wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerases II, IV and V subunit 9B (Q8L5V0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. Required for RNA silencing.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase V subunit 5A
- DNA-directed RNA polymerase V subunit 7
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerase IV subunit 7
- DNA-directed RNA polymerases II, IV and V subunit 10
Sequence:
MSTMKFCRECNNILYPKEDKEQSILLYACRNCDHQEAADNNCVYRNEVHHSVSEQTQILSDVASDPTLPRTKAVRCAKCQHGEAVFFQATARGEEGMTLFFVCCNPNCSHRWRE
Protein: Probable ATP-dependent RNA helicase DDX46 (EC 3.6.4.13) (DEAD box protein 46) (Q95TU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGRDLIGIAKTGSGKTLAFILPMFRHILDQPSMEDGDGAIAIIMAPTRELCMQIGKDIRKFSKSLGLRPVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIIDNVRPDRQTVMFSATFPRQMEALARRILKKPIEVIVGGRSVVCKEVEQHVVILNDDAKFFKLLELLGIYQEAGSIIVFVDKQENADILLRDLMKASYPCMSLHGGIDQFDRDSTIIDFKSGKVRLLIATSVAARGLDVKDLILVVNYDVPNHYEDYVHRCGRTGRAGKKGSAYTFITPEQSRYAGDIIRAMDLSGTLIPAELQALWTEYKALQEAEGKTVHTGGGFSGKGFKFDEQEFNAAKESKKLQKAALGLADSDDEEDIEQDIDQQIEQIFAAKRTVKDTSAAATAAAAAAAAAAAAAAAVSGANPALASAAAQAAAAAAAANIAIAAASAPAAAGGAPSVAMGGALSSDKLELAKRLASKINSSKNLDTKGSVVTVEPMIKGPHVTGAAATLLTARTVAEQMAAKLNNKLNYQPKEDEEGLGPLVGGTTNPFTKYEEELEINDFPQQARWKVTSKEALAQISEYSEAGLTVRGTYVPQGKNPPDGERKLYLAIESCSELAVQKAKREITRLIKEELLKLSSAHHVFNKGRYKVV
Protein: Retinol-binding protein 1 (Cellular retinol-binding protein) (CRBP) (Cellular retinol-binding protein I) (CRBP-I) (P02696)
Organism: Rattus norvegicus (Rat)
Function: Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q00915}. Lipid droplet {ECO:0000250|UniProtKB:Q00915}.
Interaction partners:
- Lecithin retinol acyltransferase
- Receptor for retinol uptake STRA6
- Transthyretin
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MPVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVTCKQVFKKVH
Protein: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5) (P34666)
Organism: Caenorhabditis elegans
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq-4, mitochondrial
- Atypical kinase coq-8, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Kynurenine 3-monooxygenase
- ApaG domain-containing protein
- 2-
Sequence:
MKGATNLFKSMRKPTNVGNFRQFSVNQVNSDNKRSEPGKKTHFGFTDVDEAEKEQKVHHVFANVAKKYDLMNDAMSMGVHRLWKDYYVGGLQVPYNAKCLDMAGGTGDIAFRILRHSPTAKVTVSDINQPMLDVGKKRAEKERDIQPSRAEWVCANAEQMPFESNTYDLFTMSFGIRNCTHPEKVVREAFRVLKPGGQLAILEFSEVNSALKPIYDAYSFNVIPVLGEILASDRASYQYLVESIRKFPNQDEFARIIREEGFSNVRYENLTFGVCSIHKGMKPRK
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A0A8I6GL10)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
Protein: Peptides MS9.1 [Cleaved into: Tau-AnmTX Ms 9a-1; AnmTx Ms 9a-2] (A0A1R3S3A8)
Organism: Metridium senile (Brown sea anemone) (Frilled sea anemone)
Function: Acts as a positive modulator of mammalian TRPA1, a non-selective cation channel involved in detection of pain, in vitro yet has an analgesic and anti-inflammatory effect in vivo.
Subcellular location: Secreted {ECO:0000269|PubMed:28077580}. Nematocyst {ECO:0000269|PubMed:28077580}.
Interaction partners:
Sequence:
MKQSLILAVLCLALVFATIEAKPKADPNIIVGGCIKCHVKNASGRCVRIVGCGVDKVPDLFSDPNIIVGGCSKCHKQDSSGNCVRIAGCGVDPVRDAE
Protein: Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Q7KN94)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|PIRNR:PIRNR000089}.
Interaction partners:
- Electron transfer flavoprotein-ubiquinone oxidoreductase
- Electron transfer flavoprotein subunit beta
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
Sequence:
MFASNTRNLMRSSILQRCKSTLVVAEHNNEVLNPITLNTISAAKKIGGDVTVLVAGTKCGPASEALSKVDGVTKVLVAENAAFNGFTAESLTPLVLAAQSQFKFTHILAGASAFGKNVLPRVAAKLDVSPISEIIDVKSDDTFVRTIYAGNAILTLKSKDAVKVITVRSTNFPPAATSGGSGAVEQAPAGDFASSLSEFVSQELTKSDRPELAGAKVIVSGGRGLKSGDNFKLLYDLADKFGAAVGASRAAVDAGFVPNDLQIGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADIGIVADLFKAVPELTGKL
Protein: DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase MmuIIIA) (DNA MTase MmuIIIA) (M.MmuIIIA) (O88508)
Organism: Mus musculus (Mouse)
Function: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Also has weak auto-methylation activity on Cys-706 in absence of DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:15456878, ECO:0000269|PubMed:20547484}. Chromosome {ECO:0000269|PubMed:20547484}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K1}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin. {ECO:0000269|PubMed:20547484}.
Interaction partners:
- DNA
- Histone-lysine N-methyltransferase EZH2
- DNA
- Histone deacetylase 1
- Histone-lysine N-methyltransferase SETDB1
- Histone-lysine N-methyltransferase SUV39H1
- DNA
- Histone-lysine N-methyltransferase EHMT2
- Histone H3.3
- Histone H3.1
Sequence:
MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
Protein: Luciferin 4-monooxygenase (Luciferase) (EC 1.13.12.7) (P08659)
Organism: Photinus pyralis (Common eastern firefly) (Lampyris pyralis)
Function: Produces green light with a wavelength of 562 nm.
Subcellular location: Peroxisome {ECO:0000269|PubMed:3554235}.
Interaction partners:
Sequence:
MEDAKNIKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVNITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMNISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIKAKKGGKSKL
Protein: DnaJ homolog subfamily B member 1 (DnaJ protein homolog 1) (Heat shock 40 kDa protein 1) (HSP40) (Heat shock protein 40) (Human DnaJ protein 1) (hDj-1) (P25685)
Organism: Homo sapiens (Human)
Function: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1586970}. Nucleus {ECO:0000269|PubMed:1586970}. Nucleus, nucleolus {ECO:0000269|PubMed:1586970}. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 1A
- Stress-induced-phosphoprotein 1
- BAG family molecular chaperone regulator 1
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 6
- E3 ubiquitin-protein ligase CHIP
Sequence:
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI
Protein: Gelation factor (Actin-binding protein 120) (ABP-120) (P13466)
Organism: Dictyostelium discoideum (Social amoeba)
Function: F-actin cross-linking protein.
Interaction partners:
- Extracellular signal-regulated kinase 2
- Gelsolin-related protein of 125 kDa
- Cofilin-1A
- Talin-B
- Fimbrin
- Actin binding protein
- Severin
Sequence:
MAAAPSGKTWIDVQKKTFTGWANNYLKERILKIEDLATSLEDGVLLINLLEIISSKKILKYNKAPKIRMQKIENNNMAVNFIKSEGLKLVGIGAEDIVDSQLKLILGLIWTLILRYQIQMSESDNSPKAALLEWVRKQVAPYKVVVNNFTDSWCDGRVLSALTDSLKPGVREMSTLTGDAVQDIDRSMDIALEEYEIPKIMDANDMNSLPDELSVITYVSYFRDYALNKEKRDADALAALEKKRRETSDASKVEVYGPGVEGGFVNKSADFHIKAVNYYGEPLANGGEGFTVSVVGADGVEVPCKLVDNKNGIYDASYTATVPQDYTVVVQLDDVHCKDSPYNVKIDGSDAQHSNAYGPGLEGGKVGVPAAFKIQGRNKDGETVTQGGDDFTVKVQSPEGPVDAQIKDNGDGSYDVEYKPTKGGDHTVEVFLRGEPLAQGPTEVKILNSDSQNSYCDGPGFEKAQAKRPTEFTIHSVGADNKPCAAGGDPFQVSISGPHPVNVGITDNDDGTYTVAYTPEQPGDYEIQVTLNDEAIKDIPKSIHIKPAADPEKSYAEGPGLDGGECFQPSKFKIHAVDPDGVHRTDGGDGFVVTIEGPAPVDPVMVDNGDGTYDVEFEPKEAGDYVINLTLDGDNVNGFPKTVTVKPAPSAEHSYAEGEGLVKVFDNAPAEFTIFAVDTKGVARTDGGDPFEVAINGPDGLVVDAKVTDNNDGTYGVVYDAPVEGNYNVNVTLRGNPIKNMPIDVKCIEGANGEDSSFGSFTFTVAAKNKKGEVKTYGGDKFEVSITGPAEEITLDAIDNQDGTYTAAYSLVGNGRFSTGVKLNGKHIEGSPFKQVLGNPGKKNPEVKSFTTTRTAN
Protein: Radish, isoform K (X2JEQ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKLRHYRSMDQPCSSTCVVIRKKTMTAICFVCNLPIMSHQVGLVWQGGNGWDDLVREQLEESTIRQRLGGRRDSAAQITTPPSTSPPPGLQRRRRSSLAQLTDILREWSGGTKQQQQHHSQQQQQQLQQASRSKAQLNRRETLADLARSLPWRTSTTTDASTGAGGSGGGGCTTYMAPRKRRESSADSGIRSMRSRRDSNTAEFVRHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESYLSSSRRDSNVAGRVTTPPPPGKYQMTKKRDSLAAPEFPNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSACQALPPPTIITSSVTPPATSPTAPKGRRDSQTQCGRVNRRDSKAGVSPERAPRLQRLQRQATAFDEGCLPGGSRRGSQPALSPDPPDDCERRTSRRDSLSPDSASRGGRRDSRTHLSPDRSHERDGSPRRHTLRRQSSSAARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQSTTEEILIARGFRRQSTTEEMIRCRNFRRQSSQSDDVCRYRGRRDSSAQIIDGTIGTMTVETTSTFFDSSTQTEPSPLYDNNHYHEECLRCNSCGLNLTGPNQKRARRFKNQILCDLHFADVALMECSDFMQQLRSFKPQSLGCAVARRKSSTTLIFPLPPQACSDEFCEEYPHNLMPTPGYWIECSRQKITMPTPHTIWDESDSEHEDIRAGSASDAYLERECSDLYEDDEDSEATPSPRKKTTIEEQWDQQGAFELISVEQETYEKYFYGTEHWNYFTSDEDLGPVILSIKQETLNGRDQFRILVRAGSYTVHGLIPASCVFADRYNREEVVRSLGKEVNLNPPLTLGQLPDTPEELLKLDQVFIKSELKVGVIFVKEDQYTEEQILDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGNDIVCVVFLEADNTRFSPACIKSHFLHTFILVRVSARIKHKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKGPMFREWLLTKIVNGERASYSAPKFARMQERTRSQMLEDLVMNLSNHAETGQIPKPYRRGSWRPIGHMRPSSPLLDSVRDQFEDYDQLAKDFTRVFLNEEPSCLTNAHLFDVVFLVGQSKQKARFIGVRAILGVRSRVFQEMLYGIQTGFGSPQIPVAEIFARPAPSLVSPQNQKPKSNNYLTVPDSDSIRPKSVPSSPMVKRAFSRLGTITAGWGRSIRNKNTNQLNPDDKKKWISSTDYRDSKDKDKDKPGNNQLAVPRLSVCADAQKVDRAKLAQTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFLRIEVVCPMLISLENYYWRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCRELQTPEIRKFEAMLAWAQHKVGKLKNHPNKDTQFEFECIMERLTRDLNLCRISPSELLTVVLPSKSMKNERIMETLMVQVNLGTYRMPELDAYRQQLRQQESAEATVQVHRAHQNHHNPPPIDARAYAMASLAAALEMQNSSNPLQSNAARDAADEEVELYASFDNAPSTSRVAAQMQAAKEARRKRWAADGASGSSGDGGCASGSSGSGRRY
Protein: Cathelicidin-2 (Fowlicidin-2) (F2XNG5)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLSCWVLLLALLGGACALPAPLSYPQALIQAVDSYNQRPEVQNAFRLLSADPEPGPGVDLSTLRALNFTIMETECTPSARLPVDDCDFKENGVIRDCSGPVSVLQDTPEINLRCRDASSDPVLVQRGRFGRFLRKIRRFRPKVTITIQGSARFG
Protein: Mastoparan-like PMM (Mastoparan-like peptide PMM2) (P85874)
Organism: Polistes major (Neotropical social wasp)
Subcellular location: Secreted {ECO:0000269|PubMed:17559065}. Target cell membrane {ECO:0000305}. Note=Assumes an amphipathic alpha-helical conformation in a membrane-like environment. {ECO:0000305|PubMed:18375018}.
Interaction partners:
Sequence:
INWKKIASIGKEVLKAL
Protein: Regulator of V-ATPase in vacuolar membrane protein 1 (Suppression of the onset of impotence protein 3) (P47104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RAVE complex, which is required for stable assembly of the vacuolar ATPase complex V-ATPase under many conditions. Required for transport between the early endosome and the late endosome/prevacuolar compartment (PVC), suggesting that assembly of vacuolar ATPase at the early endosome is required for transport from the early endosome to the PVC.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:15090613}. Note=Probably membrane-associated, associates with high density membrane compartment like early endosomes.
Interaction partners:
- Suppressor of kinetochore protein 1
- Regulator of V-ATPase in vacuolar membrane protein 2
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- Putative oligopeptide transporter YGL114W
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit C
- V-type proton ATPase subunit G
- V-type proton ATPase subunit D
Sequence:
MSLNFLPGRPNATPQTACQATWQNHTIFAYCSGNNLIILTNKFTRLQTIYTQSDCTAVDINSQNGFIALSFHNRVLIYKPIHQIMQNPKWTQCCQLFHDDTPVNCLRWSSDNELAIGSDFLSFWKIKDNFGVYQPILQWNQKQPKPVYNVIISQDSQLIVSIGKYDCNAKLWKRVSIVGEQAIFNLTMLPHPKPITAMRWKKEPDQVSKNNTASHALYTLCEDKVLRIWSCFEMEKNHTVQIWGEVPLSPTQKFCVIIDNWIIRQTLSVKDSEIFDISDSDIVILGSMTGEMEVLALNNLSQDPPKPMTKKTISHKKVKKATMLNDTRYLYLPEIQPYDNVKGKLSFLVHDLQGVIRHLLIDILQLINNKTEDLSAALEHKFTGHNKSVQKLVRSSDGEALLTTSRFSENGVWYPQKLNHGVSLRLQNTIQTESPIKFAVVHELGKQVICLLENGALQAWECPTNRKEDSEQKQSYLRVETRLKEEKKIHPIVMLNTPEPKHSHERHFTALIFSDGSIKAFEVSLTRGIFEVKSDSLDIDGDDIYKISIIDPVHQTFVSNRPLISLITKKGLTRTYKAIVNYNDRHVQWIKACEINTGIMNCTCIRGSSTGKLCIVNSTGKVMSLWDLNRGVLEYEETFHNPIEDIDWTSTEYGQSIVSIGFTGYALLYTQLRYDYTNNTPSYLPIEKIDITAHTAHNIGDSVWMKNGTFVVASGNQFYIKDKSLDLTDPFTYQSIGSRKILSNDILHLSSVLNGPLPVYHPQFLIQAIYANKLQLVKELLLRLFLALRKLDFESQDVSNLDSNLGMDPLKYFIAKDRDYPVESFPDPYPCFNKTVSLALTEQLTKTTLPYLTRHQQITLITVIEAVDEVTKNENIVDYNGVRFLLGVKLFLSHKNIQKSILMRDVSWALHSDNKEILLSSIDRHITSWNRAREYRIAYWIKEQDLVKKFEDIAKYEFSKDDKRDPSRCAIFYLALKKKQILLSLWKMAIGHPEQQKMVRFISNDFTVPRWRTAALKNAFVLLSKHRYMDAAVFFLLTDSLKDCVNVLCKQVHDMDLAIGVCRVYEGDNGPVLGELLTAQMLPETIKENDRWKASFIYWKLRKQEVAIKALLTAPIDLENNSSIVDKEVCVNRSFLVEDPALLYLYNHLRNRNLKYFIGSLNVEAKIECTLILRVTDILCRMGCNYLAVSLVKNWKFIERNSIPVQKLLKSPTKDRAYSAIGAMASEPISTARMRPSLFDKFGSPSASDIESPNPKLPNSLLDDFLQPPPNSTSSNSLAQSSSSAPRSILDEFVSPSYSQHKENLTPKAPNDSVGETDNSENRKDKLSKDILDDLSSQKPQKPKKSAITKNLLDDFV
Protein: Heat shock protein SSA2 (P10592)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
Subcellular location: Cytoplasm. Secreted, cell wall.
Interaction partners:
- Mitochondrial protein import protein MAS5
- Heat shock protein SSA1
- Protein SIS1
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Heat shock protein STI1
- Heat shock transcription factor
- Heat shock protein 104
- J domain-containing protein APJ1
- Hsp70 nucleotide exchange factor FES1
Sequence:
MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANPIMSKLYQAGGAPEGAAPGGFPGGAPPAPEAEGPTVEEVD
Protein: Uncharacterized protein DKFZp547I014 (Q53RC5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPKVKKEAPGPPKAEAKAKALKAKKVVLKGVHGHKKKKIRMSPTFQRPKTLRLWRPPRYPRKTTPRRNKLDHYAIIKFPLTTEFAMKKIKDNNTLVFTVDVKANKHQIKQAVKKLCDIDGAKVNTLMER
Protein: Metabotropic glutamate receptor 7 (mGluR7) (Q14831)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor activated by glutamate that regulates axon outgrowth through the MAPK-cAMP-PKA signaling pathway during neuronal development. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase that it inhibits.
Subcellular location: Cell membrane {ECO:0000269|PubMed:33500274}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Metabotropic glutamate receptor 2
- PRKCA-binding protein
- Metabotropic glutamate receptor 8
- Glutamate receptor ionotropic, kainate 1
- Metabotropic glutamate receptor 4
- Glutamate receptor 2
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 5
- Ras GTPase-activating-like protein IQGAP2
- Glutamate receptor 4
Sequence:
MVQLRKLLRVLTLMKFPCCVLEVLLCALAAAARGQEMYAPHSIRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNVWFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVCPEMEQAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTSNPGYRLIGQWTDELQLNIEDMQWGKGVREIPASVCTLPCKPGQRKKTQKGTPCCWTCEPCDGYQYQFDEMTCQHCPYDQRPNENRTGCQDIPIIKLEWHSPWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRVFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVFIWFGVDPPNIIIDYDEHKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSFKAVVTAATMSSRLSHKPSDRPNGEAKTELCENVDPNSPAAKKKYVSYNNLVI
Protein: Serine/threonine-protein phosphatase 4 catalytic subunit A (PP4C-A) (EC 3.1.3.16) (A8WGP3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein phosphatase that regulates many processes such as microtubule organization at centrosomes.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- Immunoglobulin
- Protein phosphatase 4, regulatory subunit 1-like.
- Double C2-like domain-containing protein alpha isoform X2
- Kinesin-like protein KIF22
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Protein yippee-like 3
- Proline-rich transmembrane protein 2
- Aspartate beta-hydroxylase domain-containing protein 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 2-A
Sequence:
MCVIMGDFTDLDRQIEQLRRCELIKENEVKALCAKAREILVEESNVQSVDSPVTVCGDIHGQFYDLKELFRVGGEVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFFDECHRKYGSATVWRYCTEIFDYLSLSAIVDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDISMICRAHQLVMEGYKWHFNDTVLTVWSAPNYCYRCGNVAAILELDEHLQKEFIIFEAAPQETRGLPSKKPVADYFL
Protein: Protein Wnt (Q0P406)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MLDGHLLLGWLSFTIIVHLISLPGPSTAYFGLTGNEPLSILPLTSQPDERAGKSHYKLCDRLKLEKKQRRMCRYRANILKRGFKETAFLYAISSAGLTHAMAKACSAGRMERCTCDEAPDLENRKAWQWGGCGDNLKYSNKFVKDFLGKRSNKDLRARIDMHNSNVGMKVIKTGVETTCKCHGVSGSCTVQTCWRQLAPFHEIGKQLKQRYETSVKVASSTNEATGEGEISQSRSQSQQPPQPDIPRTPDLLHIEDSPSFCRPSKYSAGTLARKCYKDKNCEAICCGRGHNTQSRVVTRPCQCQVRWCCYVECKQCTQKEEVYTCKG