wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1) (P62196)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62195}. Nucleus {ECO:0000250|UniProtKB:P62195}.
Interaction partners:
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 6A
- Proteasome subunit alpha type-6
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasomal ubiquitin receptor ADRM1
Sequence:
MALDGPEQMELEEGKAGSGLRQYYLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
Protein: S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (Methionine adenosyltransferase) (MAT) (O60198)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine decarboxylase proenzyme
- Uncharacterized protein C57A7.07c
- Spermidine synthase
- Aromatic amino acid aminotransferase C56E4.03
- Aromatic amino acid aminotransferase C1773.13
- Aromatic amino acid aminotransferase C569.07
- 6,7-dimethyl-8-ribityllumazine synthase
- Cystathionine beta-lyase
- Adenosylhomocysteinase
Sequence:
MAQTFLFTSESVGEGHPDKICDQISDAILDACLKDDPFSKVACETASKTGMVMVFGEITTRSQIDYQKVIRNTIKSIGYDDSEKGFDYKTCNVLVAIEQQSPDIAQGLHYEKALEELGAGDQGIMFGYATDETPEKLPLTILLAHKLNAAMSVARRDGSLPWLRPDTKTQVTIEYEEENGAVIPRRVDTIVVSAQHADSISTEDLRSEILEKIIKPTVPAHLLDEKTVYHIQPSGRFVVGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYSKVDRSAAYAARWIAKSLVAAGLARRCLVQLSYAIGVAEPLSIFVNTYGTSSKTSAELVEIIRKNFDLRPGVLVKSLKLQTPFYLSTASYGHFTDQSKPWEQPKELKF
Protein: Protocadherin related 15 (A0A8I6GK65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSPQFALWKCMPHGILLASLLIVSWGQYDDDCKLARGGPPATIVAIDEESRNGTILVDNMLIKGTAGGPDPTIELSLKDNVDYWVLLDPVKQMLFLNSTGRVLDRDPPMNIHSIVVQVQCVNKKVGTVIYHEVRIVVRDRNDNSPTFKHESYYATVNELTPVGTTIFTGFAGDNGATDIDDGPNGQIEYVIQYNPEDPTSNDTFEIPLMLTGNVVLRKRLNYEDKTRYYVIIQANDRAQNLNERRTTTTTLTVDVLDGDDLGPMFLPCVLVPNTRDCRPLTYQAAIPELRTPEELNPILVTPPIQAIDQDRNIQPPSDRPGILYSILVGTPEDYPRFLHMHPRTAELTLLEPVNRDFHQKFDLVIKAEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYNVYVYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGSKGDFVINRTTGLVSIAPGVELVVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAVLLNLQATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFTNSTYTVVVEENLPAGTAFLQIEAKDVDLGANVSYRIRSPEVKHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGTPITTVYAEDADPPGLPASRVRYRVDDVQFPYPASIFDVEEDSGRVITRVNLNEEPTTIFKLVVVAFDDGEPVMSSSATVRILVLHPGEIPRFTQEEYRPPPVSELAARGTVVGVISAAAINQSIVYSIVAGNEDDKFGINNVTGVIYVNSPLDYETRTSYVLRVQADSLEVVLANLRVPSKSNTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFTSVLRVKATDRDTGNYSAMAYRLIIPPIKEGKEGFVVETYTGLIKTAMLFHNMRRSYFKFQVIATDDYGKGLSGKADVLVSVVNQLDMQVIVSNVPPTLVEKKIEDLTEILDRYVQEQIPGAKVVVESIGARRHGDAFSLEDYSKCDLTVYAIDPQTNRAIDRNELFKFLDGKLLDINKDFQPYYGEGGRILEIRTPEAVTSIKKRGESLGYTEGALLALAFIIILCCIPAILVVLVSYRQFKVRQAECTKTARIQSAMPAAKPAAPVPAAPPPPPPPPPPGAHLYEELGESAMHNLFLLYHFEQSRGNNPVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLDNQANPARTFSFLPDEDDLSTHNPLYMESIGQRSTNSDLQPGTEFGELFVPRTQVKSQSLRGPREKIQRVWNQSVRFPRRLMWKTPNRPETIDLVEWQITRQRAECEKTRCHPSQQGSSNLMVTTEDARGSEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELGSEPDVVTSPADCTLELSPPRRPRVLNSLGSKRETPTCASDTETKRNSFEMVPHPPSISAPLPQLPLPQPPIAFTTFPLPLSSPNPPRPQLLTFSLPISTTPASSLPPPPPPSLPPPPRPPAPRLFPLPPSTSVPSTDSISTPAAKCTASVTHARETMSTTQPPASNPPCGAEPHRHPKGILRHVKNLAELEKSVSNMYSHIEKNCPPTELSKLHPFCPAEKTNMKITCDQSQETLVRVVEGIDVQTHSQSTSL
Protein: AcetylCholine Receptor (P91197)
Organism: Caenorhabditis elegans
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MIFNLINSILSLVIIHSNLCDGSVAETKLFTDLLKGYNPLERPVQNSSQPLEVKIKLFLQQILDVDEKNQIVSVNAWLSYTWFDHKLQWEPKKYGGIQDIRFPGSSDHIWKPDVLLYNSAAEDFDSTFKSNLLTYHTGTVVWIPPGVLKFVCQLDVTWFPFDDQVCEMKFGSWTFHGYAIDLQIDDDTNGTQSMDLSTYLVNGEWQVISTNAKRVVSYYKCCPEPYPTVNYYLHIRRRTLYYGFNLIIPSLLISLMAILGFMFPPDAGEKITLEVTILLAIVFFLSMVSEMTPPTSEAVPLIGVFFSCCMLVVSASVVFTIVVLNLHFRSADSHEMNPLVRRVLLEFLPWLLFMSRPGYKFVKANVIDSTDKMPKKPKNPLDCNLPSNHAGYEAQILLLHSVHTELRRVVAFYNKEEHDERIQTDWRFAAMVVDRACLLLFTVFIVISILAIMMSAPHIIA
Protein: Musashi, isoform D (A0A0B4K6K8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLFENPAVAAKLPFPYNVPPPLQAAAAAAAAVPNLSNPMENAAAAAAAAAAGLIDPHHNRDLHQALVASIANNSVAAIGGGLTTAAVLKSAAQQSQQAVQQNQNAVVVTPGLEQPKQEPAQQAALALLKENVNASAGAGQNNGQAAMGGSNKSGSSGRSTPSLSGGSGSDPAPGKLFVGGLSWQTSSDKLKEYFNMFGTVTDVLIMKDPVTQRSRGFGFITFQEPCTVEKVLKVPIHTLDGKKIDPKHATPKNRPRQANKTKKIFVGGVSQDTSAEEVKAYFSQFGPVEETVMLMDQQTKRHRGFGFVTFENEDVVDRVCEIHFHTIKNKKVECKKAQPKEAVTPAAQLLQKRIMLGTLGVQLPTAPGQLIGARGAGVATMNPLAMLQNPTQLLQSPAAAAAAQQAALISQNPFQVQNAAAAASIANQAGFGKLLTTYPQTALHSVRYAPYSIPASAATANAALMQAHQAQSVAAAAHHHQQQQQQQHHHQQQTHNAHVAAAQQQQQSHHNAVSNPASQAHSAAAAAALAANAANGAGAAGAHSLAAAAQQAGLMAGNPLNAAAAAAAAAANPAAAYSNYALANVDMSSFQGVDWSTMYGMGMYV
Protein: Leukocyte receptor cluster member 8 (Q96PV6)
Organism: Homo sapiens (Human)
Interaction partners:
- PCI domain-containing protein 2
Sequence:
MAANVGDQRSTDWSSQYSMVAGAGRENGMETPMHENPEWEKARQALASISKSGAAGGSAKSSSNGPVASAQYVSQAEASALQQQQYYQWYQQYNYAYPYSYYYPMSMYQSYGSPSQYGMAGSYGSATPQQPSAPQHQGTLNQPPVPGMDESMSYQAPPQQLPSAQPPQPSNPPHGAHTLNSGPQPGTAPATQHSQAGPATGQAYGPHTYTEPAKPKKGQQLWNRMKPAPGTGGLKFNIQKRPFAVTTQSFGSNAEGQHSGFGPQPNPEKVQNHSGSSARGNLSGKPDDWPQDMKEYVERCFTACESEEDKDRTEKLLKEVLQARLQDGSAYTIDWSREPLPGLTREPVAESPKKKRWEAASSLHPPRGAGSATRGGGAPSQRGTPGAGGAGRARGNSFTKFGNRNVFMKDNSSSSSTDSRSRSSSRSPTRHFRRSDSHSDSDSSYSGNECHPVGRRNPPPKGRGGRGAHMDRGRGRAQRGKRHDLAPTKRSRKKMAALECEDPERELKKQKRAARFQHGHSRRLRLEPLVLQMSSLESSGADPDWQELQIVGTCPDITKHYLRLTCAPDPSTVRPVAVLKKSLCMVKCHWKEKQDYAFACEQMKSIRQDLTVQGIRTEFTVEVYETHARIALEKGDHEEFNQCQTQLKSLYAENLPGNVGEFTAYRILYYIFTKNSGDITTELAYLTRELKADPCVAHALALRTAWALGNYHRFFRLYCHAPCMSGYLVDKFADRERKVALKAMIKTFRPALPVSYLQAELAFEGEAACRAFLEPLGLAYTGPDNSSIDCRLSLAQLSAF
Protein: AT31531p (Liprin-beta, isoform A) (Liprin-beta, isoform B) (Liprin-beta, isoform C) (Q9VU88)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Liprin-alpha, isoform E
- Liprin-gamma, isoform C
- GH01369p
Sequence:
MATVAEGSKMLEAALQQMDGLISSTATQAGSVSISGAGSSLTLSERNLISATNVLSTAKTLALALQQVGLAAPAPDPVTAAIISDWLETHIPRQDSDERMRRLQRDKEGLALQYQMLAERVSEQADKIIELEGLITEKSQQLCTKEEQLQRQMISSSALETQKLELMSALSELKLHRTALEQANDGGSAISANIPYGSLSNINQKAFMGSPKTPPSALRHQIKPQFHSLPRSHGKFVNNNNNRALDVNANSSGKQRNVAFASNEHILIDDNHHQAEDAMTSSFMSQFTPSPKLRERSARGLRNILGKLRRSNSSNCELTALEQAEPEFRRGGARATAGGRIEWSAQTPLFGENEKHWTTWGAQEVCNWLAYMGLGCYEDNCRKWLNANPSVSFFTASPVDIERELNLKMPLHRKKILLAIDDLTGKEFDDLTLKASSLDVTWVLRWLDDIGLPQYKDYFMQAKIDGRMLHRLTLEDLSQLHVSSCLHIASLRAGILCMRRLSWNAEGLIRRSIKVVSEDEAAATPDRDNVELWTAHRIMGWLQTIDLSEYTPNLRGAGVHGALMLYEPRFNADLLADLLSIPPSKSLLRRHLAMHFKELVGRPVILSKRDAESAPGYQPLSITAKLKPVKRTQFSLKRRKSSKSQSDVDWTEYVCPMNASVPETYLADTAKEHESSMSSN
Protein: Seizure 6-like protein 2 (Brain-specific receptor-like protein A) (BSRP-A) (Q4V9Z5)
Organism: Mus musculus (Mouse)
Function: May contribute to specialized endoplasmic reticulum functions in neurons.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000269|PubMed:16814779}. Note=In cerebellar predominantly localized to the endoplasmic reticulum.
Interaction partners:
- Aspartate beta-hydroxylase domain-containing protein 1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
Sequence:
MGTPKAQHPPPSQLLLLILLSCAWIEGLPLKEDEMMPEPGSETPTVASEDLAELLHGALLRKGPEIGFLPGSDPDPTLATPPAGQTLAAPSLPRATEPGTGPLTTAVTPKGVRGAGPTAPELLTPPPGTTAPPPPGPASPVPPLRPEGGEEETTTTIITTTTVTTTVTSPVLCNNNISEGEGFVESPDLGSTASRSVELLDCTYSIHVYPGYGIEIQVQTLNLSQEEELLVLAGGGSPGLAPRLLANSSMLGEGQVLRSPTNRLLLHFQSPRVPRGNGFRIHYQAYLLSCGFPPRPAHGDVSVTDLHPGGTATFHCDSGYQLQGEETLICLNGTRPAWTGEPPSCTASCGGTIHNATLGRIVSPEPGGAAGPNLTCRWVIEAAEGRRLHLHFERVSLDEDNDRLMVRSGGSPLSPVIYDSDMDDVPERGLISDAQSLYVELLSETPANPLLLSLRFEAFEEDRCFPPFLAHGNVTTTDPEFHPGALATFSCLPGYALEPPGPPNAIECVDPTEPHWNDTEPACKAMCGGELSEPAGVVLSPDWPQSYSPGQDCVWGLHVQEEKRILLQVEILNVREGDMLTLFDGDGPSARVLAQLRGPQPRRRLLSSGPDLTLQFQAPPGPPNPGLGQGFVLHFKEVPRNDTCPELPPPEWGWRTASHGDLIRGTVLTYQCEPGYELLGSDILTCQWDLSWSAAPPACQKIMTCADPGEITNGHRTASDAGFPVGSHVQYRCLPGYSLEGAAVLTCYSRDTGTPKWSDRVPKCALKYEPCLNPGVPENGYQTLYKHHYQAGESLRFFCYEGFELIGEVTITCVPGHPSQWTSQPPLCKVTQTTDPSRQLEGGNLALAILLPLGLVIVLGIGVYIYYTKLQGKSLFGFSGSHSYSPITVESDFSNPLYEAGDTREYEVSI
Protein: Meiotic recombination protein W68 (EC 5.6.2.2) (SPO11 protein homolog) (Q7KPA5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for meiotic recombination. Together with mei-P22, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein
- DNA repair protein Rad51 homolog
- FI03211p
- Meiotic recombination protein P22
- DNA repair protein RAD51 homolog 3
- Crossover suppressor on 3 of Gowen
- DNA repair and recombination protein RAD54-like
- Serine/threonine-protein kinase ATR
- DNA repair endonuclease XPF
- Trade embargo
Sequence:
MDEFSENIERIALELLSNLVHGNATLSVPRNSSGNVISEYRRVSYNNRGSRHSFCVLIYMLSRVHRLQVRGGSFTVRGLYYDNPLLVRSQSRIAEARLDVCRMLRTSPLSLGILAASKGLVAGDLRLLMTNGDVLDSSLYGGPLTLPTDPEKIDRIETLAEFVLIVEKESVFESLLSRNVFGTFERRFILITGKGYPDCCTRRIVHRLTEENQLAAYILVDADPFGVEIMLVYRHGSKSMSFSSQGLTTPALRWIGLHPSEIPALGTGAVALVAGDNKKINDLLARHDLEPGVRQELRMLQDVQLKAEIESVIDFLTDDYIPNKINRNLFL
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IIZ4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGSQTSKFSKTVVGNETHNSARNVLEGFAKDIKRDVSNNAKRHGKVLKGNLRDAKFYHDYSKLRDIPRSPCDLDFWFHTNVWRDKAYERDPCYGRQAKNNYNLEGAVCTNSKIKGNENKINDIGACAPYRRRNICDYNLEHLNERNVLNTHDLLGNVLVMAKREGESIVEKHPNRGSSEVCIALARSFADIGDILRGKDMYVGYDEKEKNRRKQLENKLKDIFDNIYKDLTKKKGRNGKKSALQERYNDPKGDFFQLREDWWALNREDVWKALTCSADDSEDYFIQSEGVTKSFTNPKCGHGDNEVLTNLDYVPQFLRWFTEWAEEFCRIRKIKLGKVKNECRGETSGKRYCSGDGYDCTKTDISRNIFYMDLDCPRCEEECRKYDEWIENKENELDKQKNKYTKEIEKLKDNSKSNYDKNFYLTLTKKYGSINLFLDTLKEGSHCSYNTIEDKIDFNKANQTFTSSKFCGACPFYGVKCNWKTCTEVKENEYKKKNKVDSTHTTEQPTAIDVLVTHIRGTNIPEDLKDCKKYGLFKGMRKQAWKCQYINPYDECKLSPFVKDIDVDDRILFKVLFERWLKYFIQDFNNVKDKINRCTKFEKGKDNTCIKGCKHKCECVEKWIKIKEAEWKKINQHYNQQKKHYTYSVPRWVNSYLTHQHFSSDFINALEAFKNIRGLENLKECSSDTCKIEKIRTIDDDLIKELISKLKDKCAMCKNQHKATKGKECCGKLPKTLNDQDDEEDEEYEAPPPPTPPRTQKNPCVNGQNQKVRKIRSVRRVPKRMQKQASVRVPRARQGGEREQVVKNGRQDHHLQRVLLVGEAEAEEPETAEEKKEEEKEEDTDGKVQPPPAATTPGVKPPCDIVEKHFKDKHDNTGAIDHCNPKKDYPPWKNDKSLVDEDGVYMPPRRQKLCVINLEHFKENTSDDLREAFIKCAAAETYLLWQKYKEDNNGGEDLQNQLKSGKIPEDFKRQMFYTFGDYRDFLFGTDISKLNKHTEAVKTNIDRIFPPTERTNDTIRKEFWEKNAESIWQGMLCALSYNSNDKKMDPDVQKELNSTYNYDTIKNNLEDFANRPQFLRWFIEWSDEFCRERKKKEEKVGSACKNDYEGCANTKDNGNGNCVNACNAYKKYITDKKEQYEKQAKKFDIDKSQNKPGYEDYSGKKASEYLKEKCINSSCDYMLKLKDNSNYWEKPHTTYDDNSLQNKCSCPLSPCEIVDKTLGDKTSKSYAEGCKWKYGKMPLGLGWLCNDKEGEKGKEDGLCIPPRRKRLYVKDLETFSDHTTVGLREAFIKCAAVETFFAWHEFTKEKEREYKEEKQRNGELGFIDENDQIPKDPDNPQNKIRKNGEIHEEFKSQMFYTLADYRDILFGNNIGIGNDMGKVKSNIDKVFANSSGKTPTAKKTTPKEWWEKNAKDIWEGMLCALSYDTKTKIKNEELRKKLIDPKNSNYMYEKVTFSSDNNTNLSKFTERPPFFRWFQEWGEEFCRKKKIKIDKIEKECRGPYGRNHCDGDGFDCSEIGPNENGSFAIFKCPSCAISCRSYKTWINTKKDEFKKQEKLYNKEIKDNKSNYDNIYDKEFVKNLCTDYKSVDSFLKKLKEGPCCNKNTKDSKIDFKDTEETFRNAEYCDPCPVFGVICNNGDCSNSTEKKCDAQEFKVTYDVKNKENPNKEVNMLVSDKTAKKYPGDLNGVCENSSIFEGIREDKWSCGYFCGLDICTPNKTTGDIHDKQNAPIRVLFKRWIENFLKDHNKIKDKISLCINNENRNICTDVCRKNCECIDKWIEMKMKEWKIVRDRYVKQYNVADSVVYEVRRFLEGLQPQNDLEKVKGDVNDLRDLEELSECTNTVSTENRKCRKKDVVESLLNKLKNEIRHCKNERDDSMGKESCKTLPEPTDDPQTDSDTHDTPDIPPGDVAPTFCNVPANPCGDKSATNVVNVTEVAKEMHEEAHKDMLERSVKKVESKVKDSTVESVLRADASKGEYKHEGNPDDLKHNMCNITKEHTNYQKRGGYNYRGPCTGKGNGKDTRFVIGTIWKDEDEKDETIKVLLPPRRRHMCTSNLEYLLHVNKGPLLKVEPDKINHSFLGDVLLAAKYEAEFIKTNYTRLNGQNDNGAKCRAMKYSFADIGDIIRGKDLWGIQDFKDLQTKLVTIFGKIKEEIPDIKKKYSSENPPYTTLREHWWEANRAKVWEAMQCPTIPPVTTSCDTTTVTPLVDYIPQRLRWMTEWAEWFCKMQSQEYEVLVKQCRNCRSGICENGKDDCVKCTQACNTYKQKIKKWEDQWKEISKKYKTLYQQAKGSVNGATTSSTTDEKDKDVVDFLKMLHQKNTDNTIYTTAAGFIHQEAHMTDCQKQTIFCKNTSYNDKKKYAFRHPPHDHDDACACRPPSTPVDVSRKLDTQRDPKKEESEPESEEEEDDAEEEEEPAKETATTETTQPAAPAGPPVTPVPELPGPPAPAGPAADGPIEDDEDAENEDDDDVGSATGTEDDDDDEDDDDEDEEDSADEGEGEGDGGDVGEEEDEDHGGQEAEGVVPQPAAPQPPTPQLLDDPLLKTALMSSTILWMVGIGFAALTYFLLKKKSKSSVDLLRVLNIPKGDYEMPTLKSKNRYIPYRSGSYKGKTYIYMEGDSDSGHYYEDTTDITSSESEYEELDINEIYPYQSPKYKTLIEVVLEPSKSNGNTPSKGDGNTLGDDMVPTTNTFTDEEWSELKHDFISQYIQSEPLDVPKVGVSKELPMNIGGNVLDDGINEKPFITSIHDRDLYTGEEIKYNINMGTNSMDDPTYVSNNVYSGIDLINDTLSGNQHIDIYDEVLKRKENELFGTNYKKNTSNNNVAKLTNSDPIMNQLDLLHTWLDRHRDMCEKWNKKEELLDKLNEQWNKDNDGGDIPNDNKKLNTDVSIQIDIDENKGKKEFSNMDTNVDTPTMDSILDDLETYNEPFYDIFEDDVYYDVYDENPFVDDIPMDHNKVDVPKKVHIEMKILNNTSNGSLEQQFPISDVWNI
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (Complex I-18 kDa) (CI-18 kDa) (Complex I-AQDQ) (CI-AQDQ) (NADH-ubiquinone oxidoreductase 18 kDa subunit) (Q02375)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}; Peripheral membrane protein {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}; Matrix side {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}. Note=The interaction with BCAP31 mediates mitochondria localization. {ECO:0000250|UniProtKB:O43181}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 subunit C2
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH-ubiquinone oxidoreductase chain 2
Sequence:
MAAVSMSVALRQALWGRRVATVAAVSVSKVSTRSLSTSTWRLAQDQTRDTQLITVDEKLDITTITGVPEEHIKTRKARIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNLVLTFSTKEDAVAFAEKNGWSYDVEERKVPKPKSKSYGANFSWNKRTRVSTK
Protein: DnaJ homolog subfamily B member 9 (Endoplasmic reticulum DNA J domain-containing protein 4) (ER-resident protein ERdj4) (ERdj4) (Microvascular endothelial differentiation gene 1 protein) (Mdg-1) (Q9UBS3)
Organism: Homo sapiens (Human)
Function: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9QYI6}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- X-box-binding protein 1
- Nucleotide exchange factor SIL1
- Hypoxia up-regulated protein 1
- Endoplasmin
- Heat shock 70 kDa protein 13
- Heat shock 70 kDa protein 6
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
Sequence:
MATPQSIFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTSGKGQRGSGSSFEQSFNFNFDDLFKDFGFFGQNQNTGSKKRFENHFQTRQDGGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNQHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ
Protein: carboxylesterase (EC 3.1.1.1) (Q9W243)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLRVSFSDKLKLGAKIIGHKVVQYKLGTGQTKELATKYGQLKGQQRRTLYDGEPYYSFEGIPFAQPPVGELRFRAPQPPSSWQGVRDCTYAREKPMQRNSITNAAEGSEDCLYLNVYAKRLESPKPLPVMVWIFGGGFQVGGASRELYGPDYFMKHDILLVTINYRVGVLGFLSLKDKELKIPGNAGLKDQIQALRWVKENIASFNGDPESITVFGESAGGASTHILMQTEQARGLFHRAIVQSGSALCAWATQPDRKWPQRLGKELGYAGNLESEKELLEFFQQIPASKLAQYCNSIVTQEEQRDYEILAFAPVIEPYVGDDCVIPKSQQEQLSSAWGNSIPMIIGGTSFEGLFSYRTTLDDPLYMLSAFEAIIPKQVRDAIDKEELAEMVRRLKKSYFDDPDRASMELYECLHILSIKNFWHDIHRTLLARLAYATNLPTYLYRFDMDSPHFNHYRILKCGKKVRGVCHADDISYMFYGILSSKLDKNSPEYRTIERLVGMWTSFATTGDPNCEIIAPVKWDPLRPGGVENCLNIADGLEFIPLPESKQFVVWDSFYTRESLY
Protein: Transcriptional corepressor SEUSS (AtSEU) (Q8W234)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-binding adapter subunit of the SEU-LUG transcriptional corepressor of the C class floral homeotic gene AGAMOUS during the early stages of floral meristem development. Is part of the A class cadastral complex that define the boundaries between the A and C class homeotic genes expression and function. Interacts together with APETALA2 and LEUNIG to repress AGAMOUS expression. In association with LUG, regulates petal shape through AGAMOUS-independent mechanisms. Controls cell division during petal development and enable the proper patterning of petal blade vasculature. Required for the proper elaboration of petal polarity along the adaxial/abaxial axis. May act through direct or indirect regulation of PHABULOSA and YAB1 and thus regulate cellular proliferation within the developing petal blade. In association with AINTEGUMENTA (ANT), coordinates patterning cues and cellular proliferation along the three positional axes of the developing gynoecium. Required for the development of the medial ridge and subsequent ovule initiation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:18184731}. Note=Does not localize in the nucleolus.
Interaction partners:
- Transcriptional corepressor LEUNIG
- Transcriptional corepressor LEUNIG_HOMOLOG
- Developmental protein SEPALLATA 3
- Corepressor
- Floral homeotic protein APETALA 3
- MADS-box protein AGL24
- Floral homeotic protein APETALA 1
- Transcription factor PERIANTHIA
- Axial regulator YABBY 4
- At1g68780
Sequence:
MVPSEPPNPVGGGENVPPSILGGQGGAPLPSQPAFPSLVSPRTQFGNNMSMSMLGNAPNISSLLNNQSFVNGIPGSMISMDTSGAESDPMSNVGFSGLSSFNASSMVSPRSSGQVQGQQFSNVSANQLLAEQQRNKKMETQSFQHGQQQSMQQQFSTVRGGGLAGVGPVKMEPGQVSNDQQHGQVQQQQQKMLRNLGSVKLEPQQIQAMRNLAQVKMEPQHSEQSLFLQQQQRQQQQQQQQQFLQMPGQSPQAQMNIFQQQRLMQLQQQQLLKSMPQQRPQLPQQFQQQNLPLRPPLKPVYEPGMGAQRLTQYMYRQQHRPEDNNIEFWRKFVAEYFAPNAKKRWCVSMYGSGRQTTGVFPQDVWHCEICNRKPGRGFEATAEVLPRLFKIKYESGTLEELLYVDMPRESQNSSGQIVLEYAKATQESVFEHLRVVRDGQLRIVFSPDLKIFSWEFCARRHEELIPRRLLIPQVSQLGSAAQKYQQAAQNATTDSALPELQNNCNMFVASARQLAKALEVPLVNDLGYTKRYVRCLQISEVVNSMKDLIDYSRETRTGPIESLAKFPRRTGPSSALPGPSPQQASDQLRQQQQQQQQQQQQQQQQQQQQQQQQTVSQNTNSDQSSRQVALMQGNPSNGVNYAFNAASASTSTSSIAGLIHQNSMKGRHQNAAYNPPNSPYGGNSVQMQSPSSSGTMVPSSSQQQHNLPTFQSPTSSSNNNNPSQNGIPSVNHMGSTNSPAMQQAGEVDGNESSSVQKILNEILMNNQAHNNSSGGSMVGHGSFGNDGKGQANVNSSGVLLMNGQVNNNNNTNIGGAGGFGGGIGQSMAANGINNINGNNSLMNGRVGMMVRDPNGQQDLGNQLLGAVNGFNNFDWNA
Protein: Transcription factor A, mitochondrial (mtTFA) (Mitochondrial transcription factor 1) (MtTF1) (Transcription factor 6) (TCF-6) (Transcription factor 6-like 2) (Q00059)
Organism: Homo sapiens (Human)
Function: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:1737790, ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:29445193}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18063578}.
Interaction partners:
- DNA-directed RNA polymerase, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial
- Dimethyladenosine transferase 1, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear respiratory factor 1
- GA-binding protein subunit beta-1
- Cellular tumor antigen p53
- Single-stranded DNA-binding protein, mitochondrial
- DNA polymerase subunit gamma-1
- Endoplasmic reticulum chaperone BiP
Sequence:
MAFLRSMWGVLSALGRSGAELCTGCGSRLRSPFSFVYLPRWFSSVLASCPKKPVSSYLRFSKEQLPIFKAQNPDAKTTELIRRIAQRWRELPDSKKKIYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKKELTLLGKPKRPRSAYNVYVAERFQEAKGDSPQEKLKTVKENWKNLSDSEKELYIQHAKEDETRYHNEMKSWEEQMIEVGRKDLLRRTIKKQRKYGAEEC
Protein: Protein kintoun (Dynein assembly factor 2, axonemal) (B6F1W5)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}. Dynein axonemal particle {ECO:0000250|UniProtKB:B1H1W9}. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia. {ECO:0000255|HAMAP-Rule:MF_03069}.
Interaction partners:
Sequence:
MEVGKKLELSITADEVEVLSKAIKNEKFQEMLSNYFQEISSPENVKTYQEEVTLLEQKRGNSIEFIHPSPFRALETSVDGKQRCFINICACDKVGKPESKTVRTVQRFGEKWSLPHLLQPGRQNCERKGNISTIYDVCFHPETLHLADKSEKFMDMVKEVAIQGIQKAFKVLLDKSNLKEMDIKYKGVPQSCVIRKPIPGYEAKEPPEERDLSPSTSHLPENSIDVPSKLLQKQPEEPIKPIYAIKYRSVIDLQDFRVSRESARSLRPKEIVITIDLPLLPTVHGMVLEVEEKRLLLESENPSYRLELHLSYPVDENNGKAKFNKHQRQLTVTLPVQPPLEAPQLPGGSPNPTSDPQNENQTRVEERVEEMAEKGGEQHQRGNDNGAAQGRRQVLEDQNGEKEGKKIQKRNERPEHEVKNETLRKKHDEKFELQDVQQENKGNCSNTKEVKCCRRTKDSLDSLIPTTAASPDGQKKHILTQETEKPKGSVEIPTSSQEYLKVPVTSAATAANVNASDETSKRKPTEEQLEDADEDVLPAEQRFQEPEEINVPAAGTLRQNNAAGNEKINDPHTSAGFVLQNKLMYELD