wanglab/gogpt-training-data huggingface dataset:
Protein: Protein BTN1 (P47040)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in vacuolar arginine transport. Involved in pH homeostasis. May be involved in ion homeostasis together with IST2. Not necessary for mitochondrial function or ATP synthase degradation.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10319861, ECO:0000269|PubMed:9753630}; Multi-pass membrane protein {ECO:0000269|PubMed:10319861, ECO:0000269|PubMed:9753630}.
Interaction partners:
- Protein BTN2
- 30 kDa heat shock protein
- GTP-binding protein RHB1
- Plasma membrane ATPase 2
- Ribosome maturation protein SDO1
- Arginine permease CAN1
- Protein transport protein YIF1
- Plasma membrane ATPase 1
- Increased sodium tolerance protein 2
Sequence:
MSDKSHQIYCYFWLFGLINNVLYVVILSAAVDIVGPTLPKSLVLLADIFPSLAIKLCSPFFIDRIKYSYRIWSLITMSCLGMFLVSFKNLFVCLLGISFASISSGFGEVTFLQLTHYYKQISLNGWSSGTGGAGIIGGASYMFLTSIFKVPVKLTLLVFSLLPFAFLFYFKLESNDTNLTYQSLQQIDEAEDDQLVPFPVAFTHTNASQSLYSTRQHILQTVKRLRRLVFPYMVPLTTVYLFEYLINQAVAPTLLFPINGDERSKSMPFFFHKYRDIYVTYGTLYQLGVFISRSFGHLMRMRSLYILAFLQGVNLCITVLQSWFYVTHSPWAVMILIFYEGFLGGASYVNTFLNILEQEDPDETEFAMGAVSIADSFGVFLAALLGLGLEPKLCRHQIADDRPWCRME
Protein: N(6)-hydroxylysine O-acetyltransferase (EC 2.3.1.102) (N(6)-hydroxylysine acetylase) (Q47317)
Organism: Escherichia coli
Function: Catalyzes the transfer of acetyl from acetyl-CoA to the N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Subcellular location: Cytoplasm. Cell membrane {ECO:0000305}.
Interaction partners:
Sequence:
MSGPNIVHSGYGLRCEKLDKPLNLGWGLDNSAVLHWPGELPTGWLCDALDQIFIAAPQLSAVVLPWSEWCEEPQALTLFGQVQSDIIHRSAFWQLPLWLSSPANRASGEMVFDAEREIYFPQRPPRPQGEVYRRYDPRIRRMLSFRIADPVSDAERFTRWMNDPRVEYFWEQSGSLEVQIAYLERQLTSKHAFPLIGCFDDRPVSNIEIYWAAEDRIGRHYSWQPFDRGLHLLVGEQQWRGAHYVQSWLRGVTHYLLLNEPRTQRTVLEPRTDNQRLFRHLEPAGYRTIKEFDFPHKRSRMVMADRHHFFTEVGL
Protein: Receptor-like protein kinase homolog (Q9SNA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MNSSHELLLTALIATFAIFHLVQAQEQEGFISLDCGLAPTEPSPYTEPVTTLQYSSDSNFIQSGKLGRIDTSLQTFFLKQQTTLRYFPDGIRNCYNLTVKQGTNYLIRARFTYGNYDGRNMSPTFDLYLGPNLWKRIDMTKLQNKVSTLEEITYIPLSNSLDVCLVKTNTTIPFISALELRPLPSNSYITTAGSLRTFVRFCFSNSVEDIRFPMDVHDRMWESYFDDDWTQISTSLTVNTSDSFRLPQAALITAATPAKDGPSYIGITFSTSSEERFFIYLHFSEVQALRANETREFNISINGESVADLYRPLSRTQSSTHPPMINAIEIFLVSELLQSETYENDVIAIKKIKDTYGLQLISWQGDPCVPRLYKWDGLDCTDTDTYIAPRITSLKLSSKGLTGTIAADIQYLTSLEKLDLSDNKLVGVVPEFLANMKSLMFINLTKNDLHGSIPQALRDREKKGLKILFDGDKNDPCLSTSCNPKKKFSVMIVAIVASTVVFVLVVSLALFFGLRKKKTSSHVKAIPPSPTTPLENVMSTSISETSIEMKRKKFSYSEVMKMTNNFQRALGEGGFGTVYHGDLDSSQQVAVKLLSQSSTQGYKEFKAEVDLLLRVHHINLLNLVGYCDERDHLALIYEYMSNGDLKHHLSGEHGGSVLSWNIRLRIAVDAALGLEYLHIGCRPSMVHRDVKSTNILLDENFMAKIADFGLSRSFILGGESHVSTVVAGSLGYLDPEYYRTSRLAEMSDVYSFGIVLLEIITNQRVIDKTREKPHITEWTAFMLNRGDITRIMDPNLNGDYNSHSVWRALELAMSCANPSSENRPSMSQVVAELKECLISENSLRSKNQDMSSQRSLDMSMNFDTKDVPSAR
Protein: Leucine-rich alpha-2-glycoprotein (LRG) (P02750)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Endoglin
- Cytochrome c
- Alpha-1-antichymotrypsin
Sequence:
MSSWSRQRPKSPGGIQPHVSRTLFLLLLLAASAWGVTLSPKDCQVFRSDHGSSISCQPPAEIPGYLPADTVHLAVEFFNLTHLPANLLQGASKLQELHLSSNGLESLSPEFLRPVPQLRVLDLTRNALTGLPPGLFQASATLDTLVLKENQLEVLEVSWLHGLKALGHLDLSGNRLRKLPPGLLANFTLLRTLDLGENQLETLPPDLLRGPLQLERLHLEGNKLQVLGKDLLLPQPDLRYLFLNGNKLARVAAGAFQGLRQLDMLDLSNNSLASVPEGLWASLGQPNWDMRDGFDISGNPWICDQNLSDLYRWLQAQKDKMFSQNDTRCAGPEAVKGQTLLAVAKSQ
Protein: tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Q8MSZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHYAFNYAQLDGQIVAALDVNTVANAVYAHNYGSNLVKTRNIQSLSVKEVTKLQANMLLMSPPCQPHTRQGLQRDTEDKRSDALTHLCGLIPECQELEYILMENVKGFESSQARNQFIESLERSGFHWREFILTPTQFNVPNTRYRYYCIARKGSDFPFAGGKIWEEMPGAIAQNQALSQIAEIVEENVSPDFLVPDDVLTKRVLVMDIIHPAQSRSMCFTKGYTHYTEGTGSAYTPLSEDESHRIFELVKEIDTSNQDASKSEKILQQRLDLLHQVRLRYFTPREVARLMSFPENFEFPPETTNRQKYRLLGNSINVKVVGELIKLLTIK
Protein: Novel acetylcholine receptor chaperone (Spinal cord expression protein 4) (TMEM35 gene-derived unknown factor 1) (Transmembrane protein 35A) (Q6JAM9)
Organism: Rattus norvegicus (Rat)
Function: Molecular chaperone which mediates the proper assembly and functional expression of the nicotinic acetylcholine receptors (nAChRs) throughout the brain. Essential for the proper folding, assembly, function and surface trafficking of alpha-7 (CHRNA7), alpha-4-beta-2, alpha-3-beta-2 and alpha-3-beta-4 receptors. Stably associates with ribophorin-1 (RPN1) and ribophorin-2 (RPN2) (components of the oligosaccharyl transferase (OST) complex) and with calnexin (CANX), both of which are critical for NACHO-mediated effects on CHRNA7 assembly and function (By similarity). Facilitates the proper folding and assembly of alpha-6-beta-2 and alpha-6-beta-2-beta-3 receptors and acts at early stages of the nAChRs subunit assembly. Promotes the expression of the alpha-4(2):beta-2(3) stoichiometric form over the alpha-4(3):beta-2(2) form (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:Q9D328}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle {ECO:0000269|PubMed:20685870}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:26875622}; Multi-pass membrane protein {ECO:0000255}. Note=Shedding may lead to a soluble peptide. {ECO:0000269|PubMed:20685870}.
Interaction partners:
- Golgin B1
Sequence:
MASPRTITIVALSVALGLFFVFMGTIKLTPRLSKDAYSEMKRAYKSYVRALPLLKKMGINSILLRKSIGALEVACGIVMTLVPGRPKDVANFFLLLLVLAVLFFHQLVGDPLKRYAHALVFGILLTCRLLIARKPEDRSSEKKALPESAEEQPSLYEKAPQGKVKVS
Protein: Phosphoenolpyruvate/phosphate translocator 3, chloroplastic (OsPPT3) (Q5VQL3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Phosphoenolpyruvate/phosphate translocator that transports phosphoenolpyruvate (PEP) and dihydroxyacetone phosphate.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MQRAAAASRATAWSTARHGAARVTASASFSGGGGIVAGAALPLRVRGGQLMSLPLLSGGRAVTARVAAAEAPLPADDADAAAGRERGALAETAQLGAMIVAWYLLNIYFNIYNKQVLQPLPFPYTITAFQLAFGSFVIFLMWALKLHPAPRISISQLAKIAPLAAGHMLGTVFTNMSLSKVAVSFTHTIKASEPFFTVLLSAFFLGETPSLLVLGSLVPIVGGVALASLTELSFNWIGFWSAMASNLLYQSRNVLSKKLLGGEEEALDDINLFSILTILSFLLSLPLMLFSEGVKFSPGYLRSTGLNLQELCVRAALAGFCFHGYQKLSYLILARVSPVTHSVANCVKRVVVIVASVLFFRTPISPVNALGTGVALGGVFLYSRLKRTKPKNA
Protein: ATP synthase subunit b, mitochondrial (ATPase subunit b) (FO-ATP synthase subunit b) (Q94516)
Organism: Drosophila melanogaster (Fruit fly)
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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit g
- ATP synthase subunit gamma, mitochondrial
- ATPase protein 9
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit d, mitochondrial
- Putative ATP synthase subunit f
- ATP synthase subunit alpha, mitochondrial
Sequence:
MFSRAALLTAQRPLTVAATRSAAAAAAPGGAIERRQRPEHPGKVRLGFLPEEWFQFFYNKTGVTGPYTFGVGLITYLCSKEIYVMEHEYYSGLSLGIMAIIAVKKLGPVIAKWADGEIDKIESEWKEGREAELKVLSDAIEAEKKEQWRADGALLLMEAKKENIALQLEAAFRERAMNVYSEVKRRLDYQVECRHVERRLSQKHMVNWITTNVLASISPQQEKETLNKCIADLSALALRVKSA
Protein: Serine/threonine kinase 11 interacting protein (M0QYE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XICPDRQLRRYLVLEPDAHAAVQELLAVLTPVTNVAREQLGEARDLLLGRFQCLRCGHEFKPEEPRMGLDSEEGWRPLFQKTDQSALSLKKTLKKK
Protein: ADP-ribosylation factor-like protein 5 (P34212)
Organism: Caenorhabditis elegans
Function: GTP-binding protein that may be involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). Plays a role in the shedding of pathogen spores from intestinal cells.
Subcellular location: Golgi apparatus {ECO:0000250}.
Interaction partners:
- Vps54_N domain-containing protein
- Vacuolar protein sorting-associated protein 54
Sequence:
MGLIMAKLFQSWWIGKKYKIIVVGLDNAGKTTILYNYVTKDQVETKPTIGSNVEEVSYRNLDFVIWDIGGQESLRKSWSTYYVQTDVVIVVIDSSDTTRIPIMKEQLHNMLQHEDLARAHILVLANKQDLPGAMNPAEVSTQLGLQTLRGARKWQINGCCAVKGEGLPEALEWIANNL
Protein: cDNA FLJ61264 (B7Z2Y1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYCPESAVILLSTTVLENVLQPFHFRAGTMSKLPKFEIELPAAPKSTKPSLSERDIAMATIYGQLYVLFLRHHSRTSNSTGAEVVLYHLPREGACKKMHILKLNRTGKFALNVVDNLVVVHHQDTETSVIFDIKLRGEFDGSVTFHHPVLPARSIQPYQIPITGPAAVTSQSPVPCKLYSSSWIVFQPDIIISASQGYLWNLQVKLEPIVNLLPDKGRLMDFLLQRKECKMVILSVCSQMLSESDRASLPVIATVFDKLNHEYKKYLDAEQSYAMAVEAGQSRSSPLLKRPVRTQAVLDQSDVYTHVLSAFVEKKEMPHKFVIAVLMEYIRSLNQFQIAVQHYLHELVIKTLVQHNLFYMLHQFLQYHVLSDSKPLACLLLSLESFYPPAHQLSLDMLKMLQSRLKTTCFSIQYSAFLNSETSVCEGAPISHQGNTVKNMLLFSNRFLETKL
Protein: Globin family profile domain-containing protein (A0A1D8PGJ3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- F-box domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Mnn4-4p
Sequence:
MSSFVEVKPDFVFSQYEISIIKSIWRSLDLNNPLNLKDFYYTVSAAINSTGTVTTNGVVSPKRDKFTSLIITQQDIANTISDYQVEEFIEVATSLIHHLEFGKEFPENELVQLSKRNQRIYKIYYKQYLTLGNSLMEAIEDFTNLLVGKSKRIFSRFLSILLSAILYYSNDISFVDTTTTNSNNTLNINLTATPTTTHSNASIYSELSYSMLSLNTDNTSTSAATTAEAIILEEIIKPPQLIEIQPSLPSDIDEQSQPVQSTPEDVEYAEDATITNSIYTNNTVDNGDANSGFFDSSYDYLNSFAISPDNDDDDDEYDNGQSLHEREIVGKKQQKNKSKVVYEEEEDDDDFDDTKSIVSTMSNLSSFKKWGIIRRKKSHKDKFRSSKKFIHKNILRSEK
Protein: Carminomycin 4-O-methyltransferase DauK (COMT) (EC 2.1.1.292) (Anthracycline 4-O-methyltransferase) (Q55216)
Organism: Streptomyces sp. (strain C5)
Function: Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 4-O-position of carminomycin to form daunorubicin. In vitro, it also methylates the anthracyclines rhodomycin D (10-carbomethoxy-13-deoxycarminomycin), 10-carboxy-13-deoxycarminomycin, 13-deoxy-carminomycin and 13-dihydrocarminomycin at the 4-hydroxyl position.
Interaction partners:
Sequence:
MTAEPTVAARPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRPEALLRLIRHLVAIGLLEEDAPGEFAPTEVGKLLADDHPAAQRAWHDLTQAVARADISFTRLPEAIRSGRPTYESVYGKPFYEDLAGRPDLRASFDSLLACDQDVAFDAPAAAHDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMAGTVDTARSYLRDAGLSDRVDVVEGDFFEPLPRRADAIILSFVLLNWPDHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPASTGA
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A3B3IS40)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK
Protein: CARMIL pleckstrin homology domain-containing protein (Q21301)
Organism: Caenorhabditis elegans
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
Sequence:
MSMSRSTIQELCDFVQHKPSQILGNKFFDSRIVVQVDVAHKADKYEPRIFIISKFRIFFLMGKTTSSLKIEKSFHVLAIKAIHVISEEELVIHLDDGVHKKKINIKCSIHPAVHLARQLLSAVKHYFPDFGVYLQSSIDVNPSALYTEFPSLPTASPRPCHSFRRTYAALCDFYDQPYRDEVSWDVEKIYTANKLRDLKIDDFSHLLPKDLLPIVGVLQYSAYFTGLICDAVRVSSEVIDVVLSVIRKSQNLKKLQLRSCSLPKDFITLLASAFHNNQNACLEYLDLSRNPIDDKKGFTILSSVLPRLNQLKYVNFSECQLSDKSINLLCTGLYNGMTSCKSGGMQLTELILSANPMKDDISGIINLVSISTSLRVLDFSDTGIHLDKLWNSLKFGGLQIEKLILNGCSLSKKSEGVQTAKEYFSMAVNLSHISFNNTSMPSEYLKAVLLGLASNQQLQPFRLDLDATCEKGSASVLDACIGGIRCETLSLRDNNLDGELQGVLQSLMMVTCLRRLDIGGSNMNQLKKNNKQVHVINKVLLDVVKLYSEEGCLEELNLSDCRLGAYLSVLINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIKMNHTLTHFPYPVHDAFDCMQRVERPRTVAALSQIQNCLYRNRTALGADEANCKKMFAEGVLQKMEKANDEVVGSIVDSISAFGQEPFPPKMIEIIEEFVGKFQMEGGRIISESISRTIGGDLSATSRRAEQLATARLAEVCTEQVKHVFSEWKWREMCEHVESELSKMSIGGSGDACSLGRTSSVGTGSPAMSSPFTPKRSQAGHRPRSIIGDLTSSTTSSETVGDSTEQGVNLDLPPKPSVLSHLQKARPRKRGGASSILNSSLSEDVMMTSKSSGGPENGDLADLIEEVDEVEQEPRKVPTGVRVAMIPDSSLISQVHLRPSAERTLSASSDFSLSPREASSPTTSNSKIMTSSSASDSPPPLPQRNRVGPGGAPPPLLPPKPEPRSRLIGMTSPTTPPPTADDDENANSRRSVADMARIFQK
Protein: Mitochondrial 2-oxoglutarate/malate carrier protein (OGCP) (alpha-oxoglutarate carrier) (Solute carrier family 25 member 11) (SLC25A11) (Q9CR62)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis. Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P97700}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97700}.
Interaction partners:
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Malate dehydrogenase, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
Sequence:
MAATASPGAGRMDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKTEGLKGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALVRIAREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIVKTRIQNMRMIDGKPEYKNGLDVLLKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG
Protein: Band 4.1-like protein 3 (4.1B) (Differentially expressed in adenocarcinoma of the lung protein 1) (DAL-1) (Erythrocyte membrane protein band 4.1-like 3) [Cleaved into: Band 4.1-like protein 3, N-terminally processed] (Q9Y2J2)
Organism: Homo sapiens (Human)
Function: Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction {ECO:0000269|PubMed:9892180}. Cell membrane {ECO:0000269|PubMed:9892180}; Peripheral membrane protein {ECO:0000269|PubMed:9892180}; Cytoplasmic side {ECO:0000269|PubMed:9892180}. Cytoplasm {ECO:0000269|PubMed:9892180}. Note=Detected in the cytoplasm of actively dividing cells.
Interaction partners:
- Cell adhesion molecule 1
- Protein arginine N-methyltransferase 3
- Spectrin beta chain, non-erythrocytic 1
- Band 4.1-like protein 2
- Spectrin alpha chain, non-erythrocytic 1
- Protein 4.1
- Band 4.1-like protein 1
Sequence:
MTTESGSDSESKPDQEAEPQEAAGAQGRAGAPVPEPPKEEQQQALEQFAAAAAHSTPVRREVTDKEQEFAARAAKQLEYQQLEDDKLSQKSSSSKLSRSPLKIVKKPKSMQCKVILLDGSEYTCDVEKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQVRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGSDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGEVGTGQYATTKGISQTNLITTVTPEKKAEEERDEEEDKRRKGEEVTPISAIRHEGKSPGLGTDSCPLSPPSTHCAPTSPTELRRRCKENDCKLPGYEPSRAEHLPGEPALDSDGPGRPYLGDQDVAFSYRQQTGKGTTLFSFSLQLPESFPSLLDDDGYLSFPNLSETNLLPQSLQHYLPIRSPSLVPCFLFIFFFLLSASFSVPYALTLSFPLALCLCYLEPKAASLSASLDNDPSDSSEEETDSERTDTAADGETTATESDQEEDAELKAQELEKTQDDLMKHQTNISELKRTFLETSTDTAVTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEETKQSSGEKLMDGSEIFSLLESARKPTEFIGGVTSTSQSWVQKMETKTESSGIETEPTVHHLPLSTEKVVQETVLVEERRVVHASGDASYSAGDSGDAAAQPAFTGIKGKEGSALTEGAKEEGGEEVAKAVLEQEETAAASRERQEEQSAAIHISETLEQKPHFESSTVKTETISFGSVSPGGVKLEISTKEVPVVHTETKTITYESSQVDPGTDLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: Adducin 3 (gamma) a (Q1LUP1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}.
Interaction partners:
- Xaa-Pro aminopeptidase 1
- Alpha-adducin
- Xylulokinase homolog
- Methylthioribose-1-phosphate isomerase
- Enolase-phosphatase E1
- Glypican-1
- Glypican 1b
- Guanylyl cyclase domain-containing 1
- Protein 4.1
Sequence:
MSGEPRQEVVTTPPPPSVGKREGYFDRVNENDPEYLRARNMSPDLRQDFNMMEQKKRVTQILQSPAFKDELEGMIQEQMNKGNNPTGLLALRQIADFFMSSSVAGFSTSPLSLGMVTPINDMFSVESSTMVKGEKQTRCKLASLYRIVDLFSWAHFASCYITVRVSKEQDHILIIPRGLSFAEASASNLVKVNILGDVIDQGSTNLRIDAAGFSPHAAIYSIRPDVRCIVHISTPATAAVSSMKCGLLPISQEALILGDIAYYNYQGSLDEQEERVELQKALGPTAKVLVLRNHGIVALGETIEEAFHYIYGAQYACEIQVNAFSCAGGMENLIVLDLEKFKARTQGVAQVGVNMGSQQKWRLGELEFESLMRMLDNLGYRTGYTYRHPIVREKPRHKSEVEIPATVTAFMFDEDDAPRFPLKLLQQRQQREKTRWLNSPNCYMKVNVADGASEENRRTKTTWMKSDDGGNASGTPIRIEDPNQFVPLNTNPSEVLQKRNKIREQNRFDVMTAGPQSQKLAGIVVERPPPYMGNDEEETGALPPNPFSELNEKEEHQRRLRIDADEEQLTSDDASTLSQSVSPQHTPAKEENHTGVMLNGKDDHGDEDELIKRVSQLTTSLESMEISVRSGEKIEEALTPESSPSKSPNKKKKKFRTPSFLKKNKKKEKVEA
Protein: PCNA-associated factor (PCNA-associated factor of 15 kDa) (PCNA-clamp-associated factor) (H0YMA4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRNQEPPILQHTEQQAGHTAH
Protein: Kinesin-1 heavy chain (Conventional kinesin heavy chain) (Ubiquitous kinesin heavy chain) (UKHC) (Q2PQA9)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation. Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends. Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7514426}. Cytolytic granule membrane {ECO:0000250|UniProtKB:P33176}. Lysosome membrane {ECO:0000250|UniProtKB:P33176}; Peripheral membrane protein {ECO:0000250|UniProtKB:P33176}; Cytoplasmic side {ECO:0000250|UniProtKB:P33176}. Note=Uniformly distributed between soma and neurites in hippocampal neurons. {ECO:0000269|PubMed:7514426}.
Interaction partners:
- Kinesin light chain
- Kinesin light chain 1
- Kinesin light chain 4
- Kinesin light chain 3
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Trafficking kinesin protein 1
- Glycogen synthase kinase-3 beta
- Neurofilament medium polypeptide
- Alpha-synuclein
Sequence:
MADPAECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKTLRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTADKDVAITNDKPAAAIGMAGSFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPGAVRGGGSFVQNNQPVGLRGGGGKQA