wanglab/gogpt-training-data huggingface dataset:
Protein: Probable cytochrome P450 12d1 proximal, mitochondrial (EC 1.14.-.-) (CYPXIID1) (P82712)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion membrane {ECO:0000305}.
Interaction partners:
Sequence:
MNTLSSARSVAIYVGPVRSSRSASVLAHEQAKSSITEEHKTYDEIPRPNKFKFMRAFMPGGEFQNASITEYTSAMRKRYGDIYVMPGMFGRKDWVTTFNTKDIEMVFRNEGIWPRRDGLDSIVYFREHVRPDVYGEVQGLVASQNEAWGKLRSAINPIFMQPRGLRMYYEPLSNINNEFIERIKEIRDPKTLEVPEDFTDEISRLVFESLGLVAFDRQMGLIRKNRDNSDALTLFQTSRDIFRLTFKLDIQPSMWKIISTPTYRKMKRTLNDSLNVAQKMLKENQDALEKRRQAGEKINSNSMLERLMEIDPKVAVIMSLDILFAGVDATATLLSAVLLCLSKHPDKQAKLREELLSIMPTKDSLLNEENMKDMPYLRAVIKETLRYYPNGLGTMRTCQNDVILSGYRVPKGTTVLLGSNVLMKEATYYPRPDEFLPERWLRDPETGKKMQVSPFTFLPFGFGPRMCIGKRVVDLEMETTVAKLIRNFHVEFNRDASRPFKTMFVMEPAITFPFKFTDIEQ
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (A0A8I6A3K6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNFNTILEEILIKRSQQKKKTSPLNYKERLFVLTKSVLTYYEGRAEKKYRKGFIDISKIKCVEIVKNDDGIIPCQNKFPFQVVHDANTLYIFAPSPQSRDRWVKKLKEEIKNNNNIMIKYHPKFWADGSYQCCRQTEKLAPGCEKYNLFESSIRKTLPPAPEIKRRPPPPIPPEEENTEEIVVAMYDFQATEAHDLRLERGQEYIILEKNDTHWWRARDKYGSEGYIPSNYVTGKKSNNLDQYEWYCRNTNRSKAEQLLRTEDKEGGFMVRDSSQPGLYTVSLYTKFGGEGSSGFRHYHIKETATSPKKYYLAEKHAFGSIPEIIEYHKHNAAGLVTRLRYPVSTKGKNAPTTAGFSYDKWEINPSELTFMRELGSGLFGVVRLGKWRAQYKVAIKAIREGAMCEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMERGCLLNFLRQRQGHFSRDVLLSMCQDVCEGMEYLERNSFIHRDLAARNCLVNEAGVVKVSDFGMARYVLDDQYTSSSGAKFPVKWCPPEVFNYSRFSSKSDVWSFGVLMWEIFTEGRMPFEKNTNYEVVTMVTRGHRLPRPKLASKYLYEVMLRCWQEVRLFVCVSSGSWLAGGWGVQFLQLSEGAPPALGCQTLARSFTLVLNFERNLKKQTTLTVSLILRLMLPSPVGAPPQPGP
Protein: UPF0606 protein KIAA1549 (Q9HCM3)
Organism: Homo sapiens (Human)
Function: May play a role in photoreceptor function.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q68FD9}. Note=In the retinal photoreceptor cells, localizes at the connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment. {ECO:0000250|UniProtKB:Q68FD9}.
Interaction partners:
- Serine/threonine-protein kinase B-raf
- Protein FAM131B
- H
- A-kinase anchor protein 9
- Serine/threonine-protein kinase A-Raf
- KH domain-containing RNA-binding protein QKI
Sequence:
MPGARRRRRGAAMEGKPRAGVALAPGPSGRRPSARCARRRRPGLLLPGLWLLLLARPASCAPDELSPEQHNLSLYSMELVLKKSTGHSAAQVALTETAPGSQHSSPLHVTAPPSATTFDTAFFNQGKQTKSTADPSIFVATYVSVTSKEVAVNDDEMDNFLPDTHWTTPRMVSPIQYITVSPPGLPREALEPMLTPSLPMVSLQDEEVTSGWQNTTRQPAAYAESASHFHTFRSAFRTSEGIVPTPGRNLVLYPTDAYSHLSSRTLPEIVASLTEGVETTLFLSSRSLMPQPLGDGITIPLPSLGEVSQPPEEVWATSADRYTDVTTVLSQSLEETISPRTYPTVTASHAALAFSRTHSPLLSTPLAFASSASPTDVSSNPFLPSDSSKTSELHSNSALPGPVDNTHILSPVSSFRPYTWCAACTVPSPQQVLATSLMEKDVGSGDGAETLCMTVLEESSISLMSSVVADFSEFEEDPQVFNTLFPSRPIVPLSSRSMEISETSVGISAEVDMSSVTTTQVPPAHGRLSVPASLDPTAGSLSVAETQVTPSSVTTAFFSVITSILLDSSFSVIANKNTPSLAVRDPSVFTPYSLVPSVESSLFSDQERSSFSEHKPRGALDFASSFFSTPPLELSGSISSPSEAPASLSLMPSDLSPFTSQSFSPLVETFTLFDSSDLQSSQLSLPSSTNLEFSQLQPSSELPLNTIMLLPSRSEVSPWSSFPSDSLEFVEASTVSLTDSEAHFTSAFIETTSYLESSLISHESAVTALVPPGSESFDILTAGIQATSPLTTVHTTPILTESSLFSTLTPPDDQISALDGHVSVLASFSKAIPTGTVLITDAYLPSGSSFVSEATPFPLPTELTVVGPSLTPTEVPLNTSTEVSTTSTGAATGGPLDSTLMGDAASQSPPESSAAPPLPSLRPVTAFTLEATVDTPTLATAKPPYVCDITVPDAYLITTVLARRAVQEYIITAIKEVLRIHFNRAVELKVYELFTDFTFLVTSGPFVYTAISVINVLINSKLVRDQTPLILSVKPSFLVPESRFQVQTVLQFVPPSVDTGFCNFTQRIEKGLMTALFEVRKHHQGTYNLTVQILNITISSSRVTPRRGPVNIIFAVKSTQGFLNGSEVSELLRNLSVVEFSFYLGYPVLQIAEPFQYPQLNLSQLLKSSWVRTVLLGVMEKQLQNEVFQAEMERKLAQLLSEVSTRRRMWRRATVAAGNSVVQVVNVSRLEGDDNPVQLIYFVEDQDGERLSAVKSSDLINKMDLQRAAIILGYRIQGVIAQPVDRVKRPSPESQSNNLWVIVGVVIPVLVVMVIVVILYWKLCRTDKLDFQPDTVANIQQRQKLQIPSVKGFDFAKQHLGQHNKDDILIIHEPAPLPGPLKDHTTPSENGDVPSPKSKIPSKNVRHRGRVSPSDADSTVSEESSERDAGDKTPGAVNDGRSHRAPQSGPPLPSSGNEQHSSASIFEHVDRISRPPEASRRVPSKIQLIAMQPIPAPPVQRPSPADRVAESNKINKEIQTALRHKSEIEHHRNKIRLRAKRRGHYEFPVVDDLSSGDTKERHRVYRRAQMQIDKILDPTASVPSVFIEPRKSSRIKRSPKPRRKHQVNGCPADAEKDRLITTDSDGTYRRPPGVHNSAYIGCPSDPDLPADVQTPSSVELGRYPALPFPASQYIPPQPSIEEARQTMHSLLDDAFALVAPSSQPASTAGVGPGVPPGLPANSTPSQEERRATQWGSFYSPAQTANNPCSRYEDYGMTPPTGPLPRPGFGPGLLQSTELVPPDPQQPQASAEAPFAARGIYSEEMPSVARPRPVGGTTGSQIQHLTQVGIASRIGAQPVEIPPSRGSQYGGPGWPSYGEDEAGRREATHMLGHQEYSSSPLFQVPRTSGREPSAPSGNLPHRGLQGPGLGYPTSSTEDLQPGHSSASLIKAIREELLRLSQKQSTVQNFHS
Protein: Glycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) (P15505)
Organism: Gallus gallus (Chicken)
Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7440562}.
Interaction partners:
- Serine hydroxymethyltransferase
- Glycine cleavage system H protein, mitochondrial
- Dihydrolipoyl dehydrogenase
- Beta_elim_lyase domain-containing protein.
- Sarcosine dehydrogenase.
- Methylenetetrahydrofolate dehydrogenase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Methylenetetrahydrofolate reductase
- Trifunctional purine biosynthetic protein adenosine-3
- Alanine--glyoxylate and serine--pyruvate aminotransferase.
Sequence:
MQSCGRWWGRLAARGAPRHLRPAAGGPRRQQQRWGGGEAARCIEQLLPRHDDFCRRHIGPREREKREMLSAVGVQSVEELMDKTIPASIRLRRPLRMDDHVVENEILETLYNIASKNKIWRSYIGMGYYNCSVPQPIARNLLENAGWVTQYTPYQPEVSQGRLESLLNYQTMVCDITGMDVANASLLDEGTAAAEAMQLCHRQNKRRKFYIDARCHPQTIANYTGVITELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFSELIERAHQNGTLACCATDLLALCILKPPGEFGVDVVLGSSQRFGVPLCYGGPHAAFFAVKENLVRMMPGRMVGVTRDANGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMYGVYHGSDGLKDIARRVHNATLILAEGLRRAGHKLHHDLFFDTLTVTCGCSVKEVLDRAALRKINVRIYSDGRLGVSLDETVNEKDLDDILWIFGCESSAELVAEGMGEETKGILSTPFKRTSKFLTHQVFNSYHSETNIVRYMKRLENKDISLVHSMIPLGSCTMKLNSSAELAPISWKEFANIHPFVPLDQAQGYQQLFKDLEKDLCEITGYDKISFQPNSGAQGEYAGLAAIKAYLNAKGERHRSVCLIPRSAHGTNPASAQMAGMKIQPIEVDKNGSIDISHLKAMVDKHKENLAAIMITYPSTNGVFEEEIGDVCDLIHKHGGQVYLDGANMNAQVGLCRPGDYGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPYLPTHPVIKIQTDKDACPLGTVSAAPWGSSAILPISWVYIKTMGAKGLKHASEIAILNANYMAKRLEKHYKILFRGVRGYVAHEFILDTRPFKKTANIEAVDLAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKGELDRFCDAMISIRQEIADIEEGRMDPQVNPLKMSPHTLNCVTSSKWDRPYSREVAAFPLPFVKPESKFWPTIARIDDIYGDQHLVCTCPPMEAYESPFSEQKRASS
Protein: Ca/calmodulin-dependent protein kinase phosphatase-N (Protein phosphatase 1E (EC 3.1.3.16)) (Q53VM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAGSANEEKTFKRFLELFLREMRPPIQEDVPLPTRPLSDLISEDEVEGECLDLCLQHLCKYNCPFSLAAALARGTADSILQSDLSLYHLNKSVEDGTETETETETETQTQIDSVKLARLVFNKLCETCSQWLKDFPYRRRHLPYYETSIHAIKNMRRKMEDKHVVIPDFNTLFNLQDQEEQAYFAVFDGHGGVDAANYAANHLHVNLVRQEMFSQDAGEALCHSFKLTDERFIKKAKSENLRCGTTGVVTFLRGRTLYVTWLGDSQVMMVKRGQPVELMKPHKPDREDEKKRIEALGGCVIWFGTWRVNGSLSVSRAIGDSEHKPYICGDADCSTFNLDGSEDYLILACDGFYDTVNPEEAVRVVSDHLQENNGDTAMVAHKLVASARDAGSSDNITVIVVFLRDPRLPPPSDEPEEQQDEEPLEDAGEEEEEEEAVDALQSELVCQDGGAENGGKNRGGWPLQQCSAPADLAYEDRMDSFTDRTSLSITGPDVHAETGCFRIPASSGLPPTRTVTPDLIPSNSRAGAAWRPYQEDDPSGYRQKPQPNPRVPSYMQTTSDGQLLEVAALFSQEGRKKRRLDVLPLRRESQRLTRRARESHGPLSCFPSVPYPLRSSERKPGIAFPHVTHSKRV
Protein: Cullin-4 (Cul-4) (O14122)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair. Also has a role as a scaffold for assembling ubiquitin ligases. Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me. ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:18345014}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- RING-box protein pip1
- Chromatin modification-related protein rik1
- Rik1-associated factor 1
- Cell division cycle protein cdt2
- DNA damage-binding protein 1
- Rik1-associated factor 2
- COP9 signalosome complex subunit 5
- Cullin-1
- DNA excision repair protein ckn1
Sequence:
MPPEAKRIVVKGFDPRKSRQRQETYYVTMIDRLNMALQVVMAGLGLKTGYQELYSGVENLTRADQASRCFNILQHHMSSGIQLLKDSAESFIQLEGTETDTNACTVVVGCWNKWLERVEIVQNIFYYMDKTFLSHHPDYPTIEELSLSLFREKLMAVKNIQIPFLNSLLQSFENLHSSKSTDHAYLQDAMLMLHRTEMYSSVFVPMYLVMLSRFYDTESSQKIQELPLEEYLEYAMSSLEREDAYVEKFDIVRDKKSIRETVQRCLITSHLDTLTKGISQFIEKRDAHSCKLLYALLQFNHETEYLIQPWSDCLVDVGFKLVNDESKDDTLVQELLSFHKFLQVVVDESFLHDETLSYAMRKAFETFINGAKGSQREAPARLIAKYIDYLLRVGEQASGGKPLKEVFSEILDLFRYIASKDIFEAYYKLDIAKRLLLNKSASAQNELMLLDMLKKTCGSQFTHSLEGMFRDVNISKEFTSSFRHSKAAHNLHRDLYVNVLSQAYWPSYPESHIRLPDDMQQDLDCFEKFYLSKQVGKKISWYASLGHCIVKARFPLGNKELSISLFQACVLLQFNNCLGGEGISYQDLKKSTELSDIDLTRTLQSLSCARIRPLVMVPKSKKPSPDTMFYVNEKFTDKLYRVKINQIYLKEERQENSDVQEQVVRDRQFELQASIVRVMKQKEKMKHDDLVQYVINNVKDRGIPLVSDVKTAIEKLLEKEYLEREDNDIYTYVT
Protein: Factor of interpulse interval (RE62123p) (Q9VR25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRLIGFILNLAALTAVAWANHHESLSLSPAEHSVVRYTNESLIVQCRSPDPKVELHWKSPKGEIIREHKGRIHIEQTSTEQLKIVFAHIALADKGNWSCEAADGSLHSKSFDLIVYQKITFTENATVMTVKEGEKATILCEVKGEPQPNVTWHFNGQPISAGAADDSKFRILADGLLINKVTQNDTGEYACRAYQVNSIASDMQERTVLMKIEHKPIWSKTPFVSLKYAYINGTATLMCEALAEPPANFTWYRKHNKLHSNNRLYTIQSDSYWSSLTIHVLNTSAFDNYRCRARNDLGTIERTTRLEQGEKPPSPANFQLRGFNSNTFDVVLSAPRGPPDSPMGVNGFRIEYMTEMEFKTDAGKWTNARRKDYAFEEGATFLLTNLEPDTVYLVRAASRNLAGFSDFTKVEKYKTLSLEPRVSSGVKETRNMCVELGVMTLMVLMRPFLG
Protein: BcDNA.GH07066 (Minotaur, isoform A) (Minotaur, isoform E (EC 2.3.-.-, EC 2.3.1.15)) (Q9Y137)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 4, isoform D
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
- Phospholipid/glycerol acyltransferase domain-containing protein
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
Sequence:
MLTTVLNFAQRVAEISLLGGIEIASVALIVYYIFAKTRAPVIIASLFPNLNLSYRTSYLSKINTIRSDLLVTLRSSNEPKTQNSVAHGIGTQNMLELTPHSGQKPFKKLFDWGVLFPYVAQVVRSEKFEYRQVTEIVHNDAVLKHAIKQAAEQTLREQRYAKNGHRLLTRSASGDQEAQEEEDEKRGISYQAILRKQEQRAISILKDMGSTLNNGLLAFTSWILYKLLPCFLSGVVTNTKQIEMLKTATERSPGTPLIFVPLHRSHLDYIMVTWILTNNDIRSPLVAAGNNLQIPVFGGLLRGLGAFFIKRKIDPVEGKKDVLYRAALHLYLTHALKQGHNVEFFIEGGRTRTGKPCMPKGGILSVIVNAFMDGSIPDALLVPVSVNYERLVDGNFVREQKGEKKIPESFGKAISGIWKALKSNYGLMRIDFNEPYSIRELVNSYNKIAREDGNIAKVYKPSARVLQHNQSTSSLYGTDVVCEEHRNLIESISRQVVFDCAAATSVMSTNALAFLLLTRFRNGAEEQILSEALDDLRNSLSGCKDIGFSGESSQIVAYACDLLGSGLVTRSRDENGRLVIKAVNSVESFIELAYYSNMLTPHFALSSILLTTFHSLLPETENKKEAAVSRKKLIDTALENCQIYRYEFILNKPTQVLENLLYQQLDDLLISGCVLTEKLHDDLPNGAEGRRLANVLAECLDEDGYEDVRDGEADEPKLLFASETPSQQRYICEVLAPFAWTYVTVAQSLQILHKNSMLESEFISFVINDLSSKVKRGSCIYAESISTDSVRNCLKLLEKWSVIEVCNQQGMRLISLNTLYEMSRESLNSIVKKIDAIVPKFNSGYFSVTP
Protein: Ras association domain-containing protein 2 (P50749)
Organism: Homo sapiens (Human)
Function: Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation.
Subcellular location: Nucleus. Cytoplasm. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}. Note=Translocates to the cytoplasm in the presence of STK3/MST2 and STK4/MST1.
Interaction partners:
- Serine/threonine-protein kinase 3
- Serine/threonine-protein kinase 4
- Ras association domain-containing protein 4
- Ras association domain-containing protein 5
- GTPase KRas
- Ras association domain-containing protein 7
- Ras association domain-containing protein 1
Sequence:
MDYSHQTSLVPCGQDKYISKNELLLHLKTYNLYYEGQNLQLRHREEEDEFIVEGLLNISWGLRRPIRLQMQDDNERIRPPPSSSSWHSGCNLGAQGTTLKPLTVPKVQISEVDAPPEGDQMPSSTDSRGLKPLQEDTPQLMRTRSDVGVRRRGNVRTPSDQRRIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYVVHTSGEKQKLKATDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPVLKSFIQKLQEEEDREVKKLMRKYTVLRLMIRQRLEEIAETPATI
Protein: Calcium/calmodulin-dependent protein kinase kinase (CaM-KK) (CaM-kinase kinase) (EC 2.7.11.17) (Q3Y416)
Organism: Caenorhabditis elegans
Function: Calcium/calmodulin-dependent protein kinase which phosphorylates cmk-1. Component of a calcium-triggered signaling cascade involved in CRE-mediated transcriptional activation, probably through cmk-1-mediated crh-1/CREB phosphorylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:37166173}.
Interaction partners:
- Calmodulin-like protein
- Calmodulin
- EF-hand domain-containing protein
- Calmodulin-like protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Uncharacterized calcium-binding protein B0563.7
- CBS domain-containing protein
Sequence:
MKNTFARYSLTIPSIPENVISHLRQWNEWMVGDTSDDSPGPSSTVSTMTTTGTVDRRSLLSAASMVRQQSDTTGVRRLVRARAVQEDDEAGPHSSNNLAATMSPNLSRPTRYVKSVSQQRSESYIQLNQYRLMEEIGQGSYGIVKLAYNEEDKNLYALKVLDKMKLLKNFACFRQPPPRRNKENAAPSVLRNPLQLVQKEIAILKKLSHPNVVKLVEVLDDPNDNYLYMVFEFVEKGSILEIPTDKPLDEDTAWSYFRDTLCGLEYLHYQKIVHRDIKPSNLLLSDIGQVKIADFGVSCEFEGIDAFLSGTAGTPAFMAPEALTEGANHFYSGRAQDIWSLGITLYAFVIGTVPFVDNYIIALHKKIKNDPIVFPEAPILSEALQDIILGMLKKDPGHRLMLHEVKVHTWVTRDGTVPMSSEQENCHLVTVTEEEIENCVRVIPRLDTLILVKAMGHRKRFGNPFRNKLSAQSSIRDRRKSSSVKDPTYVPPPNSPPATSNNNLNSTKVDRPEIKCIEMNLSGLTLKVDEAMQSKVESARQ
Protein: Kaptin (Actin binding protein) (Predicted), isoform CRA_a (Kptn protein) (B2RYG4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Integrin alpha FG-GAP repeat containing 2
- KICSTOR subunit 2
- DEP domain containing 5, GATOR1 subcomplex subunit
- NPR2-like, GATOR1 complex subunit
- GATOR complex protein NPRL3
- GATOR2 complex protein WDR24
- GATOR2 complex protein MIOS
- WD repeat domain 59
- Lysosome-associated membrane glycoprotein 1
- S-adenosylmethionine sensor upstream of mTORC1
Sequence:
MGEAAVAEGPCPLREDSFTRFSSQSNVYGLAGGADGRGELLAATLKGKVLGFRYQDLRQKIRPVAKELQFNYIPVDAEIVSIDTFNKSPPKRGLVVGITFIKDSGDKGSPFLNIYCDYEPGSEYNLDSIAESCLNLELQFTPFQLCHAEVQVGDQLETVFLLSGNDPAIHLYKENEGLHQFEEQPVENLFPELTNLTSSVLWLDVHNLPGSSQRLSALGCQSGYVRVAHVDQKNREILQTWTIQQDGPISRVIVFRPSTSEATKDSPQQEGYSLLVASMLEPAVVYWDLLNKGLDDQLLLPGSDQFDSVLCGLVTDVDLDGQPEVLVATYGQELLCYKYHGLPEASRGFRLLWRRSFASPLLAMAHVDLTGDGLRELAVVSLKGVHILQHSLIQASELVLTRLRHQVEQRKHQQGLGDKAGPRPEEPPAS
Protein: Gastric inhibitory polypeptide (GIP) (Glucose-dependent insulinotropic polypeptide) (P01281)
Organism: Sus scrofa (Pig)
Function: Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.
Subcellular location: Secreted.
Interaction partners:
- Gastric inhibitory polypeptide receptor
- Glucagon-like peptide 1 receptor
- Dipeptidyl peptidase 4
- G protein-coupled receptor 119
- Pro-glucagon
- 5-hydroxytryptamine receptor 4
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Lutropin-choriogonadotropic hormone receptor
- Beta-1 adrenergic receptor
- Follicle-stimulating hormone receptor
Sequence:
YAEGTFISDYSIAMDKIRQQDFVNWLLAQKGKKSDWKHNITQ
Protein: glutamate dehydrogenase [NAD(P)(+)] (EC 1.4.1.3) (Q8JG17)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MYRYFGELLSRGAGSALASGCVDSALPASASLMRVRQYSEQPDDPNFFRMVEGFFDRGAAIVEDKLVEDLKSRETPEQKTKRVKGILRIIKPCNQVRSVSFPIKRDNGEWEVVEGYRAQHSQHRTPCKGGIRYSEEVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINVKNYSDNELEKITRRFTIELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYANTIAHTDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSMLGLNPGFQDKTFIIQGFGNVGLHSMRYLHRYGAKCVGIAEYDGSIYNPEGIDPKQLEDYKLQHGTIVGFPGAQPYEGSLLEAQCHILIPAASEKQLTRNNAHRIKAKIIAEGANGPTTPDADKIFLENKVMVIPDMYLNAGGVTVSYFEWLKNLEHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKQGGPIPIVPTADFQARVAGASEKDIVHSGLATPMERSARQIMRTASKYNLGLDLRTAAYVNAIEKVFKVYNEAGITVT
Protein: ATP synthase peripheral stalk subunit d, mitochondrial (ATPase subunit d) (ATP synthase peripheral stalk subunit d) (P13620)
Organism: Bos taurus (Bovine)
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 F
- ATP synthase F
- ATP synthase subunit e
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MAGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANVAKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEKMRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL
Protein: V-type proton ATPase subunit G2 (V-ATPase subunit G2) (Vacuolar H(+)-ATPase subunit G isoform 2) (Vacuolar proton pump subunit G2) (O82629)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit e2
- V-type proton ATPase subunit c''1
Sequence:
MESAGIQQLLAAEREAQQIVNAARTAKMTRLKQAKEEAETEVAEHKTSTEQGFQRKLEATSGDSGANVKRLEQETDAKIEQLKNEATRISKDVVDMLLKNVTTVNN
Protein: DNA dC->dU-editing enzyme APOBEC-3A (A3A) (EC 3.5.4.38) (Phorbolin-1) (P31941)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- DNA dC->dU-editing enzyme APOBEC-3B
- Cytidine deaminase
- Putative C->U-editing enzyme APOBEC-4
- Cullin-5
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Apolipoprotein B-100
- DNA dC->dU-editing enzyme APOBEC-3H
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN
Protein: Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17) (Q9QZX7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
Interaction partners:
- Phosphoserine phosphatase
- L-serine dehydratase/L-threonine deaminase
- Serine hydroxymethyltransferase, cytosolic
- Cystathionine beta-synthase
- Serine dehydratase-like
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- D-amino-acid oxidase
- Disrupted in schizophrenia 1 homolog
- Serine palmitoyltransferase 1
Sequence:
MCAQYCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEVKNVCIVLSGGNVDLTSLNWVGQAERPAPYQTVSV
Protein: YTH domain-containing family protein 1 (Dermatomyositis associated with cancer putative autoantigen 1 homolog) (DACA-1 homolog) (P59326)
Organism: Mus musculus (Mouse)
Function: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex (By similarity). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs. Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts. Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells. In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation. Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (By similarity). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32943573}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9BYJ9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9BYJ9}.
Interaction partners:
- N
- RNA demethylase ALKBH5
- Elongation factor 2
- Pre-mRNA-splicing regulator WTAP
- N
- YTH domain-containing family protein 3
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Alpha-ketoglutarate-dependent dioxygenase FTO
- Eukaryotic translation initiation factor 3 subunit B
- Insulin-like growth factor 2 mRNA-binding protein 3
Sequence:
MSATSVDPQRTKGQDNKVQNGSLHQKDAVHDNDFEPYLSGQSNPSNSYPSMSDPYLSSYYPPSIGFPYSLSEAPWSTAGDPPIPYLTTYGQLSNGDHHFMHDAVFGQPGGLGNNIYQHRFNFFPENPAFSAWGTSGSQGQQTQSSAYGSSYTYPPSSLGGTVVDGQTGFHSDSLNKAPGMNSLEQGMVGLKIGDVTTSAVKTVGSVVNSVALTGVLSGNGGTNVNMPVSKPTSWAAIASKPAKPQPKMKTKSGPIVGGALPPPPIKHNMDIGTWDNKGPAPKASAPQQTPSPQAAPQPQQVAQPLPVQPPPLVQPQYQSPQQPLQPRWVAPRNRNAAFGQSGGANSDSNSVGNAQPTSAPSVESHPVLEKLKAAHSYNPKEFDWNLKSGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDGAFRSMSSKGPVYLLFSVNGSGHFCGVAEMKSPVDYGTSAGVWSQDKWKGKFDVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIASYKHTTSIFDDFSHYEKRQEEEEVVRKERQNRNKQ