wanglab/gogpt-training-data huggingface dataset:
Protein: K+/Cl-Cotransporter (H2KZC2)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTLTSTSMLRSTSIPVTNKAHDFEPEPTSSTSTNTVTSRRSSGGSGSGLGPASKKPPNMHINIPTDEGAERIPLCEQHSPLALYEQDYDTQGQKIGTMLRKLSVYNATEATSVEADEKPKAAAAKMGTIMGVFLPCLQNIFGVLFFIRLAWIIGTAGVFQAFFVVLTCVSVTFLTSISLSAIATNGVVPSGGPYYMISRNLGPELGGAVGILFYLGTTIAASMYITGAIEILLLYIYPQAKLFDDIYHNFRVLGTVLLLILGLIVMAGVKFVNRCALPLVIVVILCILSAILGVFVRYDGSDSLKFCMVGDRPVDLSTYFEKTQVQPNCTADGLQDLFCSTNGTCDHYYDRMKNIKVWKSSGMPAIREERAIKGIASGVFFDNLWPKYLRAGEVLSKDRKDKGDLNRGGHPSYIYAESVTNFMILVGVFFPSATGIMAGSNRSGNLRDAAKSIPLGTLAAQNFSSFIYLLGVVLFGASVSEMFIRDKYGRSAMGKLIISEISWPFPQVILFGCFMSTAGAGMQSLTGAPRLLQAIAADDVLPFLKPFRKMDSRGEPIRAILLTLAICECGILIAVIENITALITQFFLMCYLGVNAACALQSLLKSPGWRPGFRYFHWSLSMIGAILCVAVMFISAWHFALFAIIIGAGVYKYIEYAGAEKEWGDGLRGLGLSAARFALLNLDDKPQHSRNWRPQLLVLAPDVESANTNGILSFVSQLKAGKGLTLVAHCMEGEYADNYLKAQAVQEKLKAVVKKNKIKGFCDVLVTSNVIEGISCLVQTSGLGGMRHNTVVLSWPNDWKAEQEWVVANKFVSAIRAISAAKCAIMVPKYAEKFPANGTKVSGFIDVWWVVHDGGLLMLLPFLLRQHKTWKNTTVRLFAIAQMEDNNVQMKTDLEKFLYHLRIDAAVNVIEMTDSDISDYTYERTMKMEERNQYLKNLNKSDRDKDIQNHLEIVTRERKLSRINEEAPAVVPEQRNLEVVDEEQEDGKSENGSAKIEHKGVRFSDDEDSKEVKVGNGTLERDREERQRKRRYNVHKMHTAVKLNELMRQKSSDAQLVFVNLPGPPDADSDSYYMDFIEALTEGLDRVLLVRGTGAEVVTIYS
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 (A0A2R8YES3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQPDPVLQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSIVPEEEQAANKGEEKKDDENIPMETEETHLEETTESQQNGEEGTSTPEDKESGQEGVDSMAEEGTSDSNTGSESNSATVEEPPTDPIPEDEKKE
Protein: Arylsulfate sulfotransferase AssT (EC 2.8.2.22) (Aryl sulfotransferase AssT) (Q8FDI4)
Organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Function: Catalyzes the transfer of sulfuryl groups between phenolic compounds.
Subcellular location: Periplasm {ECO:0000305|PubMed:18565543}.
Interaction partners:
- Thiol:disulfide interchange protein DsbL
- Protein-disulfide oxidoreductase DsbI
- Putative tail component of prophage
- Putative tail component of prophage
Sequence:
MFDKYRKTLVAGTVAITLGLSASGVMAAGFKPAPPAGQLGAVIVDPYGNAPLTALVDLDSHVISDVKVTVHGKGEKGVEISYPVGQESLKTYDGVPIFGLYQKFANKVTVEWKENGKVMKDDYVVHTSAIVNNYMDNRSISDLQQTKVIKVAPGFEDRLYLVNTHTFTAQGXDLHWHGEKDKNAGILDAGPATGALPFDIAPFTFIVDTEGEYRWWLDQDTFYDGRDRDINKRGYLMGIRETPRGTFTAVQGQHWYEFDMMGQVLEDHKLPRGFADATHESIETPNGTVLLRVGKSNYRRDDGVHVTTIRDHILEVDKSGRVVDVWDLTKILDPKRDALLGALDAGAVCVNVDLAHAGQQAKLEPDTPFGDALGVGPGRNWAHVNSIAYDAKDDSIILSSRHQGVVKIGRDKQVKWILAPSKGWEKPLASKLLKPVDANGKPITCNENGLCENSDFDFTYTQHTAWISSKGTLTIFDNGDGRHLEQPALPTMKYSRFVEYKIDEKKGTVQQVWEYGKERGYDFYSPITSIIEYQADRNTMFGFGGSIHLFDVGQPTVGKLNEIDYKTKEVKVEIDVLSDKPNQTHYRALLVRPQQMFK
Protein: NS5 protein (Q8B489)
Organism: dengue virus type 2
Interaction partners:
Sequence:
SGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRHKKATYEQDVDLGSGTRTVWRKGEKPNLYTLEKNTEKRLQEHEPHLRDDQNHPYKTWAYHGSYEIEQAGSASSLVEWSSSAADKTLGRLSTGDKYVKTRYDSFWPTTCCKRKGGYYSPHTDGRRTATRENRSRVALGLPRREKKTSTVHQRKSHKEDEKQSSSGSHMGQWYEVSVGMWNQRRKKAVEDLWQLENFECWRKVWNMCILRSVKIREWTSSSWWIRRQQRQMAHVARSTLRSVQSVRMVEWRPYGLQRGLLESTWQEKRGINWVWCQERWLSWKDEHYKSMMPHTGIHVSPYRMIKIKRWWRSTWQENWRIMLSASDSWRGESRSSEYDTWYCDRLYWASYHGETRGAVDKVGRMRPAISAWWVHTKLGQCHANDAWDASVTWQPQRRSQSNIGWRAVGRGRLQLIAIRGDDSVARPVCDRFARGLAAQKVMVKLTKDRRQPEPSRGWNDWTQVLLRLDDHHELLMRDDTSCVKSWTIDVELLERSEMSAVRIATSICDVLSESSYSVDEWHSMLMLSWLRSIGRWCTRCWSVTLVHIVASDGVHRGTAWMGDDVDMLQSEWVWSKKTRDEDKLHGSWKKSHTWEKRRPMCGSLVGKQAGYLGKEHPNSNKSSQIPYRQWGYTQLHAIHEEIQKGRGRGRCPVVEGKTNMKQGWKSGRIKPWYGKNYATCEPLQGRKKKSGHYKCHSLSKLCSLWLHLRRCKKSGKPQAMEACYMAVSGLAVRG
Protein: Acidic leucine-rich nuclear phosphoprotein 32 family member B (Acidic protein rich in leucines) (Putative HLA-DR-associated protein I-2) (PHAPI2) (Silver-stainable protein SSP29) (Q92688)
Organism: Homo sapiens (Human)
Function: Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription. Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis. Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes. Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1. Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity).
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:17178712, ECO:0000269|PubMed:24823948, ECO:0000269|PubMed:31217244}. Cytoplasm {ECO:0000269|PubMed:17178712}. Note=Accumulates in the nuclei at the S phase. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Lacks a nuclear localization signal.
Interaction partners:
- Exportin-1
- Acidic leucine-rich nuclear phosphoprotein 32 family member A
- Importin subunit alpha-6
- ELAV-like protein 1
Sequence:
MDMKRRIHLELRNRTPAAVRELVLDNCKSNDGKIEGLTAEFVNLEFLSLINVGLISVSNLPKLPKLKKLELSENRIFGGLDMLAEKLPNLTHLNLSGNKLKDISTLEPLKKLECLKSLDLFNCEVTNLNDYRESVFKLLPQLTYLDGYDREDQEAPDSDAEVDGVDEEEEDEEGEDEEDEDDEDGEEEEFDEEDDEDEDVEGDEDDDEVSEEEEEFGLDEEDEDEDEDEEEEEGGKGEKRKRETDDEGEDD
Protein: Photosystem I reaction center subunit IX (PSI-J) (P12192)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May help in the organization of the PsaE and PsaF subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00522}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00522}.
Interaction partners:
- Photosystem I reaction center subunit VIII
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit V, chloroplastic
- Chlorophyll a-b binding protein
- Chlorophyll a-b binding protein
- Chlorophyll a-b binding protein
- Photosystem I reaction center subunit III
Sequence:
MRDIKTYLSVAPVLSTLWFGALAGLLIEINRLFPDALSFPFFSF
Protein: C2H2-type domain-containing protein (Q582R4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQHTLSECEPQRRGVNELALKTHSSSVSSKQSYGVSSSRSVQLSASQLTTVCVRQAMVNQAQGLLTDNSNEVTTLSNGAIGYQNQRPSYATKEGCAAPSLSVAELSAVATNGSTVCKRLIVKDTPKEHCAAQPLLIENDNAQKTNDWNTSVAMTGCLEVESTPAPSSGPRQCSLCRRYLTDPDDPVQHKRMCQEKKLFCPLLCGKLLRRGDITRHVRETALEHNPLPLPSGPDYPEEHPAHVLAVVMNMFLEKNSGDKRADEQFSLDLPPRRIRLSETSSSSVAASRRLSLNSTLCEKKPESDAVTPPKIQTSADVPLTQSSTGLPEPQARSPPTISQERDITYTIESELTSGNDNSVVATDANDNNTSTFGKASAAVSAEEPDAARTTSELYNSRVPRKRSHSSNVESGCTSRSGGFGMANCKGFRPEAPVSKGSSENGQALKELLIRINLQHEEVEKLREQRGAYDLSNVEDVKQRDEIMDAVRNVVTAFDGKNRSIHNDCKQLMGKTSLAPDLFLNVLHSWRSLDRHWNEVRVTLCDTARI
Protein: Matrix protein (P08325)
Organism: Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan) (VSNJV)
Function: Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibits interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity).
Subcellular location: Virion {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus {ECO:0000250|UniProtKB:P03519}. Host cytoplasm {ECO:0000250|UniProtKB:P03519}. Note=In the virion, forms a double layer around the helical nucleocapsid, the inner matrix layer binding to the N helix and the outer matrix layer binding to the envelope glycoprotein. About 2480 copies of M are present in the virion. {ECO:0000250|UniProtKB:P03519}.
Interaction partners:
Sequence:
MSSFKKILGLSSKSHKKSKKMGLPPPYDESCPMETQPSAPLSNDFFGMEDMDLYDKDSLRYEKFRFMLKMTVRSNKPFRSYDDVTAAVSQWDNSYIGMVGKRPFYKIIAVIGSSHLQATPAVLADLNQPEYYATLTGRCFLPHRLGLIPPMFNVQETFRKPFNIGLYKGTLDFTFTVSDDESNEKVPHVWDYMNPKYQSQIQQEGLKFGLILSKKATGTWVLDQLSPFK
Protein: Gap1 (A1C3L5)
Organism: Streptococcus parasanguinis
Interaction partners:
Sequence:
MFYFVPSWYNGQRQWYYDTPWWFRVKNRMTFDDSVNQVKMFLQGQEEIGLMILNYQPQLRYFLHKQNIFGIYYWSFFDDIQNITRSYTKIIHLKDLNWPEGCEFLYSPFAVVVRLKGEIFAIVNYAEDGNLHSVSFQKNGKVTKDYIFDDRGFLSSILYYDIDERPLYQDYLNINGVWQVREFLKKENDPTPILMINDFSDQTFSKKYYNGWEELIKERLAIFQNNHVENEDVFVLASDTQHNQLVSSIFKEHRKIYSFFGNRFNLENLGQDRISINDATFLVVDTEKNEELLRKTCENLVFKSIPIVRLSPFDSRLRLGHSQTVKEQIIYFHIDNIELDELYSVIAIILELMTLHLDIELRIVTFRQDFQLDLLKTWIIDFIKTNHFEDLLFKQISEGENEIEDEGEIELSRIAMECFTNENQIIKCLDTARLVIDLGIEPDLYTQIASISAGIPQINRVSSDYVIHQKNGLVISDISKLSSAIEFYFDGLFNWNEALIYAVRKMSDYTSGKILKQWKGMLKKK
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4JDB5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGAASDALTYSLMAQQPPSGPPHAGGQQITPGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: Endonuclease NucS (EC 3.1.-.-) (Nuclease for ssDNA) (Q9V2E8)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. Binds to ssDNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00722}.
Interaction partners:
- Endonuclease V
- Intein/rRNA intron-related DNA endonuclease
- DNA repair and recombination protein RadA
- Endonuclease III lyase)
- Uncharacterized protein
- Flap endonuclease 1
- DNA polymerase sliding clamp
- Crossover junction endodeoxyribonuclease Hjc
Sequence:
MRKVIIKENPSEEEIKELLDLAEKHGGVVTIFARCKVHYEGRAKSELGEGDRIIIIKPDGSFLIHQNKKREPVNWQPPGSKVTFKENSIISIRRRPYERLEVEIIEPYSLVVFLAEDYEELALTGSEAEMANLIFENPRVIEEGFKPIYREKPIRHGIVDVMGVDKDGNIVVLELKRRKADLHAVSQLKRYVDSLKEEYGENVRGILVAPSLTEGAKKLLEKEGLEFRKLEPPKKGNEKRSKQKTLDFFTP
Protein: Protein Aster-C (GRAM domain-containing protein 1C) (Q8IYS0)
Organism: Homo sapiens (Human)
Function: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8CI52}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8CI52}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS). {ECO:0000250|UniProtKB:Q8CI52}.
Interaction partners:
- CD151 antigen
- GRAM domain-containing protein 2B
- Protein Aster-B
Sequence:
MEGAPTVRQVMNEGDSSLATDLQEDVEENPSPTVEENNVVVKKQGPNLHNWSGDWSFWISSSTYKDRNEEYRRQFTHLPDTERLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETTISIALKNITFMTKEKTARLIPNAIQIVTESEKFFFTSFGARDRSYLSIFRLWQNVLLDKSLTRQEFWQLLQQNYGTELGLNAEEMENLSLSIEDVQPRSPGRSSLDDSGERDEKLSKSISFTSESISRVSETESFDGNSSKGGLGKEESQNEKQTKKSLLPTLEKKLTRVPSKSLDLNKNEYLSLDKSSTSDSVDEENVPEKDLHGRLFINRIFHISADRMFELLFTSSRFMQKFASSRNIIDVVSTPWTAELGGDQLRTMTYTIVLNSPLTGKCTAATEKQTLYKESREARFYLVDSEVLTHDVPYHDYFYTVNRYCIIRSSKQKCRLRVSTDLKYRKQPWGLVKSLIEKNSWSSLEDYFKQLESDLLIEESVLNQAIEDPGKLTGLRRRRRTFNRTAETVPKLSSQHSSGDVGLGAKGDITGKKKEMENYNVTLIVVMSIFVLLLVLLNVTLFLKLSKIEHAAQSFYRLRLQEEKSLNLASDMVSRAETIQKNKDQAHRLKGVLRDSIVMLEQLKSSLIMLQKTFDLLNKNKTGMAVES
Protein: Chromosome 19 open reading frame 47 (A0A2R8Y6U9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTDEDLAWDSDNDSSSSVLQYAGVLKKLGRGPAKASPQPALTVKAKATSSATTAAAPTLRRLALSSRSGLERKPESLSKVSIIKRLGAAALVPEAQDSQVTSTKSPTVRCVLPDPPVPPASQRPPRRRWRRAC
Protein: SWIRM domain-containing protein YOR338W (Q99326)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Haze protective factor 1
- Protein EAP1
- Protein NAM8
- Protein SCP160
- ATP-dependent RNA helicase DHH1
- Nuclear fusion protein BIK1
- Uncharacterized globin-like protein YNL234W
- Nuclear segregation protein BFR1
- Uncharacterized protein YGR035C
- Uncharacterized oxidoreductase YNL181W
Sequence:
MLDNMQFHSPAPEHPQLNGGINKIPASHKIGYKLNQQVQRLAVVRNNIEERLNSMESSHGQISDSSVVRAIDASIDDFLIPSPPLSPKLRQCPIISQPQLVNVESDHRELIMLTPVWEAGLNSQKYNHNTRNFLSQYSFFRDMKTTKRIPNKENRKLKVVKSVVNSEALPKRRRYDRKIKRRSRELYEDDGNRSENYDEESAQEVPVRSVTPIRQVKRSLHTISSPLASQGVVNNVPKYIPSMSWEKLPDYSPPLHTLPNSNNKVLKVEWKGSPMDLNHDPLKQRLHPAELVLAQILRLPCDLYLDSKRRFFLEKVHRFKKGLPFRRTDAQKACRIDVNKASRLFAAFEKVGWLQDKHFEKYL
Protein: Probable ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-specific-processing protease 16) (O74442)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable ubiquitin carboxyl-terminal hydrolase 2
- Probable ubiquitin carboxyl-terminal hydrolase 1
- Ubiquitin thioesterase otu2
- Putative ubiquitin thioesterase otu1
- Uncharacterized J domain-containing protein C17A3.05c
- Ubp5-interacting protein ftp105
Sequence:
MSLATLQGQSLDFAVKHSLDDLLKNPVRFRPAVVSSPSVPEGTYTVLNNPKQSTVSRKSFSAPTSPTRNKRSGSSSQEYKKSSGTRGDGANDFVDEDPAFIPPARILFPEEKLSMEWDNIMPNAPGLVNLGNTCFMNSVLQLMTQTPPLVQYLLSGQHSLSCRMNACVLCRMEQHVARAYPNKGTKRASAFKPSGIQSMLKVISSHFRPYRQEDAHEFMRYLVDAWQKSCLQNHKNLDHPSRETSVVHRIFGGYLRQQILCSVCKKPSNTYQALLDLSVDAKGSSLADSLKHFVHAEKLTKQNKYRCENCKQLVDASKQMTIYRAPNILTIHFKRFTFNGFQSSKISKQISYPESFNLGPYMSDPNCSCWYELIGVLVHAGGSTRSGHYYSFCKSSNGVWLKFDDDFVSNSSIDRVLNQQAYILQYKRKSTSSSKHKLNTENTVTKTSNKKRRKISF
Protein: Elongator complex protein 5 (Dermal papilla-derived protein 6 homolog) (Retinoic acid-induced protein 12) (Q99L85)
Organism: Mus musculus (Mouse)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Involved in cell migration.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8TE02}. Cytoplasm {ECO:0000250|UniProtKB:Q8TE02}.
Interaction partners:
- Elongator complex protein 4
- Elongator complex protein 1
- Elongator complex protein 3
- Elongator complex protein 6
- Elongator complex protein 2
- Cytoplasmic tRNA 2-thiolation protein 1
- Protein KTI12 homolog
- Cytosolic iron-sulfur assembly component 2B
- Adenylyltransferase and sulfurtransferase MOCS3
Sequence:
MLDSLLAIGGLVLLRDSVEWEGRSLLKALIKKSALRGEQVHVLGCEVSEEEFREGFDSDVNSRLVYHDLFRDPLNWSKPGEAVPEGPLKALRSMCKRTDHGSVTIALDSLSWLLCHIPCVTLCQALHALSQQNGDPGDNSLVEQVRVLGLLHEELHGPGSMGALNTLAHTEVTLSGKVDQTSASILCRRPQQRATYQTWWFSVLPDFSLTLHEGLPLRSELHPDHHTTQVDPTAHLTFNLHLSKKEREARDSLTLPFQFSSEKQKALLHPVPSRTTGHIFYEPDAFDDVDPEDPDDDLDI
Protein: ATP synthase subunit alpha, chloroplastic (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) (P0C2Z4)
Organism: Oryza sativa (Rice)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
Interaction partners:
Sequence:
MATLRVDEIHKILRERIEQYNRKVGIENIGRVVQVGDGIARIIGLGEIMSGELVEFAEGTRGIALNLESKNVGIVLMGDGLMIQEGSFVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIVASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQDVICVYVAIGQRASSVAQVVTTFHEEGAMEYTIVVAEMADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELQAFAQFASALDKTSQNQLARGRRLRELLKQSQANPLPVEEQIATIYIGTRGYLDSLEIGQVKKFLDELRKHLKDTKPQFQEIISSSKTFTEEAEILLKEAIQEQLERFSLQEQT
Protein: Retinoic acid receptor RXR-alpha-B (Nuclear receptor subfamily 2 group B member 1-B) (Retinoid X receptor alpha-B) (Q90415)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (By similarity). The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (By similarity). The high affinity ligand for rxrs is 9-cis retinoic acid (By similarity). In the absence of ligand, the rar/rxr heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (By similarity). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Nuclear receptor subfamily 1, group H, member 3
- Retinoic acid receptor alpha-A
- Thyroid hormone receptor alpha-A
Sequence:
MPVPEQKQTVQLSSPMNAVSSSEDIKPPLGLNGVMKVPAHRIGTLSLSLTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCMIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRAKERSEAEFGGCANEDMPVEKILEAELAVEPKTETYVEANLSPSANSPNDPVTNICQAADKQLFTLVEWAKRIPHFSDLPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHTAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPSEVEALRERVYASLEAYCKHKYPDQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQIT
Protein: N-acylphosphatidylethanolamine synthase (NAPE synthase) (EC 2.3.1.-) (Lysoglycerophospholipid acyltransferase) (Monolysocardiolipin acyltransferase) (Q9ZV87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyltransferase that catalyzes the N-acylation of phosphatidylethanolamine to form N-acylphosphatidylethanolamine (N-acyl-PE) (e.g. NAPEs containing C16:0, C16:1, C18:0, and C18:1). Mediates also the formation of acylphosphatidylglycerol (acyl-PG) from lysoglycerophospholipid by O-acylation. Uses acyl-CoA as acyl donors. Acylates 1-acyllysophosphatidylethanolamine (1-acyllyso-PE) and 1-acyllysophosphatidylglycerol (1-acyllyso-PG) at the sn-2-position.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19447891}; Single-pass membrane protein {ECO:0000269|PubMed:19447891}.
Interaction partners:
- Cardiolipin synthase
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- Tafazzin family protein
- Lysophospholipid acyltransferase 2
- Lysophospholipid acyltransferase 1
- Probable lysophospholipase BODYGUARD 3
- Phospholipase SGR2
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
Sequence:
MGKIMEWAARSDHLGGIPRNTVIMAVSAFAKAVANLCNKSSVHNADTLMNLVQSRPPGVPLITVSNHMSTLDDPVMWGAFKGLLSLDPELARWVLAAEDICFRNPIFSYIFRTGKCIPITRGGGIYQENMNEALQRLKDGSWLHTFPEGKVFQDDVPIRRLKWGTASLIARSPVTPIVLPIIHRGFEEMMPENYNNGRRPLVPLPNKHLKVVVGEPIEFDVPMMVETAVLDSRHVTPPLQEVKWPVLTSAGQVLDETAQRHLYIALSEKIQSSLETLRLLAKRL