wanglab/gogpt-training-data huggingface dataset:
Protein: Pharynx and intestine in excess protein 1 (Protein pie-1) (Q94131)
Organism: Caenorhabditis elegans
Function: Maternally provided PIE-1 is required for germline cell fate determination. Functions as a repressor of RNA polymerase II-dependent gene expression in the developing germline. Required for expression of nos-2 in P4 germline blastomere cells. Inhibits the histone deacetylase activity of hda-1. Represses transcriptional activation of cdk-9 and cit-1.1, which are members of the P-TEFb complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:30279189, ECO:0000269|PubMed:34003111}. Cytoplasm {ECO:0000269|PubMed:30279189, ECO:0000269|PubMed:34003111}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasmic granule {ECO:0000269|PubMed:34003111}. Note=Initially associates with both centrosomes of the mitotic spindle. Rapidly disappears from the centrosome destined for the somatic daughter and persists in the centrosome of the daughter that becomes the next germline blastomere. Accumulates in larger cytoplasmic granules (P granules), which are visible around the nuclei in the micrographs.
Interaction partners:
- Zinc finger protein mex-5
- K Homology domain-containing protein
- Protein unc-119
- Zinc finger protein mex-6
- Probable histone H2B 4
- CCCH-type zinc finger protein oma-1
- Zinc finger-interacting factor 1
- CCCH-type zinc finger protein oma-2
- PIP-1
- Guanyl-specific ribonuclease pgl-1
Sequence:
MAQTKPIAEQMAALNNSDDTSFAADRSNSLLNATCPARIQNSVDQRKINRSFNDSLSSGYSGKWLRPKREALKITPLAQIDEAPATKRHSSAKDKHTEYKTRLCDAFRREGYCPYNDNCTYAHGQDELRVPRRRQEYYSRDPPRERRDSRSRRDDVDTTINRSSSSASKHHDENRRPSNNHGSSNRRQICHNFERGNCRYGPRCRFIHVEQMQHFNANATVYAPPSSDCPPPIAYYHHHPQHQQQFLPFPMPYFLAPPPQAQQGAPFPVQYIPQQHDLMNSQPMYAPMAPTYYYQPINSNGMPMMDVTIDPNATGGAFEVFPDGFFSQPPPTIIS
Protein: Mitochondrial coiled-coil domain protein 1 (P59942)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14527716}.
Interaction partners:
Sequence:
MVLPLPWLSRYHFLRLLLPSWSLAPQGSHGCCSQNPKASMEEQTSSRGNGKMTSPPRGPGTHRTAELARAEELLEQQLELYQALLEGQEGAWEAQALVLKIQKLKEQMRRHQESLGGGA
Protein: CUGBP Elav-like family member 4 (CELF-4) (Bruno-like protein 4) (CUG-BP- and ETR-3-like factor 4) (RNA-binding protein BRUNOL-4) (Q9BZC1)
Organism: Homo sapiens (Human)
Function: RNA-binding protein implicated in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Promotes exclusion of both the smooth muscle (SM) and non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14973222}. Cytoplasm {ECO:0000269|PubMed:14973222}.
Interaction partners:
- CCAAT/enhancer-binding protein delta
- Protein bicaudal D homolog 1
- ATP-dependent DNA helicase DDX11
Sequence:
MYIKMATLANGQADNASLSTNGLGSSPGSAGHMNGLSHSPGNPSTIPMKDHDAIKLFIGQIPRNLDEKDLKPLFEEFGKIYELTVLKDRFTGMHKGCAFLTYCERESALKAQSALHEQKTLPGMNRPIQVKPADSESRGGSSCLRQPPSQDRKLFVGMLNKQQSEDDVRRLFEAFGNIEECTILRGPDGNSKGCAFVKYSSHAEAQAAINALHGSQTMPGASSSLVVKFADTDKERTMRRMQQMAGQMGMFNPMAIPFGAYGAYAQALMQQQAALMASVAQGGYLNPMAAFAAAQMQQMAALNMNGLAAAPMTPTSGGSTPPGITAPAVPSIPSPIGVNGFTGLPPQANGQPAAEAVFANGIHPYPAQSPTAADPLQQAYAGVQQYAGPAAYPAAYGQISQAFPQPPPMIPQQQREGPEGCNLFIYHLPQEFGDAELMQMFLPFGFVSFDNPASAQTAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 pre-mRNA-processing factor 4 homolog) (M9PGI7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADDKSYDSSNNSETEERRAKHKKAKKHKKHKKSSTGKTEKDRHVHKKQKKAKKRPHRTSESTNESDAPENAKLKLSQNCGLSSKFTEIMQKASRNGADFRVGKPLLPTDPSSLVEEITKTIQNKMLPVLEVASSSSESDVPADAASPIILSIIEDELNLEELMRQKALLQARLGAYMSDPEAEDKGDLLPHTHSQQLVVHTKSVLKAVTSVPQPQPSKSAAPLATATSKHANIKKSTTHNSNESDVILLDDSSGGQRTPSPTPEKRRRHASPLPAAPRSRCRRDRRSRDRDRSPPRRRASDQQTQVRPRSRNRNMEDLRQEINRDKQRERRDHSRDRDRRGLDRPPPPTDMRPGRARERDVRPSRMQRSHSRSKFESDRRRERERQKDRDRGGGRVGARSGTDNGDRDRYKGSLSEGQNKLDKESSDEEVNVNIDILEEDDEERIIELRRKKREELLKLGTGQESPAPHNSVSYESRSTSQGSSQRERPLRTPSPTMPCPNPLISEIPKDREDMDNSTSQKTCSAKEKRNEWDMFADQDVDSNFDVSRKISPNTIVQNKHQHENPALTDNWDDAEGYYRVRIGEVLDNRYLVNGYTGQGVFSNVVRGRDQARGQANVAIKIIRNNEIMHKTGLRELEILKKLNDADPEDRFHCLRLYRHFFHKQHLCMVFEPLAMNLREVLKKYGKNVGLHIKAVRSYTQQLFLALKLLKKTGILHADIKPDNILVNENNLILKLCDFGSASAISDNEITPYLVSRFYRSPEIILGIPYDYGIDTWSAGCTIYELYTGKILFSGKSNNQMLKFFMDVKGKIPNRIIRKGQFREQHFDQSCNFLYHEIDKLTEREKIVVMPVVKPSRSLQQELIADQNLPDDQHRKVTQLKDLLENMFALDPAKRISLNQALVHPFIQEKM
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) (Q8WR08)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MRFQWFLSASASLSLFLLLDFVVWIHGERDFNVNDSQVPVIEPKDVPAYKQDPYVTELMSCQNTPSEIVLSLLLKKHDWSELTATKRAHVQAKLAKFFAIPKEFISLDSVSKRELRSMHKLAMRKGGKGNKNIETLNRRLGRASFMIGCGPSYFVMGEPIAKQIAHQMKDGTIGALTEENFGLWFIWRKELKSRSNRKRRQSEGSGADEDDYDYGDDDEEVAEPSTEVPPVTTHAHRHHHGALEVSEKIVSPESVSSSAVPLVPDVEEEIEESVSKLESVISKTIENTKNIKELPVLGEADDGEDEEEVELQQLGVPLAAEIVPDETTSAAATRATEMVKPVDLDEQEISVDSGAVPAIDVEASATPTPSMSARETQKPFSPYDATSSVSSSFSPVASIASGSEAGEDSTSVSTPHLSPANSPTVMPTELDRNGLATTSSSSSSSASPPPSSSVPTQATQPTTSASSFSSSSSTTTTSTTATVSTTTTASSTATTTTTTTTLSESPKEGGEPDAISSGNNSLANNELSTPATPTSSVATTTASTPESSSISSNFVSTDYMEPQPEENSPPIIKTRLQKLAVTSGKAFTFHVLPETFYDAEDQGNLRLALTDKDGHELKANSWLQFNADKRELYGLPLDDTVSRWQYRLSATDSGNASVTETVEISVQQHRAVRTINHEISVFVRINEKPGHNIDWQLKLINAVARTLDDSTNSAVVVREIRQTPHDPHSATFVYFNETLPTSECPEKELKDIIARLDANRLSDLVQPQLGIKSITGQLIGSCQKDLTQVKPTQHMTKNVPPMPRNQVDRVNASLGQLLVYKVPADTFYDANDNQLTLTLKTRDHLELSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVAEDSGGLSAHDALVVVVSPAPKRDFGFFFKAYLSIKHERFNADLQRKFVERVAKLNGDPTTGQIQIRSITTHHDSDGTIVNFYNTTLYRKHNSCREKEVAMTRSVYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSRPEEPTHKSSFGEDYMITFVWPIVIIVAMLVAASIIACCLHWCRQRSGKMELGDEEERKSFRAKGIPVIFQDEYEEKPEIGNKSPVILKDEKPPLLPPSYNTSNMNGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP
Protein: Sex hormone-binding globulin (Q64HD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Pentraxin family member
Sequence:
MKYLKEVIILLLCPCLILLCRRAAGDQISGRGTINLAHRQQKWTPAMQTCANLSDIRSIRSFFEFRTLDPEGAVFYGDTKEGQDWFVLSLRDGIPEMQIGKADILVSVKGGRKLNDGAWHLLELRSEGKFVVLEVNNEVELVVGLHSKLAEEQLTGKIRLALGGMLVDKQKLFHPFEPEMDACIRGGHWLNLSTPWDTDSTWEPRPCSSEIKKGSYFPGTGVAVFNTSDLPALKTEEAGITVEIFGSWIGTTLSLQSTGFLYVLEGDKDDKLGLKDGSTEFPSEPATLTFTILKNSLVVNSKPKVKSETLDFLSMWKNGMLLTFGGVPGDSEVAKSNPYLRGCLEKIVVQGQVIDLDRAAYKHTAVSSHSCPTEAMNELTL
Protein: TOG domain-containing protein (Q388B8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEHAFASETKYGRRLNMYLCHCSSEEAIFPATALRLHTQTSTGWQSARLCTYPQELGLSFSGEVELDYIRVLCHESNIPTRIEVFVAEASDGSTKLNVVTPYENSNFQRIGYVHFSAGNESAVGIRELKTIKVCRKCVFVKFLILNPYSSSFNTFNQVGIIAMAGHGRLVKSIQRESTKRICVVGETVEVPLEKMLPPILNKLPSAPSGSDKFGEVDAVTRRRLAELLRVKEHAVMTEDYDLAGALKPVLATLEDVGREIYALEQRKNAAVEEEDYASAKKLRDDIEGMRRTAYLVSINRVHTIRRRSVDNAVEVRNIQHNNICSDEKQKEENQCRGLSPPPAPRVFSPSTFDEMPVGGAGYYRLVDGETGANDRNHGIADVVGDVDVLSACVIQGKEKWEELLLRAIVTISGCQSLELDVEDESVAEGKRFEKVFGSVCCGCLFGKRGKLREAAIRAICTPSVFVSLLGHADNITEMLLSYVVLPTRGLNDATTSVVIASCDAVRAIAEQLEGVPPLSSLNSHLSPVLSALVARLGDSNNRIRERAESALLSVAKSALDVVVVALVSNPQKKKQHTVPHRVHASRIAVLNNLVDMYGADGAVSTNLEAQNILSEVVLPCMQHSSGEVRDAASSLFAKLLLVAPSIAQRSIGVLKPTQWSAVEHYLSELTGGACDEGFSREVDTSDRLLPRTGFVPCATPTSAESVTGSASAGRDAASKTCHFCGEFNEGFVEASLDIHFIRACPMLCPCPLCDQVTEIATLQQHLTGECENRHLVRECPRCKEAVRVEDIERHIAAESCIKAVPTHSVCPLCHARFKAGMKGWLTHLAAPPGCPKNPKKYDGSGPITE
Protein: Succinate dehydrogenase iron-sulfur subunit (EC 1.3.5.1) (P07014)
Organism: Escherichia coli (strain K12)
Function: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Fumarate reductase flavoprotein subunit
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Fumarate hydratase class I, aerobic
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA
Protein: FI18283p1 (Stripe, isoform C) (E1JIP0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIMEGLETLVAPTHHAFLLTETAAAAHFNVLSFDTCLFKTSTAAQSSGSPSTATYLSPAQFGGSHHGGASTSSNSLNSSSTASSSSTSSSLLHYTTASAAAAAAAAAAASANNSVLRARNQTATPTQGGSPGHVAVQPSATASSGRSSASHLSLLNTSGQHSPTSSAVEQVEAHKQLIEALPGDLNTPVTTSSDIPSFFGPTTVVEPPPITGSIESEDLSLEPQVISVASPVLSHCSPLKEERSTPPALAIVKEESSNAMNAAAAAAAAAAQQQHQQQQQHQQQLPSPQLGVLAGPMSPPSNSLGNSWGLPSPDKTMFQPPLFSLPAHYATMQQQQQQQQQQQQQQQQQQAAGAAPSPYDDGRAAAAAAAQHAELLGLTMDCTPLLLKQPPPSYAGASAGFPGLGDLHSSHEQQLQQQQYVRSQPKYQWLDSPADYAQQQQQVQQVQQQQQQQQTLVLPGPTSSASSSNAALGVLIPKQENYPDMQPSSNGTGYSGGSGGSSAAAAAAAAAAAAAVQLAEYSPSTSKGHEILSQVYQQSTVPLKLVPVKPRKYPNRPSKTPVHERPYACPVENCDRRFSRSDELTRHIRIHTGQKPFQCRICMRSFSRSDHLTTHIRTHTGEKPFSCDICGRKFARSDEKKRHAKVHLKQRIKKEKVRGEQQQQQQQQQQQQQQQQQQQLQQQQEQHHLSLQQHQQYQQHHLLHSADLAIVTSSASM
Protein: Sterile20-like kinase, isoform A (EC 2.7.11.-) (Q8MLP1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFITNLKKVFHLGGGEAKKKRLYNNIKMDTDPAEFWEMVGELGDGAFGKVYKAQHKEQKRFAAAKMCQLEDEENLSDHMVEIDILSEIKHPNIVELYEAFSIDDKLWMLIEYCDGGALDSIMVELEKPLTEPQIAYVCKHMTEGLTFLHRNKVIHRDLKAGNVLLTMEGGVKLADFGVSAKNKHTMQKHDTFIGTPYWMAPELVLCETFRDNPYDHKVDIWSLGITLIELAQMEPPNSEMSPMRVLLKIQKSEPPKLEQPSRWSKEFNDFLKKSLVKDPQVRPTTDVLMQHAFINRNLDAKPIKDLLLEYKAEVVEEVVDDETEEPRNSALQLDLDDDSASLQSQDIDKLPGTPTSILRDAKEQSQPSSSLPIAAAATAAAAATTTTKATTPDRPNHTKDDNAEAAAQQPPHTKVPAPAPPSSQQTPPPQVQQPPTPPAQPTAAVLQKKPEDVAAVAETSEKTESDKKHFVKKGKAPPPPSPLGLANAKPAASDSQTSPKKLATPEPTSPVTTAIEVAIGQEAMEPKPQPPSPTASSIVSVQSVASSSSSGSVSNAVLSSSTSLITINSDPPTPHHHQPLPPQPQHLILPNSLESVSQITVVTSTHPPVIIDNSVMPPQNEVIIVSNDMNKSTHLHESSTDDDFPSLDDSLGDATTPPHKQSSMILAVNEPAGVVPAPPSQPQTSSTVHARKLDESEVLIVSPSYADDDSAYNTASGSHSHDHSDHLMDTSHVSVVTVGDEGVKVKDSSNELVKRQPNGVGIVPEDVNIIVNRFKQEKRSPDSSLSENGSVRGRRGIEVLVGGSGGSDVDSIGTNTSQESRHETDHNNKQQYPAAALMPPPPPSLTNNHNHETIDEEEEVVIRPKARVPAVVKSANAQGLTKEEIELRNLRKKTRKRTRKFEIDGVQMTTTTSRVIYGDDENGRIYDDHDFRKQELRELKLLQKQEKKQQTELHLKEQQAKEQQDRRFEQERSSLEKTYEADMDMLARQHKQLVEKTEQTQENELRSSSKRIRSEQEQELKIFRENLKQEIRLLKQEVDLFPKDKRKDEFKQRRSAMELDHEEKERAFLDSLKERHELLLRRLSEKHRDHLATINRNFLQQKQNAMRTREALLWELEEKQLHERHQLSKRHVKELCFMQRHQMIIRHEKELDQVKRMLQRKEEDMVKKQTMEKRALPKRIRAERKARDLMFRESLRISTNLDPEIERDRLKKFQEQEKKRYMQEERRFEVKHQKQLEELRATRESAIKELEQLQNEKRRALVEHEHSKLSEIDERLKGELREWREQLVPRKQVCMQIPV
Protein: S-sulfocysteine synthase (EC 2.8.5.1) (O-phospho-L-serine-dependent S-sulfocysteine synthase) (OPS-dependent S-sulfocysteine synthase) (O-phosphoserine sulfhydrylase) (EC 2.5.1.65) (Q79FV4)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the synthesis of S-sulfocysteine, utilizing O-phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S-sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as a sulfur donor and O-acetylserine (OAS) as acceptor substrate.
Interaction partners:
- Uncharacterized MFS-type transporter Rv0849
- Transposase
- Lipoprotein LpqS
- Multicopper oxidase MmcO
- O-acetylserine sulfhydrylase
- L-cysteine desulfhydrase Cds1
- Phosphoserine aminotransferase
- Bifunctional enzyme CysN/CysC
- Putative permease Rv2963
- Serine acetyltransferase
Sequence:
MRSRQTRDRYRLLPEGYQVTPGRNRHPGTMVGNTPVLWIPELSGTSDPDRGFWAKLEGFNPGGMKDRPALYMVECARARGDIAPGAAIVESTGGTLGLGLALAGKVYRHPVTLVTDPGLEPIIARMLTAYGAGVDMVTQPHPVGGWQQARKDRVAQLMAEYPGAWNPNQYGNPDNVGAYRSLALELVAQLGRIDVLVCSVGTGGHSAGVARVLREFNPDMRLIGVDTIGSTIFGQPASNRLMRGLGSSIYPRNVDYRAFDEVHWVAPPEAVWACRSLAATHYASGGWSVGAVALVAGWAARNLPADTTIAAVFPDGPQRYFDTIYNDAYCNEHELLGGQPPTEPDEIASPLDAVVTRWTRSTTVIDPTQVVS
Protein: Terpene cyclase paxA (EC 5.4.99.-) (Paxilline synthesis protein A) (E3UBL5)
Organism: Penicillium paxilli
Function: Paxilline synthesis protein A: Part of the gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD. The exact role of paxA in paxilline biosynthesis is still unknown.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTSITTSVLVLHSLLAANFKYYQSFQNGFIDMLSAMADSNSVSGLPGQLCREYTGIRPLDTFLTSCTVFFWPTFQGEIPGLSLYGIAFASAMIPMWLIIVIDVHRRRQPFGALVELIAFAGPLIQCIGPGLVMPLLLARIHTPSRDSKSASQFDYRTFIPSMIIGYILPLLLASLPAPLILSYHNKQQFIAIWQGWPLYSSVLMWAFRRRSGHVHCSRHKGLKHACIFALACSSAGHLVLLSLTWLWSLSYWGYIQSAPWNEPPLASLEAGVLRFLQWDYTLSASATLSWAIAFRHEVVQQKSLRISLLSLLRCLIGIVFLGPCSMVALLYWQTCSLQEEAGQKAPAKDKQLDQEI
Protein: DNA replication licensing factor MCM6 (EC 3.6.4.12) (Minichromosome maintenance protein 6) (AtMCM6) (F4KAB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cell division cycle 45
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM3
- Origin of replication complex subunit 5
- Minichromosome maintenance 10
- Cell division control protein 6 homolog
- Mini-chromosome maintenance complex-binding protein
Sequence:
MEAFGGFVMDEQAIQVENVFLEFLKSFRLDANKPELYYEAEIEAIRGGESTMMYIDFSHVMGFNDALQKAIADEYLRFEPYLRNACKRFVIEMNPSFISDDTPNKDINVSFYNLPFTKRLRELTTAEIGKLVSVTGVVTRTSEVRPELLYGTFKCLDCGSVIKNVEQQFKYTQPTICVSPTCLNRARWALLRQESKFADWQRVRMQETSKEIPAGSLPRSLDVILRHEIVEQARAGDTVIFTGTVVVIPDISALAAPGERAECRRDSSQQKSSTAGHEGVQGLKALGVRDLSYRLAFIANSVQIADGSRNTDMRNRQNDSNEDDQQQFTAEELDEIQQMRNTPDYFNKLVGSMAPTVFGHQDIKRAVLLMLLGGVHKTTHEGINLRGDINVCIVGDPSCAKSQFLKYTAGIVPRSVYTSGKSSSAAGLTATVAKEPETGEFCIEAGALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPVGGRYDKSKPLKYNVNLPPAILSRFDLVYVMIDDPDEVTDYHIAHHIVRVHQKHEAALSPEFTTVQLKRYIAYAKTLKPKLSPEARKLLVESYVALRRGDTTPGTRVAYRMTVRQLEALIRLSEAIARSHLEILVKPSHVLLAVRLLKTSVISVESGDIDLSEYQDANGDNMDDTDDIENPVDGEEDQQNGAAEPASATADNGAAAQKLVISEEEYDRITQALVIRLRQHEETVNKDSSELPGIRQKELIRWFIDQQNEKKKYSSQEQVKLDIKKLRAIIESLVCKEGHLIVLANEQEEAAEAEETKKKSSQRDERILAVAPNYVIE
Protein: 2-keto-3-deoxy-6-phosphogluconate-responsive transcriptional regulator of central carbohydrate metabolism HexR (Q8EE97)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- 2-dehydro-3-deoxy-phosphogluconate aldolase
- Phosphogluconate dehydratase
- Glucose-6-phosphate 1-dehydrogenase
- Transcriptional repressor of fatty acid degradation PsrA
- Pyruvate kinase
- NAD
Sequence:
MNTLEKVQKSLTHFSKSERKVAEVILASPQTAIHSSIATLAKMADVSEPTVNRFCRRLDTKGFPDFKLHLAQSLANGTPYVSRHVEEDDSPESYTTKIFESSMASLDTARQSLDVAAINKAVDILTQAKTISFFGLGASASVAHDAQNKFFRFNVPVICFDDVLMQRMSCINSNEGDVVVLISHTGRTKSLIEIARLARENGAAVIGITARNSPLSMECTLPVTMEVPEDTDMYLPMASRLAQLVTIDVLATGFTLRRGPRFRDNLKRVKEVLKESRINKDPIL
Protein: Ribonucleoside-diphosphate reductase small chain (EC 1.17.4.1) (Q382Q1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- dTMP kinase
- dTMP kinase
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
- Guanylate kinase, putative
- Guanylate kinase, putative
Sequence:
MPPKSHKRSRKEGEVEEPLLTENPDRYVIFPIKYPDIWQKYKEAESSIWTVEEIDLGNDMTDWEKLDDGERHFIKHVLAFFAASDGIVLENLAERFMCEVQVPEVRCFYGFQIAMENIHSETYSVLIDTYVVDPDEKQRLLHAIRTIPCIEKKAKWAIEWIGSQTSFPTRLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYEKYIVNKLPRDRVLEIICNAVLIEREFICDALPVRLIGMNSQLMTQYIEFVADRLLVSLGYDRHYNSKNPFDFMDMISLQGKTNFFEKKVGEYQKAGVMSSERSSKVFSLDADF
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (Q6TNU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- WRN RecQ-like helicase.
- Proliferating cell nuclear antigen
- DNA ligase
- DNA polymerase.
- DNA polymerase beta
- DNA replication helicase/nuclease 2.
- DNA repair nuclease APEX1
- DNA repair protein XRCC1
- Polymerase
- Double-strand break repair protein
Sequence:
MGIHGLAKLIADHAPSAIKEHEIKSYFGRKIAIDASMCIYQFLIAVRQDGNVLQNEDGETTSHLMGMFYRTIRMLESGIKPVYVFDGKPPQLKSGELEKRVERRAEAEKLLAQAQEAGEQENIDKFSKRLVKVTKQHNEECKKLLSLMGVPYIEAPCEAEASCAALVKAGKVYATATEDMDGLTFGTTVLLRHLTASEAKKLPIQEFHFSRILQDMELTHQQFIDLCILLGCDYCGTIKGIGPKRAIDLIKQHGSIEEILENIDPNKHPAPEDWLYKEARGLFLEPEVVDGTSVDLKWNEPDEDGLIQFMCAEKQFSEDRIRNGCKKITKSRQGSTQGRLDTFFTVTGSISSKRKEPETKGSAKKKQKTSATPGKFKKGK
Protein: BAR/IMD domain-containing adapter protein 2 (Brain-specific angiogenesis inhibitor 1-associated protein 2) (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate) (p58/p53) (Q60437)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQAEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPVWQQACADPNKIPDRAVQLMQQIASSNGSILPSTLSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGPDSEDYNPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAVPPPDYGTSSRAFPTQTAGTFKQRPYSVAVPAFSQGLDDYGARSVSSADVEVARF
Protein: Interferon gamma receptor 2 (IFN-gamma receptor 2) (IFN-gamma-R2) (Interferon gamma receptor accessory factor 1) (AF-1) (Interferon gamma receptor beta-chain) (IFN-gamma-R-beta) (Interferon gamma transducer 1) (P38484)
Organism: Homo sapiens (Human)
Function: Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG). Ligand binding stimulates activation of the JAK/STAT signaling pathway. Required for signal transduction in contrast to other receptor subunit responsible for ligand binding.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15356148, ECO:0000269|PubMed:15924140, ECO:0000269|PubMed:27599734}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10605012}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:23963039}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23963039}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10605012}. Note=Has low cell surface expression and high cytoplasmic expression in T cells. The bias towards cytoplasmic expression may be due to ligand-independent receptor internalization and recycling. {ECO:0000269|PubMed:10605012, ECO:0000269|PubMed:15356148}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Interferon gamma
- Interferon gamma receptor 1
- Tyrosine-protein kinase JAK1
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Signal transducer and activator of transcription 1-alpha/beta
- Cytochrome b-c1 complex subunit 7
- Interleukin-12 receptor subunit beta-1
Sequence:
MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL