6.3.1.2) (GS1-2) (Glutamate--ammonia ligase) (O82560)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Cytoplasm.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- glutamate synthase
- Ferredoxin--nitrite reductase, chloroplastic
- glutamine--fructose-6-phosphate transaminase
- glutamine--fructose-6-phosphate transaminase
- glutamate synthase
- Formamidase
- glutamate dehydrogenase
- glutamate dehydrogenase
- Aminotransferase class I/classII large domain-containing protein
Sequence:
MSLLSDLINLNLSDITDKVIAEYIWVGGSGMDMRSKARTLSGPVKDPSKLPKWNYDGSSTGQAPGQDSEVILYPQAIFKDPFRRGSNILVMCDAYTPAGEPIPTNKRNNAAKIFGHPDVAAEEPWYGLEQEYTLLQKDVQWPLGWPLGGFPGPQGPYYCGTGANKAFGRDIVDSHYKACIYAGINISGINGEVMPGQWEFQVGPSIGISAADELWVARYILERITEIAGVVLSFDPKPIQGDWNGAGAHTNYSTKSMRNDGGYEVIKKAIAKLEKRHKEHIAAYGEGNERRLTGRHETADMNTFVWGVANRGASIRVGRDTEKAGKGYFEDRRPASNMDPYVVTSMIAETTILWKP
Protein: HTH tetR-type domain-containing protein (Q8DNK2)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Interaction partners:
- HTH tetR-type domain-containing protein
Sequence:
MTNIDRRISKTKKAIYQAFIQLLNAKGYEATTVQDIIDLADVGRSTFYCHYESKELLLDQLCRYLFHHLFEREQAISTEDYLAHLFLHFHKNQDHITSLLFSKNDYFLRQLHKELEHHVYSVLADNLKEAHPNLPTSYLQHLVMSNFIETLTWWLKKGQDFTDQEVVQFYLDLLIPKN
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Q8WRF5)
Organism: Taenia solium (Pork tapeworm)
Interaction partners:
Sequence:
MKAVCVMRGEEGVKGVVHFTQAGDAVKVHAEFEGLKPGKHGFHVHEFGDTTQGCTSAGAHFNPHGKNHGAPDAAERHVGDLGNVTAGADGKATLDLTDKMISLTGEHSVIGRSLVIHVDPDDLGLGGHELSLITGNAGGRVACGIIGIAKSE
Protein: Kynurenine--oxoglutarate transaminase 1 (EC 2.6.1.7) (Cysteine-S-conjugate beta-lyase) (EC 4.4.1.13) (Glutamine transaminase K) (GTK) (Glutamine--phenylpyruvate transaminase) (EC 2.6.1.64) (Kynurenine aminotransferase 1) (Kynurenine aminotransferase I) (KATI) (Kynurenine--oxoglutarate transaminase I) (Q8BTY1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16773}.
Interaction partners:
- Kynurenine 3-monooxygenase
- Kynureninase
- Kynurenine formamidase
- Aspartate aminotransferase, mitochondrial
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Cystathionine gamma-lyase
- Cystathionine beta-synthase
- Aspartate aminotransferase, cytoplasmic
- Adenosylhomocysteinase
- S-adenosylhomocysteine hydrolase-like protein 1
Sequence:
MSKQLQARRLEGIDHNPWVEFTRLSKEYDVVNLGQGFPDFSPPDFAVQAFQQATTGNFMLNQYTSAFGYPPLTKILASFFGKLLGQEMDPLKNVLVTVGAYGALFTAFQALVDEGDEVIIIEPAFNCYEPMTMMAGGRPVFVSLRLSPAPKGQLGSSNDWQLDPTELASKFTPRTKILVLNTPNNPLGKVFSKKELELVAALCQQHDVLCFSDEVYQWLVYDGHQHISIASLPGMWERTLTIGSAGKSFSATGWKVGWVMGPDNIMKHLRTVHQNSIFHCPTQAQAAVAQCFEREQQHFGQPSSYFLQLPQAMGLNRDHMIQSLQSVGLKPLIPQGSYFLIADISDFKSSMPDLPGAMDEPYDTRFAKWMIKNKGLSAIPVSTFYSQPHHKDFDHYIRFCFVKDKATLQAMDKRLCSWKGEPQA
Protein: tRNA N(3)-cytidine methyltransferase METTL8, mitochondrial (EC 2.1.1.-) (Methyltransferase-like protein 8) (mRNA N(3)-methylcytidine methyltransferase METTL8) (EC 2.1.1.-) (Q9H825)
Organism: Homo sapiens (Human)
Function: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of mitochondrial tRNA(Ser)(UCN) and tRNA(Thr). N(3)-methylcytidine methylation modification regulates mitochondrial translation efficiency and is required for activity of the respiratory chain. N(3)-methylcytidine methylation of mitochondrial tRNA(Ser)(UCN) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by TRIT1 as prerequisite. May also mediate N(3)-methylcytidine modification of mRNAs. The existence of N(3)-methylcytidine modification on mRNAs is however unclear, and additional evidences are required to confirm the role of the N(3)-methylcytidine-specific mRNA methyltransferase activity of METTL8 in vivo.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:34774131, ECO:0000269|PubMed:35017528}. Note=Mitochondrial protein: the cytoplasmic or nuclear localization observed by some groups is either the result of an incorrect localization caused by N-terminal tagging that interferes with mitochondrial targeting, or splice isoforms that lack the N-terminal mitochondrial transit sequence. {ECO:0000269|PubMed:34774131}.
Interaction partners:
- Tax1-binding protein 3
- Probable methyltransferase-like protein 25
Sequence:
MNMIWRNSISCLRLGKVPHRYQSGYHPVAPLGSRILTDPAKVFEHNMWDHMQWSKEEEAAARKKVKENSAVRVLLEEQVKYEREASKYWDTFYKIHKNKFFKDRNWLLREFPEILPVDQKPEEKARESSWDHVKTSATNRFSRMHCPTVPDEKNHYEKSSGSSEGQSKTESDFSNLDSEKHKKGPMETGLFPGSNATFRILEVGCGAGNSVFPILNTLENSPESFLYCCDFASGAVELVKSHSSYRATQCFAFVHDVCDDGLPYPFPDGILDVILLVFVLSSIHPDRTLFI
Protein: Transposon Ty1-DR3 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q99231)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNRSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSINSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKDSRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSNDLNIESDHDFQSDIELYPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTDSGGMHRLDVPLLAPMSQSNTHESSYASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Nascent polypeptide-associated complex subunit alpha (NAC-alpha) (Alpha-NAC) (allergen Hom s 2) (Q13765)
Organism: Homo sapiens (Human)
Function: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10982809, ECO:0000269|PubMed:12689679, ECO:0000269|PubMed:15299025, ECO:0000269|PubMed:20214399}. Nucleus {ECO:0000269|PubMed:12689679, ECO:0000269|PubMed:15299025, ECO:0000269|PubMed:20214399}. Note=The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus. {ECO:0000269|PubMed:10982809, ECO:0000269|PubMed:20214399}.
Interaction partners:
Sequence:
MPGEATETVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM
Protein: Endo-beta-N-acetylglucosaminidase EndoS (EC 3.2.1.96) (Endoglycosidase S) (Q99Y92)
Organism: Streptococcus pyogenes serotype M1
Function: Endoglucosidase that acts as a host immune evasion factor by mediating hydrolysis of the N-linked glycan from the Fc region of host immunoglobulin-gamma (IgG) during infection. Specifically catalyzes the hydrolysis of the beta-1,4 linkage between the first two N-acetylglucosamine residues of the complex-type N-linked glycan located on 'Asn-297' of the Fc region of IgG antibodies (IGHG1, IGHG2, IGHG3 or IGHG4), thereby preventing interaction between IgGs and Fc receptors and ability to activate the complement pathway. Shows a specificity for biantennary complex type N-glycans; does neither cleave larger complex type glycans nor oligomannose and nor hybrid-type glycans. Specifically acts on IgGs; does not act on immunoglobulin alpha, beta, delta or mu.
Subcellular location: Secreted {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:18182097}. Host extracellular space {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:18182097}.
Interaction partners:
Sequence:
MDKHLLVKRTLGCVCAATLMGAALATHHDSLNTVKAEEKTVQVQKGLPSIDSLHYLSENSKKEFKEELSKAGQESQKVKEILAKAQQADKQAQELAKMKIPEKIPMKPLHGSLYGGYFRTWHDKTSDPTEKDKVNSMGELPKEVDLAFIFHDWTKDYSLFWKELATKHVPKLNKQGTRVIRTIPWRFLAGGDNSGIAEDTSKYPNTPEGNKALAKAIVDEYVYKYNLDGLDVDVEHDSIPKVDKKEDTAGVERSIQVFEEIGKLIGPKGVDKSRLFIMDSTYMADKNPLIERGAPYINLLLVQVYGSQGEKGGWEPVSNRPEKTMEERWQGYSKYIRPEQYMIGFSFYEENAQEGNLWYDINSRKDEDKANGINTDITGTRAERYARWQPKTGGVKGGIFSYAIDRDGVAHQPKKYAKQKEFKDATDNIFHSDYSVSKALKTVMLKDKSYDLIDEKDFPDKALREAVMAQVGTRKGDLERFNGTLRLDNPAIQSLEGLNKFKKLAQLDLIGLSRITKLDRSVLPANMKPGKDTLETVLETYKKDNKEEPATIPPVSLKVSGLTGLKELDLSGFDRETLAGLDAATLTSLEKVDISGNKLDLAPGTENRQIFDTMLSTISNHVGSNEQTVKFDKQKPTGHYPDTYGKTSLRLPVANEKVDLQSQLLFGTVTNQGTLINSEADYKAYQNHKIAGRSFVDSNYHYNNFKVSYENYTVKVTDSTLGTTTDKTLATDKEETYKVDFFSPADKTKAVHTAKVIVGDEKTMMVNLAEGATVIGGSADPVNARKVFDGQLGSETDNISLGWDSKQSIIFKLKEDGLIKHWRFFNDSARNPETTNKPIQEASLQIFNIKDYNLDNLLENPNKFDDEKYWITVDTYSAQGERATAFSNTLNNITSKYWRVVFDTKGDRYSSPVVPELQILGYPLPNADTIMKTVTTAKELSQQKDKFSQKMLDELKIKEMALETSLNSKIFDVTAINANAGVLKDCIEKRQLLKK
Protein: Cofilin/actin depolymerizing factor, putative (Q580V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- CAP/Srv2p
- Profilin
- Coronin
- Actin-interacting protein 1
- Actin A
- Clathrin heavy chain
- Actin-like protein 3, putative
- Actin-like protein 2, putative
- Actin-like protein, putative
- Flagellar attachment zone protein 1 conserved domain-containing protein
Sequence:
MAMSGVSVADECVTALNDLRHKKSRYVIMHIVDQKSIAVKTIGERGANFDQFIEAIDKNVPCYAAFDFEYTTNDGPRDKLILISWNPDSGAPRTKMLYSSSRDALVPLTQGFQGIQANDASGLDFEEISRKVKSNR
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Q38BE0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083}.
Interaction partners:
- Alpha-1,3-mannosyltransferase, putative
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Glycosyltransferase, putative
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Phosphatidic acid phosphatase, putative
- mannose-1-phosphate guanylyltransferase
- GPI mannosyltransferase 3
- Mannosyltransferase
- GDP-mannose 4,6-dehydratase
- Mannosyltransferase
Sequence:
MTVKYSIIVPAYKECGNLEPLTKQVFDALADDGFSKNEVEMVIVDDNSRDGSVEVVEKVRNEGYGVRIEVRTNDRGLSSAVIHGISASKGSFILVMDADLQHPPKTVPRLLRALEKPGVEFVCGTRYGAGVEIDKDWPLHRRFISWGARLLARPLTPLSDPMSGFFGLRVDVFQRGREVVNPIGYKIALELFVKCAVRKYEEVGFNFAARTVGESKLTGKVIVNYLEHLKLLYFYVYGTALTVLLVLLPLIFYCFYILL
Protein: Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin-2) (P63027)
Organism: Homo sapiens (Human)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles (By similarity). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17313651}; Single-pass type IV membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P63045}. Note=Colocalizes with PRKCZ and WDFY2 in intracellular vesicles (PubMed:17313651). {ECO:0000269|PubMed:17313651}.
Interaction partners:
- Synaptosomal-associated protein 23
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Syntaxin-2
- Syntaxin-4
- Synaptotagmin-1
- Synaptophysin
- Complexin-1
- Syntaxin-3
- Syntaxin-1B
Sequence:
MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST
Protein: Histone acetyltransferase MOF (EC 2.3.1.48) (Males-absent on the first protein) (O02193)
Organism: Drosophila melanogaster (Fruit fly)
Function: Histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation as part of the male-specific lethal (MSL) complex. Dosage compensation insures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes. May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males where it is recruited by the MSL complex. As part of the nonspecific lethal (NLS) complex may associate with promoters of X chromosomal as well as autosomal genes and positively regulate their transcription through chromatin modification.
Subcellular location: Nucleus {ECO:0000269|PubMed:20620954}. Chromosome {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:28510597}. Note=When part of MSL complex, specifically localizes to many sites on the male X chromosome: displays a bimodal distribution binding to promoters and the 3' ends of genes (PubMed:11014199, PubMed:18510926, PubMed:22421046, PubMed:28510597). Recruited to the male X chromosome following association with roX1 and roX2 non-coding RNAs (PubMed:11014199). As part as the NSL complex, associates with promoters of housekeeping genes on X chromosome and autosomes genes (PubMed:18510926, PubMed:20620953). {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:28510597}.
Interaction partners:
- Protein male-specific lethal-3
- Dosage compensation regulator mle
- E3 ubiquitin-protein ligase msl-2
- Protein male-specific lethal-1
- GH01794p
- KAT8 regulatory NSL complex subunit 2
- Reduction in Cnn dots 1, isoform E
- Protein MBD-R2
- Non-specific lethal 1, isoform M
- Protein will die slowly
Sequence:
MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLSANVEAISDDSSETSSSDDDEEEEEDEDDALTMEHDNTSRETVITTGDPLMQKIDISENPDKIYFIRREDGTVHRGQVLQSRTTENAAAPDEYYVHYVGLNRRLDGWVGRHRISDNADDLGGITVLPAPPLAPDQPSTSREMLAQQAAAAAAASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRYDEINHVQKSHAELTATQAALEKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTRCAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTSKTIQDHLQLPQFKQPKLTIDTDYLVWSPQTAAAVVRAPGNSG
Protein: AP complex subunit sigma (Q9GQM7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
Sequence:
MIRFILIQSRAGKTRLAKWYMNFDGDEKQKLIEEVHAVVTVRDAKHTSFVEFRNFKIVYRRYAGLYFCICVDVNDNNLCYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYSVVDEMFLAPEIRETSQTKVLKQLLTLNSLE
Protein: Protein kinase, putative (Q585U8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitogen-activated protein kinase 5, putative
- cyclin-dependent kinase
Sequence:
MERYKLRPYPSARTPSSALYLCVDQLTERELAVKVIGKGNPSADRRVRRLLHGVQMVARAGPHQNLIAVHGVYDSDGNVYVFMDYAEGGTLLNYIKRRGPLPEGVTIQVVRQLLEALAHLHGRGVMHRDIKAENILIREPTEGRKPLGRVCICDYGFATCSTPTNECVGSPGYCAPEIALIGITQGPKADENGYCYDEKCDIWSLGVTTYAMLSGQLPFTGGTPTDVFKSILRDSVPFSSPTWGNVSHEAKKFVLYLMTFKASNRPSARAALGHPWLVV
Protein: Monothiol glutaredoxin-S4 (AtGrxS4) (Protein ROXY 13) (O23419)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Acid phosphatase-like protein
- At2g16660/T24I21.7
- Protein NRT1/ PTR FAMILY 4.7
Sequence:
MDKLQKMISEKSVVIFSKNSCCMSHTIKTLFIDFGVNPTIYELDEINRGKEIEQALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLVPMLKRVGALWL
Protein: Uncharacterized protein At2g33420 (O22792)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Kinetochore protein SPC24 homolog
Sequence:
MTHHHRRESFSVTPSTMGGSVVLCPNTDLLWPFGKLEGLDRDDIRETAYEIFFTACRSSPGFGGRTALTFYSNHNSNDHHGDGGGGIGSGGSTGVGSGFGSSGRKEVVTTPTSRVKRALGLKMLKRSPSRRMSTIGAAGGAATSLSPGGMNSSAGHISPGAGFLTVQPSRPRRPLTSAEIMRQQMKVTEQSDSRLRKTLLRTLVGQTGRRAETIILPLELLRHLKTSEFGDIHEYQLWQRRQLKVLEAGLLLHPSIPLDKTNNFAMRLREVVRQSETKPIDTSKTSDTMRTLTNVVVSLSWRGTNGNPTDVCHWADGYPLNIHLYVALLQSIFDVRDETLVLDEIDELLELMKKTWSTLGITRPIHNLCFTWVLFHQYVVTSQMEPDLLGASHAMLAEVANDAKKLDREALYVKLLNSTLASMQGWTEKRLLSYHDYFQRGNVGLIENLLPLALSSSRILGEDVTISQGKGQEKGDVKLVDHSGDRVDYYIRSSIKNAFSKVIENTKAKIAATDEGEEAAGTLLQLAKETEELALRERECFSPILKRWHSVAAGVASVSLHQCYGSILMQYLAGRSFISRDTVEVLQTAGKLEKVLVQMVAEDSEECEDGGKGLVREMVPYEVDSIILRLLRQWVEEKLKAVQECLFRAKETETWNPKSKSEPYAQSAGELMKLAKDTIDEFFEIPIGITEDLVHDIAEGLEQLFQEYTTFVASCGARQSYIPTLPPLTRCNRDSRFVKLWKRATPCTTSNEDLKYTTSVISDGHHPRPSTSRGTQRLYIRLNTLHFLSSHIHSLNKTLSLNPRILPATRKRYRHRNNNSSSYFDFTYAGIESACQHVSEVAAYRLIFLDSNSVLYESLYVGEVANARIRPALRIMKQNLTLMSAILADRAQSLAMREVMKSSFEAFLMVLLAGGYSRVFYRSDHSIIEEDFENLKRVFCTCGEGLIPEEVVDREAETVEGVIQLMSQPTEQLMEDFSIVTCETSGMGMVGSGQKLPMPPTTGRWNRSDPNTILRVLCHRNDRVANQFLKKSFQLPKRR
Protein: Enolase 1, chloroplastic (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 1) (2-phosphoglycerate dehydratase 1) (Q9C9C4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Phosphoglycerate mutase-like protein 4
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
- Phosphoglycerate kinase 3, cytosolic
- Plastidial pyruvate kinase 1, chloroplastic
- Phosphoglycerate kinase 1, chloroplastic
Sequence:
MALTTKPHHLQRSFLSPSRVSGERYLESAPSCLRFRRSGVQCSVVAKECRVKGVKARQIIDSRGNPTVEVDLITDDLYRSAVPSGASTGIYEALELRDGDKSVYGGKGVLQAIKNINELVAPKLIGVDVRNQADVDALMLELDGTPNKSKLGANAILGVSLSVCRAGAGAKGVPLYKHIQETSGTKELVMPVPAFNVINGGSHAGNSLAMQEFMILPVGATSFSEAFQMGSEVYHTLKGIIKTKYGQDACNVGDEGGFAPNVQDNREGLVLLIDAIEKAGYTGKIKIGMDVAASEFFMKDGRYDLNFKKQPNDGAHVLSAESLADLYREFIKDFPIVSIEDPFDQDDWSSWASLQSSVDIQLVGDDLLVTNPKRIAEAIKKQSCNALLLKVNQIGTVTESIQAALDSKAAGWGVMVSHRSGETEDNFIADLSVGLASGQIKTGAPCRSERLSKYNQLLRIEEELGNVRYAGEAFRSP
Protein: Tropomodulin-4 (Skeletal muscle tropomodulin) (Sk-Tmod) (Q9JLH8)
Organism: Mus musculus (Mouse)
Function: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NZQ9}. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments. {ECO:0000250|UniProtKB:Q9NZQ9}.
Interaction partners:
- Alpha-adducin
- Beta-adducin
- Gamma-adducin
- Myosin-binding protein C, fast-type
- Alpha-actinin-3
- Dematin
- Nebulin
- Troponin T, fast skeletal muscle
- Tropomyosin alpha-1 chain
- Myosin light chain 1/3, skeletal muscle isoform
Sequence:
MSSYQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERDDLVPYTGEKKGKPFIQPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSNKQYYDAICSGEICNTEGISSVVQPDKYKPVPDEPPNPTNIEEMLKRVRSNDKELEEVNLNNIQDIPIPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMAVLKAVRENATLTELRVDNQRQWPGDAVEMEMATVLEQCPSIVRFGYHFTQQGPRARAAHAMTRNNELRRQQKKR
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PMV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEEETQLEEKNSLRVEGDNIYVRHSNLMLEELDKAQEDILKHQASISELKRNFMESTPEPRPNEWEKRRITPLSLQTQGSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKVVEREEAVPEASPVTQAGASVITVETVIQENVGAQKIPGEKSVHEGALKQDMGEEAEEEPQKVNGEVSHVDIDVLPQIICCSE
Protein: PAC1 receptor Hop2 isoform (Pituitary adenylate cyclase-activating polypeptide type I receptor isoform 2 precursor) (Q5C8U8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MYRQAARETFLILFLIISLMWPIHSEISNCVIKREEERCLERIALHDPKDDQKFECPWEWDNLTCWQAASVGDVVEVNCPELFEFMSPEEGLGKISRNCTEFGWSEPYPHYVDACMTDENTTKPDMYYASVKALYTVGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIKDGVLYAEEDSDHCFVHTVGCKAVMVFFHYCVMSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTIWAVLRLHFDDSGCWDMNDNTALWWVIKGPVVASIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLCAQKCFSEPTQAVQHSCRMSELSTITLRLARSTLLLIPLFGIHYTVFAFSPEDFSKRERLVFELGLGSFQGFVVAVLYCFLNGEAQSEIKRKWRSWTVNRYFAVDLKQQRHPSLASSGVNGGTQLSILSKSSSQIRMSSPLAETVNLNLPT