wanglab/gogpt-training-data huggingface dataset:
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTB5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Ribosome-associated molecular chaperone SSB
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Transcription factor
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQAAMNPHNTVFDAKRLIGRNFNDNEVQTDAKHFPFKLVDVDGKPQIEVEFKGETKKFTPEQISSMVLGKMKETAEQFLGSAVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGGEENVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFKRKNKKDLSSNQRAMRRLRTACERAKRTLSSSAQTSIEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDSKLDKSAVHEIVLVGGSTRIPKVQKLVTDFFNGKEPNRSINPDEAVAYGAAVQAAILTGDQSSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEIFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIERMVAEAEKFKEEDEKESERIASKNQLESIAYSLKSSISEAGDKLEEADKEAVSKKAEEVIQWLDNNTTATKEEYDDQLKELQEIANPIMTKLYQAGGAPGGAGAAGGFPGGAPPAPEAEGPTVEEVD
Protein: Beta-galactosidase (EC 3.2.1.23) (Acid beta-galactosidase) (Lactase) (P23780)
Organism: Mus musculus (Mouse)
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P16278}.
Interaction partners:
- Lysosomal protective protein
- N-acetylgalactosamine-6-sulfatase
- Alpha-galactosidase A
- Lysosomal acid glucosylceramidase
- Lactase/phlorizin hydrolase
- Beta-hexosaminidase subunit beta
- Sialidase-1
- Beta-hexosaminidase subunit alpha
- Galactose mutarotase
- N-acetylglucosamine-6-sulfatase
Sequence:
MLRVPLCTPLPLLALLQLLGAAHGIYNVTQRTFKLDYSRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLKMKMAGLNAIQMYVPWNFHEPQPGQYEFSGDRDVEHFIQLAHELGLLVILRPGPYICAEWDMGGLPAWLLEKQSIVLRSSDPDYLVAVDKWLAVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDYDYLRFLVHRFRYHLGNDVILFTTDGASEKMLKCGTLQDLYATVDFGTGNNITQAFLVQRKFEPKGPLINSEFYTGWLDHWGKPHSTVKTKTLATSLYNLLARGANVNLYMFIGGTNFAYWNGANTPYEPQPTSYDYDAPLSEAGDLTKKYFALREVIQMFKEVPEGPIPPSTPKFAYGKVALRKFKTVAEALGILCPNGPVKSLYPLTFTQVKQYFGYVLYRTTLPQDCSNPKPIFSSPFNGVRDRAYVSVDGVPQGILDRNLMTALNIRGKAGATLDILVENMGRVNYGRFINDFKGLISNMTINSTVLTNWTVFPLNTEAMVRNHLWGREASDEGHLDGRSTSNSSDLILPTFYVGNFSIPSGIPDLPQDTFIQFPGWSKGQVWINGFNLGRYWPTMGPQKTLFVPRNILTTSAPNNITVLELEFAPCSEGTPELCTVEFVDTPVIS
Protein: Uncharacterized protein P27G11.16 (Q9C109)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MGSCLRFFKQGAILHENNTNFTERSSSVFFECNPCYSIEKLKSNRILIAVRLFSFAFSSFSTTLRILRDFIIAASKCEFEKIWSTTFSISFLSFNFKSSESPSL
Protein: Nuclear factor of activated T cells 3 (H3BRS1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XLDDRRPITLCVCVRARVCDLEPDDCASIYIFNVDPPPSTLTTPLCLPHHGLPSHSSVLSPSFQLQSHKNYEGTCEIPESKYSPLGGPKPFECPSIQITSISPNCHQELDAHEDDLQINDPEREFLERPSRDHLYLPLEPSYRESSLSPSPASSISSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEETWHQQYGLGHSLSPRQSPCHSPRSSVTDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLNASVHGGSGLGPAVFPFQYCVETDIPLKTRKTSEDQAAILPGKLELCSDDQGSLSPARETSIDDGLGSQYPLKKDSCGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPAHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYNEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMVVTGSNFLPESKIIFLEKGQDGRPQWEVEGKIIREKCQGAHIVLEVPPYHNPAVTAAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDVNEIIGRDMSQISVSQGAGVSRQAPLPSPESLDLGRSDGL
Protein: NADH-quinone oxidoreductase subunit D (EC 7.1.1.-) (NADH dehydrogenase I subunit D) (NDH-1 subunit D) (P9WJH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit N
Sequence:
MTAIADSAGGAGETVLVAGGQDWQQVVDAARSADPGERIVVNMGPQHPSTHGVLRLILEIEGETVVEARCGIGYLHTGIEKNLEYRYWTQGVTFVTRMDYLSPFFNETAYCLGVEKLLGITDEIPERVNVIRVLMMELNRISSHLVALATGGMELGAMTPMFVGFRAREIVLTLFEKITGLRMNSAYIRPGGVAQDLPPNAATEIAEALKQLRQPLREMGELLNENAIWKARTQGVGYLDLTGCMALGITGPILRSTGLPHDLRKSEPYCGYQHYEFDVITDDSCDAYGRYMIRVKEMWESMKIVEQCLDKLRPGPTMISDRKLAWPADLQVGPDGLGNSPKHIAKIMGSSMEALIHHFKLVTEGIRVPAGQVYVAVESPRGELGVHMVSDGGTRPYRVHYRDPSFTNLQSVAAMCEGGMVADLIAAVASIDPVMGGVDR
Protein: Cytochrome b561 and DOMON domain-containing protein At4g12980 (Protein b561A.tha15) (Q9SV71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a catecholamine-responsive trans-membrane electron transporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g03540
- Filament-like plant protein 2
- At2g45180
- Kinesin-like protein KIN-5A
- 65-kDa microtubule-associated protein 4
- TSK-associating protein 1
- Microtubule-associated protein RP/EB family member 1C
- Protein ENDOSPERM DEFECTIVE 1
- Kinesin-like protein KIN-12A
- tRNA
Sequence:
MDSSYLRISLSFLFWALLLSPAVSQSSSCSSQTFSGVKSYPHCLDLPDLKAILHYSYDASNTTLAVVFSAPPSKPGGWIAWAINPKSTGMAGSQALVASKDPSTGVASVTTLNIVSYSSLVPSKLSFDVWDVKAEEAANDGGALRIFAKVKVPADLAASGKVNQVWQVGPGVSNGRIQAHDFSGPNLNSVGSLDLTGTTPGVPVSGGGGAGNSRIHKRNIHGILNAVSWGLLFPIGAMIARYMRIFESADPAWFYLHVSCQFSAYVIGVAGWATGLKLGSESKGIQYNTHRNIGICLFSIATLQMFAMLLRPRKDHKFRFVWNIYHHGVGYSILILGIINVFKGLSILNPKHTYKTAYIAVIGTLGGITLLLEVVTWVIVLKRKSAKSTKPLKA
Protein: Serine/arginine-rich splicing factor 5 (Delayed-early protein HRS) (Pre-mRNA-splicing factor SRP40) (Splicing factor, arginine/serine-rich 5) (Q13243)
Organism: Homo sapiens (Human)
Function: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.
Subcellular location: Nucleus.
Interaction partners:
- SRSF protein kinase 1
- Serine/arginine-rich splicing factor 11
- Serine/arginine-rich splicing factor 3
- Splicing factor U2AF 65 kDa subunit
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoprotein A1
- Pre-mRNA-splicing factor SLU7
- Splicing factor U2AF 35 kDa subunit
- Serine/arginine-rich splicing factor 7
- RNA-binding protein 25
Sequence:
MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHSRSRSRSRSRTRSSSRSRSRSRSRSRKSYSRSRSRSRSRSRSKSRSVSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN
Protein: Protein QUIRKY (Multiple C2 domain and transmembrane region protein 15) (B8XCH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in Ca 2(+)-dependent signaling and membrane trafficking. Plays a role in fruit dehiscence (Probable). Components of the machinery involved in organ development mediated by the receptor-like kinase STRUBBELIG (SUB).
Subcellular location: Cell membrane {ECO:0000269|PubMed:24173806, ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29259105}. Golgi apparatus membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Cell junction, plasmodesma {ECO:0000269|PubMed:25256344}.
Interaction partners:
- Protein STRUBBELIG
- Syntaxin-121
- Tetratricopeptide repeat
- CRS1 / YhbY
- At1g11210)
- C-terminal binding protein AN
- F28K20.8 protein
- Fas-binding factor-like protein
- Protein SODIUM POTASSIUM ROOT DEFECTIVE 1
- SWI-SNF-related chromatin binding protein
Sequence:
MNTTPFHSDPPPSRIQRKLVVEVVEARNILPKDGQGSSSAYVVVDFDAQKKRTSTKFRDLNPIWNEMLDFAVSDPKNMDYDELDIEVYNDKRFGNGGGRKNHFLGRVKIYGSQFSRRGEEGLVYFPLEKKSVFSWIRGEIGLKIYYYDEAADEDTAGGGGGQQQQQQQQQFHPPQQEADEQQHQQQFHPPPQQMMNIPPEKPNVVVVEEGRVFESAQSQRYTETHQQPPVVIVEESPPQHVMQGPNDNHPHRNDNHPQRPPSPPPPPSAGEVHYYPPEVRKMQVGRPPGGDRIRVTKRPPNGDYSPRVINSKTGGGETTMEKKTHHPYNLVEPMQYLFVRIVKARGLPPNESAYVKVRTSNHFVRSKPAVNRPGESVDSPEWNQVFALGHNRSDSAVTGATLEISAWDASSESFLGGVCFDLSEVPVRDPPDSPLAPQWYRLEGSGADQNSGRISGDIQLSVWIGTQVDEAFPEAWSSDAPHVAHTRSKVYQSPKLWYLRVTVLEAQDLHIAPNLPPLTAPEIRVKAQLGFQSARTRRGSMNNHSGSFHWHEDMIFVAGEPLEDCLVLMVEDRTTKEATLLGHAMIPVSSIEQRIDERFVPSKWHTLEGEGGGGGGGGGPGGGGGGGPYCGRISLRLCLEGGYHVLEEAAHVCSDFRPTAKQLWKPPIGILELGILGARGLLPMKAKNGGKGSTDAYCVAKYGKKWVRTRTITDSFDPRWHEQYTWQVYDPCTVLTVGVFDNWRMFSDASDDRPDTRIGKIRIRVSTLESNKVYTNSYPLLVLLPSGMKKMGEIEVAVRFACPSLLPDVCAAYGQPLLPRMHYIRPLGVAQQDALRGAATKMVAAWLARAEPPLGPEVVRYMLDADSHAWSMRKSKANWYRIVGVLAWAVGLAKWLDNIRRWRNPVTTVLVHILYLVLVWYPDLVVPTAFLYVVMIGVWYYRFRPKIPAGMDIRLSQAETVDPDELDEEFDTIPSSRRPEVIRARYDRLRILAVRVQTILGDFAAQGERIQALVSWRDPRATKLFIAICLVITIVLYAVPAKMVAVALGFYYLRHPMFRDTMPTASLNFFRRLPSLSDRLI
Protein: Possible beta-1,3-glucanase (O07242)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Glucanase
- Possible muconolactone isomerase
- Possible conserved membrane protein
- 1,4-beta-xylanase
Sequence:
MLMPEMDRRRMMMMAGFGALAAALPAPTAWADPSRPAAPAGPTPAPAAPAAATGGLLFHDEFDGPAGSVPDPSKWQVSNHRTPIKNPVGFDRPQFFGQYRDSRQNVFLDGNSNLVLRATREGNRYFGGLVHGLWRGGIGTTWEARIKFNCLAPGMWPAWWLSNDDPGRSGEIDLIEWYGNGTWPSGTTVHANPDGTAFETCPIGVDGGWHNWRVTWNPSGMYFWLDYADGIEPYFSVPATGIEDLNEPIREWPFNDPGYKVFPVLNLAVGGSGGGDPATGSYPQEMLVDWVRVF
Protein: Thiol:disulfide interchange protein TlpA (Cytochrome c biogenesis protein TlpA) (P43221)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: Involved in cytochrome aa3 assembly.
Subcellular location: Cell membrane; Single-pass type II membrane protein; Periplasmic side.
Interaction partners:
- Blr1131 protein
- Cytochrome c oxidase subunit 2
- Alkyl hydroperoxide reductase C
- Anti-oxidant protein
- Peptide methionine sulfoxide reductase MsrA
- Peptide methionine sulfoxide reductase MsrA
- Peptide methionine sulfoxide reductase MsrA
- Glutathione-dependent peroxiredoxin
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyl dehydrogenase
Sequence:
MLDTKPSATRRIPLVIATVAVGGLAGFAALYGLGLSRAPTGDPACRAAVATAQKIAPLAHGEVAALTMASAPLKLPDLAFEDADGKPKKLSDFRGKTLLVNLWATWCVPCRKEMPALDELQGKLSGPNFEVVAINIDTRDPEKPKTFLKEANLTRLGYFNDQKAKVFQDLKAIGRALGMPTSVLVDPQGCEIATIAGPAEWASEDALKLIRAATGKAAAAL
Protein: GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol dimannoside mannosyltransferase (EC 2.4.1.-) (Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (P0CF99)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Function: Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 6 of the alpha-1,6-linked mannose residue of the triacyl phosphatidylinositol dimannoside (Ac3PIM2) to generate triacyl phosphatidylinositol trimannoside (Ac3PIM3).
Interaction partners:
Sequence:
MRVVQVANFYGPRSGGLRTAVDRLGAEYCASGHEVFLIVPGARTERHLLRTGVVRITLPAKHIPYTGGYRAVMPGAVRTVLETLRPDALEVSDRLTLRSLGRWGREHGVTTVMISHERLDRFAGQLLPRRAAQKFADFANARTAANYDTVVCTTGFAREEFDRIGATNTVTVPLGVDLKTFHPRRRCARVRQHWATPTQILLVHCGRLSVEKHADRSIDALAALCDAGVDARLVIAGEGPLRARLERKATGLPIDFTGFISDRHAVAGLLASADVALAPGPHETFGLAALESLACGTPAVVSRTSALTEIITADSGACADNRPEAIAHAVRTIVSRPERHRRRCARRRAEIFTWQRAAASMLATLGAMAVSTRCGDTQDTA
Protein: Deoxyguanosine kinase, mitochondrial (XldGK) (EC 2.7.1.113) (Q6GPW6)
Organism: Xenopus laevis (African clawed frog)
Function: Phosphorylates deoxyguanosine in the mitochondrial matrix with high efficiency but shows very low activity against other deoxynucleosides.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9QX60}.
Interaction partners:
- 5'-nucleotidase
- 5'-nucleotidase
- 5'-nucleotidase
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- 5'
- 5'
- Guanylate kinase-like domain-containing protein.
- Guanylate kinase
- Cytosolic purine 5'-nucleotidase
Sequence:
MKSQTTKPLQQSISTNLSSNKEMQVKRLSVEGNIAVGKSTFLRLLSNTFQEWSFATEPLKKWQNIQSTSFQTTTSSKPPMDNLLQLMYDDPKRWSYTFQTFSCMSRFKIQIQPLSEPVLKQQEHVQIFERSVYSDRYIFAKTLYELQHLNEMEWTLYQEWHTFLIQEFSRRVALDGIIYLWATPEKCFERLQRRARKEEKTLQLQYLEKLHDQHESWLTKKTTEVSFENMKNIPVLLLNVEEDFENNSAAGDELNNRVKAFVAGL
Protein: Periodic tryptophan protein 2 (AtPWP2) (Q8VYZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA. Plays a role early in ribosome biogenesis, especially in the maturation of 5.8S rRNA. Required for guard cell functions.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:23382868}. Nucleus {ECO:0000269|PubMed:19929880}.
Interaction partners:
- Probable RNA 3'-terminal phosphate cyclase-like protein
- AT1G07840 protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Transducin family protein / WD-40 repeat family protein
- Bystin
- Uncharacterized protein At3g06530
- Protein SLOW WALKER 1
- F18K10.11 protein
- Protein TORMOZ EMBRYO DEFECTIVE
- Nucleolar protein
Sequence:
MEFRFENLLGAPYRGGNAVITKNTQLISPVGNRVSVTDLSKNHSVTLPLETSTNICRLASSPDGTFLLAVDEQNRCLFINLPRRVVLHRITFKDKVGALKFSPNGKFIAVGIGKLVEIWRSPGFRRAVLPFERVRTFANSDDKVVSLEWSLDSDYLLVGSRDLAARLFCVRKLKGVLNKPFLFLGHRDSVVGCFFGVDKMTNKVNRAFTIARDGYIFSWGYTEKDVKMDESEDGHSEPPSPVTPDRADEVMVENGGGVGTELKKRKEYDGKGLESDEEGDDDDEEYMHRGKWVLLRKDGCNQASAKVTACDYHQGLDMVVVGFSNGVFGLYQMPDFICIHLLSISRQKLTTAVFNERGNWLTFGCAKLGQLLVWDWRTETYILKQQGHYFDVNCVTYSPDSQLLATGADDNKVKVWNVMSGTCFITFTEHTNAVTALHFMADNHSLLSASLDGTVRAWDFKRYKNYKTYTTPTPRQFVSLTADPSGDVVCAGTLDSFEIFVWSKKTGQIKDILSGHEAPVHGLMFSPLTQLLASSSWDYTVRLWDVFASKGTVETFRHNHDVLTVAFRPDGKQLASSTLDGQINFWDTIEGVLMYTIEGRRDIAGGRVMTDRRSAANSSSGKCFTTLCYSADGGYILAAGTSRYICMYDIADQVLLRRFQISHNLSLDGVLDFLHSKKMTEAGPIDLIDDDNSDEEGGIDKQSRGNLGYDLPGSRPNRGRPIIRTKSLSIAPTGRSFAAATTEGVLIFSIDDTFIFDPTDLDIDVTPEAVEAAIEEDEVSRALALSMRLNEDSLIKKCIFAVAPADIKAVAISVRQKYLERLMEALVDLLENCPHLEFILHWCQEICKAHGSSIQRNYRTLLPALRSLQKAITRAHQDLADMCSSNEYTLRYLCSVPNNH
Protein: Putative JmjC domain-containing histone demethylation protein 1 (EC 1.14.11.27) (Heterochromatin-destabilizing protein epe1) ([Histone-H3]-lysine-36 demethylase 1) (O94603)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be a histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code (By similarity). Represses transcriptional silencing by negatively affecting heterochromatin stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:12773576}.
Interaction partners:
- Chromatin-associated protein swi6
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Histone deacetylase clr3
- Histone H3.1/H3.2
- Protein argonaute
- Bromodomain-containing protein C631.02
- Suppressor of kinetochore protein 1
- Histone H4
- NAD-dependent histone deacetylase sir2
- Protein Dicer
Sequence:
MDSWLEYDDIINQDIDIPSNDLSGSGTLCVGVHSSLLENSLNSIDSFISSKEEISWCGNQSTPIATKSHLSCINPQYVNPFDTSPVSVDTEFQDTYLLDAPSFAQPHFSERQSVDKTRSRCLSRNRRRKRHPNLHKNHQRLLGMSFPQDGFRRMPAESVNFSYFRDTGFNEPTIFPSSDTQNTRQLNLSKIATLIGYDCPLALVDVVTQKQIPNKMDMESWVKYMSLEPSKRGRIYDVLSLEVSTTKLAYYVRKPNIVRDLDLVNTVWPPGSFALGEYPHVDTYCLMSAENSYTEFHIEFGGSSAYYNILDGCKIFYLIPGTSKNWEAYTAWLTSSNDSDKKFLPNMVDVCYCVEVHSQQTILVPSGWIYAVVTPCDTISIAGNFLTFLHIYPQLSIYNLELQLGIEKEYQYPYFESIMWYTAIHFYLAFPDNSSRDGIDDIIAEYETGRLFDINAFTEQELDGFEELLNYLYIRAQILRDCDIIIDIYNEPVKISKNNGYNSAYTMVPPDLDEICVDFVQKFGAWITYHHRRSAKHPSCNCFSHLQTKLIDSGPKPANNSYQHQSNFIGVVISTNHNIIKKCQESQIQTGKNNCSFQLVKKRIKSTKKAPSWRSIIKAFKKRENTRCNFLSSLHATTFREDIVVRPKIKSFVLEQLIFQALFSFAINWTPSFFLNHSNFENIALSKETFNFGGEANCENTDTTLFTTWGDQGFRPSDSICYNDFNLLETANSDAEASIHELELQPLNAVNEREVDISQTDMTPSTALDTRVDTRVDSLPEFSNLILSPSSNDDSFQLDDLLSPSSSNLKQQIQKVVPQNSLEFSVGEKEKKAAEYSLLHTFSYKRLSMENEKPDTTKVPLKYNIQHEEMKAYRRKNDLEYIDQHFASSKSGISNGRNNNKEVNLTKAENVGIKKRRIMKNENNIYDFEDHSPVREKWGHRLRSRGAS
Protein: Phosphatidylinositol transfer protein alpha isoform (PI-TP-alpha) (PtdIns transfer protein alpha) (PtdInsTP alpha) (Phosphatidylinositol-transfer protein 35 kDa isoform) (PI-TP 35 kda isoform) (Q2HJ54)
Organism: Bos taurus (Bovine)
Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions (By similarity). Preference order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and for PI is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 > C20:3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus {ECO:0000250|UniProtKB:P53810}.
Interaction partners:
- PITPNM family member 3
Sequence:
MVLLKEYRVILPVSVEEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTLENVHKLEPEAWKHVEVIYIDIADRSQVLSKDYKAEEDPAKYKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEDETKRQLDEMRQKDPVKGMTADD
Protein: Snaclec rhodocytin subunit alpha (Aggretin alpha chain) (Rhodoaggretin subunit alpha) (Q9I841)
Organism: Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Function: Elicits platelet aggregation by the binding to the C-type lectin domain family 1 member B (CLEC1B/CLEC2). Binding leads to tyrosine phosphorylation in the cytoplasmic tail of CLEC1B, which promotes the binding of spleen tyrosine kinase (Syk), subsequent activation of PLC-gamma-2, and platelet activation and aggregation. Binding to GPIbalpha (GP1BA) and alpha-2/beta-1 (ITGA2/ITGB1) may also induce aggregation, but this is controversial.
Subcellular location: Secreted.
Interaction partners:
Sequence:
GLEDCDFGWSPYDQHCYQAFNEQKTWDEAEKFCRAQENGAHLASIESNGEADFVSWLISQKDELADEDYVWIGLRAQNKEQQCSSEWSDGSSVSYENLIDLHTKKCGALEKLTGFRKWVNYYCEQMHAFVCKLLPY
Protein: Basic leucine zipper transcriptional factor ATF-like 2 (B-ATF-2) (Suppressor of AP-1 regulated by IFN) (SARI) (Q8N1L9)
Organism: Homo sapiens (Human)
Function: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system. Following infection, participates in the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes (By similarity). Selectively suppresses CCN1 transcription and hence blocks the downstream cell proliferation signals produced by CCN1 and inhibits CCN1-induced anchorage-independent growth and invasion in several cancer types, such as breast cancer, malignant glioma and metastatic melanoma. Possibly acts by interfering with AP-1 binding to CCN1 promoter.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Basic leucine zipper transcriptional factor ATF-like 3
- Basic leucine zipper transcriptional factor ATF-like
- Transcription factor Jun
- Transcription factor ETV7
- Guanylate-binding protein 5
- Interferon regulatory factor 1
- Ankyrin repeat domain-containing protein 22
Sequence:
MHLCGGNGLLTQTDPKEQQRQLKKQKNRAAAQRSRQKHTDKADALHQQHESLEKDNLALRKEIQSLQAELAWWSRTLHVHERLCPMDCASCSAPGLLGCWDQAEGLLGPGPQGQHGCREQLELFQTPGSCYPAQPLSPGPQPHDSPSLLQCPLPSLSLGPAVVAEPPVQLSPSPLLFASHTGSSLQGSSSKLSALQPSLTAQTAPPQPLELEHPTRGKLGSSPDNPSSALGLARLQSREHKPALSAATWQGLVVDPSPHPLLAFPLLSSAQVHF
Protein: Lysyl oxidase homolog (EC 1.4.3.13) (A6MH35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239, ECO:0000256|RuleBase:RU367046}.
Interaction partners:
Sequence:
MFFTISNFIFFLYLLQGLNNLTSAQSSAQWRNRVRWVNNGQVFSLMSTGSEFHAPVPSRRQSRVYQSSRTDAVPGRSMQIRLEAMDRPANSAPDSALLGPDRAQYIMANSRAPGARQMQVMQRHRAPPASRNNSTVPSEYSGGGGRTGENTRRGQAVANFQQIAAPTDNSNTVNSDNENEARTPNVPAEQGATSETMPGDDPRNRNTVFYNIYPPGGRTIIPRRPPPGTGYGTRFFQNGLPDLVPDPYSIQAGSYIQRVQMYALRCAAEENCLARTAYRPTVRDLDYRVLLRFPQKVRNMGTADFLPVKPRHQWEWHSCHQHYHSMDAFSHYDLLDISTGRKVAEGHKASFCLEDTGCDPGFHRRYACTAHTQGLSPGCHDTYAANIDCQWIDITDVPPGNYILKVTVNPDFLVAESDFSNNVVRCEVIYTGIYIQTRNCIITG
Protein: Autophagy protein 12-like (APG12-like) (Q9VTU1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for autophagy.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Autophagy protein 5
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy-related 16, isoform F
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related 1, isoform B
- Autophagy-related 8a, isoform A
- Autophagy-related 8b, isoform A
- Autophagy-related 18a, isoform E
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MAETPESQAALSTSSSTPADKDGSKICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYYCKNQAWG
Protein: CRS2-associated factor 1, chloroplastic (Chloroplastic group IIA intron splicing facilitator CRS2-associated factor 1) (Q84N49)
Organism: Zea mays (Maize)
Function: Required for the splicing of group IIB introns in chloroplasts. Forms splicing particles with CRS2. Interacts with RNA and confers intron specificity of the splicing particles.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12881426}.
Interaction partners:
Sequence:
MATARLPSRSFLSPAQQSYPRLPASVRLCLSHHEQPPTGPKRHRRAATSHPAFSAAARGRAKKIPIADTDEPAAGVRVTDRGISYRLDGAPFEFQYSYTEAPRARPVALREAPFMPFGPEATPRPWTGRKPLPKSRKELPEFDSFVLPAPGKKGVKPVQSPGPFLAGMEPRYQSVSREDILGEPLTKEEVSELVKGSLKSKRQLNMGRDGLTHNMLENIHSHWKRKRVCKIKCKGVCTIDMDNICHQLEEKVGGKVIHRQGGVIFLFRGRNYNYRTRPCFPLMLWKPVAPVYPRLVTKVPGGLTPDEATEMRTRGHQLPPICKLGKNGVYANLVNQVREAFEACDLVRVDCSGLNKSDCRKIGAKLKDLVPCILLSFEFEHILMWRGSDWKSSLPPLENSYEVTKVQESFSGKESNEKVTHSGNVLAQIELVSAATSHKNWNLDEGQEKFKDSTDSDMVLNSAKDVPALFHSTGISRTEPSADIPLEYSPLNPVCDIMDPSLNCRSIPTNNCESRALVEKSEHCPDDYNLEMKRKRNDGTKGTVVLNSGSKVEGLLCLLEQAIHSGRALVLSEDELADSDLVYEKSVAFTKSIPRRLVFENTRRKSSARRNVPDNHARTKTHLVENKMLSSPVENKFIVNGGSAMQTIDHGQEFLSDVVHQGTLRVDELAKLLA
Protein: X protein (p10) (P0DOF0)
Organism: Borna disease virus (strain V) (BDV)
Function: Plays an essential role in the inhibition of host apoptosis. Mediates host mitochondria-mediated apoptosis through interaction with the mitochondrial antiviral signaling protein/MAVS and thereby promotes viral persistence in host central nervous system. Within the host nucleus, regulates viral RNA synthesis and polymerase complex assembly.
Subcellular location: Host nucleus. Host mitochondrion {ECO:0000269|PubMed:19211764, ECO:0000269|PubMed:23702035, ECO:0000269|PubMed:26700735}.
Interaction partners:
Sequence:
MSSDLRLTLLELVRRLNGNATIESGRLPGGRRRSPDTTTGTTGVTKTTEGPKECIDPTSRPAPEGPQEEPLHDLRPRPANRKGAAVE