wanglab/gogpt-training-data huggingface dataset:
Protein: D-serine transporter DsdX (P08555)
Organism: Escherichia coli (strain K12)
Function: A D-serine-specific transporter, may function as a H(+) symporter.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- D-serine dehydratase
- D-serine/D-alanine/glycine transporter
Sequence:
MHSQIWVVSTLLISIVLIVLTIVKFKFHPFLALLLASFFVGTMMGMGPLDMVNAIESGIGGTLGFLAAVIGLGTILGKMMEVSGAAERIGLTLQRCRWLSVDVIMVLVGLICGITLFVEVGVVLLIPLAFSIAKKTNTSLLKLAIPLCTALMAVHCVVPPHPAALYVANKLGADIGSVIVYGLLVGLMASLIGGPLFLKFLGQRLPFKPVPTEFADLKVRDEKTLPSLGATLFTILLPIALMLVKTIAELNMARESGLYILVEFIGNPITAMFIAVFVAYYVLGIRQHMSMGTMLTHTENGFGSIANILLIIGAGGAFNAILKSSSLADTLAVILSNMHMHPILLAWLVALILHAAVGSATVAMMGATAIVAPMLPLYPDISPEIIAIAIGSGAIGCTIVTDSLFWLVKQYCGATLNETFKYYTTATFIASVVALAGTFLLSFII
Protein: SH3 domain-containing protein (Q84R15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAESSGTTLMDLISADPTPVPAQSTSSSASSTASQPTSASASSSSHLHHPMSTKTTLGEKKSKRATLMQIQNDTISVAKAALNPVKANIMPQRQRQKKKPVSYSQLARSIHELAATLDQKSSQKQLVNHVFPKLAVYNSVDPSLAPSLLMLNQQCEDRNVLRYVYYYLARILSDTGMTPGGGIPTPNWDALADIDAGGGVTRADVVPRIVNQLTNEATNSEFEFHARRLQALKALTYSPSGNSELLSKLYEIVFGILEKVGDVPHKRKKGVFGTKGGDKESIMRSNLQYAAMSALRRLPLDPGNPLFLHRAAQGVFFADPVAVRHSLEILSELATRDPYTVAMTLEKLASPTGALQDILHMNDVLARVSLARLCHSISRARALDERPDIRSQFNSILYQLLLDPSERVCYEAILCILGKHDNTERMDERAAGWYRLTREILKLPEAPSLSSKDKSNKTKRPQPLIKLVMRRLESSFRSFSRPVLHAAARVVQEMGKSRAAAFAMGLQDIDESVHVNAFSDALDDAETNESSHPEGIRRTSSISAGPGRSDTIASLLAALMEVVRTTVACECVYVRAMVIKALIWMQSPDESLDELKSIIASELSDPGWPAALVNDVLLTLHARFKATPDMAVILLEIARIFATKVPGKIDADVLQLLWKTCLVGAGPDGKHTALEAVTIVLDLPPPQPGSMAGLTSIDRVSASDPKSALALQKLVQAAVWFLGENANYAASEYAWESATPPGTALMMLDADKMVAAASSRNPTLAGALTRLQRCAFSGSWEVRIVAIQALTTIAIRSGEPFRLQIYEFLYTLAEGGVQSQLSEMHLSNGEDQGASGTGLGVLITPMLKVLDEMYVGQDELIKDIRHHDNANKEWKDEELKKLYENHERLLDFVSMFCFIPRAKYLPLGPISAKLIDTYRTKHNITASTGSTDPAVVATGISDLIYESTQPAPAASNSSGLDDDLVNAWAANLGDDGLLGNNAPAMSRVNEFIAGVGTDAPDVEEENVFSRPSVGYDDMWAKTLLETSELEEEDARSGSSSPDSAGSVESSISSHFGGMNYPSLFSSKPSSQATAKSGGSKYQSTYEGYGSPIREEPPPPYSYSEPQSRESFENPVAGSGSRSYESDDEEPRKSTGTRFGTALYDFTAGGDDELNLTAEEELEIEYEVDGWFYVKKKRPGRDGKMAGLVPVLYVNQS
Protein: RE10062p (Q8IGX4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLPLLLPLFLSLTAGQLVNQPPQFVPGTGDMSRFSLSENTPVGSPVFQLKGTDPEGGRLKYSISGPVFSVDRETGVVRLRQELDRETQDTVEVIISITDEGIYGTEPNTVSQRRVIPVRYYNDNQPTFLGRPYTASVSESLPVGSELSVEPPIVVVDRDEGINSEVQMKCLEENDICDIFEVRAVKISDGNYTARVALKQQLDFESRPSYILTISASDSALDNRLSSLATISINVIDIQDQPPIFTNAPYSATVPENTPAGVSILTVKAVDGDVGIPREIFLSLEDEPFGHFELVPFGDPRDGTAVLQTTSEPLDRENAEILQNGGVYVFSIRATELIDGAIPAEHSLTRVTIVVTDVDDHQPTFSGPHFNVSITENLANGMPLPGLSIFVDDRDMGENSRYELSLRDVFNAARVFEVSPTESQGRTPVVVKVLNASRLDYDVVDPDLRKFEFDLVASVKGVEKAKTRVEIHLLDANDNAPVFDQGTYRFTAAENLPVDAIIGHVKATDLDSGEFGHVRYVLKGFGADNFYVNPETGGVYLLKPLDYEKQSSYSLTVVAIDGGQREANANLFVGVTDVNDNHPNFESKEYSRTIREGAALFEPQFFVRAHDADGPSQGNGRVKYSIVSENSIAGNVFRIEPDTGEIVIQKAARSMDTERGEYELVVSATDFGIPPLSNTTRVLVRVGISGNQRPIFRGHFQNMENLPIIGPPSYRVSIPENAAAGSNVTSVSAHDPDGLDSLLRYRIVGANDNFEIDEISGLITVSPQARIDRDSNMNSFEIIVNAVDSGTPIPETATTTVYVNVKDINDERPKFEQNSYATYVSERTAVGESVLRVKAIDKDLNSKLEYSMVGPVAATTKAGVSIANRSNYRLQEAFRVDSQSGEIFVNGTLRHDVAAIIIFTVGVRDLNAEVDPEGQVDTTEVTVYVQSFQDTNPVFKNTGWTSSRPVIDVKIKEEMPIDSALFILQAEDPVTRQPITSFELIEPKQVDYFQVAERTGEVILKKRLDYEALGDTGPEFELQVRANSADRQRSTVSRVNITVENVNDNSPRFERNSYQATIIENRPHPERVIRVRALDKDAVLNARDERLGYHKIIYSLQGEHAMLFDINNTTGEIIVASGQTIDRERTPRIQLQIKAEDSPGRPTDAKQSVVELQIEVLDVNDNAPEFTQKKYSTVIPENAQIDSFVLQLEAVDADEGLGGEVRYELVNEGEANGLFKIDTKSGLISTRRNLTGKGRAHPYVLIVRAQDNGNQMPKQPTLSTDTDVRIYIGDVSANDGVPYFLSPRVGQMANVTENAVTGAPVFQVIASDPDDESTPSGTITYRILPDTPDAEAFVIDAHSGLITTRQSMDRETKDMYRILLEVSDNGQPKQSATRILQIAILDVDDHEPRFAREAGAGPLSMSVREEEPAGTIVGNFSALDEDLGENAAIDYVIIDGNNEQLFTIERNNESLAILKTKKPIDREQVESFTLTIKCLKLGEPGYKFIGDPYDRQDLSHLRINVRVLDIDDNLPKFEQPDPTVGIRINVPIDTVVTTLKASDADAEAPPVGLSIENVTFVPQFYKRSRSLAVGNLHNLFTLNNRTGELRTGGSFADYVDGYFLMRVMANNSVQPKRQAHSNLKVFVIRDKSLLKFVFARPPNEIQHNIRPFQEQLQKKLKPLGLELHVLDTQVFTRPDMSLDFTATSSCFQMFKNGAALSFNEMQKLMNSQQLRQELIDIYAAYGVSEVESCSVRRTHAAAIFAGMLTSAGAWLVFLAALIGLAALVSLCTACCLKKKLKRHSKRSLQASLRTPTEHTATSYSYSMPAVLYSEPIYGPL
Protein: Bcl-2-like protein 13 (Bcl2-L-13) (Bcl-rambo) (Protein Mil1) (Q9BXK5)
Organism: Homo sapiens (Human)
Function: May promote the activation of caspase-3 and apoptosis.
Subcellular location: [Isoform 2]: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA type A receptor associated protein like 1
- FUN14 domain-containing protein 1
- Dynamin-1-like protein
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Peptidyl-prolyl cis-trans isomerase FKBP8
- CMRF35-like molecule 6
- Optineurin
Sequence:
MASSSTVPLGFHYETKYVVLSYLGLLSQEKLQEQHLSSPQGVQLDIASQSLDQEILLKVKTEIEEELKSLDKEISEAFTSTGFDRHTSPVFSPANPESSMEDCLAHLGEKVSQELKEPLHKALQMLLSQPVTYQAFRECTLETTVHASGWNKILVPLVLLRQMLLELTRRGQEPLSALLQFGVTYLEDYSAEYIIQQGGWGTVFSLESEEEEYPGITAEDSNDIYILPSDNSGQVSPPESPTVTTSWQSESLPVSLSASQSWHTESLPVSLGPESWQQIAMDPEEVKSLDSNGAGEKSENNSSNSDIVHVEKEEVPEGMEEAAVASVVLPARELQEALPEAPAPLLPHITATSLLGTREPDTEVITVEKSSPATSLFVELDEEEVKAATTEPTEVEEVVPALEPTETLLSEKEINAREESLVEELSPASEKKPVPPSEGKSRLSPAGEMKPMPLSEGKSILLFGGAAAVAILAVAIGVALALRKK
Protein: Protein EMSY-LIKE 3 (AtEML3) (F4K2F0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the regulation of chromatin states (Probable). Contributes to basal immunity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9C7C4, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- DUF724 domain-containing protein 7
- Transcription initiation factor TFIID subunit 12
- Paired amphipathic helix protein Sin3-like 2
- Transcription factor bHLH48
Sequence:
MDYRPSDSSGTDDDLPPSHQGRYQRNARPTGNGRPSVLNSAPLSRVHNEMETQIHLIEQEAYSSILRAFKAQSDAITWEKESLITELRKELRVSDEEHRELLSRVNADEMIRRIREWRKANSLQSSVPQLVHDAPSPAVSGSRKKQKTSQSIASLAMGPPSPSLHPSMQPSSSALRRGGPPPGPKTKKPKTSMQYPSTGIAGRPQAGALTNEPGESGSYDPLVGRKVWTKWPDDNQYYEAVITDYNPVEGRHALVYDINSANETWEWVNLKEISPGDIRWEGEDPGISRKGGHPGQGRGTKTMARGGPASNAGGRGRGSMRMQQPKTQNGIGKKALGEIEILHTETLLKEVEKVFGSVNPNPAEVEKAKRVLRDHELALMDAIAKLEEISDGESGNI
Protein: Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-2-1 (IbF6H2-2-1) (EC 1.14.11.61) (EC 1.14.11.62) (2-oxoglutarate-dependent dioxygenase F6H2-2-1) (2OGD F6H2-2-1) (G9M9M3)
Organism: Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Function: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity toward caffeoyl-CoA.
Interaction partners:
Sequence:
MPSTTLSTVLSDINDFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPIEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDAVEYLKSCEMVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPRPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE
Protein: Small ribosomal subunit protein uS19 (30S ribosomal protein S19) (P0A7U3)
Organism: Escherichia coli (strain K12)
Function: In the E.coli 70S ribosome in the initiation state it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states, contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.
Interaction partners:
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL20
- Elongation factor G
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
- Large ribosomal subunit protein bL9
Sequence:
MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK
Protein: THO complex subunit 2 (E2QCS8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Hpr1
- THO complex subunit 5
- THO complex protein 7
- FI07663p
- THO complex subunit 6
- ATP-dependent RNA helicase WM6
- LD24793p
- RNA and export factor binding protein 2, isoform A
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
Sequence:
MQRSTDRLRRLKKLKSVTGAQDGVGGGDAAATADNRTSASSDTNGAAASSGAGGNQPGTLNPEVFKHLDKSGRSEFLKYLKHQLQDAADTPVYDKNGVFKQGISNAIYQLLWQTLRFTHKKDIVLHLLLEVVALHADFPSLIVDVVNILDSETSLITDGLQEERHAFVQLVKDLDRVIPESLLKERLEIDTLQEAGIVKNKSFYSKFIKVKTKLYYKQRRFNLFREESEGFAKLITELNQEFDENTTPESIMDIIKSLIGCFNLDPNRVLDIIIESFETRPDRWNLFIPLLRSYMPTGAIICEVLGYKFCHFKDSRTPRSLYHVCALLLKHGVIALNDVYVWLTPNDGSIKADWEEDLADAREMVRKLNLIQTNKKEDEKDPPPPPSVKKFNEEKYNANQKFGLCEALLKVGDWENAYKIIQKLPEQAVVLQEPIARAIADLIHLSVENIYYKKCFKAPAGRRPSRNRLYEDSKLVAKMQAKEFGDLRKYTWPMANVLGPAMHYDTVLMYKLIRIMRKLVVDMGVDSLNGPPPNSEAEQHYYDIMSSLDACILPSLLYLDNNCSMSEEIWAVLKYFPYHFRYSLYARWKNDSYQLHPNLIRRCGLAQRDIKALMKRVSKENVKQLGRLVGKYSHCAPGLLFDYILLQIQIYDNLIGPVCDLLKYLTALSFDCLGYCIIESLTLTGRLRFKDDGTSLSLWLQSLASFCGTIYKKYSIELSGLLQYVANQLKSQKSLDLLILREIVHKMAGVESCEEMTNDQLQAMCGGEQLRGEAGYFSQVRNTKKSSNRLKEALANNDLAVAICLLMAQQKHCVIYRETAAHSHLKLVGNLYDQCQDTLVQFGTFLGSTYSVDEYVERLPSIITMLREYHINTDVAFFLARPMFTHQINQKYDQLRKDDPNAKKLTTTQKLQKYLEATQLIMNPIVESVRPLHSSKVWEDISPQFLVTFWSLSMYDLHVPNESYQREVAKLKQLAQQAAEGKDSNQSKNKKEQERYIALMEKLNDERKKQHEHVDKISQRLQEQKDSWFLLRSGKSAKNDTITQFLQLCLFPRCTFTALDALYCAKFVHTIHNLKTSNFSTLLCYDRIFCDITYSVTSCTEGEATRYGRFLCAMLETVMRWHADQAVFNKECANYPGFVTKFRVSNQFSEANDHVGYENYRHVCHKWHYKITKAIVFCLDSKDFMQIRNALIILMRILPHYPVLSKLAQIIERKVDKVREEEKTKRPDLYAIASSYIGQLKLKTPHMLKESVFHQIAERPNKESPTSVGAPAAATRSDKLSPTSPSGNTQGTRAPGGAAPFYNSEQKSVIKEPDAKAASTTRESKSQRGEGNNVTLVSTATSTASNNERESKQRDLPAPRESQSRSKDDQQEQANNGSNGSRQSESRNRDVERDRHDQQDQRSISSHRSSRDIVRVKERTEAELHQRSRERSQRLEELEAQQRKREKTSRRGGEERIRHGDGVETVDLVGSTDNRHYEEFEGRMRDLSSVSNESNGSLHHRQRSHETIEFEKVDSKRRKLESSTSSSKKVEELVDSVKKARALKTKERNKDKLSDEERDARKDRKLGRKRDRVDESNSNEHKRRREGQNGEEELRDRERHREKSPRERSHEKFDRERGGASGSRAEERQYISKSARSSRVNY
Protein: Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34) (Q00721)
Organism: Rotavirus A (strain RVA/SA11-4F/G3P6[1]) (RV-A) (Simian Agent 11 (strain 4F))
Function: Plays an important role in stimulating the translation of viral mRNAs. These mRNAs are capped but not polyadenylated, instead terminating in a conserved sequence 'GACC' at the 3' that is recognized by NSP3, which competes with host PABPC1 for EIF4G1 binding. The interaction between NSP3 and host EIF4G1 stabilizes the EIF4E-EIF4G1 interaction, thereby facilitating the initiation of capped mRNA translation.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094}.
Interaction partners:
Sequence:
MLKMESTQQMAVSIINSSFEAAVVAATSALENMGIEYDYQDIYSRVKNKFDFVMDDSGVKNNLIGKAITIDQALNNKFGSAIRNRNWLADTSRPAKLDEDVNKLRMMLSSKGIDQKMRVLNACFSVKRIPGKSSSIIKCTKLMRDKLERGEVEVDDSFVDEKMEVDTIDWKSRYEQLEQRFESLKSRVNEKYNNWVLKARKMNENMHSLQNVISQQQAHIAELQVYNNKLERDLQNKIGSLTSSIEWYLRSMELDPEIKADIEQQINSIDAINPLHAFDDLESVIRNLISDYDKLFLMFKGLIQRCNYQYSFGCE
Protein: Trigger factor (TF) (EC 5.2.1.8) (PPIase) (Q9WZF8)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Subcellular location: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL3
- Elongation factor Ts
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL2
Sequence:
MEVKELERDKNRVVLEYVFGAEEIAQAEDKAVRYLNQRVEIPGFRKGRIPKNVLKMKLGEEFQEYTLDFLMDLIPDTLKDRKLILSPIVTERELKDVTARVVVEVHEEPEVRIGDISKIEVEKVDEEKVLEKYVERRIEDLRESHALLEPKEGPAEAGDLVRVNMEVYNEEGKKLTSREYEYVISEDEDRPFVKDLVGKKKGDVVEIEREYEGKKYTYKLEVEEVYKRTLPEIGDELAKSVNNEFETLEQLKESLKKEGKEIYDVEMKESMREQLLEKLPEIVEIEISDRTLEILVNEAINRLKREGRYEQIVSSYESEEKFREELKERILDDIKRDRVIEVLAQEKGISVNDEELEKEAEELAPFWGISPDRAKSLVKARQDLREELRWAILKRKVLDLLLQEVKVKVVEPKGEGDDSEGKEDN
Protein: Uncharacterized protein, isoform B (EC 3.1.6.-) (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Q9VVM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD23158p
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MSTHLDKFSSATSLLTGFVLCIALSNGIVATSDKPNIIIIMADDLGFDDVSFRGSNNFLTPNIDALAYSGVILNNLYVAPMCTPSRAALLTGKYPINTGMQHYVIVNDQPWGLPLNETTMAEIFRENGYRTSLLGKWHLGLSQRNFTPTERGFDRHLGYLGAYVDYYTQSYEQQNKGYNGHDFRDSLKSTHDHVGHYVTDLLTDAAVKEIEDHGSKNSSQPLFLLLNHLAPHAANDDDPMQAPAEEVSRFEYISNKTHRYYAAMVSRLDKSVGSVIDALARQEMLQNSIILFLSDNGGPTQGQHSTTASNYPLRGQKNSPWEGALRSSAAIWSTEFERLGSVWKQQIYIGDLLPTLAAAAGISPDPALHLDGLNLWSALKYGYESVEREIVHVIDEDVAEPHLSYTRGKWKVISGTTNQGLYDGWLGHRETSEVDPRAVEYEELVRNTSVWLQLQQVSFGERNISELRDQSRIECPDPATGVKPCLPLEGPCLFDIEADPCERSNLYAEYQNSTIFLDLWSRIQQFAKQAHPPNNKPGDPNCDPRFYHNEWTWWQDEKASSSGTIGVMKVFTLLVVFIFTSSCIN
Protein: Vacuolar protein sorting-associated protein 16 homolog (A0A8I5ZY36)
Organism: Rattus norvegicus (Rat)
Subcellular location: Late endosome membrane {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007949}. Lysosome membrane {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007949}. Note=Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. {ECO:0000256|PIRNR:PIRNR007949}.
Interaction partners:
Sequence:
MDCYTANWNPLGDSAFYRRKYELYSMDWDLKEELKDCLVAAAPYGGPIALLRNCWRKEKAASVRPVLEMYSASGMPLASLWCSHGQCRHTGEVLQNRVLDARIFHTEFGSGVAILTGAYRFTLSANVGDLKLRRMPEVPGLQSAPSCWTTLCHERVAHILLAVGPDLYLLDHATCSAVTPAGLAPGVSSFLQMAVSFTYRYLALFTDTGYIWMGTASLKEKLCEFNCNIRAPPKQMVWCSRPRSKEKAVVVAWERRLMVVGNAPESIQFVLDEDSYLVPELDGVRIFSRSTHEFLHEVPVASEEIFKIASMAPGALLLEAQKEYEKESQKADEYLREIQELGQLIQAVQQCIEAAGHEHQPDMQKRLLRAASFGKCFLDRFPPDSFVHMCQDLRVLNAIRDYHIGIPLTYTQYKQLTIQVLLDRLVLRRLYPLAIQICEYLRLPEVQGVSRILAHWACYKVQQKDVSDEDVARAINQKLGDTPGVSYSDIAARAYGCGRAELAIKLLEYEPRSGEQVPLLLKMKRSKLALSKAIESGDTDLVFTVLLHLKNELNRGDFFMTLRNQPMALSLYRQFCKHQELDTLKDLYNQDDNHQELGSFHIRASYAAEERIEGRVAALQTAADAFYKAKNEFAAKATEDQMRLLRLQRRLEDELGGRFLDLSLHDTVTTLILGGHNKRAEQLARDFRIPDKRLWWLKLSALADLEEWEELEKFSKSKKSPIGYLPFVEICMKQHNKHEAKKYASRVGPEQKVKALLLVGDVAQAADVAIEHRNETELSLVLSHCTGTTDGAIADKIQRARAQAQKK
Protein: Flagellar radial spoke protein 3 (P12759)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Protein 3 may attach the radial spoke to the outer doublet microtubule or is required to form a stable spoke structure.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:17967944}. Note=Radial spoke. {ECO:0000305|PubMed:17967944}.
Interaction partners:
Sequence:
MVQAKAQQQLYTHAAEPKAVQQRRAKYREDETTQTLPTANIMFDRRVVRGNTYAARILPADATQTQTKGPSPASTKKRTTRTLPPRTPEAVDGRRHIDIQTDVYLEELTDTVPEADTSTQTDAFLDRPPTPLFVPQKTGTDAITQIENGDLFDFDFEVEPILEVLVGKVLEQGLMEVLEEEELAAMRAHQEHFEQIRNAELVATQRMEAAERRKLEEKERRMQQERERVERERVVRQKVAASAFARGYLSGIVNTVFDRLVSSGYIYDPVMREVETAFMPWLKEQAIGYLARGVVARRVVDKLVEDAAAALAANRSTLADKAASTAATVDAWAERQAKMEAELQGKELEAVRRRPTFVLRELKPAVASADAVEAAAAELTAQAEEAANAKWEADKAEAAEKARAEAEAAAEEQKALLEELAATAAAEAEERGEEPPAEPPSLPDGVEPVDVEAEVAKAVEAVPKPPVKEVTDIDILSYMMDKGAITKDAIIQALAVHALGDKAYTNHPAFAEAEGA
Protein: (E2-independent) E3 ubiquitin-conjugating enzyme FATS (EC 2.3.2.-) (Centrosomal protein C10orf90) (E2/E3 hybrid ubiquitin-protein ligase FATS) (Fragile-site associated tumor suppressor homolog) (FATS) (Q96M02)
Organism: Homo sapiens (Human)
Function: Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage. Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits ubiquitin ligase (E3) activity and assemble ubiquitin polymers through 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-63'- (K63)-linkages, independently of the ubiquitin-conjugating enzyme (E2). Promotes p53/TP53-dependent transcription of CDKN1A/p21, leading to robust checkpoint response. Mediates CDKN1A/p21 protein stability in a ubiquitin-independent manner. Interacts with HDAC1 and prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21 (By similarity). May have a role in the assembly of primary cilia (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20844083}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20844083}. Note=Localizes to the actin cytoskeleton in a proportion of cells. Colocalizes with centriolar acetylated tubulin. {ECO:0000269|PubMed:20844083}.
Interaction partners:
- Dedicator of cytokinesis protein 1
Sequence:
MLKLSGEGLRDSYHSRRDQIALKNLQSDVTEAKSDFTKETLASQNTKMISSIVISQMIDENKSRENRASLPLPCAIAQSRAHHAKQSLANRSGVNIHRAFALLPGRLGIPAPSDERGPEAELPPKEERPCGGPRRGFASITITARRVGPPARALVWGTAGDSLCPKCRAEDTLFQAPPALANGAHPGRHQRSFACTEFSRNSSVVRLKVPEAHTGLCERRKYWVTHADDKETSFSPDTPLSGKSPLVFSSCVHLRVSQQCPDSIYYVDKSLSVPIEPPQIASPKMHRSVLSLNLNCSSHRLTADGVDGLVNREPISEALKQELLEGDQDLVGQRWNPGLQESHLKETPSLRRVHLGTGACPWSGSFPLENTELANVGANQVTVRKGEKDHTTHCHASDHANQLSIHIPGWSYRAVHTKVFSGSSKRQQGEVCMTVSAPPVEQKPTRHFLPIGDSSPSDDCLSRDLSEPTERRHQSFLKPRILFPGFLCPLQDVCASLQEDNGVQIESKFPKGDYTCCDLVVKIKECKKSEDPTTPEPSPAAPSPAPRDGAGSPGLSEDCSESQQTPARSLTLQEALEVRKPQFISRSQERLKKLEHMVQQRKAQRKEDLRQKQSLLPIRTSKKQFTIPHPLSDNLFKPKERCISEKEMHMRSKRIYDNLPEVKKKKEEQRKRVILQSNRLRAEVFKKQLLDQLLQRNAV
Protein: O-acyltransferase (Q8ST50)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}.
Interaction partners:
Sequence:
MTTNKDPQDKEPGKAEQPTKNSGSSGVGIMKRLRRSASATEHNLSSLRNRKSTQNLFDQHGNPIDLRQYRKVLDKDENGNGTNGSEKKLRYRRTQSVTRAEEISNKEEKQRRAQPGRPIHRPRDSLFSWSSGFTNFSGLVNWGFLLLCIGGLRLGLENLLKYGIRINPLDWFFFISGHNEGEGHNALILSIYSLVHISLCLAVEKGLAMEIIAEGLGLFIQIVNIVVLVCLPVVTIHLKGHAFSLMGASTVCFFYSVLFLKLWSYVQTNMWCRQTYYQKNPRERRPSITLAELKKGVLNGGEEDEDVSKLVQYPDNLTYNDLLYFLCAPTLCYELNFPRTSRVRKRFLLKRLLEVVIGVNVVMALFQQWIIPSVRNSLIPFSNMDVALATERLLKLALPNHLCWLCFFYLMFHSFLNAVGELLNFADRNFYCDWWNANNIDTFWRTWNMPVHRWCVRHLYIPVVQMGYSSRQASTIVFLFSAVFHEYLVSVPLQIYKIWAFMGMMGQIPLSAISKSIEKKLGPRMGNIIVWASIILGQPLCIMAYYHDYVVQHFKNSLNGTDYSS
Protein: Transport and Golgi organization protein 2 homolog (Q6ICL3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31276219, ECO:0000269|PubMed:32909282, ECO:0000269|PubMed:36961129}. Mitochondrion {ECO:0000269|PubMed:32909282, ECO:0000269|PubMed:35197517, ECO:0000269|PubMed:36961129}. Golgi apparatus {ECO:0000269|PubMed:26805781}. Note=Localizes predominantly to mitochondrion. Deteted in close proximity to endoplasmic reticulum and lipid droplets. {ECO:0000269|PubMed:36961129}.
Interaction partners:
- Mitochondrial ribosomal protein L40
Sequence:
MCIIFFKFDPRPVSKNAYRLILAANRDEFYSRPSKLADFWGNNNEILSGLDMEEGKEGGTWLGISTRGKLAALTNYLQPQLDWQARGRGELVTHFLTTDVDSLSYLKKVSMEGHLYNGFNLIAADLSTAKGDVICYYGNRGEPDPIVLTPGTYGLSNALLETPWRKLCFGKQLFLEAVERSQALPKDVLIASLLDVLNNEEAQLPDPAIEDQGGEYVQPMLSKYAAVCVRCPGYGTRTNTIILVDADGHVTFTERSMMDKDLSHWETRTYEFTLQS
Protein: (S)-8-amino-7-oxononanoate synthase BioU (EC 2.6.1.121) (8-amino-7-oxononanoate carboxylating dehydrogenase) (Q55650)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+ (By similarity). A coupled Synechocystis BioU/BioD assay produces dethiobiotin from DAN. Complements a bioA deletion in E.coli but not a bioD1 deletion.
Interaction partners:
- Ferredoxin-dependent glutamate synthase 1
- Ferredoxin-dependent glutamate synthase 2
Sequence:
MENNSLAPLRVGILGFGGLGQAAARLLAPKQEMKLVAVADRHGYLYDADGIDVDNAVQAYTQQGSVGKAKKGQMSEQSIEDLIGEGEVDGYFLALPNLPNTFMADVTRQFIASGWQGVLVDALKRTSAVEQLITLREDLAQAGITYMTGCGATPGLLTAAAAIASQSFQEIHQVKITFGVGIANWEAYRATIREDIAHMPGYNVDKAQAMTDAEVAALLDQTNGILALEDMEHADDIMLELAGICHRDQVTVGGVVDTRNPKKPLSTHVKITGRTFEGKISSHTFTLGDETSMAANVCGPAFGYLKAGYGLHRQGLKGLFTAADVMPKFVR
Protein: ATP synthase F(0) complex subunit k, mitochondrial (ATP synthase membrane subunit DAPIT, mitochondrial) (Diabetes-associated protein in insulin-sensitive tissues) (HCV F-transactivated protein 2) (Up-regulated during skeletal muscle growth protein 5) (Q96IX5)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:21345788, ECO:0000269|PubMed:29917077}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MAGPESDAQYQFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT
Protein: BZIP domain-containing protein (A7RQI7)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- BZIP domain-containing protein
- BZIP domain-containing protein
- Uncharacterized protein
- Stress-activated protein kinase JNK
- Stress-activated protein kinase JNK
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
Sequence:
PLPPIDLELQEIVKRERKKQKNRVAASKCRRKKLEREAQLEVRVQQLKEKSIELNAVASALRQQVGELKQRVLEHVAFGCQLPAVTNSAY