wanglab/gogpt-training-data huggingface dataset:
Protein: LOW protein: PPR containing-like protein (F4J1L5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAMLGNVLHLSPMVLATTTTTKPSLLNQSKCTKATPSSLKNCKTIDELKMFHRSLTKQGLDNDVSTITKLVARSCELGTRESLSFAKEVFENSESYGTCFMYNSLIRGYASSGLCNEAILLFLRMMNSGISPDKYTFPFGLSACAKSRAKGNGIQIHGLIVKMGYAKDLFVQNSLVHFYAECGELDSARKVFDEMSERNVVSWTSMICGYARRDFAKDAVDLFFRMVRDEEVTPNSVTMVCVISACAKLEDLETGEKVYAFIRNSGIEVNDLMVSALVDMYMKCNAIDVAKRLFDEYGASNLDLCNAMASNYVRQGLTREALGVFNLMMDSGVRPDRISMLSAISSCSQLRNILWGKSCHGYVLRNGFESWDNICNALIDMYMKCHRQDTAFRIFDRMSNKTVVTWNSIVAGYVENGEVDAAWETFETMPEKNIVSWNTIISGLVQGSLFEEAIEVFCSMQSQEGVNADGVTMMSIASACGHLGALDLAKWIYYYIEKNGIQLDVRLGTTLVDMFSRCGDPESAMSIFNSLTNRDVSAWTAAIGAMAMAGNAERAIELFDDMIEQGLKPDGVAFVGALTACSHGGLVQQGKEIFYSMLKLHGVSPEDVHYGCMVDLLGRAGLLEEAVQLIEDMPMEPNDVIWNSLLAACRVQGNVEMAAYAAEKIQVLAPERTGSYVLLSNVYASAGRWNDMAKVRLSMKEKGLRKPPGTSSIQIRGKTHEFTSGDESHPEMPNIEAMLDEVSQRASHLGHVPDLSNVLMDVDEKEKIFMLSRHSEKLAMAYGLISSNKGTTIRIVKNLRVCSDCHSFAKFASKVYNREIILRDNNRFHYIRQGKCSCGDFCLTDDDLEVLKGCLDLGFGFNYDEIPALCKTLPALELCYSMSQKNLDDKHTPSLQLPIGRSLVPSCDNPDDVKARLKCWAQARRRRFQKGIGRSEFN
Protein: Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homolog) (O14980)
Organism: Homo sapiens (Human)
Function: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap.
Subcellular location: Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.
Interaction partners:
- Snurportin-1
- GTP-binding nuclear protein Ran
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup88
- 60S ribosomal export protein NMD3
- E3 SUMO-protein ligase RanBP2
- ATP-dependent RNA helicase DDX3X
- Phosphorylated adapter RNA export protein
- Ran GTPase-activating protein 1
- Exportin-2
Sequence:
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
Protein: SUR7 family protein FMP45 (Q07651)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in sporulation and affects the sphingolipid composition of the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11784867, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17078969}; Multi-pass membrane protein {ECO:0000269|PubMed:11784867, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17078969}. Note=Concentrates within cortical patches at the membrane.
Interaction partners:
- Protein HBT1
- Non-classical export protein 2 homolog 1
- Uncharacterized protein YNL195C
- Catalase T
- Non-classical export protein 2
- Probable glucose transporter HXT5
- Reticulon-like protein 2
- Phosphate metabolism protein 7
- Transketolase 2
- Protein GRE1
Sequence:
MIFKRFVNLLVFLFLLGAGLLTFFLILSGGRESGTLKNFYWLQADTNGFNSAPSTTRWYNYNWCGYEDGQLANCSSRAPAKPFSPRDNFGNSVNLPSSFRNNRDTYYYLSRVGWAMLLISLFFIVLALVPGFLATFLPFKAVPVLYCVLSWLAFFFIILAACLYTGCYVKARKTFRNSGRSARLGPKNFAFIWTSVFLMLVNAIWSTIFSATHKAHSTYSDHDMYAQYESPSVDTGAQMEKSTYNSGATDGAGPITAAPVVGQPQPTTTTTPAGNGKFFQKLKTRKQVPSAELEPAGDGGLAGPVTVRD
Protein: DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3) (P49916)
Organism: Homo sapiens (Human)
Function: Isoform 3 functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as DNA ligase in mitochondrial base-excision DNA repair.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}. Note=Contains an N-terminal mitochondrial transit peptide. {ECO:0000269|PubMed:10207110}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000305|PubMed:10207110}. Note=Contains an N-terminal mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial transit peptide. {ECO:0000269|PubMed:10207110}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000305|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.
Interaction partners:
- DNA repair protein XRCC1
- DNA polymerase beta
- Bifunctional polynucleotide phosphatase/kinase
- X-ray repair cross-complementing protein 6
- Tyrosyl-DNA phosphodiesterase 1
- Poly [ADP-ribose] polymerase 2
- Poly [ADP-ribose] polymerase 1
- Aprataxin
- DNA repair nuclease/redox regulator APEX1
- Aprataxin and PNK-like factor
Sequence:
MSLAFKIFFPQTLRALSRKELCLFRKHHWRDVRQFSQWSETDLLHGHPLFLRRKPVLSFQGSHLRSRATYLVFLPGLHVGLCSGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQITQHIADLSSKAAGTPKKKAVVQAKLTTTGQVTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAPSSPTPKRSLSSSKCDPRHKDCLLREFRKLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFHGDVYLTVKLLLPGVIKTVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDEFLLRLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNAQEVEKEPGQRRALSVQASLMTPVQPMLAEACKSVEYAMKKCPNGMFSEIKYDGERVQVHKNGDHFSYFSRSLKPVLPHKVAHFKDYIPQAFPGGHSMILDSEVLLIDNKTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYFNDVSLMDRPLCERRKFLHDNMVEIPNRIMFSEMKRVTKALDLADMITRVIQEGLEGLVLKDVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPGSQKWCTVTKCAGGHDDATLARLQNELDMVKISKDPSKIPSWLKVNKIYYPDFIVPDPKKAAVWEITGAEFSKSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKEKADFTVVAGDEGSSTTGGSSEENKGPSGSAVSRKAPSKPSASTKKAEGKLSNSNSKDGNMQTAKPSAMKVGEKLATKSSPVKVGEKRKAADETLCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC
Protein: Protein kinase C and casein kinase substrate in neurons 2 (Protein kinase C and casein kinase substrate in neurons protein 2) (F1QC13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004599}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004599}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004599}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004345}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004565}.
Interaction partners:
- EH domain-containing protein 2b
- Platelet endothelial aggregation receptor 1
- Zinc finger, MIZ-type-containing 2.
Sequence:
MSDFNDSLIDVSSDSFWEVGNYKRSVKRVDDGNRLCNDLMSCLHERARIEKSYSTQLTDWAKRWRQTIEKGPQYGTVERAWCALMTEAEKVSDLHMEVKAALMAEDFEKIKNWQKDAYHKQMIGGFKETKEAEDGFRKAQKPWAKKLKEMETMKKAYHTACKEEKTATSRENSSKLDNSNPEAQKKLQEKVEKCQQEVQKTKERYEKSLEDLDKVTPQYMENMEQVFEQWQQFEGKRLSFFKEVLLEVKQHLDLSSNHKYTTVYHTLQDTIQGADPQEDLKWFRSNHGPGMTMNWPQFEEWSMDLNRTLSRRETKRRPAEGVTLTAISHNPEQSSRVSSVPAVSSSEAACLNPFDDDDDDEDEDEEPVVTHTHSSPVKHEEAVAQTAAVEKAPAPAAITAADDDDDEESGNPFSSSSANGNPFEEEPSTEMCVPVRAVYDYEGQEQDELSFKAGDELVKLSEEDEQGWCKGRLSNGTVGLYPANYVEDLQ
Protein: Pik3c2b protein (A2RSK1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHHKEESRAKQNTEPSLISWDEPALDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSISPPEGLPNSTSQDPQPGPDPWPKGSLSGDYLYIFDGSEGRCSLSPGSGDTDGSCKKLSPPPLPPRVSIWDAPPLPPRKGSPSPSKISQPNDINSFSSAEQPPDKLLVAQDPEEGELPDGRGQGHTLGSVDYDGINDAITRLNLKSTYDSEISSDATRGWKEGRGPLDFNKDTSGKPVARSKTMPPQVPPRTYTSRYANRKNATPGNNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRTGSDIQDYSLTGCVWSTVTPSPEHLGDEVNLKVTVLCDSLREPLTFTCNCSSTVDLLIHQTLCYTHDELREVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDISIRLQLMEQKAIRSDLARTVNDDQSPSTLNYLIHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAICNALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLSVRENREKVVEALTAAILDLVELYCSTFNADFQTAVPGSRKHDLVQEACHFPGALAFTVYGTHRIPIIWATSYEDFYLSCSLSHGGKELCSPLQTRRAHFSKYLFHLIIWDQQ
Protein: Chordin-like protein 1 (Neuralin-1) (Neurogenesin-1) (Ventroptin) (Q9BU40)
Organism: Homo sapiens (Human)
Function: Antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation. May play a role in embryonic bone formation (By similarity). May also play an important role in regulating retinal angiogenesis through modulation of BMP4 actions in endothelial cells. Plays a role during anterior segment eye development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRKKWKMGGMKYIFSLLFFLLLEGGKTEQVKHSETYCMFQDKKYRVGERWHPYLEPYGLVYCVNCICSENGNVLCSRVRCPNVHCLSPVHIPHLCCPRCPDSLPPVNNKVTSKSCEYNGTTYQHGELFVAEGLFQNRQPNQCTQCSCSEGNVYCGLKTCPKLTCAFPVSVPDSCCRVCRGDGELSWEHSDGDIFRQPANREARHSYHRSHYDPPPSRQAGGLSRFPGARSHRGALMDSQQASGTIVQIVINNKHKHGQVCVSNGKTYSHGESWHPNLRAFGIVECVLCTCNVTKQECKKIHCPNRYPCKYPQKIDGKCCKVCPGKKAKELPGQSFDNKGYFCGEETMPVYESVFMEDGETTRKIALETERPPQVEVHVWTIRKGILQHFHIEKISKRMFEELPHFKLVTRTTLSQWKIFTEGEAQISQMCSSRVCRTELEDLVKVLYLERSEKGHC
Protein: N-succinylglutamate 5-semialdehyde dehydrogenase (EC 1.2.1.71) (Succinylglutamic semialdehyde dehydrogenase) (SGSD) (O50174)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Interaction partners:
- N-succinylarginine dihydrolase
- Succinylglutamate desuccinylase
- Succinylornithine transaminase/acetylornithine aminotransferase
- Arginine N-succinyltransferase subunit alpha
- Arginine N-succinyltransferase subunit beta
- Topoisomerase II
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Arginine/ornithine transport ATP-binding protein AotP
- NAD-specific glutamate dehydrogenase
- Oligopeptide transporter, OPT family
Sequence:
MSTHYIAGQWLAGQGETLESLDPVGQGVVWSGRGADATQVDAAVCAAREAFPAWARRPLEQRIELLERFAATLKSRADELARVIGEETGKPLWESATEVTSMVNKVAISVQAFRERTGEKSGPLADATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNCVVFKPSELTPKVAELTLKAWIQAGLPAGVLNLVQGGRETGVALAAHRGLDGLFFTGSSRTGNLLHSQFGGQPQKILALEMGGNNPLVVEEVADLDAAVYTIIQSAFISAGQRCTCARRLLVPQGAWGDALLARLVAVSATLRVGRFDEQPAPFMGAVISLSAAEHLLKAQEHLIGKGAQPLLAMTQPIDGAALLTPGILDVSAVAERPDEEFFGPLLQVIRYSDFAAAIREANATQYGLAAGLLSDSRERFEQFLVESRAGIVNWNKQLTGAASSAPFGGIGASGNHRPSAYYAADYCAYPVASLESPSVSLPATLTPGISL
Protein: Odorant receptor 46a, isoform A (P81919)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSKGVEIFYKGQKAFLNILSLWPQIERRWRIIHQVNYVHVIVFWVLLFDLLLVLHVMANLSYMSEVVKAIFILATSAGHTTKLLSIKANNVQMEELFRRLDNEEFRPRGANEELIFAAACERSRKLRDFYGALSFAALSMILIPQFALDWSHLPLKTYNPLGENTGSPAYWLLYCYQCLALSVSCITNIGFDSLCSSLFIFLKCQLDILAVRLDKIGRLITTSGGTVEQQLKENIRYHMTIVELSKTVERLLCKPISVQIFCSVLVLTANFYAIAVLSDERLELFKYVTYQACMLIQIFILCYYAGEVTQRSLDLPHELYKTSWVDWDYRSRRIALLFMQRLHSTLRIRTLNPSLGFDLMLFSSIVNCSYSYFALLKRVNS
Protein: Family 48 cellulase (Q19VP0)
Organism: Myxobacter sp. AL-1
Interaction partners:
Sequence:
MKRKLEASKGGRIMDNKTRFMQLYEQIKNPQNGYFSPEGIPYHSVETLICEAPDYGHMTTSEAYSYWLWLEAMFGRYTQDWSKLEAAWDNMEKYIIPVNEGDGNEEQPTMNYYNPSSPATYAAEHRYPDLYPSALTGQYPAGNDPLDSELRSTYGSNETYLMHWLLDVDNWYGFGNLLNPSHTAVYVNTYQRGEQESVWETVPHPSQDNQTFGKPNEGFMSLFTKENQTPAPQWRYTNATDADARAVRGIYWARRWGYSNTKYLEKAKKMGDFLRYGMYDKYFQEIGSTADGSPSRGTGKNACHYLMAWYTAWGGGLGQYANWAWRIGASHVHQGYQNPVASYALSTAEGGLVPNSSTARSDWEQALKRQLELYTWLLSSEGAVTGGATNSWNGSYSAYPQNVSTFYGMAYTEAPVYHDPPSNNWFRMQVWPLKRVAELYYIFAEKGDKSSGNFQMAKHVIEKWIAYSLNYVFVGERPVTDEEGYYLNEAGERVLGGQYPQIAVQSDPGEFWIPANLEWNGQPDPWKGFDSFTGNPGLHVTTKNPSQDVGVLGSYIKTLVFFAAGTKAETGGFTALGNKAKNVAKELLDAAWNKNDGIGIAAEEEHEDYIRYFTKEVYFPNGWSGKNGQGNTIPGSNTVPSDPAKGGNGVYISHADLRPKIKNDPMWPYLENKYQTSWNPNTGKWENGLPTFVYHRFWSQVDMATAYAEYDRLIGNA
Protein: Formyl-CoA:oxalate CoA-transferase (FCOCT) (EC 2.8.3.16) (Formyl-coenzyme A transferase) (Formyl-CoA transferase) (P69902)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as an acceptor.
Interaction partners:
- Oxalyl-CoA decarboxylase
- Uncharacterized transporter YfdV
- Protein YfdX
- Acetyl-CoA:oxalate CoA-transferase
- HTH-type transcriptional regulator YdeO
- Probable multidrug resistance protein EmrY
- Protein YdeP
- Probable multidrug resistance protein EmrK
Sequence:
MSTPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRDIPDIDALYFTMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGAIDHMGFTWEHIQEINPRLIFGSIKGFDECSPYVNVKAYENVAQAAGGAASTTGFWDGPPLVSAAALGDSNTGMHLLIGLLAALLHREKTGRGQRVTMSMQDAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVPRGGNAGGGGQPGWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHARQPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLRQSGSVVEVEQPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELGYSDDEIAAMKQNHAI
Protein: Superkiller complex protein 8 (Ski8) (Meiotic recombination REC14 protein homolog) (WD repeat-containing protein 61) [Cleaved into: Superkiller complex protein 8, N-terminally processed (WD repeat-containing protein 61, N-terminally processed)] (Q9GZS3)
Organism: Homo sapiens (Human)
Function: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C.
Subcellular location: Nucleus {ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:18445686}. Cytoplasm {ECO:0000269|PubMed:18445686, ECO:0000305|PubMed:16024656}.
Interaction partners:
- Superkiller complex protein 3
- Superkiller complex protein 2
- RNA polymerase-associated protein LEO1
- Parafibromin
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein CTR9 homolog
- RNA polymerase II-associated factor 1 homolog
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- DNA excision repair protein ERCC-6
Sequence:
MTNQYGILFKQEQAHDDAIWSVAWGTNKKENSETVVTGSLDDLVKVWKWRDERLDLQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQIKSIDAGPVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYDCPI
Protein: E3 ubiquitin-protein ligase UHRF2 (EC 2.3.2.27) (Np95/ICBP90-like RING finger protein) (Np95-like RING finger protein) (Nuclear protein 97) (Nuclear zinc finger protein Np97) (RING finger protein 107) (RING-type E3 ubiquitin transferase UHRF2) (Ubiquitin-like PHD and RING finger domain-containing protein 2) (Ubiquitin-like-containing PHD and RING finger domains protein 2) (Q96PU4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair. Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them. This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest. Ubiquitinates also PCNP leading to its degradation by the proteasome. Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteosomal degradation. Promotes also DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation. Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:12176013, ECO:0000269|PubMed:23404503, ECO:0000269|PubMed:27129234, ECO:0000269|PubMed:27743347, ECO:0000269|PubMed:29923055, ECO:0000269|PubMed:30335751}. Chromosome {ECO:0000269|PubMed:27129234}. Note=Enriched at genomic loci that are enriched for 5-hydroxymethylcytosine (5hmC). {ECO:0000269|PubMed:27129234}.
Interaction partners:
- Proliferating cell nuclear antigen
- DNA
- Histone deacetylase 1
- PEST proteolytic signal-containing nuclear protein
- Retinoblastoma-associated protein
- DNA
- DNA
- Cellular tumor antigen p53
- Zinc finger protein 131
- Ubiquitin-conjugating enzyme E2 D1
Sequence:
MWIQVRTIDGSKTCTIEDVSRKATIEELRERVWALFDVRPECQRLFYRGKQLENGYTLFDYDVGLNDIIQLLVRPDPDHLPGTSTQIEAKPCSNSPPKVKKAPRVGPSNQPSTSARARLIDPGFGIYKVNELVDARDVGLGAWFEAHIHSVTRASDGQSRGKTPLKNGSSCKRTNGNIKHKSKENTNKLDSVPSTSNSDCVAADEDVIYHIQYDEYPESGTLEMNVKDLRPRARTILKWNELNVGDVVMVNYNVESPGQRGFWFDAEITTLKTISRTKKELRVKIFLGGSEGTLNDCKIISVDEIFKIERPGAHPLSFADGKFLRRNDPECDLCGGDPEKKCHSCSCRVCGGKHEPNMQLLCDECNVAYHIYCLNPPLDKVPEEEYWYCPSCKTDSSEVVKAGERLKMSKKKAKMPSASTESRRDWGRGMACVGRTRECTIVPSNHYGPIPGIPVGSTWRFRVQVSEAGVHRPHVGGIHGRSNDGAYSLVLAGGFADEVDRGDEFTYTGSGGKNLAGNKRIGAPSADQTLTNMNRALALNCDAPLDDKIGAESRNWRAGKPVRVIRSFKGRKISKYAPEEGNRYDGIYKVVKYWPEISSSHGFLVWRYLLRRDDVEPAPWTSEGIERSRRLCLRLQYPAGYPSDKEGKKPKGQSKKQPSGTTKRPISDDDCPSASKVYKASDSAEAIEAFQLTPQQQHLIREDCQNQKLWDEVLSHLVEGPNFLKKLEQSFMCVCCQELVYQPVTTECFHNVCKDCLQRSFKAQVFSCPACRHDLGQNYIMIPNEILQTLLDLFFPGYSKGR
Protein: Transposon Ty1-OR 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)] (Q92393)
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:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNSNKRIIAKLKMQYDTKIINLGESDDEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPNGRKLGAPGQPGLYINQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH