wanglab/gogpt-training-data huggingface dataset:
Protein: Ral GTPase-activating protein subunit alpha-2 (250 kDa substrate of Akt) (AS250) (p220) (Q2PPJ7)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16490346}.
Interaction partners:
- Ral GTPase-activating protein subunit beta
- Ras-related protein Ral-A
- NF-kappa-B inhibitor-interacting Ras-like protein 2
- RAC-beta serine/threonine-protein kinase
- Glucose-fructose oxidoreductase domain-containing protein 1
Sequence:
MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDANDLKQFFETNYSQIYFIFYENFIALENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVMSSRGPCTLETLINPSPSVADVKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLDIPHLRPKPVYITTTRDNENIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAVQERAPELDGGGPTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRMVYEMVQRILLSTRGYVNFVNEVFHQAFLLPSCEIAVTRKVVQVYRKWILQDKPVFMEEPDRKDVAQEDAEKLGFSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEENTNVKAGVQALLQVFLTNSANIFLLEPCAEVPVLLKEQVDACKAVLIIFRRMIMELTMNKKTWEQMLQILLRITEAVMQKPKDKQIKDLFAQSLAGLLFRTLMVAWIRANLCVYISRELWDDFLGVLSSLTEWEELINEWANIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCVLDPQKGTTVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNIVRQKATEVEECQQSENAPAAGSGHLTVGQQQQVLRSSSTSDIPEPLCSDSSQGQKAENTQNSSSSEPQPIQENKGHVKREHEGITILVRRSSSPAELDLKDDLQQTQGKCRERQKSESTNSDTTLGCTNEAELSMGPWQTCEEDPELNTPTDVVADADARHWLQLSPTDASNLTDSSECLTDDCSIIAGGSLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHARVFCYLYELWYKLAKIRDNLAISLDNQSSPSPPVLIPPLRMFASWLFKAATLPNEYKEGKLQAYRLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDILNTIIRHCPPRFFSLGFPGFSMLVGDFITAAARVLSTDILTAPRSEAVTVLGSLVCFPNTYQEIPLLQSVPEVNEAITGTEDVKHYLINILLKNATEEPNEYARCIAVCSLGVWICEELAQCTSHPQVKEAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETSLPRKMAEILVATVAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSVLLHPVSTAVLEEQHSARAPLLDYIYRVLHCCVCGSSTYTQQSHYILTLADLSSTDYDPFLPLANVKSSEPVQYHSSAELGNLLTVEEEKKRRSLELIPLTARMVMAHLVNHLGHYPLSGGPAILHSLVSENHDNAHVEGSELSFEVFRSPNLQLFVFNDSTLISYLQTPTEGPVGGSPVGSLSDVRVIVRDISGKYSWDGKVLYGPLEGCLAPNGRNPSFLISSWHRDTFGPQKDSSQVEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSLTPCGMNYDQEKEIIEVILRQNAQEDEYIQSHNFDSAMKVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILSNERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFIAITKKPEVPFFGPLFDGAIVSGKLLPSLVCATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTD
Protein: Indolethylamine N-methyltransferase (Indolamine N-methyltransferase) (EC 2.1.1.49) (EC 2.1.1.96) (Aromatic alkylamine N-methyltransferase) (Amine N-methyltransferase) (Arylamine N-methyltransferase) (Thioether S-methyltransferase) (TEMT) (P40936)
Organism: Mus musculus (Mouse)
Function: Catalyzes the N-methylation of tryptamine and structurally related compounds (By similarity). Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:3350800}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Indoleamine 2,3-dioxygenase 2
- Amine oxidase [flavin-containing] A
- Aromatic-L-amino-acid decarboxylase
- Diamine oxidase [copper-containing]
- Indoleamine 2,3-dioxygenase 1
- Serotonin N-acetyltransferase
- Amine oxidase
- Amine oxidase
- Amine oxidase
Sequence:
MEGKVYIGGEDYEKEFTPKDYLTTYYSFHSGPVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFREIIVTDYTPQNLQELQKWLKKEPGAYDWSSIVQHACELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGSAQVPLADCVLTFLAMECACPDIDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKEVVEKAIQDAGCQVLKCNCVSLSYSEAYCSHDGLCFVVARKGPSA
Protein: GTP binding protein (O44026)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MRNINLVVLGDGGVGKSSLIIQYVRNRFVVKYEATIEDVYQKAVEVDAQPTVLTIVDTSGQDVFGGMRYKYIRKCHGVILVYSVIDAESFSHIKAIHTQLCRARGSPSIPCVLVGNKVDEVKHRAVSSEEASKFAAQFMYPLLEVTAKDHSMAAAVFETLVRSIRGEESWLECRSPNVIFPPAATISEVRDEVHQLELPSVDLVDEHEEESPGIANRKKKSGCTML
Protein: Cilia- and flagella-associated protein 36 (Coiled-coil domain-containing protein 104) (Q95Y36)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:27930654}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:27930654}. Note=Localizes to the base of the cilium. {ECO:0000269|PubMed:27930654}.
Interaction partners:
- ADP-ribosylation factor-like protein 3
- ADP-ribosylation factor-like protein 13B
- Protein fam-161
- Protein rpi-1
- Protein maph-9
Sequence:
MLRRFSKKNKNPEGGSDDASRKQKKLLSKFLEFITSSIWSIPIASFIESQSVVFDRQQMETDVYIMIHKEYSQLIDTLIECFCEDVGTTPTELVAAIQLFNQKDVSQQYKVALEPLLAAQNFNVFVPMMMRKNIELQLQALQMIEFMCGLIPSVLQLEDGETLRNMKKLSPEETERYVLISVLRHSKDEYDSMQKGSEELEMMAQNSRIQREALEQEIRKEEILLQQALDEGARAQNQNQNQGTSSTQTDGVNAPLRSVAAMMAATFAIDTATSTDDVTYKFLDQSTGTMTSSTGVSVGTLTNTGVSSGTMTSGVDTGTDADGTVGRPKSAKRVGSAVGKRSVSKGTPSEDAKKSSGSSSPDEAEKSKRERPGTSVKKAIGIVAANSEMSSNGTQMDVPVDEEGTKKRPGTTSKKSIATVTASPEMSSKTTQMEPEQDGEGKKRPETSKGANERKYSNAGLEDIVGPKSSPHEEKKSSHPSSRKGSKATDENAPATRPPSRKAAGGSHEPRAKTPNQKNKDERPTTRRSSVDKNAPKRNDSVPRERKSSVSHDESKPPKPIGPLRGNKYDGDVVLGRAESPGIDHGPRRKNLNDVNSHLVDTNRLNSSDVRVRAQYLREQRDKLLQMKNAERIKQMTDIQQNASLERPKTAARAREILDKDKKEAVAIRKEISDKLKTQILTLHH
Protein: Protein tolkin (EC 3.4.24.-) (Tolloid-related protein) (Tolloid-related protein 1) (Q9VC47)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000269|PubMed:12537569, ECO:0000269|PubMed:15872004, ECO:0000269|PubMed:17119021}. Perikaryon {ECO:0000269|PubMed:32994163}. Cell projection, axon {ECO:0000269|PubMed:32994163}.
Interaction partners:
- Dorsal-ventral patterning protein Sog
- Dorsal-ventral patterning protein tolloid
- Uncharacterized protein, isoform B
Sequence:
MRRRRGTPLGVSWTNCVLLLATGLLVVLISVHAKNPRPHRGLPAPAPAPVPASVDQVATENAHRREPTVDGSVLQRLSGSDRAVDEDEDVDEDEDEGLKHQHLEHRQQFDAYLGTIRRLRRPYRSKYTIEQLMRLHVTPKVSGDIDMDPCKAGGFMGDIALPEGDSGPVVAHTPIDDEEQERQEVEQLLADSPSPVHDPPSVSGAANSGPTKFNATFQLDLEKLKQEVYHEGLQVEEEGLTDIIRKKTKLPSSGPVNLKAGQSQSQSQSANEPVKPGSESPSDYAQASSYKNEVLPPSEQRIHTDKPARLTLAEIGPKFSNKTQSLHRNVDTRKIQSDNKDIEDDSGNNFVAERRPSQIVPTSLPEQRSTPAHVYSNAGGNGMQLDDEVDFLHSRGVVRRRHRRGPKQRRSNQHLEHEVKLQRLREELSRPVIEAHHHQSHHQKQAQHRQHHQSHHRKKHRRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVPEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEMKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFDVVCGGELSVDDAVGRLESPNYPLDYLPNKECVWKITVPESYQVALKFQSFEVENHDSCVYDYVEVRDGPGQDAPLIGVFCGYKPPPNMKSSGNSMYVKFVSDTSVQKAGFSAVFMKEVDECETQNHGCEHECINTLGGYECSCRIGFELHSDKKHCEDACGGVIEYPNGTITSPSFPEMYPLLKECIWEIVAPPKHRISLNFTHFDLEGTAHQQSDCGYDSVTVYSKLGENRLKRIGTFCGSSIPPTATSESNALRLEFHSDKSIQRSGFAAVFFTDIDECAVNNGGCQHECRNTIGSYICMCHNGYSMHENGHDCKEGECKYEISAPFGTIFSPNYPDSYPPNADCVWHFITTPGHRIKLIFNEFDVESHQECTYDNVAVYDGESESSSVLGRFCGDKIPFPISSTSNQMYMVLKTDKNKQKNGFTASHSTACGGYLRATSQVQQFYSHARFGNQDYDDGMDCEWTIAAPDNSYVQLIFLTFDIESSENCTFDYVQVFSDIDDVYGQYGPMYGQYCGNVLPQDINSMTHSLLVRFKTDGSVPMKGFSASYVAVPNSGEYDHSDEDVENSYSSEMVTPFPGSLKSIYIEDTQEETDEYSDFSGNQLVFNGQYRGRYSLPKRYYSGKA
Protein: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa) (GlcNAc-T IVa) (GnT-IVa) (N-acetylglucosaminyltransferase IVa) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa) [Cleaved into: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form] (Q9UM21)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity).
Subcellular location: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9D4R2}.; SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]: Secreted {ECO:0000250|UniProtKB:O77836}.
Interaction partners:
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
- Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Solute carrier family 2, facilitated glucose transporter member 2
Sequence:
MRLRNGTVATALAFITSFLTLSWYTTWQNGKEKLIAYQREFLALKERLRIAEHRISQRSSELNTIVQQFKRVGAETNGSKDALNKFSDNTLKLLKELTSKKSLQVPSIYYHLPHLLKNEGSLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGETDIDYVHGVVANLEKEFSKEISSGLVEVISPPESYYPDLTNLKETFGDSKERVRWRTKQNLDYCFLMMYAQEKGIYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMFQAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQHVGLHSSLSGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWAITPIAGDYILFKFDKPVNVESYLFHSGNQEHPGDILLNTTVEVLPFKSEGLEISKETKDKRLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKATN
Protein: Fc of IgG low affinity IIIa receptor isoform 1 (A0A1W2PQB1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MGGGAGERLFTSSCLVGLVPLGLRISLVTCPLQCGIMWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK
Protein: C3H1-type domain-containing protein (Q388B6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEYPAEFHTPSTVYQEGCTTSPSPTPMFPKVSNLVTGIWERPSESHDAGCLKDYAVREMRDATQSNAQPTSVPSPRCTSNVNDGFRIPPYDTFLPTCDKERSQISAPTVDGVSINALSSLFSSEPILAENTVPSGDWDVFFPLRECWNSSSRPPTPTIPLGVCANITDTPPKLHLSNAIGEVCPQSADMQRPFFSLEEDTESEEVCALPVNFGTTYCSEGNIVEALIAQLAANGDSVVPTSINKVYAPQGQRTSSAMSSFQEGTVRNAKRGAAVSDPLAAHLLDNTTDIYEGVAGRHVAATAVCEGQQRHVPPFAICCSPIDLPGVGNGRAMNERHRGFIQHRQRGADTASRSGKGGLAPGSWHLGRRPLYSLPFPLVDHSMLSDLYRDTPQDQELRRIINSNGPGGPLMSSEWPPRTKSCVVKMLRQLHAKVLLQHLRVVSFARRDLYGVVRLFDSWNGKGIPPPGVMFGSYYFYTMSKFGREMCLKHNGRERAGGFCRGCDYAQRGPNFRCRYQHACLFCLSDDHGWFDETCCQRYVALQQKMVELRITDAVAQALLDALETEDEPIRRKG
Protein: Protein NrfC (P0AAK7)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes.
Interaction partners:
- Protein NrfD
- Cytochrome c-type protein NrfB
- Cytochrome c-552
- Probable cytochrome c-type biogenesis protein NrfE
- Formate-dependent nitrite reductase complex subunit NrfG
- Formate-dependent nitrite reductase complex subunit NrfF
- Ferredoxin-type protein NapG
- Formate dehydrogenase, nitrate-inducible, major subunit
- Formate dehydrogenase, nitrate-inducible, cytochrome b556
- Formate dehydrogenase-O major subunit
Sequence:
MTWSRRQFLTGVGVLAAVSGTAGRVVAKTLNINGVRYGMVHDESLCIGCTACMDACREVNKVPEGVSRLTIIRSEPQGEFPDVKYRFFRKSCQHCDHAPCVDVCPTGASFRDAASGIVDVNPDLCVGCQYCIAACPYRVRFIHPVTKTADKCDFCRKTNLQAGKLPACVEACPTKALTFGNLDDPNSEISQLLRQKPTYRYKLALGTKPKLYRVPFKYGEVSQ
Protein: Cholesteryl ester transfer protein (Lipid transfer protein I) (P47896)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL. Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:24293641, ECO:0000303|PubMed:1931878}. Note=Secreted in plasma. {ECO:0000303|PubMed:1931878}.
Interaction partners:
- Apolipoprotein B-100
- Apolipoprotein F
- Apolipoprotein E
- Phosphatidylcholine-sterol acyltransferase
- Hepatic triacylglycerol lipase
- P-type phospholipid transporter
- Apolipoprotein C-III
- Apolipoprotein A-II
- Apolipoprotein D
- Apolipoprotein C-I, basic form
Sequence:
MLAATVLTLALLGNVHACSKGTSHKAGIVCRITKPALLVLNQETAKVIQSAFQRANYPNITGEKAMMLLGQVKYGLHNIQISHLSIASSRVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWGLGIDQSVDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINIISNIMADFVQTRAASILSDGDIGVDISLTGDPIITASYLESHHKGYFIYKNVSEDLPLPTFSPALLGDSRMLYFWFSEQVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPRISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIMTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESVQSFLQSMITTVGIPEVMSRLEAVFTALMNSKGLSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS
Protein: Dipeptidyl aminopeptidase BI (DAP BI) (EC 3.4.14.-) (O07834)
Organism: Pseudoxanthomonas mexicana
Function: Sequentially removes dipeptide units (NH3-P2-P1-) from the amino termini of peptides and proteins. Is able to catalyze the removal of Asp-Arg from the amino termini of angiotensins I and II. Has slight endopeptidase activity on N-terminally blocked peptide derivatives which contain arginine residues at the P1 position. Does not hydrolyze Ala-Ala-Ala and Ala-Ala-Ala-Ala substrates or isulin beta chain.
Interaction partners:
Sequence:
MKPTSLLLAATVLMSTPITSALAASATPPDVAKKPHVVKAPHGAERNDEYYWLRDDKRENKEMLAYLNAENAYTDAVMAPLKPLEDKLYDEVVARIKQDDASVPYRERGWWYYARFVTGKDYPVHARRKDGPGVDAVSIQAANAAGDFAGEQVLLDVNALGAGKDYYNVGDYEVSQDNRLLAYADDTNGRRQYTIRFKNLDTGELLPDTVTNAEPNLVWSDDGRTLFYVDKDPETLLSKRVKAHVLGTPASQDALVYEEEDDSFYMGIGRSRDDKFICISVESTVSSEMRCTPAASPGVFTVLAPRERDVEYQADHLGDRWVIRTNADGATNFKIVTAPTDSTSRKDWKDWVAHRDDVFVEGFELFDGFSVVAERANALESLRVIKADGSSDYVKADESAYSMGLSANPETGTDWLRYSYTSMTTPATTYEINTKTGERRQLKQQPVPGYDASKYVTERVWAPARDGKTKIPVTLVYRKDVARDGKAPMLQYAYGSYGASMDPNFSITNVSLLDRGVVYALAHIRGGQEMGRAWYDDGKLYNKINTFTDFIDVTDYLVKEGYAAKDRVAAMGGSAGGLLMGAVSNMAPEKYKVILTLVPFVDVVTTMLDPTIPLTTNEYDEWGNPEEKGYYDYILTYSPYDNLQAKAYPAMFVGTGLWDSQVQYWEPAKYVARLRDLNTGKGPVVFRTNMEAGHGGKSGRFRQYRERAEMFAFMLDQLGVASK
Protein: Tumor protein p53-inducible nuclear protein 1 (Stress-induced protein) (Thymus-expressed acidic protein) (TEAP) (p53-dependent damage-inducible nuclear protein 1) (p53DINP1) (Q9QXE4)
Organism: Mus musculus (Mouse)
Function: Antiproliferative and proapoptotic protein involved in cell stress response which acts as a dual regulator of transcription and autophagy. Acts as a positive regulator of autophagy. In response to cellular stress or activation of autophagy, relocates to autophagosomes where it interacts with autophagosome-associated proteins GABARAP, GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and plays a major role in p53/TP53-driven oxidative stress response. Possesses both a p53/TP53-independent intracellular reactive oxygen species (ROS) regulatory function and a p53/TP53-dependent transcription regulatory function. Positively regulates p53/TP53 and p73/TP73 and stimulates their capacity to induce apoptosis and regulate cell cycle. In response to double-strand DNA breaks, promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor suppressor by inducing cell death by an autophagy and caspase-dependent mechanism. Can reduce cell migration by regulating the expression of SPARC.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11557757}. Nucleus, PML body {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Cellular tumor antigen p53
- Homeodomain-interacting protein kinase 2
Sequence:
MFQRLNKMFVGEVTTSSSQEPEFSEKEDDEWILVDFIDTCPGFSAEEEEEDEDIGEESSAEHTSVFSCLPASLECLTDTSDSCFLQFESCPMEESWFITPPPCFTAGGLTTIKVETSPMENLLIEHPSMSVYAVHNSCPGLSEASCGNDEYNSSGPRMEAQSEMGKHIHCCVAALAAQATFLEQPKSFRPSQWIKGHSERQSLNRNGLRRQNLTRDCHTRQMKHSGWVVHQPCPRQYNY
Protein: Ubiquitin-conjugating enzyme E2 2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 2) (Lethal protein 70) (Ubiquitin carrier protein 2) (Ubiquitin-protein ligase 2) (P35129)
Organism: Caenorhabditis elegans
Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Mediates the selective degradation of short-lived and abnormal proteins. Plays a role in the DNA damage response. In particular, in response to ionizing radiation, associates with the E3 ubiquitin-protein ligase brc-1-brd-1 heterodimer on chromatin to activate E3-ubiquitin ligase activity of the heterodimer, and thus its DNA damage repair mechanisms. Required, cell autonomously, for death of the linker cell, a male-specific cell which guides the elongation of the gonad; perhaps acting as part of the ubiquitin proteasome system (UPS) and modulated by heat shock transcription factor hsf-1.
Subcellular location: Nucleus {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:26952214}. Chromosome {ECO:0000269|PubMed:16628214}. Cytoplasm {ECO:0000269|PubMed:26952214}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- E1 ubiquitin-activating enzyme
- Polyubiquitin-A
- Ubiquitin thioesterase otubain-like
- Anaphase-promoting complex subunit 11
- Ubiquitin-conjugating enzyme E2 variant 1
- RING-box protein 1
- Ubiquitin conjugation factor E4 ufd-2
- Probable glutaryl-CoA dehydrogenase, mitochondrial
- UBiquitin Conjugating enzyme
Sequence:
MALKRIQKELQDLGRDPPAQCSAGPVGDDLFHWQATIMGPPESPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRERYNQLAREWTQKYAM
Protein: EGF-like repeat and discoidin I-like domain-containing protein 3 (Developmentally-regulated endothelial cell locus 1 protein) (Integrin-binding protein DEL1) (O35474)
Organism: Mus musculus (Mouse)
Function: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.
Subcellular location: Secreted.
Interaction partners:
- Hephaestin
- Ceruloplasmin
Sequence:
MKHLVAAWLLVGLSLGVPQFGKGDICNPNPCENGGICLSGLADDSFSCECPEGFAGPNCSSVVEVASDEEKPTSAGPCIPNPCHNGGTCEISEAYRGDTFIGYVCKCPRGFNGIHCQHNINECEAEPCRNGGICTDLVANYSCECPGEFMGRNCQYKCSGPLGIEGGIISNQQITASSTHRALFGLQKWYPYYARLNKKGLINAWTAAENDRWPWIQINLQRKMRVTGVITQGAKRIGSPEYIKSYKIAYSNDGKTWAMYKVKGTNEEMVFRGNVDNNTPYANSFTPPIKAQYVRLYPQICRRHCTLRMELLGCELSGCSEPLGMKSGHIQDYQITASSVFRTLNMDMFTWEPRKARLDKQGKVNAWTSGHNDQSQWLQVDLLVPTKVTGIITQGAKDFGHVQFVGSYKLAYSNDGEHWMVHQDEKQRKDKVFQGNFDNDTHRKNVIDPPIYARFIRILPWSWYGRITLRSELLGCAEEE
Protein: Zinc transporter ZIP2 (Solute carrier family 39 member 2) (Zrt- and Irt-like protein 2) (ZIP-2) (hZIP2) (G3X943)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NP94}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Zinc transporter ZIP4
- Zinc transporter ZIP11
- Zinc transporter SLC39A7
- Zinc transporter ZIP9
- Zinc transporter ZIP12
- Zinc transporter 6
- Probable ATP-dependent DNA helicase HFM1
Sequence:
MEVLLGVKIGCLLALLVLTLGCGLTPIYVKWFQMDAATGHHHRVLSLLGCTSAGVFLGAGLMHMTAEALEGIESEIQKFVEQNSTGSKGNSSRDAASSYVEYPYGELVISLGFFFVFLLESLALQCCHGAAGGSTVQEEEWGGTHAFGFHKHPAVPSPSRGPLRALVLLLSLSFHSVFEGLAVGLQATVAATIQLCVAVLAHKGLVVFSVGLRLGKIGTGPRWATFCILSLALMSPVGLALGLTVAGGASGQTQGLAQAVLEGIAAGTFLYVTFLEILPRELACPEAPLAKYSCVAAGFAFMALIALWA
Protein: Kinesin family member 1B (Kinesin-like protein KIF1B isoform X17) (Kinesin-like protein KIF1B isoform X22) (E9QDE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSGASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNPKEPKTFSFDYSYWSHTSPDDPSFASQNQVYNDIGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEGQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKDEVSRLKELLRAQGLGDILDTPMGCLTASPSSGSLCSQAGLQSVSSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNGKRVNSAVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPVEPVDWTFAQRELLEKQGIDMKQEMEKRLTEMEILYKKEKEEADQLLEQQRLVYESKLQELQKQVETRSLAAETPDEEEEEEEEDEVPWTQHKYELAQWAFRKWRYHQFTSLRDQLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPLPPELLPPEPEKERDARPFPRTVVAVEVQDLKNGATHYWSLEKLKQRLDQMREMYDRAGEMASSNQGDDGEGALTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTTDSEITELADERQSEMEDFMDDEAFVDDTSSDAGTEEGSDIFSDGQDPFYDRSPWFILVGRAFVYLSNLLYPVPLVHRVAVVTEKGDVRGFLRVGVQAIAADEEAPDYGSGVRQSGTAKISFDNEYFKKNDFTSVAMTRSGLSLEELRIVEGQGQSSEVITPSEEMNRINEMDLKLGNVDTKLGDGLAEHLEVGSIFTFRVTVLQASGIPAEYADIFCQFNFLHRHDEAFSTEPLKNTGRGAPLGFYHVQNISVEVTESFIEYIKTKPIVFEVFGHYQQHPLHIHGQDVVSPSQPSRKYYPPPMPLSKPVPATKLNTITKSNLGQCVSKYDLLAWFEISELEPTGEYIPAVVDHTGGLPCHGTYLLHQGIQRRITVTLIHEKGSELHWKDVRELVVGRIRNKPEVDDSAADAVLSLNIISAKNLKSSHNSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAIITKDICMVFYSRDAKISPPRSLRNLFGSGYSKTPDCNKVTGVYELSLCKIADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELDKMEQLHEVEKTRHLLLLREKLGETPPPKSLSESLSPSLSSGTLSTSTSISSQISSTTFESAITPSESSGYDSTDIESLVDREKELATKCLRLLTHTFNSEYNQMCNSISDCKFSDISPMGRDPSVSSFSSATLTPSSTCPSLSDSRTPEANSRATSPSGSDYENFPMVPILETSYLARAGKHEFLNLVPNIEEMRPGSVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQAMLKTPHTFAMCTKHRGILLQANNDKDMNDWLYAFNPLLAGTIRSKLARRRSGVMKN
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (K7ESH9)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKVCAIEWLIYKKHIFT
Protein: Transcription initiation factor IIB (EC 2.3.1.48) (General transcription factor TFIIB) (B1APE1)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECGLVVGDRVIDVGSEWRTFSNDKATKDPSRVGDSQNPLLSDGDLSTMIGKGTGAASFDEFGNSKYQNRRTMSSSDRAMMNAFKEITTMADRINLPRNIVDRTNNLFKQVYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVDLITTGDFMSRNWRYCWCC
Protein: Syntaxin-8 (SNARE protein related to mammalian syntaxin 8) (ULP1-interacting protein 2) (P31377)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: t-SNARE which may play a role in determining the specificity of membrane fusion, protein transport and vesicle trafficking within the Golgi/endosomal and plasma membrane/endosomal systems.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:12453154}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12453154}.
Interaction partners:
- t-SNARE VTI1
- Vacuolar v-SNARE NYV1
- Syntaxin PEP12
- Syntaxin VAM3
- Synaptobrevin homolog YKT6
- t-SNARE affecting a late Golgi compartment protein 1
- Synaptobrevin homolog 2
- t-SNARE affecting a late Golgi compartment protein 2
- Vacuolar morphogenesis protein 7
- Protein SSO1
Sequence:
MDVLKLGYELDQLSDLVEERTRLVSVLKLAPTSNDNVTLKRQLGSILELLQKCAPNDELISRYNTILDKIPDTAVDKELYRFQQQVARNTDEVSKESLKKVRFKNDDELTVMYKDDDEQDEESPLPSTHTPYKDEPLQSQLQSQSQPQPPQPMVSNQELFINQQQQLLEQDSHLGALSQSIGRTHDISLDLNNEIVSQNDSLLVDLENLIDNNGRNLNRASRSMHGFNNSRFKDNGNCVIILVLIVVLLLLLLVL