wanglab/gogpt-training-data huggingface dataset:
Protein: Aquaporin-3 (Aquaglyceroporin-3) (Q803U6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}.
Interaction partners:
- Aquaporin
- Aquaporin
- Uncharacterized protein.
- Aqp8a protein
- Aquaporin 1a
- Aquaporin-4
Sequence:
MGWQKSVLDKLAQTFQIRNKLLRQGLAECLGTLILVMFGCGSLAQLKLSEGSHGLFLTANLAFGFGATLGILVCGQVSGGHLNPAVTFALCLLGREKWRKFPVYFLFQTLGSFLGAAIIFAEYHDAIYDYAGESNELLVLGEKETAGIFATYPSKYLTPLNGFFDQVIGTASLIVCILAIVDPYNNPIPQGLEAFTVGFSVLIIGLSMGFNSGYAVNPARDFGPRLFTAMAGWGSEVFTARDYWFLVPIFAPFIGAVIGVIVYQLMVGWHVEGEARDKKAKAREEVMNLNDVASKE
Protein: Platelet glycoprotein IX (GP-IX) (GPIX) (Glycoprotein 9) (CD antigen CD42a) (O88186)
Organism: Mus musculus (Mouse)
Function: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Platelet glycoprotein Ib alpha chain
- Platelet glycoprotein Ib beta chain
- Platelet glycoprotein V
- von Willebrand factor
- Integrin alpha-IIb
- Tyrosine-protein kinase Lyn
- Integrin beta-3
- Trem-like transcript 1 protein
- Platelet glycoprotein VI
- Thrombopoietin receptor
Sequence:
MTTWGLLFLLWPATTDTQACPRPCTCQSLETMGLKVNCEGQGLTALPVIPAHTRQLLLANNSLRSVPPGAFDHLPQLWDLDVTHNPWHCDCSLTYLRLWLEDHMPEALMHVYCASPDLATRRPLGQLTGYELGSCGWKLPPSWAYPGVWWDVSLVAVAVLGLILLAGLLNTFTESRN
Protein: Hybrid signal transduction histidine kinase B (EC 2.7.13.3) (Q54YH4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts in the cytokinin signal transduction pathway that regulates spore germination. Required for the maintenance of spore dormancy. Does not appear to act as a cytokinin receptor. Probably undergoes ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, which is followed by transfer of the phosphoryl group to a conserved aspartate residue in the receiver domain.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Acyl-CoA-binding protein
Sequence:
MEKSEQTNSFESSNNNNNNIDSNINNNLENNNNKNNNNNNNNNNNNNNNNNNIENSIDKNNKEDNSLVGVNSHRKHRTRLKSKKGNKHETKKEIDYKDLLIKLPHNAVSNFNSLENESSDNLTPPPPINSSPLPLPLSLPLPLSLPLPLPLPLPLPLPLPPNKENIEINMEDIIIPENKIKNKNNNNNIDINNNNNNNNEKQTSIIEMEDLDKLKQPKINEGSTGKKGKSHFFSFLQRGDKTNSSILKSSEQPTHKKTKTNINTPPDYPIHYFGHHKRFSSSSDEGSDNSKSQHSSVNTPTLSRHNIDSLPESQQSQKQSQQQSQQPQQQNKTKQIQQTILNNNNDNLNEVTPIKKSSLPTLEVSPIQSNIINNQTTEKHNSGGFTALTSASAMNHQNQRRYREHHQINHQQQQQQHHRHYHHHINSGGSSGSSDKFDYVSATGLSTKNGFNPKSLDVDHFPISDKRNNINIQAPSTPVQSRNYPLFTTQSPKNANSASKSKNKLKNLKRKIASSITGNNPSGISSSAFNHSFSSWNNNNSVYTGGNSGGGSGGGGSGGGGGGGGGGGGIGTPSSFLDDNNNLNNGENFKNSNSYNNNNGSNRSISHDEWLRQFYHKHLERYEKTKAVDYLIIKPWNFISWILRPSRIANYQSKILYRRAYILNFLNLVLFVVYLLSTILSSNEWFIFAPGILLSVIYFFLGKINNKMYLIAFLTISTAVAINITSIIYDLTHTRPTDKLIFSWDLLVMIMVPLLFPSIVYSIVILISVAVTYIGLGIYVQSSHNFYLLDAYDSFGELLRSIIIVFVILMFYTILSSVDLKEIERKESRIQSLFRISNEALVVHKDGLITDANPAFESMFQIKLQDLLYPIQSGIWEFLPALEGMFEPGASKLFDNPDMGVIETTGIDSSGRTFQVEVRTNKATYDGEPVDVISIIDITGRKQLMEADYALRKAEAANEAKVIFLTTVSHELRTPINGVLASADILERTTLDSTQKEFLNCIKLSGNYLLDLINDILDYSKIEAGKMEIIKYDFSILKMLDNSIRIVSKNIYEKGLDLCIFIDPNVPVIVNGDQRRIKQILLNFLSNSIKFTNHGQIIIRVKLESDDSTHSLIKFDVEDSGIGIKTEHLNQLFASFSQIDSGNSRKYQGTGLGLSISKRLCKMMGGDVKVKSEFGVGSTFSFTIPCGIPNTTTRFSLQSLGSAIYMGEDIQGINKPIGKKKYGASGVVGIVIDSNKYTRKSISQYFAILKISCVDFENKKEFENYLSTLATVDQTTNPQVYLVITSIIDINQLTTNGLPRDRIYHWILMESPNEERKLPLEFENRFVKPAQFADIVRCLYKIDSINFFIEQMAGSPYKASKDLQSGGSSNESGDGGRSLSGGGGGVGSNGNGNGGGGLDSNISPSELSSSEHQLISTPLSDVNEFEDINLINQSLSGLGPSAKVLNSTYFNGLSQSSKIYNNNNRNGVGIGNHHHDHYYQHRHHHSLPPEEIDYDESPFLFLNKPIRKVYHSQPSTPVTNGIALMDSSSKSPSIPSSSSASASALSPNSRHSNELGNGKTTQSFVFSPTSRKFSLNDSFNPSISTIVLPQVSYSPSMQGGNFPINMESVYKKIESHNNNFKRSESKPSTPTFLSNQPSPATSNSPQLLQSPTTSTTGSINLSPHRSPNIRLPLEVRSGSLSSLKPLREDEELESISDDHTSHLKGSSHSINQQIPSTIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQKPQQQQQKPTTTTTTTSTQLPQNIEKTTTTTTTSTTKPTATSSSSSSSKTTKTQQQQHHPTTTTTTKSEKIEKTAAATTSEKIEKILLVEDNFVNVKIFSKLLKDSGYIFDVAHNGVEAVECVKKGAYDLILMDCQMPEMDGFEATTAIRELEKSNLIESPPSKKHSHVVIVALTANSGYKDKQKCLSVGMNDFLQKPIKTSDILIQMIKKHLN
Protein: Brother of CDO (Protein BOC) (Q6AZB0)
Organism: Mus musculus (Mouse)
Function: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Sonic hedgehog protein
- Desert hedgehog protein
- Indian hedgehog protein
- Protein patched homolog 1
- Growth arrest-specific protein 1
- Protein patched homolog 2
- Protein smoothened
- Cell adhesion molecule-related/down-regulated by oncogenes
- Cysteine dioxygenase type 1
- Low-density lipoprotein receptor-related protein 2
Sequence:
MTTCRRERPILTLLWILMATAGCLADLNEVPQVTVQPMSTVQKLGGTVILGCVVEPPWMNVTWRFNGKELNGSDDALGVFITRGTLVIAALNNHTVGRYQCVARMPAGAVASVPATVTLANLQDFKLDVQHVIEVDEGNTAVIACHLPESHPKAQVRYSVKQEWLEASRDNYLIMPSGNLQIVNASQEDEGMYKCAAYNPVTQEVKTSGSGDRLRVRRSTAEAARIIYPLEAQTVIVTKGQSLILECVASGIPPPRVTWAKDGSSIAAYNKTRFLLSNLLIDTTSEEDSGTYRCMASNGVGDPGAAVILYNVQVFEPPEVTVELSQLVIPWGQSAKLTCEVRGNPPPSVLWLRNAVPLTSSQRLRLSRRALRVVSVGPEDEGVYQCMAENAVGSAHAVVQLRTARPDTTLRPGRDTKPIAATPPMPPSRPSRPDQMLREQPGLVKPPTSSVQPTSLKCPGEEQVAPAEAPIILSSPRTSKTDSYELVWRPRHEGSSRTPILYYVVKHRKVTNSSDDWTISGIPANQHRLTLTRLDPGSLYEVEMAAYNCAGEGQTAMVTFRTGRRPKPEIVASKEQQIQRDDPGASLQSSSQPDHGRLSPPEAPDRPTISTASETSVYVTWIPRGNGGFPIQSFRVEYKKLKKVGDWILATSAIPPSRLSVEITGLEKGISYKFRVRALNMLGESEPSAPSRPYVVSGYSGRVYERPVAGPYITFTDAVNETTIMLKWMYIPASNNNTPIHGFYIYYRPTDSDNDSDYKKDMVEGDRYWHSISHLQPETSYDIKMQCFNEGGESEFSNVMICETKARKFSGQPGRPPPLTLAPPQPPPLETMERPVGTGAMVARASDLPYLIVGVVLGSIVLIIVTFIPFCLWRAWSKQKHTTDLGFPRSALLSSSCQYTMVPLEGLPGHQANGQPYLGGVSGRACVSRVHGSRGCPAATVGCPGRKPQQHCPGELAQQREDTNSQLRQPIVSNGYDLQNQQVARGPQCASGVGAFLYTLPDDSTHQLLQPQDCCHLQKQPVTTCQTAVRRTSESPGLESSWDPPYHSGPRCCLGLVPVEEVDSSDSCQVGGGDWSSQHPSGTYTGQERGMRFSPSPSVHVSFETPPPTI
Protein: Phenoloxidase subunit 1 (EC 1.14.18.1) (PO 1) (Tyrosinase 1) (Q27451)
Organism: Bombyx mori (Silk moth)
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MSDAKNNLLLFFDRPSEPCFMQKGEENAVFEIPDNYYPEKYQRVSNAIGNRFGSDAGRMIPIRNIALPNLDLPMELPYNEQFSLFVPKHRKLAGRLIDIFMGMRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAESFPDKFMDPKVFRQAREVSSVVPSGARMPIVIPSNYTASDTEPEQRVAYFREDIGINLHHWHWHLVYPFDAADRAIVNKDRRGELFYYMHQQIIARYNVERMCNNLSRVRRYNNFRAAIEEGYFPKLDSTVASRAWPPRFAGTTIRDLDRPVDQIRSDVSELETWRDRFLQAIENMSVMLPNGRQLPLDEETGIDVLGNLMESSIISRNRPYYGDLHNMGHVFISYSHDPDHRHLEQFGVMGDSATAMRDPVFYRWHAYIDDIFHLYKYKLTPYGNDRLDFPNIRVSSVSIEGGGTPNTLNTLWEQSTVDLGRGMDFTPRGSVLARFTHLQHDEYNYVIEVNNTGGSSVMGMFRIFIAPTVDESGKPFSFDEQRKLMIELDKFSQGVKPGNNTIRRKSIDSSVTIPYERTFRNQADRPADPGTAGAAEFDFCGCGWPHHMLVPKGTTQGYPMVLFVMVSNWNDDRVEQDLVGSCNDAASYCGIRDRKYPDRRAMGFPFDRPAPAATTLSDFLRPNMAVRDCIVRFTDRTRQRGQQG
Protein: Dihydroorotase, mitochondrial (DHOase) (EC 3.5.2.3) (O04904)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase, chloroplastic
- Dihydropyrimidine dehydrogenase
- Carbamoyl phosphate synthase small chain, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Uridine 5'-monophosphate synthase
- Alpha/beta-Hydrolases superfamily protein
- Uridine/cytidine kinase UKL1, chloroplastic
- Purine-uracil permease NCS1
- Uridine/cytidine kinase UKL1, chloroplastic
Sequence:
MIKTLVSPYSGFGSQKLKFDRSSEKVKTRAVRMELTITQPDDWHLHLRDGDLLHAVVPHSASNFKRAIVMPNLKPPVTSTAAAIIYRKFIMKALPSESSFDPLMTLYLTDKTLPEEIRLARESGVVYAVKLYPAGATTNSQDGVTDLFGKCLPVLEEMVKQNMPLLVHGEVTDPSIDVFDREKIFIETVLQPLIQRLPQLKVVMEHITTMDAVNFVESCKEGSVGATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREAIVKAVTSGSKKFFLGTDSAPHERSRKESSCGCAGIYSAPIALSLYAKVFDEAGALDKLEAFTSFNGPDFYGLPRNSSKITLKKSPWKVPDVFNFPFGEIVPMFAGETLQWQPLK
Protein: Pumilio RNA binding family member 1 (E9PL65)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGG
Protein: RING1 and YY1-binding protein (Death effector domain-associated factor) (DED-associated factor) (Q8CCI5)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites. Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (By similarity). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis. May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (By similarity). May bind to DNA. May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3.
Subcellular location: Nucleus {ECO:0000269|PubMed:17070805}. Cytoplasm {ECO:0000250|UniProtKB:Q8N488}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17070805}. Note=Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies. {ECO:0000269|PubMed:17070805}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Lysine-specific demethylase 2B
- Polycomb group RING finger protein 1
- E3 ubiquitin-protein ligase RING2
- Transcriptional repressor protein YY1
- Polycomb group RING finger protein 5
- Polycomb group RING finger protein 6
- Polycomb group RING finger protein 2
- Polycomb complex protein BMI-1
- Polycomb group RING finger protein 3
Sequence:
MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKPDKEKPEKDKDISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF
Protein: Cytochrome c domain-containing protein (Q18853)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Cytochrome c oxidase subunit 1
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 4
- Probable NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- Cytochrome b-c1 complex subunit 6
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Cytochrome b
Sequence:
MQRAVVQGSKRGLAALAGVTAASGMGLVYALENSVSASGDNVHPYALPWAHSGPFSSFDIASVRRGYEVYKQVCAACHSMKFLHYRHFVDTIMTEEEAKAEAADALINDVDDKGASIQRPGMLTDKLPNPYPNKKAAAAANNGAAPPDLSLMALARHGGDDYVFSLLTGYLEAPAGVKVDDGKAYNPYFPGGIISMPQQLFDEGIEYKDGTPATMSQQAKDVSAFMHWAAEPFHDTRKKWALKIAALIPFVAVVLIYGKRHIWSFTKSQKFLFKTVKGREPPKAQ
Protein: Armadillo repeat containing 5 (J3KQ26)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVTLGAGVRLFTGVYPVVLNQIRATSEASAITRTTMPAPELTSTSRAEDTRDTGVQLRKRKIPQARHSRKRQRTFSFRSLGSAARSGAESEARAKMAAAKPTLTDSLSFCLAQLAAAAGEALGGEKDPATNETPLSRALLALRTRHIKAAGGIERFRARGGLRPLLALLRRAAAAGSAPSQAGPGSAPSSAASGASSPAPASGPAPSAVSSSSPTPPVRLRKTLDLALSILADCCTEGACRTEVRRLGGILPLVTILQCMKTDSIQNRTARALGNLAMEPESCGDIHCAGAVPLLVESLTACQDSQCLQSVVRALRNLADSPQHRLALAQQGAVRPLAELLATAPDAALTLALVRALLELSRGCSRACAEQLSLGGGLGPLVSLASHPKRAVREGTILILANLCAQGLIRPALGNAGGVEVLVDELRQRRDPNGASPTSQQPLVRAVCLLCREAINRARLRDAGGLDLLMGLLRDPRASAWHPRIVAALVGFLYDTGALGRLQALGLVPLLAGQLCGEAGEEEEEGREAASWDFPEERTPERAQGGSFRSLRSWLISEGYATGPDDISPDWSPEQCPPEPMEPASPAPTPTSLRAPRTQRTPGRSPAAAIEEPWGREGPALLLLSRFSQAPDPSGALVTGPALYGLLTYVTGAPGPPSPRALRILSRLTCNPACLEAFVRSYGAALLRAWLVLGVAPDDWPAPRARPTLHSRHRELGERLLQNLTVQAESPFGVGALTHLLLSGSPEDRVACALTLPFICRKPSLWRRLLLEQGGLRLLLAALTRPAPHPLFLFFAADSLSCLQDLVSPTVSPAVPQAVPMDLDSPSPCLYEPLLGPAPVPAPDLHFLLDSGLQLPAQRAASATASPFFRALLSGSFAEAQMDLVPLRGLSPGAAWPVLHHLHGCRGCGAALGPVPPPGQPLLGSEAEEALEAAGRFLLPGLEEELEEAVGRIHLGPQGGPESVGEVFRLGRPRLAAHCARWTLGSEQCPRKRGLALVGLVEAAGEEAGPLTEALLAVVMGIELGARVPA
Protein: Cyclin-D-binding Myb-like transcription factor 1 (Cyclin-D-interacting Myb-like protein 1) (mDmp1) (Q8CE22)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator which activates the CDKN2A/ARF locus in response to Ras-Raf signaling, thereby promoting p53/TP53-dependent growth arrest. May also cooperate with MYB to activate transcription of the ANPEP gene. Binds to the consensus sequence 5'-CCCG[GT]ATGT-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:10097151, ECO:0000269|PubMed:16878159, ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:9488476}.
Interaction partners:
Sequence:
MSTVEEDSDTVTVETVNSVTFTQDTDGNLILHCPQNDPDEVDSEDSTEPPHKRLCLSSEDDQSIDDATPCISVVALPLSENDQSFEVTMTATTEVADDELSEGTVTQIQILQNDQLDEISPLGTEEVSAVSQAWFTTKEDKDSLTNKGHKWKQGMWSKEEIDILMNNIERYLKARGIKDATEIIFEMSKDERKDFYRTIAWGLNRPLFAVYRRVLRMYDDRNHVGKYTPEEIEKLKELRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNTGKWTEEEEKRLAEVVHELTSTEPGDIVTQGVSWAAVAERVGTRSEKQCRSKWLNYLNWKQSGGTEWTKEDEINLILRIAELDVADENDINWDLLAEGWSSVRSPQWLRSKWWTIKRQIANHKDVSFPVLIKGLKQLHENQKNNPVLLENKSGSGVPNSNCNSSVQHVQIRVARLEDNTAISPSPMAALQIPVQITHVSSTDSPAASVDSETITLNSGTLQTFEILPSFHLQPTGTPGTYLLQTSSSQGLPLTLTTNPTVTLAAAAPASPEQIIVHALSPEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSLSQEELTVDSDLHSSDFPEPPDALEADTFPDEIPRPKMTIQPSFNNAHVSKFSDQNSTELMNSVMVRTEEEIADTDLKQEEPPSDLASAYVTEDLESPTIVHQVHQTIDDETILIVPSPHGFIQASDVIDTESVLPLTTLTDPIFQHHQEASNIIGSSLGSPVSEDSKDVEDLVNCH
Protein: Uncharacterized protein (Q9VVH6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- non-specific serine/threonine protein kinase
- FI08029p
- LP10147p
- GEO12017p1
- Testis-enriched HMG-box-containing protein 1
- Uncharacterized protein
- eIF-4F 25 kDa subunit
- IP09476p
- IP08114p
- Cytosol aminopeptidase
Sequence:
MPYHDRAKARLENEVVLLRSEVSSLRSKHNQHRKYRQEQVVLQARMEQEIQLLQSELAAAQSNRNERECGGAEQCSVLSQQLEKLDEHVAKQEKYIAFLEEQINLTRNKYQQRMTEVRQNAELVEKEMKRVRREMKTIAEQAGEVDSLKNQVGFLTAKLERRNAIISRYEAQQEEMISIMASLQKKKVKKTRHQKIHNNHDDKADVRSIPSEQLPMPKPSDQIKHRKKRKFGEGDKEDSSSAGSDKPPSFEANPRSSKIRSHNLDCLSSALKNKLSNQQQSTVEG
Protein: Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2) (P98198)
Organism: Homo sapiens (Human)
Function: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. May contribute to the maintenance of membrane lipid asymmetry.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:25315773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20961850}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. {ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:25315773}.
Interaction partners:
- Cell cycle control protein 50A
- Cell cycle control protein 50B
Sequence:
MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNILTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDYFRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLCYIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENKFPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIFGFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNIMVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGDPHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVHEMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTTMDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMMLLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIVTGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHSLAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSMIKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSLVIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTLAQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGRTGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPSGGADKPLKG
Protein: Ethylene-responsive transcription factor RAP2-10 (Protein RELATED TO APETALA2 10) (Q9SW63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
METATEVATVVSTPAVTVAAVATRKRDKPYKGIRMRKWGKWVAEIREPNKRSRIWLGSYSTPEAAARAYDTAVFYLRGPSARLNFPELLAGVTVTGGGGGGVNGGGDMSAAYIRRKAAEVGAQVDALEAAGAGGNRHHHHHQHQRGNHDYVDNHSDYRINDDLMECSSKEGFKRCNGSLERVDLNKLPDPETSDDD
Protein: Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier atg8) (A2QPN1)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Besides its function in nutrient recycling, autophagy plays important roles in physiological adaptation by organelle turnover (such as mitochondrial turnover) and protection against cell death upon carbon depletion in submerged cultures.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}.
Interaction partners:
Sequence:
MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGDC
Protein: WD repeat domain 62 (A0A0G2K8E8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMAALAAGGYARSDTIEKLSSVMAGVPARRNQSSPPPAPPLCLRRRTRLAAAPEDTVQNRVTLEKVLGITAQNSSGLTCDPGTGHVAYLAGCVVVNGHRPAVRIWDVEEKTQVAEMLGHKYGVACVAFSPNMKHIVSMGYQHDMVLNVWDWKKDIVVASNKVSCRVIALSFSEDSSYFVTVGNRHVRFWFLEASTEAKVTSTMPLVGRSGILGELHNNIFCGVACGRGRMAGNTFCVSYSGLLCQFNEKRVLDKWINLKVSLSSCLCVSDELIFCGCTDGIVRIFQAHSLLYLTNLPKPHYLGIDVAQGLDSSFLFHRKAEAVYPDTVALTFDPIHQWLSCVYKDHSVYIWDVKDINEVSKIWSELFHSSFVWNVEVYPEFEDQRACLPSGTFLTCSSDNTIRFWNMDSGSDTQWRKNIFSDSLLKVVYVENDIQHLQDMSHFPDRGSENGTPMDMKAGVRVMQVSPDGQHLASGDRSGNLRIHELHFMDELIKVEAHDAEVLCLEYSKPETGVTLLASASRDRLIHVLNVEKNYNLEQTLDDHSSSITAIKFAGTRDVQMISCGADKSIYFRSAQQTSDGLHFVRTHHVAEKTTLYDMDIDITQKYVAVACQDRNGWSLRQTAQGDMCLFPQVHVDPSGTFLATSCSDKSISVIDFYSGECVAKMFGHSEIVTGMKFTYDCRHLITVSGDSCVFIWHLGPEITTCMKQHLMEINHQEQQHLPKDQKWSGPPSQETSASTPSEIRSLSPGEQTEDEMEEECEPEETLKTPSKESLDPDPRCLLTNGKLPLWAKRLLGDDDVTDSSAFHAKRSYQPHGRWAERAEQEPLKTILDAWALDSYFTPMKPGNLEDSVLDSVEPQNLAGLLSECSPENGHTAPGEGLVSYLCHSESGSPKEDSRGHPSYLPLQREGTETRELILCSPEVEVTVTGMHREYYEEAEAGPEDQQGDSYLRVSSVSSKDQSPPEDSGESEAELECSFAAAHVSAPRTDPGPHLTMTGKPEHSSTDELAQPGVPGLGNGSLPQTPEQEKFLRHHFETLTDAPAEELFPGSLGDIKISETDDYFFNPRLSISTQFLSRLQKTSRFPPRLPLHLMKSPEVQPVGQGGNQPKAGPLRAGTGYMSSDGTNVLSGQMAEETPEASCLPTPPITGLASCVPPSSVIPTDRKPPTPTSGLTTGREQSIPAPSPCSYLESTTSSHAKMTRSTSLGDSEGPVTGELPRPLHKPVSPGQEPQAVPTTVALTSSVKGHEPALPAWGNHEARASLRLTLSSVCEQLLSPPQLEPPTTPVWSQEAVDVPPSMAVTVASFSAPSPEDMSTLGLHSSVFLPKTSASGPLTPPAHPNSLQLLETRSRMPGSTPALLEPTPDASSGSPDSPGHCGEPGRRAEVPPPGPLELDSVESVLYRLQTAFQEALDLYRMLASSNQLGAEQQQAQTELASAFHWIHHQLEASNCVGAASVAPPLTLPSPGPPSPPTLCPLASPNLQALLEHYSELLVQAVRRKVRGD
Protein: Transporter PPE51 (Proline-proline-glutamate family protein 51) (PPE family protein 51) (Protein PPE51) (P9WHY3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:32139546, ECO:0000305|PubMed:35136132}.
Interaction partners:
- Uncharacterized PPE family protein PPE50
Sequence:
MDFALLPPEVNSARMYTGPGAGSLLAAAGGWDSLAAELATTAEAYGSVLSGLAALHWRGPAAESMAVTAAPYIGWLYTTAEKTQQTAIQARAAALAFEQAYAMTLPPPVVAANRIQLLALIATNFFGQNTAAIAATEAQYAEMWAQDAAAMYGYATASAAAALLTPFSPPRQTTNPAGLTAQAAAVSQATDPLSLLIETVTQALQALTIPSFIPEDFTFLDAIFAGYATVGVTQDVESFVAGTIGAESNLGLLNVGDENPAEVTPGDFGIGELVSATSPGGGVSASGAGGAASVGNTVLASVGRANSIGQLSVPPSWAAPSTRPVSALSPAGLTTLPGTDVAEHGMPGVPGVPVAAGRASGVLPRYGVRLTVMAHPPAAG
Protein: Voltage-gated potassium channel Kch (P31069)
Organism: Escherichia coli (strain K12)
Function: K(+)-specific ion channel. May play a role in the defense against osmotic shock.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:8824224}; Multi-pass membrane protein {ECO:0000269|PubMed:8824224}.
Interaction partners:
- Protein YciI
- Trk system potassium uptake protein TrkH
- Trk system potassium uptake protein TrkG
- Glutathione-regulated potassium-efflux system protein KefC
Sequence:
MSHWATFKQTATNLWVTLRHDILALAVFLNGLLIFKTIYGMSVNLLDIFHIKAFSELDLSLLANAPLFMLGVFLVLNSIGLLFRAKLAWAISIILLLIALIYTLHFYPWLKFSIGFCIFTLVFLLILRKDFSHSSAAAGTIFAFISFTTLLFYSTYGALYLSEGFNPRIESLMTAFYFSIETMSTVGYGDIVPVSESARLFTISVIISGITVFATSMTSIFGPLIRGGFNKLVKGNNHTMHRKDHFIVCGHSILAINTILQLNQRGQNVTVISNLPEDDIKQLEQRLGDNADVIPGDSNDSSVLKKAGIDRCRAILALSDNDADNAFVVLSAKDMSSDVKTVLAVSDSKNLNKIKMVHPDIILSPQLFGSEILARVLNGEEINNDMLVSMLLNSGHGIFSDNDELETKADSKESAQK
Protein: Protein Vpu (U ORF protein) (Viral protein U) (P05919)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular location: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:8331740}.
Interaction partners:
Sequence:
MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL