wanglab/gogpt-training-data huggingface dataset:
Protein: Boi2p (A0A1D8PRW9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Elf1p
- Elongation factor 3
- Proteasome regulatory particle base subunit
- HECT-type E3 ubiquitin transferase
- Polyubiquitin
- RING-type E3 ubiquitin transferase
- Proteasome regulatory particle lid subunit
- Phosphatidylinositol-3-phosphate-binding protein
- Proteasome regulatory particle lid subunit
- Proteasome regulatory particle lid subunit
Sequence:
MDGGDTYICIKQFNARLGDELSLKIGDKIQVLADDREYNDGWYMGKNLLTGEAGLYPKTFTQLITNNDSKTLLRSRSRRMMAPKSSDQETTPKDTTTPVVSSNLNPNTPPNYPPTLSSSTEPSHLAEPMSQLNLNKDSQSSQYTGSHLNSQIDRALQELQGSNADLTNSGNSFNEHRNHHYNNNTNNNNNNNNNAATSNNYKQPQLMSKKSNDSLSSQYQYQSQSQQPKHLSGDKSRQSLTDDLDPLKANTWTPKQVSSYFALVLGFDMDVAGKFAQHKITGEILFELDLNLLKELDIDSFGTRFKLYKEIGKLKELNTEGVKDKQLRTDSSSTGSTGKNDTTSSALNSPPTASTTLHDAVPHIDDNDMLNNTGKQQTQLMPSAVLTNTSDYNNNSQQRSGSQHHQRKRSSSVDVAPQQYLASDSTFMSPRRAPQPPSGESPIDTSYKFGAGSEYDRPPSHYGMYMTRTNASSHALGSSSPGINSRPASSIYDSFSNHNRNGSSTSKQHHKRNSSVTNNNNNNNGNSNHKHHHRRHSSVFSYLSSGNDDSAKPTPKLLSSKFQSNNLYKGGDDGHGDFTSSSNNNNNNSKLVSPAQIKRETTSGQSSLHESGSKSKGKSQIFDLSNSPVDIDDAKFSPKKSNSVSVRTKSMDAIGGNGDDRRVASDSTGLSQSKPNNSSRLKGIRATSTQSFRSLTGSKKSKTSAFQEGIREITPDEAIKTASHSGYMSKRSNNNLAWRTRYFTLHGTRLSYFQSLKDKKEKGLIDITAHKVIPIDSASDDTDKADRYAAMYASTTFAGNYCFKLVPPAPGFKKGLTFTQPKTHYFAVETEEEMRAWVKALMQATIDIDDSVPVVSSCSTPTVSLNKAQELLAKAREETKLRDEQLKANGYIRSLEDINDTSFSASLDYPDMSGDIGFGSTSPVAATSAPKLTLDTNFNRKSSGTMGTTGTIGTPGTSGGTVPTTPQIPRSSSQSGGFASPYLLASGLLSPKSGGGAGPGGIVSSSSPINENGPLRNSTSNSEYFGDITYKSLKPPSRQNSQYASITSGGGSIGFGYGSNNSGLGGPATAIGGGGGGVLSSSTPYSTGSGSTASSMNYNNHNNNNNNNNSVNSPINEFRSSRDLKSSSSPTTTTGTSSTSGKKPQSRRTSDKMLGFSSDASGSHTFVIKPKK
Protein: Immunoglobulin heavy variable 4-34 (Ig heavy chain V-II region ARH-77) (P06331)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDLLHKNMKHLWFFLLLVAAPRWVLSQVQLQQWGAGLLKPSETLSLTCAVYGGSFSGYYWSWIRQPPGKGLEWIGEINHSGSTNYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCAR
Protein: Rab-3A-interacting protein (Rab3A-interacting protein) (Rabin-3) (Rabin8) (SSX2-interacting protein) (Q96QF0)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12007189, ECO:0000269|PubMed:31467083}. Nucleus {ECO:0000269|PubMed:12007189}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12221131}. Cell projection, lamellipodium. Vesicle {ECO:0000269|PubMed:31467083}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:31467083}. Note=Predominantly cytoplasmic but a small proportion colocalizes with SSX2 in the nucleus. Activation of protein kinase C results in redistribution to the periphery of lamellipodia. {ECO:0000269|PubMed:12007189}.
Interaction partners:
- Ras-related protein Rab-8A
- Ras-related protein Rab-11A
- BBSome complex member BBS1
- Rab11 family-interacting protein 3
- BBSome complex member BBS4
- Exocyst complex component 6
- BBSome complex member BBS5
- BBSome complex member BBS7
- BBSome complex member BBS2
- Protein PTHB1
Sequence:
MGLKKMKGLSYDEAFAMANDPLEGFHEVNLASPTSPDLLGVYESGTQEQTTSPSVIYRPHPSALSSVPIQANALDVSELPTQPVYSSPRRLNCAEISSISFHVTDPAPCSTSGVTAGLTKLTTRKDNYNAEREFLQGATITEACDGSDDIFGLSTDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLVLSSSPTSPTQEPLPGGKTPFKKGHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKEEL
Protein: PUF nine target 1 (Q385B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Chromosomal passenger protein
- DNA ligase, putative
Sequence:
MLSRAPRPNNRLIVVCSCIKNVSGWPFWKFQQMRKVKGVTDLCMLAFNSSGGSFEASITGSDYTLKNYENVVGYRQDMLEDFLQRCHDPGRSYFVYGGHGMGDYLELEENKLALQCHELASILGKRKFEAMVFDSCFMASLECAYQLRHNTRYIGACEGYVWAPDPNLDQHVFNQYSASAMSRFKHPKNILLAIQRDYCNKSPLADFAVLDTTHVESLKKYVEEHVMQRVYDRATFYNSEQQQRLSSIAQKELQNAYEDIKCGAKMLAAAPLTAQAPLCTALRRDSGDLIPKKKKREPARLALLRAAHFEHALYPSEVDDKHILDLKSYLIDMAREEEEGALVLPKGSELISTSGACGALKGPPPRTGVVEVHGSLPPRETHNSARYGRDSRHKGLDLFHRVVISHRQPRRKSIYASHLGGLSFPVLEYSPLSKPLRDWEGMDKKELLRKAREFLRKGVVEGVQMSESGASECGVRGGSSSITENSDSVASSMVSPQNVKLGIAPSALMRASLTTPSSGAPGQTVSSENG
Protein: Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450(BM-3)) (Cytochrome P450BM-3) (Fatty acid monooxygenase) (Flavocytochrome P450 BM3) [Includes: Cytochrome P450 102A1 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)] (P14779)
Organism: Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19) (Bacillus megaterium)
Function: Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions. Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products. Marginal activity towards short chain lengths of 8-10 carbons. Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG
Protein: DAB adaptor protein 1 (H0ZH85)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Intersectin 2
- Reelin
- Very low-density lipoprotein receptor
- LDL receptor related protein 8
- Amyloid-beta A4 protein
- Unconventional myosin-VI
- Intersectin-1
Sequence:
MSTETELQVAVKTSTKKDSKKKGQDRSEATLIKRFKGDGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGIVAVARSKGEHKQKVFLTVSFGGIKIFDEKTGLLQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREEMEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIREPETEENIYQVPTSQKKEGVYDVPKSQPVSLENGNLLLDIDENLVSVTQAVTQLELFGDMSTPPDVTSPPTPATPGDAFIPSSSQSLPASTDMFGSVPFSTAAVPSGYVAMGAVLPSFWGQQPLVQQQLAMGAQAPVAQVMQGGQPIAWGQPGIFPPTQQPWPSVPGQFQPAAFMPTQTVLPLQAAMFQGTIAPIATVPPTSDSNRSSPQTDRPRQKMGKEMFKDFQMAQPPPVPSRKPDQPSLSCTSEAFSSYFNKVGMAQEADDCDDFDISQLNLTPVTSTTPSTNSPPTPAPRQSSPSKSSASHTSDPAADDLFEEGFESPSKSEEPEAEAEPLYAQINRPKK
Protein: Protein Shroom4 (Q1W617)
Organism: Mus musculus (Mouse)
Function: Probable regulator of cytoskeletal architecture that plays an important role in development. May regulate cellular and cytoskeletal architecture by modulating the spatial distribution of myosin II.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17009331}. Note=Shows partial colocalization with the cytoplasmic pool of F-actin.
Interaction partners:
- Lysine-specific demethylase 6A
- Uncharacterized protein CXorf38 homolog
Sequence:
MESRPGSFQYVPVQLQGGAPWGFTLKGGLEHCEPLTVSKIEDGGKAALSQKMRTGDELVNINGTPLYGSRQEALILIKGSFRILKLIVRRRNTPVSRPHSWHVAKLLEGCPDVATTMHFPSEAFSLSWHSGCNTSDVSVQWCPLSRHCSTEKSSSIGSMESLEQPGQPTYEGHLLPIDQNMYPSQRDSAYSSFSASSNASDCALSLKPEEPPSTDCVMPGPGPIKVTDDQANVSENSGSSHSTSEDHVTSTSHASSYSDEGHHSGPAKMARGPPEPPVRSDSLPASRAQLLNGEQHRASEPVDSLPQKEKPGLETVLPPRSSNQFCCLSGQDQVTDEDHQNCELSKPSESSQDDCEHLLIEDSSKALDSPKAHDKGSNKEFGLLKEASADLANTLNFGAIPHLRGTMEHRHSAPEQLLASHLQQVHLDSRGSKGMELPIGQDGHQWTVSPLHNNPKGKKSPSLPTGGTQDQTRKERKTTPLDDKLMASVHQSQSDVLLGEVDGHPNRAGRASSDLTSQQPSATCSSVQQTRDFLSAHKIVDHTEASEEGDNEPKECGRLGGRRSGGPRGRSIQNRRRSERFATNLRNEIQRRKAQLQKSKGPLSQLCDTNEAVEETQEPPESPPLSASNASLLPSYKNVPSPGDKVFNKSMILRARSSECLSQASESSKARGGVEGRMSPGQRSGQSSLALNTWWKASDSSTLDTEKANAHHGVCRGHWRWSPEHNAQPQVALSTEAPSNPDDSKELKTSTPQAGEEAVLMPFADRRKFFEESSKSLSTSHLPGLTTHNNKPFIQRQKPIDQNFQSVSYRDLRCHPLDQSYHSADQSYHAADQSYHSLSPLQSETPTYPECFATKGRDNSLCCKPVHHGDCDYHRTCSHPCSAQGTVRHDPCICCSGEICPALLKRNLLPKCHNCRCHHHQCIRCTGCCHGPQHSAHEDSSMAPGNAWKSRKAAIQEFPVDKWKPITGNRKTSHSGREMAHSKAGFSLSTPFRPCIENPALDLSNYRAVSSLDILGDFKRASNKPEESSVYEDENSVASMPRPLRSRAFSESHISLEPQNTQAWGKHQRESFSKGSETQPDTLGARKKVFPPPRPPPPNWEKYRLFRAAQLQQQQQQQQQQQQQQRCEEEEEKEQEEEGEKEEDLPPQYFSSELTGSCAPNTEEQPQSLKMGHQEASRQGSQSLQEQEAFALHPSNFVPPVRGCTVPQPEKAQHPCYYGTHGLWRTTEQEATVTPKQEFQHFSPPKGASGIPTSYSAYYNISVAKAELLNKLKQQPEMAEAGLGEEGVDYELAQKKIQLIESISRKLSVLREAQRGLLDDINANAALGEEVEANLKAVCKSNEFEKYHLFIGDLDKVVNLLLSLSGRLARVENALNSIDSESNQEKLVLIEKKQQLTNQLADAKELKEHVDGREKLVFGMVSRYLPQDQLQDYQHFVKMKSALIIEQRELEEKIKLGEEQLKCLKESLHLGPSNF
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q6IRR4)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MSSILPFTPPVVKRLLGWKKSASGTTGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYSRLWRWPDLHSHHELKAVENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPSTLSPVNHNLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
Protein: Uncharacterized protein (Q38CJ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLESFEFDQERKEALNTVAELIASTIEGAESQDVHDVLSSSLHLPHNWQEIVQKRAEQRRKLSATFTLFCEETIATPSTDGNAALDISEAPATCFLPELRPKTMPPVTTSATRGFECPSCGNHWDVVDARKSLRNSNTSSAVRELSNADVGFCPVCEDI
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (P19117)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Adenylyl-sulfate kinase
- Plasma membrane ATPase 1
- Plasma membrane ATPase 2
- Putative inorganic pyrophosphatase C3A12.02
- ATP synthase subunit alpha
- ATP synthase subunit 5, mitochondrial
- V-type proton ATPase subunit c
- ATP synthase subunit gamma, mitochondrial
- Putative purine nucleoside phosphorylase
- Probable V-type proton ATPase 20 kDa proteolipid subunit
Sequence:
MSEYTTREVGALNTLDYQVYVEKNGTPISSWHDIPLYANAEKTILNMVVEIPRWTQAKLEITKEATLNPIKQDTKKGKLRFVRNCFPHHGYIWNYGAFPQTYEDPNVVHPETKAKGDSDPLDVCEIGEARGYTGQVKQVKVLGVMALLDEGETDWKVIVIDVNDPLAPKLNDIEDVERHMPGLIRATNEWFRIYKIPDGKPENSFAFSGECKNRKYAEEVVRECNEAWERLITGKTDAKSDFSLVNVSVTGSVANDPSVSSTIPPAQELAPAPVDPSVHKWFYISGSPL
Protein: RING-type domain-containing protein (Q381F3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEKRTNTFSSTLEKVITAFFYNGHAGRSRALSMGLQVPLWLWTHQVTVESERSTRELQKTVNLVCWFNDNGANLTQVAIIVPGDVKTKLGAQLKHALQGRAHDAQSGISDDVSLPTLLAPHELTAMNKRDKMVHQYEVVIYLLTLPPTKKHLQAAMQQDQFIADAVAGAGGAFILVTDVGWTTPRFTTQWPQWKALVMKLKGELVSISFNEGDKLPADAQLPSLMGPRIPLCCSRHADQRQLEYGIVPIVRGCRRLCLKPFVCQREEHVCMEQCHPRVSHSNCPYACQTAMPCGHECLHSCSELCNCFEVIEKPLTCSHAVIIGLDQATLQPIYATVRHVFKGSCADAFLPCAVEYPTECCRCLGPLSTTCSEATRCGHSLENKTLLCAACIRLEREVRAKVLGDLLIQTEEAKQRMKREVQRSAHQQRKASSQGLFLVGSRVTICDVTKVIKPLCAETDFPGVEFVDYEATDFYSSMDGAYGTFISRHVDIDDLSEVRNLIRLRDGKHVLVADGGVQLLRALTSAITQQAATLLLTYNGHGKERGDAGSTASGEAFETAFKMVGSQFYLAVPVPFGDTLISDKIVQVTAVNPASPETVIVECRIPSISSQTDETQVNDTINDNPSPPKRLRLEHSSSHPGHLRASIEVVSLTVPVTALESMEGYSKGKEVLVLDPSRQVVHPYDVQAFGAILQHVLDTDLRSAVISSVPVAKDTPFTLLGVVNPPVSFADRYGPCAVLRQRKQLVTVRARPHLRSGKRSPGSAPTPSGINTAYAHSARNGDDGDVVVIIPFVFTAADELLEAENSLDAAALQQLEQRVRDTIAVKSDELAIRNDEEAFHRQRQMPEVMEEELSRDRVAYSIPIPLPTAELLASVRVRHARLLCASATSLRLSKQKDAMAVKQQQLGLTKWLEAVRQRHEQDTEADAAYFRALQQKETAQ
Protein: Kelch-like protein 15 (Q96M94)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex. Acts as an adapter for CUL3 to target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits. Acts as an adapter for CUL3 to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR).
Subcellular location: Nucleus {ECO:0000269|PubMed:27561354}.
Interaction partners:
- Cullin-3
- DNA endonuclease RBBP8
Sequence:
MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDTFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPTSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNSWLQMADMSVPRSEFAVGVIGKFIYAVAGRTRDETFYSTERYDITNDKWEFVDPYPVNKYGHEGTVLNNKLFITGGITSSSTSKQVCVFDPSKEGTIEQRTRRTQVVTNCWENKSKMNYARCFHKMISYNGKLYVFGGVCVILRASFESQGCPSTEVYNPETDQWTILASMPIGRSGHGVTVLDKQIMVLGGLCYNGHYSDSILTFDPDENKWKEDEYPRMPCKLDGLQVCNLHFPDYVLDEVRRCN
Protein: Sterile alpha motif domain containing 4B (M0R0X3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMFRDQVGILAGWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQVPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGMKDVPSWLKSLRLHKYAALFSQNQL
Protein: Probable purine permease 16 (AtPUP16) (O04508)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEEFQGPEPRGQMMSENPRSLELNQRKWWISVFICGFLIFAGDSLVMLLLNFFYVQDNRSESDQDRQYKGTWTQALIQNAAFPILIPFFFILSSPKPNPETVSNQTNNGWFRVLSLYVSLGVLVSVYSKLYALGKLYVGWGILLSTQLILTSLFSAFINRLKFNRWIIISIIFTLGADFFGGPAFAGTPNEDETDPYDIKAWLILIFPTLAFSLSLCLMQLGFDKVLVKTKRYGNKKVFRMVLEMQICVSFIATLICTVGLFASGEFKELKGDSERFKKGKTYYILSLVGLALSWQVWAVGLLGLVLLVSGLFADVVHMGASPVVALLVVLAFDFMDDEFGWQRRGALLGAVLALASYFYSLHTKKKKEIAELNKRENNNSEA
Protein: E3 ubiquitin-protein ligase SMURF1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF1) (SMAD ubiquitination regulatory factor 1) (SMAD-specific E3 ubiquitin-protein ligase 1) (Q9CUN6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway (By similarity). Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of MAVS. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 6
- Mothers against decapentaplegic homolog 1
- TGF-beta receptor type-1
- E3 ubiquitin-protein ligase SMURF2
- Mothers against decapentaplegic homolog 5
- Runt-related transcription factor 2
- TGF-beta receptor type-2
- Protein patched homolog 1
- Mothers against decapentaplegic homolog 2
Sequence:
MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGPLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE
Protein: Transcription termination factor Rho (EC 3.6.4.-) (ATP-dependent helicase Rho) (Q72BR3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Transcription termination/antitermination protein NusG
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- Transcription termination/antitermination protein NusA
- DNA-directed RNA polymerase subunit beta'
- Polyribonucleotide nucleotidyltransferase
- Ribosome maturation factor RimP
- DNA-directed RNA polymerase subunit omega
- Thioredoxin
- CTP synthase
Sequence:
MNLSELKIKSMQELMELAEQFKVENASGMRKQELIFALLQACASQNGAIYGDGVLEILPDGFGFLRSPLCSYMPGPDDIYVSPSQIRRFALRKGDVVSGQIRPPKEGERYFALLKVTEIGFEPPENAKNLVLFDNLTPIYPDRQFIMENGDKNYSSRIIDIMAPIGCGQRGLIVAPPRTGKTMLLQTIANSINANSPDTYLIVLLIDERPEEVTDMERTVKNAEVVSSTFDEPPQRHVQVCEMVLEKAKRLVERKRDVVILLDSITRLGRAYNAVTPSSGRVLSGGLDANALQRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMEIYLDRHLSEKRVFPAIDINRTGTRKEDLLLSDEVLNRVWILRKILAPMSSIDSMEFLLDKMRGTKSNRDFMNCMNK
Protein: Ketol-acid reductoisomerase, chloroplastic (EC 1.1.1.86) (Acetohydroxy-acid reductoisomerase) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Protein KARI) (Q65XK0)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- dihydroxy-acid dehydratase
- Acetolactate synthase 1, chloroplastic
- Ketol-acid reductoisomerase
- Acetolactate synthase small subunit
- Os02g0608600 protein
- Probable acetolactate synthase 2, chloroplastic
- Kinesin-like protein KIN-14I
- Os04g0389100 protein
- Os09g0124100 protein
- Os03g0680400 protein
Sequence:
MAASTTLALSHPKTLAAAAAAAPKAPTAPAAVSFPVSHAACAPLAARRRAVTAMVAAPPAVGAAMPSLDFDTSVFNKEKVSLAGHEEYIVRGGRNLFPLLPEAFKGIKQIGVIGWGSQGPAQAQNLRDSLAEAKSDIVVKIGLRKGSKSFDEARAAGFTEESGTLGDIWETVSGSDLVLLLISDAAQADNYEKIFSHMKPNSILGLSHGFLLGHLQSAGLDFPKNISVIAVCPKGMGPSVRRLYVQGKEINGAGINSSFAVHQDVDGRATDVALGWSVALGSPFTFATTLEQEYKSDIFGERGILLGAVHGIVEALFRRYTEQGMDEEMAYKNTVEGITGIISKTISKKGMLEVYNSLTEEGKKEFNKAYSASFYPCMDILYECYEDVASGSEIRSVVLAGRRFYEKEGLPAFPMGNIDQTRMWKVGEKVRSTRPENDLGPLHPFTAGVYVALMMAQIEVLRKKGHSYSEIINESVIESVDSLNPFMHARGVAFMVDNCSTTARLGSRKWAPRFDYILTQQAFVTVDKDAPINQDLISNFMSDPVHGAIEVCAELRPTVDISVPANADFVRPELRQSS
Protein: Kallikrein 1-related peptidase b5 (EC 3.4.21.35) (Glandular kallikrein K5) (mGK-5) (Tissue kallikrein-5) (P15945)
Organism: Mus musculus (Mouse)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Interaction partners:
- Plasma protease C1 inhibitor
- Pregnancy zone protein
- Alpha-2-macroglobulin-P
- Kininogen-1
- B2 bradykinin receptor
- Kallikrein 1-related peptidase b3
- Angiotensin-converting enzyme
- B1 bradykinin receptor
- Antithrombin-III
- Corneodesmosin
Sequence:
MWFLILFLALSLGGIDAAPPVQSRIFGGFNCEKNSQPWQVAVYRFTKYQCGGVLLNANWVLTAAHCHNDKYQVWLGKNNFFEDEPSAQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLKKPADITDVVKPIDLPTEEPKLGSTCLASGWGSITPVIYEPADDLQCVNFKLLPNEDCVKAHIEKVTDVMLCAGDMDGGKDTCMGDSGGPLICDGVLHGITSWGPSPCGKPNVPGIYTKLIKFNSWIKDTIAKNA
Protein: Heat shock cognate 70 kDa protein 3 (HSC70-3) (Q54BE0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function in protein folding and assembly, and disassembly of protein complexes.
Interaction partners:
- DnaJ homolog subfamily A member 1 homolog
- Heat shock protein
- FAD-binding FR-type domain-containing protein
- Methyltransferase type 12 domain-containing protein
- Uncharacterized protein
- DUF51 family protein
- MATH domain-containing protein
- Type-2 histone deacetylase 1
- Heat shock cognate 90 kDa protein
- Luminal-binding protein 1
Sequence:
MTSIGIDLGTTYSCVGVWLNDRVEIIANDQGNRTTPSYVAFNDTERLIGDAAKNQVAMNPINTVFDAKRLIGRKFSDSVVQSDMKHWPFKVITNKNDDKPLIQVDFKGETKTFSPEEISSMVLSKMKETAESYLGKPVNNAVITVPAYFNDGQRQATKDAGTISKLNVQRIINEPSAAAIAYGLDKKGSKSGEIKVLIFDLGGGTFDVSLLSIDDGVFEVLATAGDTHLGGEDFDNRLVNHFVDEFKRKHKKDIMGNQRALRRLRTACERAKRTLSSSSQASVEIDSLYDGIDFYTSITRARFEELCSDLFNNCIEPVEKVLKDCKLDKKSIDEIVLVGGSTRIPKVQQLIQNLFNGKELNKSINPDEAVAYGAAVQAAILSGDKSSRISELIFIDVAPLSLGIETVGGVMTNIVPRNTIIPCKKTQTFSTHTDNQSGVLIQVYEGERTMTKDNNLLGKFELTGIPPAPRGTPQIEVSFDVDSNGILNVTAEDKTTKKVEKITITNDKGRLSLKDITKMVEDAEKFKEQDQQQKERIESKNNLENYIFSVKNSINDQKIISKLSKSDKNIIESETESTLKWLESNQSAEKDEFNQKISDLESIVNPILSKFYQGNNNPKPTTTTFNQDLD
Protein: Growth hormone secretagogue receptor type 1 (GH-releasing peptide receptor) (Ghrelin receptor) (A8CGH2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRSWPNRTDCLSPVNCSWEENYWNYYFNGSYRGPVPPENLFPIPVLMGITITCALLFLAGVTGNVMTILVVSKYRDMRTTTNLYLCSMAVSDLLIFLCMPPDVYRLWKYRPWIFGDTFCKLFQFVSECCTYSTILNITALSVERYLAICFPLRAKRLVTKRRVRALIIFLWLVSLLSAGPVFVLVGVEHETRPAAGNSVTAGGAEGQTEIDTSECKPTQYAVESGLLAAMALVSSVFFFLPVFCLTVVYSLIGRRLWKRRRENSIGANVAHRDKSNRQTVKMLAVVVFAFVLCWLPFHLHRYLMSHSSEGSSPLWSLFTQYCSLVSTVLFYLSAAINPVLYNTMSRKYRSAAAQLFGLQETQPPRGRTASTVKGESSPAWTESTVSL