wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL18m (39S ribosomal protein L18, mitochondrial) (L18mt) (MRP-L18) (Q3ZBR7)
Organism: Bos taurus (Bovine)
Function: Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9H0U6}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL62
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein mS25
- Large ribosomal subunit protein uL4m
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL55
Sequence:
MALRSRSWELLPVCRNPGCRVAAFSTSAKPVVKPEADPVGNEAVAPEFTNRNPRNLELLAVARKERGWGTVWPSREFWHRLRVIRSQHHIEALVEHRNGQVVVSASTREWAIKKHLYSTKSVVACESVGRVLAQRCLEAGINFMVYQPTPWEAASDSMKRLQIGMIEGGVVLQEPRRIYE
Protein: Bruchpilot, isoform G (A8DY79)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MSRDDYNPVTSSGVRSPGRVRRLQELPTVDRSPSRDYGAPRGSPLAMGSPYYRDMDEPTSPAGAGHHRSRSASRPPMAHAMDYPRTRYQSLDRGGLVDPHDREFIPIREPRDRSRDRSLERGLYLEDELYGRSARQSPSAMGGYNTGMGPTSDRAYLGDLQHQNTDLQRELGNLKRELELTNQKLGSSMHSIKTFWSPELKKERALRKEESAKYSLINDQLKLLSTENQKQAMLVRQLEEELRLRMRQPNLEMQQQMEAIYAENDHLQREISILRETIKDLECRVETQKQTLIARDESIKKLLEMLQAKGMGKEEERQMFQQMQAMAQKQLDEFRLEIQRRDQEILAMAAKMKTLEEQHQDYQRHIAVLKESLCAKEEHYNMLQTDVEEMRARLEEKNRLIEKKTQGTLQTVQERNRLTSELTELKDHMDIKDRKISVLQRKIENLEDLLKEKDNQVDMARARLSAMQAHHSSSEGALTSLEEAIGDKEKQMAQLRDQRDRAEHEKQEERDLHEREVADYKIKLRAAESEVEKLQTRLERAVTERERLEIKLEASQSELGKSKAELEKATCEMGRSSADWESTKQRIARLELENERLKHDLERSQNVQKLMFETGKISTTFGRTTMTTSQELDRAQERADKASAELRRTQAELRVTQSDAERAREEAAALQEKLEKSQGEVYRLKAKLENAQGEQESLRQELEKAQSGVSRIHADRDRAFSEVEKIKEEMERTQATLGKSQLQHEKLQNSLDKAQNEVDHLQDKLDKACTENRRLVLEKEKLTYDYDNLQSQLDKALGQAARMQKERETLSLDTDRIREKLEKTQVQLGRIQKERDQFSDELETLKERSESAQTLLMKAARDREAMQTDLEVLKERYEKSHAIQQKLQMERDDAVTEVEILKEKLDKALYASQKLIDEKDTSNKEFEKMLEKYDRAQNEIYRLQSRCDTAEADRARLEVEAERSGLAASKAREDLRKLQDESTRLQEACDRAALQLSRAKECEDNARSELEHSRDRFDKLQTDIRRAQGEKEHFQSELERVTYELERAHAAQTKASASVEAAKEEAAHYAVELEKMRDRYEKSQVELRKLQDTDTFGRETRRLKEENERLREKLDKTLMELETIRGKSQYESESFEKYKDKYEKIEMEVQNMESKLHETSLQLELSKGEVAKMLANQEKQRSELERAHIEREKARDKHEKLLKEVDRLRLQQSSVSPGDPVRASTSSSSALSAGERQEIDRLRDRLEKALQSRDATELEAGRLAKELEKAQMHLAKQQENTESTRIEFERMGAELGRLHDRLEKAEAEREALRQANRSGGAGAAPHPQLEKHVQKLESDVKQLAMEREQLVLQLEKSQEILMNFQKELQNAEAELQKTREENRKLRNGHQVPPVAAPPAGPSPAEFQAMQKEIQTLQQKLQESERALQAAGPQQAQAAAAAGASREEIEQWRKVIEQEKSRADMADKAAQEMHKRIQLMDQHIKDQHAQMQKMQQQMQQQQQAAQQAVQQAAQQQQSAAGAGGADPKELEKVRGELQAACTERDRFQQQLELLVTELEKSKMSNQEQAKQLQTAQQQVQQLQQQVQQLQQQMQQLQQAASAGAGATDVQRQQLEQQQKQLEEVRKQIDNQAKATEGERKIIDEQRKQIDAKRKDIEEKEKKMAEFDVQLRKRKEQMDQLEKSLQTQGGGAAAAGELNKKLMDTQRQLEACVKELQNTKEEHKKAATETERLLQLVQMSQEEQNAKEKTIMDLQQALKIAQAKVKQAQTQQQQQQDAGPAGFLKSFF
Protein: Protein spinster homolog 1 (Protein not really started) (Spinster-like protein) (Spns1) (Q7ZU13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Mediates the rate-limiting, proton-dependent, lysosomal efflux of lysophospholipids. Selective for zwitterionic headgroups such as lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE). Essential player in lysosomal homeostasis. Critical for embryogenesis. Involved in the regulation of developmental senescence.
Subcellular location: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Major facilitator superfamily domain-containing 9.
- PX domain-containing protein.
- SV2-related protein a.
- Putative transporter SVOPL
- Protein unc-93 homolog A
- Major facilitator superfamily domain-containing 13A
Sequence:
MSQADADITPFFADDNEGEGPVENGVGSPLPEDEEEESPSGVTDRRAIMTVIVLCYINLLNYMDRFTVAGVLPDIEHFFGIGDGTSGLLQTVFICSYMFLAPLFGYLGDRYNRKLIMCVGIFFWSVVTLASSFIGKDHFWALLLTRGLVGVGEASYSTIAPTIIADLFVKEKRTNMLSIFYFAIPVGSGMGYIVGSKVDTVAKDWHWALRVTPGLGLLAVFLLMLVVQEPKRGAIEAHPEHTLHRTSWLADMKALCRNPSFILSTFGFTAVAFVTGSLALWAPAFLFRAGVFTGVKQPCFKAPCDDSDSLIFGAITVVTGILGVASGVQASKLLRTRTPRADPLVCAAGLLLAAPFLYLSIMFAQASTVATYVFIFLGETFLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAISPYLIGVVSDSIKESNSYMWEFRSLQMSLLLCSFVAVAGGAFFLATAVFIEKDRDLAENYVPSDDAPIVVPRSGRSTKVSVSSVLI
Protein: Precursor of CEP4 (PCEP4) [Cleaved into: C-terminally encoded peptide 4 (CEP4)] (Q3EBM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that represses primary root growth rate. Promotes shoot growth and modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 4]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- Precursor of CEP8
- AT3G14830 protein
- Epstein-barr nuclear antigen
- Precursor of CEP15
- Precursor of CEP14
- Precursor of CEP6
- Precursor of CEP7
- Precursor of CEP13
- Precursor of CEP9
- Protein IDA-LIKE 5
Sequence:
MVSRGCSITVLFRFLIVLLVIQVHFENTKAARHAPVVSWSPPEPPKDDFVWYHKINRFKNIEQDAFRPTHQGPSQGIGHKNPPGAP
Protein: T. brucei spp.-specific protein (Q38B03)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAKKTTKKKQTTSERAASAETQGRKAGRGALSKFEEFDVSQVLQKEQESQQVAVQVDGQPDVAASGEIAPLVSTTSEQVRVGMACEGDAAAGEGAADPTAAPLAIPQLIPPEPPIEVPADDELVPLPTLQVVPMMNRTAEAQCGLLKEPAPPTTIRRVTQPGAPAPAMPTSLMELLCS
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (Q38BV6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pyruvate kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Transketolase
- Fructose-bisphosphate aldolase
- Pyruvate, phosphate dikinase
- phosphoenolpyruvate carboxykinase
- Transaldolase
- Enolase, putative
- Nucleolar GTP-binding protein 2
Sequence:
MTIQKVHGREVLDSRGNPTVEVEVTTERGVFRSAVPSGASTGVYEACELRDGDKKRYVGKGCLQAVKNVNEVIGPALIGRDELKQEELDTLMLRLDGTPNKGKLGANAILGCSMAISKAAAAAKGVPLYRYLASLAGTKELRLPVPCFNVINGGKHAGNALPFQEFMIAPVKATSFSEALRMGSEVYHSLRGIIKKKYGQDAVNVGDEGGFAPPIKDINEPLPILMEAIEEAGHRGKFAICMDCAASETYDEKKQQYNLTFKSPEPTWVTAEQLRETYCKWAHDYPIVSIEDPYDQDDFAGFAGITEALKGKTQIVGDDLTVTNTERIKMAIEKKACNSLLLKINQIGTISEAIASSKLCMENGWSVMVSHRSGETEDTYIADLVVALGSGQIKTGAPCRGERTAKLNQLLRIEEELGAHAKFGFPGWS
Protein: Pseudin-2 (P83189)
Organism: Pseudis paradoxa (Paradoxical frog)
Function: Antimicrobial peptide with activity against fungus (C.albicans) and Gram-positive and Gram-negative bacteria (S.aureus and E.coli). Also has low hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:11689009}.
Interaction partners:
Sequence:
GLNALKKVFQGIHEAIKLINNHVQ
Protein: Skp1-related protein (G5EDD8)
Organism: Caenorhabditis elegans
Interaction partners:
- Cullin-1
- Cullin-6
- F-box/WD repeat-containing protein lin-23
- RING-box protein 1
- Uncharacterized protein T27F2.1
- F-box domain-containing protein
- DUF38 domain-containing protein
Sequence:
MADQKEASEAAKNREIKISSSDDEIFLVPRNVIRLSNTLNTLLVDLGLDDDEGTNAEPIPVQNVTASILKKVINWCTKHQSDPIPTEDSEKKTDGSIQDWDKKFLDIDQGTLFELILAANYLDIKGLLDVACQSVANMIKGKSPDEIRRAFNIKDDFTAEEREQIRKENAWCDD
Protein: DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68) (WD repeat-containing protein An11 homolog) (P61962)
Organism: Homo sapiens (Human)
Function: Involved in craniofacial development. Acts upstream of the EDN1 pathway and is required for formation of the upper jaw equivalent, the palatoquadrate. The activity required for EDN1 pathway function differs between the first and second arches (By similarity). Associates with DIAPH1 and controls GLI1 transcriptional activity. Could be involved in normal and disease skin development. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Subcellular location: Cytoplasm. Nucleus. Note=Overexpression of DIAHP1 or active RHOA causes translocation from the nucleus to cytoplasm.
Interaction partners:
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- DNA damage-binding protein 1
- Paired box protein Pax-6
- Dual specificity tyrosine-phosphorylation-regulated kinase 1B
- Cullin-4B
- Cullin-4A
- DET1- and DDB1-associated protein 1
- Homeodomain-interacting protein kinase 2
- DNA excision repair protein ERCC-8
- Activating molecule in BECN1-regulated autophagy protein 1
Sequence:
MSLHGKRKEIYKYEAPWTVYAMNWSVRPDKRFRLALGSFVEEYNNKVQLVGLDEESSEFICRNTFDHPYPTTKLMWIPDTKGVYPDLLATSGDYLRVWRVGETETRLECLLNNNKNSDFCAPLTSFDWNEVDPYLLGTSSIDTTCTIWGLETGQVLGRVNLVSGHVKTQLIAHDKEVYDIAFSRAGGGRDMFASVGADGSVRMFDLRHLEHSTIIYEDPQHHPLLRLCWNKQDPNYLATMAMDGMEVVILDVRVPCTPVARLNNHRACVNGIAWAPHSSCHICTAADDHQALIWDIQQMPRAIEDPILAYTAEGEINNVQWASTQPDWIAICYNNCLEILRV
Protein: Wide awake, isoform B (Wide awake, isoform F) (Q9VCW7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFLLPHSRTDSQSNSQSQLCISRHSQPKNAKLRDDHDETGSSELDSPPLGDENASANGQLSVHRQPVQLRSKIPGNTPHPRASKMSKKQLKLAQAQLDKLTQNNLHLHALFSAVEHGHLEKARTILESTDVDVNSINNDGLSALDLAVLSNNRSMTRMLLQHGAVEGSQFSVDTIGTKLNGLLKDAESRIHDLSGPEGLCPPVFASRPSISSIIIGNSSASVTGCTGSEVEKQIGIWERRVKGLRRLQLGWDQARPPDAPASVVVDVTGDNSISVQILEPFEGAIGTKFKVQWSTRADFNNVVGESELLEWISFHGTMGAQCHISGLTQGRRYFLRAACGNVKGWGTYRTSVPASVVPSTWRDLDNREDRFVGRHRILDNLFTAVRLARPADVSELTLDPASAQRRNPKKKTTIKQLFSVTTKFQKTLRRGIYFSCIIHCDDKVLVTSEDFPPVIEVDESYPSALHMDYYWLMKVACTWEDVKSLRSDMERNLTSAVHFRTKLLSAVCQMQSALGITDLGQLYYKPLRDAQGTVVLTCVQSVKSQKAVSILNSRWVPVSKLQKKLGALHEDYTINELLISSIGDQLHYQQAALQRLEPGLYLGYLKMQCSIDQIQVVVPVKTPNVLPHCKVRENSHITAEEWQVLHRYSSDPLRLPLDFSAQGGDGASGATATTEVQRLFLYDLTNAMHKLFASMNIKIADATTHRLYDVEVIEHSPDISFLVVCPSAESSCAVPGQSELLLQRDDLASLSIQAFEMIHLRTYQPAIIQKYARLSCILELDTALATHSLREAFSSSELQAAKERLATLQELSASLTIVWKSVRWLMDVVAYARNKNAQPSLAMREILDFAQQRQDEAVATSAGGSANKQLLQLPIRESKFSKTGQGRGSWPGPGTSEDQSQNKPEHSKSEQNLELSAITPVEPASNQVPTQQQQPQQQSQQQQLLQVSNISEYAGSICSEVSFRKNSGDSMSSTYTSRSFYSAVDSASDGNSTNSVFAIPPSRSDDTLADALRHSQAVAAQRKRTSSNIASHTNPLITVHSSSSAPYLAGSSVSLRSGNGAFATDLEHKPLKPATKAASSANLREGGPYLKSTLAELRAVGGEEPVASTSKASSMKSLSRQSSEEDSASCSSLNAEQTSGIIQVYTAYSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMAVVLKGNNGPIYGPEMLENFCLVAVIGARERCLRDDFKPLQLQNPWKKGRLYVRKKHELLAAIEHSNRKSHLI
Protein: Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH 1) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (Q6GIL8)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MAVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQGRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYTDKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASCTTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARAAAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEKQDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMSVGDRQLVKVAAWYDNEMSYTAQLVRTLAYLAELSK
Protein: Protein SNORC (Secondary ossification center-associated regulator of chondrocyte maturation protein) (Q6UX34)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of chondrocyte maturation and postnatal endochondral ossification. May inhibit cell growth stimulation induced by FGF2.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9CXL7}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9CXL7}. Note=Appears as reticular-like structures throughout the cytoplasm and adjacent to the plasma membrane. In proliferation and hypertrophic chondrocytes, detected intracellulary and in the pericellular extracellular matrix. In primary spongiosa, detected only in the extracellular matrix. {ECO:0000250|UniProtKB:Q9CXL7}.
Interaction partners:
Sequence:
MASCLALRMALLLVSGVLAPAVLTDDVPQEPVPTLWNEPAELPSGEGPVESTSPGREPVDTGPPAPTVAPGPEDSTAQERLDQGGGSLGPGAIAAIVIAALLATCVVLALVVVALRKFSAS
Protein: DEK oncogene (DNA binding), isoform CRA_b (DEK proto-oncogene) (H0Y993)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKEVNISVFQV
Protein: Metabotropic GABA-B receptor subtype 3, isoform A (Metabotropic GABA-B receptor subtype 3, isoform D) (Metabotropic GABA-B receptor subtype 3, isoform E) (Metabotropic GABA-B receptor subtype 3, isoform G) (Q9VPS7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- IP03705p
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MRIIQPVQGTRYGPWPAVGLRLVLALAWATSAAAAMESSAELQALGYEAIRPGAASISTSSPSSSPPGESASTVTAGGTPIPPRSDWKYKRTKVKRRQQRLNSHSNLPGSTNASHAHHLLNLPPRQRYLKVNQVFESERRMSPAEMQRNHGKIVLLGLFELSTSRGPRPDGLSELGAATMAVEHINRKRLLPGYTLELVTNDTQCDPGVGVDRFFHAIYTQPSTRMVMLLGSACSEVTESLAKVVPYWNIVQVSFGSTSPALSDRREFPYFYRTVAPDSSHNPARIAFIRKFGWGTVTTFSQNEEVHSLAVNNLVTELEAANISCAATITFAATDFKEQLLLLRETDTRIIIGSFSQELAPQILCEAYRLRMFGADYAWILHESMGAPWWPDQRTACSNHELQLAVENLIVVSTHNSIVGNNVSYSGLNNHMFNSQLRKQSAQFHGQDGFGSGYGSRISIAATQSDSRRRRRRGVGGTSGGHLFPEAISQYAPQTYDAVWAIALALRAAEEHWRRNEEQSKLDGFDYTRSDMAWEFLQQMGKLHFLGVSGPVSFSGPDRVGTTAFYQIQRGLLEPVALYYPATDALDFRCPRCRPVKWHSGQVPIAKRVFKLRVATIAPLAFYTIATLSSVGIALAIAFLAFNLHFRKLKAIKLSSPKLSNITAVGCIFVYATVILLGLDHSTLPSAEDSFATVCTARVYLLSAGFSLAFGSMFAKTYRVHRIFTRTGSVFKDKMLQDIQLILLVGGLLLVDALLVTLWVVTDPMERHLHNLTLEISATDRSVVYQPQVEVCRSQHTQTWLSVLYAYKGLLLVVGVYMAWETRHVKIPALNDSQYIGVSVYSVVITSAIVVVLANLISERVTLAFITITALILTSTTATLCLLFIPKLHDIWARNDIIDPVIHSMGLKMECNTRRFVVDDRRELQYRVEVQNRVYKKEIQALDAEIRKLERLLESGLTTTSTTTSSSTSLLTGGGHLKPELTVTSGISQTPAASKNRTPSISGILPNLLLSVLPPVIPRASWPSAEYMQIPMRRSVTFASQPQLEEACLPAQDLINLRLAHQQATEAKTGLINRLRGIFSRTTSSNKGSTASLADQKGLKAAFKSHMGLFTRLIPSSQTASCNAIYNNPNQDSIPSEASSHPNGNHLKPIHRGSLTKSGTHLDHLTKDPNFLPIPTISGGEQGDQTLGGKYVKLLETKVNFQLPSNRRPSVVQQPPSLRERVRGSPRFPHRILPPTCSLSALAESEDRPGDSTSILGSCKSIPRISLQQATSGGTWKSMETAGKSRLSLGDSQEEEQQAPANGTE
Protein: Tissue alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucosidase I) (Alpha-L-fucoside fucohydrolase 1) (Alpha-L-fucosidase 1) (P17164)
Organism: Rattus norvegicus (Rat)
Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P04066}.
Interaction partners:
- Plasma alpha-L-fucosidase
- Beta-galactosidase
- Alpha-galactosidase
Sequence:
MWDLKSEWWAVGFGLLLLLAASAQAGGLAPHHYTPDWPSLDSRPLPRWFDEAKFGLFVHWGVYSVPAWGSEWFWWHWQGEQSSAYVRFMKENYPPGFSYADFAPQFTARFFHPEEWADLFQAAGAKYVVLTAKHHEGFTNWPSAVSWNWNSKDVGPHRDLVGELGAAVRKRNIRYGLYHSLFEWFHPLYLLDKKNGLKTQHFVSTKTMPELYDLVNRYKPDLIWSDGEWECPDSYWNSTEFLAWLYNESPVKDQVVVNDRWGQNCSCRHGGYYNCEDKYRPHSLPDHKWEMCTSVDKASWGYRRDMSMSTIVDENEIIEELVQTISLGGNYLLNIGPNKDGVIVPIFQERLLAVGKWLQINGEAIYASKPWRVQSERNKTVVWYTTKDSAVYATFLHWPEDGVVNLQSPKMTSATKITMLGMEGELHWTQDPLEGVLITLPQLPPGTFPVESAWTLKLTKVN
Protein: Ceramide transfer protein (Collagen type IV alpha-3-binding protein) (Q9Y128)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- LD30122p
- Steroidogenic acute regulatory protein-like
Sequence:
MDTNAGESLGASPPSSNEAAAGSQSQSDASEEEEYLDNSIELRGYLSKWTNYIYGWQPRYIVLKDGTLSYYKSESESDFGCRGAISLTKATIKAHESDELRFDVVVNNLNNWCLRAETSEDRMHWVDVLQLYKADSGSTDTTSLRRHGSTMSLQSNTISLTSGGSLKKTQRNLREKVGELETFKDILFGQIETLQRYFDACSEVNKNNAQPLDLGDGLKSIDFKGESITFRATTSGVLTTLQHCLEIIAESDESWKRKLEREIDKRRRSEDQSKKLKDEVEKMKRLSYPGPDFEEGPHSTLPEDEFFDAVETGLDKIEEDMQLRFKLKLQSQISQTLVNVPHEAVAEGEEAREEFGTGAEATSHALWPEIDRVCKEQLHYAREGVGQDGNGWQIFADEGEIKMYKREEEVNGLVMDPLKAYHTVQGVTAREMCHYFFMPEFRNDWETTLEDCTILEKISADTLLFLQTHKRIWPASQRDAQFWSHMRKITDNLEPGARDMWVVCNNSTEYAKQESKNGKCVRIFLTVILACQTHLPEGYVKGQPLNRNDLTCKITYCSVVNPGGWAPASALRAVYKREYPKFLKRFTGYVIDQCKDKPIMF
Protein: V-type proton ATPase subunit E (V-ATPase subunit E) (V-ATPase 27 kDa subunit) (Vacuolar proton pump subunit E) (P22203)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit c
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B
Sequence:
MSSAITALTPNQVNDELNKMQAFIRKEAEEKAKEIQLKADQEYEIEKTNIVRNETNNIDGNFKSKLKKAMLSQQITKSTIANKMRLKVLSAREQSLDGIFEETKEKLSGIANNRDEYKPILQSLIVEALLKLLEPKAIVKALERDVDLIESMKDDIMREYGEKAQRAPLEEIVISNDYLNKDLVSGGVVVSNASDKIEINNTLEERLKLLSEEALPAIRLELYGPSKTRKFFD
Protein: Cytochrome b-c1 complex subunit 7 (B2RYS2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b
- Ubiquinol-cytochrome c reductase, complex III subunit X.
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MAGRPAVAASSKWLDGFRKWYYNAAGFNKLGLMRDDTMHETEDVKEAIRRLPENLYNDRMFRIKRALDLSMRHQILPKDQWTKYEEDKFYLEPYLKEVIRERKEREEWAKK
Protein: Transcription factor TGAL4 (bZIP transcription factor 79) (OsbZIP79) (Q53Q70)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR3
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- BTB/POZ domain and ankyrin repeat-containing protein NPR2
- BTB/POZ domain and ankyrin repeat-containing protein NPR5
Sequence:
MGEASSSSGHPRQNPHVLGYGFHGAMPNSLPSANLFEQQGGANYFGELEEALMQQVATLRRTQQTATTTSTLHHGDTTPFSTTATAAATARPPPTLDIFPSWPMRSLHTPKEGSNVTADTTDSESSSKNNSNQNASSDQHVLVGDMAGQFDQIPQQEQHKKMATNSPTHSSKTGKALDPKTMRRLAQNREAARKSRLRKKAYIQQLESSKLKLAQMEQDIHRARSQGLLLGAPGGNTSSGAAMFDVDYARWLEEDSQRMAELHGGLHAHLPDSDLRAIVDDTLTHYDHLFNLKGMAAKADVFHLITGMWATPAERCFLWMGGFRPSELLKTLTPQLDPLTEQQVVGICNLQQSSQQAEEALSQGLDQLHQSLAETVAGGSPLDDPNVGSFMGHMAIALGQLSNLEGFVIQADNLRQQTIHQMHRILTVRQAARCFLAIGEYHNRLRALSSLWASRPREILVADEGNCGELSIAAHPSESQYSAF
Protein: Tubulin beta chain (Q4TZT6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MREILHIQGGQCGNQIGAKFWEVVCAEHGIDSTGRHGGDSELQLERINVYYNEASCGRFVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENANECMVLDNGSFFQICFRTLKLVTPSFGDLSHLISAAMSGVTCCFRFAGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGRMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSTVCDIPPIGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADDEEYEEEEEYEAEA
Protein: Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1) (P78552)
Organism: Homo sapiens (Human)
Function: Binds with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-4 receptor subunit alpha
- Interleukin-13
- Interleukin-4
- Non-receptor tyrosine-protein kinase TYK2
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Interleukin-13 receptor subunit alpha-2
- Signal transducer and activator of transcription 6
- Tyrosine-protein kinase JAK3
- Interleukin-5
Sequence:
MEWPARLCGLWALLLCAGGGGGGGGAAPTETQPPVTNLSVSVENLCTVIWTWNPPEGASSNCSLWYFSHFGDKQDKKIAPETRRSIEVPLNERICLQVGSQCSTNESEKPSILVEKCISPPEGDPESAVTELQCIWHNLSYMKCSWLPGRNTSPDTNYTLYYWHRSLEKIHQCENIFREGQYFGCSFDLTKVKDSSFEQHSVQIMVKDNAGKIKPSFNIVPLTSRVKPDPPHIKNLSFHNDDLYVQWENPQNFISRCLFYEVEVNNSQTETHNVFYVQEAKCENPEFERNVENTSCFMVPGVLPDTLNTVRIRVKTNKLCYEDDKLWSNWSQEMSIGKKRNSTLYITMLLIVPVIVAGAIIVLLLYLKRLKIIIFPPIPDPGKIFKEMFGDQNDDTLHWKKYDIYEKQTKEETDSVVLIENLKKASQ