wanglab/gogpt-training-data huggingface dataset:
Protein: Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase) (Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein) (Q06489)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Methylthioribulose-1-phosphate dehydratase
- S-methyl-5'-thioadenosine phosphorylase
- Enolase-phosphatase E1
- Acireductone dioxygenase-requiring))
- Polyol phosphate phosphatase PYP1
- Uncharacterized membrane protein YLR326W
- Purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase 1
Sequence:
MSLEAIVFDRSEPENVSVKVLDQLLLPYTTKYVPIHTIDDGYSVIKSMQVRGAPAIAIVGSLSVLTEVQLIKHNPTSDVATLYSLVNWESTKTVLNKRLDFLLSSRPTAVNLSNSLVEIKNILKSSSDLKAFDGSLYNYVCELIDEDLANNMKMGDNGAKYLIDVLQKDGFKDEFAVLTICNTGSLATSGYGTALGVIRSLWKDSLAKTDKADSGLDNEKCPRMGHVFPLETRPYNQGSRLTAYELVYDKIPSTLITDSSIAYRIRTSPIPIKAAFVGADRIVRNGDTANKIGTLQLAVICKQFGIKFFVVAPKTTIDNVTETGDDIIVEERNPEEFKVVTGTVINPENGSLILNESGEPITGKVGIAPLEINVWNPAFDITPHELIDGIITEEGVFTKNSSGEFQLESLF
Protein: Torsin-1A-interacting protein 1 (H0Y4R4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00037876}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037876}.
Interaction partners:
Sequence:
XKTTRSSSQYIESFWQSSQSQNFTAHDKQPSVLSSGYQKTPQEWAPQTARIRTRMQKVTGQPQNASFVKRNRWWLLPLIAALASGSFWFFSTPEVETTAVQEFQNQMNQLKNKYQGQDEKLWKRSQTFLEKHLNSSHPRSQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVRAIRIDGTDKATQDSDTVKLEVDQELSNGFKNGQNAAVVHRFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLGTSLGLKEVEEKVRDFLKVKFTNSNTPNSYNHMDPDKLNGLW
Protein: Casein kinase II subunit alpha 3 (CK II alpha 3) (EC 2.7.11.1) (Casein kinase II alpha 1 polypeptide pseudogene) (Q8NEV1)
Organism: Homo sapiens (Human)
Function: Probable catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Amplification-dependent oncogene; promotes cell proliferation and tumorigenesis by down-regulating expression of the tumor suppressor protein, PML. May play a role in the pathogenesis of the lung cancer development and progression.
Interaction partners:
- Casein kinase II subunit beta
- Catenin beta-1
- Segment polarity protein dishevelled homolog DVL-1
- FUN14 domain-containing protein 1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Major prion protein
- NF-kappa-B inhibitor alpha
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-2
- Casein kinase II subunit alpha'
Sequence:
MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWRLGCMLASMIFRKEPFFHGRDNYDQLVRIAKFLGTEDLYGYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANVMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAATGAQQ
Protein: Scarecrow-like protein 33 (AtSCL33) (GRAS family protein 12) (AtGRAS-12) (P0C883)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGSYSAGFPGSLDWFDFPGLGNGSYLNDQPLLDIGSVPPPLDPYPQQNLASADADFSDSVLKYISQVLMEEDMEDKPCMFHDALSLQAAEKSLYEALGEKYPVDDSDQPLTTTTSLAQLVSSPGGSSYASSTTTTSSDSQWSFDCLENNRPSSWLQTPIPSNFIFQSTSTRASSGNAVFGSSFSGDLVSNMFNDTDLALQFKKGMEEASKFLPKSSQLVIDNSVPNRLTGKKSHWREEEHLTEERSKKQSAIYVDETDELTDMFDNILIFGEAKEQPVCILNESFPKEPAKASTFSKSPKGEKPEASGNSYTKETPDLRTMLVSCAQAVSINDRRTADELLSRIRQHSSSYGDGTERLAHYFANSLEARLAGIGTQVYTALSSKKTSTSDMLKAYQTYISVCPFKKIAIIFANHSIMRLASSANAKTIHIIDFGISDGFQWPSLIHRLAWRRGSSCKLRITGIELPQRGFRPAEGVIETGRRLAKYCQKFNIPFEYNAIAQKWESIKLEDLKLKEGEFVAVNSLFRFRNLLDETVAVHSPRDTVLKLIRKIKPDVFIPGILSGSYNAPFFVTRFREVLFHYSSLFDMCDTNLTREDPMRVMFEKEFYGREIMNVVACEGTERVERPESYKQWQARAMRAGFRQIPLEKELVQKLKLMVESGYKPKEFDVDQDCHWLLQGWKGRIVYGSSIWVPL
Protein: Bifunctional protein FolD [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] (P54382)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Interaction partners:
- Serine hydroxymethyltransferase
- Transcription antitermination protein NusB
- Methionyl-tRNA formyltransferase
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthesis protein PurH
- Aminomethyltransferase
- Exodeoxyribonuclease 7 large subunit
- Phosphoribosylamine--glycine ligase
- Formyltetrahydrofolate deformylase
- Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase
Sequence:
MTATIIDGKETAREKREQLAKEVEELKKQGVTPGLAVILIGDDPASHSYVRGKKKAAETMGMNFKLDQFDSSLTEAELLSIIDQYNQDPEFHGILVQLPLPDHISEKAVIERISPDKDVDGFHPLNVGKMLLGEDTFLPCTPHGIVELLKKTNIDLSGKEVVVVGRSNIVGKPVGQLLLNENATVTYCHSRTENITEHTKKADILVVAVGRANFISADQIKEGAVVIDVGVNRLENGKLCGDVEFEGAKEKASFITPVPGGVGPMTITMLAHNTVKSAKRTLS
Protein: Multiple C2 and transmembrane domain-containing protein 1 (D4ABL6)
Organism: Rattus norvegicus (Rat)
Function: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (By similarity). Overexpression in cultured neurons significantly inhibits neuronal transferrin endocytosis, secretory vesicle retrieval, cell migration, and oxidative stress from glutamate toxicity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:26195140}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:26195140}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A1ZBD6}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 11
Sequence:
MEPRGAAAGEPEPAVSPSFQARLWKNLQLGVGKGKGGGGGRAGGPERRTAATPTPSLPPPKTTQDVGSTGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRLREHLLPVAKGSSTAAGTVGVTPPGGRSPDSAPSSSASSSLSSSPQPPPRGDRIRDEGTRRGSPEAHLCHQKSSSLPGTACLEQLLEPAPPPAEPARRPAEPQSLQKGEELDCSQKINPVETSNADVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGRKEVFRSKIIHKNLNPVWEEKACVLIDHLREPLYIKVFDYDFGLQDDFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGEPRDVTMLMRKSWKRSSKFQTQSLRLSDQHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTLNPQWREQFDFHLYEERGGVMDITAWDKDAGKRDDFIGRCQVDLSSLSREQTHKLELQLEEGEGHLVLLVTLTASATVSISDLSVNSMEDHKEREEILKRYSPLRIFNNIKDVGFLQVKVIRAEGLMAADVTGKSDPFCVVELNNDRLLTHTVYKNLNPEWNKVFTFNIKDIHSVLEVTVYDEDRDRSADFLGRVAIPLLSIQNGEQKAYVLKNKQLTGPTKGVIHLEIDVIFNAVKASLRTLIPKERKYIEEENRLSKQLLLRNFIRTKRCVMVLVNAAYYVNSCFDWDSPPRSLAAFVLFLLVVWNFELYMIPLLLLLLLTWNYFLIISGKDNRQRDTVVEDMLEDEEEEDDRDDKDGEKKGFINKIYAIQEVCVSVQNILDEAASLGERVKNTFNWTVPFLSWLAIIALCVFTAILYFIPLRYIVLVWGINKFTKKLRSPYAIDNNELLDFLSRVPSDVQVVQYQELKPDHSHSPYKRKKNNLG
Protein: Rho GTPase-activating protein 10 (GTPase regulator associated with focal adhesion kinase 2) (GRAF2) (Graf-related protein 2) (Rho-type GTPase-activating protein 10) (A1A4S6)
Organism: Homo sapiens (Human)
Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:32344433}. Note=Association to cell membrane is dependent on PH domain. Colocalized with MICAL1, RAB8A, RAB8B and RAB10 on endosomal tubules (PubMed:32344433). {ECO:0000250, ECO:0000269|PubMed:32344433}.
Interaction partners:
- Serine/threonine-protein kinase PAK 2
- Serine/threonine-protein kinase N3
- Transforming protein RhoA
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Catenin beta-1
- Rho GTPase-activating protein 26
- C2 domain-containing protein 2
- Cell division control protein 42 homolog
Sequence:
MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHLQEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFFLKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQNIVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDSLSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATVADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
Protein: Uncharacterized membrane protein YoaK (C1P602)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Single-pass membrane protein {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}. Note=May be able to insert into the membrane in both orientations. Relies on YidC for insertion.
Interaction partners:
- Uncharacterized protein YoaJ
- Diguanylate cyclase DgcP
- Uncharacterized protein YshB
- Uncharacterized protein YqfG
- Uncharacterized membrane protein YpdK
Sequence:
MRIGIIFPVVIFITAVVFLAWFFIGGYAAPGA
Protein: AP-1 complex subunit mu-2 (AP-mu chain family member mu1B) (Adaptor protein complex AP-1 subunit mu-2) (Adaptor-related protein complex 1 subunit mu-2) (Clathrin assembly protein complex 1 mu-2 medium chain 2) (Golgi adaptor HA1/AP1 adaptin mu-2 subunit) (Mu-adaptin 2) (Mu1B-adaptin) (Q9WVP1)
Organism: Mus musculus (Mouse)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-1 complex subunit gamma-1
- AP-1 complex subunit gamma-like 2
- AP-1 complex subunit beta-1
- AP-1 complex subunit sigma-3
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit sigma-2
- AP-1 complex subunit mu-1
- AP-4 complex subunit beta-1
- Trans-Golgi network integral membrane protein 1
- AP-2 complex subunit beta
Sequence:
MSASAVFILDVKGKPLISRNYKGDVPMTEIDHFMPLLMQREEEGVLAPLLSHGRVHFLWIKHSNLYLVATTLKNANASLVYSFLYKTVEVFCEYFKELEEESIRDNFVIVYDLLDELMDFGFPQTTDSKILQEYITQQGNKLETGKSRVPPTVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGTIKLKVFLSGMPELRLGLNDRVLFELTGRSKNKSVELEDVKFHQCVRLSRFDNDRTISFIPPDGDFELMSYRLSTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANGVEISVPVPSDADSPRFKTSVGSAKYVPEKNVVIWSIKSFPGGKEYLMRAHFGLPSVETEEVEGRPPIGVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTS
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 2) (1-AGP acyltransferase 2) (1-AGPAT 2) (Lysophosphatidic acid acyltransferase beta) (LPAAT-beta) (Q8K3K7)
Organism: Mus musculus (Mouse)
Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15120}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Membrane-bound glycerophospholipid O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Lysocardiolipin acyltransferase 1
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 4
- Glycerol-3-phosphate acyltransferase 3
Sequence:
MDPWPWLTAALLLLLLLVQLSRTARFYAKVGLYCVLCLSFSAAASIVCLLRHGGRTVDNMSIISWFVRSFKYVYGLRFEVSGQKKLEVDGPCVIISNHQSILDMMGLMEILPKRCVQIAKRELMFTGPVGLIMYLGGVYFINRQQARTAMSVMADLGDLMVKENLKVWIYPEGTRNDNGDLLPFKKGAFYLAIQAQVPIIPVVYSSFSSFYNVKTKLFTSGTIKVQVLDAVPTNGLTDADVTKLVDTCYQSMRATFLQISQIPQENSAIKEPGVLPAQ
Protein: Brevinin-2Rb (P86023)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
GLMSTLKGAATNAAVTLLNKLQCKLTGTC
Protein: GCN5-related N-acetyltransferase 5, chloroplastic (EC 2.3.1.255) (EC 2.3.1.48) (Q9LR91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:32633465}.
Interaction partners:
- GCN5-related N-acetyltransferase 7, chloroplastic
- GCN5-related N-acetyltransferase 10, chloroplastic
- GCN5-related N-acetyltransferase 8
- GCN5-related N-acetyltransferase 4, chloroplastic
- Acyl-CoA N-acyltransferases
- GCN5-related N-acetyltransferase 1, chloroplastic
- GCN5-related N-acetyltransferase 9
- GCN5-related N-acetyltransferase 6, chloroplastic
- N-terminal acetyltransferase B complex catalytic subunit NAA20
- N-terminal acetyltransferase A complex catalytic subunit NAA10
Sequence:
MAALSISLAFSVDSLKPTQSTKFGFSSSSHRYPLLYSCKSHRSNLRFAFPPSSVSTATETGEENSKSTGNYAFLEESFRTGRFLSNDELEKLKTLEGFAYFQELESGSMWVRVMRHEEMDSTVHLLAESFGESMLLPSGYQSVLRFLIKQYLIERREVLPHAVTLVGFFRKKVDEFSDDGEEEAVMAGTVEVCLEKRGANASPPSPTPPKESPYICNMTVKEDLRRRGIGWHLLKASEELISQISPSKDVYLHCRMVDEAPFNMYKKAGYEVVKTDTVLVLLMLQRRKHLMRKKLLPLCTNPIVEMVGSDNELTSSANV
Protein: Short-chain dehydrogenase/reductase family protein (Q54FW2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- IWS1 family protein
- 4-hydroxyphenylpyruvate dioxygenase
- TNF receptor-associated protein 1 homolog, mitochondrial
- Strictosidine synthase family protein
Sequence:
MSQNDKKVFYITGASKGFGLELTNQLLERGFNVVATSRNKQQLSNSVNNKFVTNDNFLALQVDLTSNESVKNSIDETISKFTRIDVIINNAGYSQCGTIEELTDKEIRDNFECNVFGVISVIRNALPHLRINKFFANGPRIINISSIAGFTGSFPGFSIYSSTKFALEGLTEGLNEDLKEFGIHASTVLPGYFRTSFLEKGSVAVPSHPIKEYTAVRKIQEIHENQINGNQQGDPVKGCKVIIDHALSENPTTHLFLGPDSMKYAQSKIEAIQNDIKSNYDAASKTDFTN
Protein: Nuclear receptor subfamily 1 group H member 3 (cDNA FLJ56172, highly similar to Oxysterols receptor LXR-alpha) (B4DXU5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MQQTSWNPLGGTCKQPPGRTHSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPMAPDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Protein: L-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.2) (Q38A39)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Citrate synthase
Sequence:
MAKSFLKWTGGLVIAGGVYAKIKYKSAYEAVHLDEAATVRAFSTFSIDNRREFYDVAVVGGGIVGVATAREIKQRFPSKRVIMLEKEADVALHQSSHNSGVVHAGMYYKQNSLMARLCPRGHDLIMEYCRKNKLPLDRVGKLIVAVKETEIPAVENLYKQGVENGVRDLKMLRGEEEIKRVEPNVRGLCALYSPDTAITDFSAVARHMLKELLADRQRGFVAQFCYEALDFVGVSIQSSEGSKVTTPQEMVLIRGREGGQLGPEKTVMAKNVVMCCGLSNDLLAQRSGTPLSHIGRKVKQTFSFRGRYYQLRPEARKLVSMNVYPAPEEWKGISVGVHFTPTVDERRGRQVIIGPGSSVATHRYGYSPYCFDADYCFKSFFSKGGWVSLVSNIGTVFRMFVLDTNRQAFLREAQKLIPSLQDSDMEESFCGVMGVAVTPDGKMENDLAMEFSRPRVVVPAVLKPGKVVELVPKSDVASDGSAVNDRPLMLNVRNAPSPAATASMAIAEAIVDASAEQFRW
Protein: Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Insulin receptor-binding protein Grb-IR) (Q13322)
Organism: Homo sapiens (Human)
Function: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin-stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2.
Subcellular location: Cytoplasm {ECO:0000250}. Note=When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity). {ECO:0000250}.
Interaction partners:
- Insulin-like growth factor 1 receptor
- GRB10-interacting GYF protein 2
- Insulin receptor
- Insulin-like growth factor 1
- E3 ubiquitin-protein ligase NEDD4
- GRB10-interacting GYF protein 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Insulin
- Epidermal growth factor receptor
- Insulin receptor substrate 1
Sequence:
MALAGCPDSFLHHPYYQDKVEQTPRSQQDPAGPGLPAQSDRLANHQEDDVDLEALVNDMNASLESLYSACSMQSDTVPLLQNGQHARSQPRASGPPRSIQPQVSPRQRVQRSQPVHILAVRRLQEEDQQFRTSSLPAIPNPFPELCGPGSPPVLTPGSLPPSQAAAKQDVKVFSEDGTSKVVEILADMTARDLCQLLVYKSHCVDDNSWTLVEHHPHLGLERCLEDHELVVQVESTMASESKFLFRKNYAKYEFFKNPMNFFPEQMVTWCQQSNGSQTQLLQNFLNSSSCPEIQGFLHVKELGKKSWKKLYVCLRRSGLYCSTKGTSKEPRHLQLLADLEDSNIFSLIAGRKQYNAPTDHGLCIKPNKVRNETKELRLLCAEDEQTRTCWMTAFRLLKYGMLLYQNYRIPQQRKALLSPFSTPVRSVSENSLVAMDFSGQTGRVIENPAEAQSAALEEGHAWRKRSTRMNILGSQSPLHPSTLSTVIHRTQHWFHGRISREESHRIIKQQGLVDGLFLLRDSQSNPKAFVLTLCHHQKIKNFQILPCEDDGQTFFSLDDGNTKFSDLIQLVDFYQLNKGVLPCKLKHHCIRVAL
Protein: Methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase (MNO) (EC 1.1.99.37) (Methanol dehydrogenase (nicotinoprotein)) (Methanol:NDMA oxidoreductase) (Q9RCG0)
Organism: Amycolatopsis methanolica
Function: Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It can also use various other primary alcohols, polyols and formaldehyde. In addition, MNO is able to produce methylformate from methanol plus formaldehyde, and possesses a formaldehyde dismutase and a NADH-dependent formaldehyde reductase activity.
Interaction partners:
Sequence:
MQVDELLKPFPIKEFHPFPRALLGPGAHEMIGPEALKLGFKKTLVMTSGLRGSDIVHKITESMKYHGLEVVLYDKVESNPKDYNVMDAVKLYQENKCDSFVSIGGGSSHDACKGARISVAHDGRNVNDFEGFNKSENPRNPPHIAVSTTAGTGSETSWAYVITDTTTDPDNPHKYVAFDDASVATLAIDDPVLYYSCPIDYTAQCGFDVLAHASEPYVSRLNFEPSLGNALRAIKLTAENLRQATWNPSELSGREGMMYAQYIAAQAFNSGGLGIIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFADMAEAMGVDTHGMTDVQAADALAAAIRLLRDVGIPEKFTDVTQDSYSKNRLGQGPTKFYEQASVIKGDDEDVDRITNHVLGDACTPGNAKECTFETVRPVVDHCMNGDLDDLLS
Protein: Ethylene-response factor C3 (Sl.ERF.C.3) (Ethylene-responsive element-binding factor C3) (Ethylene-responsive transcription factor C3) (A0A3Q7I5Y9)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcription activator that binds to the GCC-box cis-acting elements found in the promoter regions of ethylene-responsive genes. Acts downstream of MYC2 in the jasmonate-mediated response to Botrytis cinerea infection. With MYC2 forms a transcription module that regulates pathogen-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
Interaction partners:
- EIL3
- Suberization-associated anionic peroxidase 1
Sequence:
MDYSSRDDLLFHYNSLPFNVNDTQDMLLYNLVAEGSSQETVNSSSSYGIKEEEVTSYEEERKDKNYRGVRKRPWGKYAAEIRDSTRNGVRVWLGTFDNAEEAALAYDQAAFAMRGSMAILNFPVEIVKESLNEMKCRFDGNCSPVIELKKRYSMRRKSVSRKNRARKDVVVFEDLGAEYLEELLISSESITNW
Protein: Ornithine decarboxylase antizyme 3 (AZ3) (ODC-Az 3) (A1BPI0)
Organism: Rattus norvegicus (Rat)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells (By similarity).
Subcellular location: [Isoform 1]: Nucleus {ECO:0000250|UniProtKB:Q9R109}. Cytoplasm {ECO:0000250|UniProtKB:Q9R109}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum {ECO:0000269|PubMed:21712390}.
Interaction partners:
- Ornithine decarboxylase
- Antizyme inhibitor 1
- Antizyme inhibitor 2
- Antizyme inhibitor 2
- Outer dense fiber protein 1
- Tubulin polymerization-promoting protein family member 2
- Uncharacterized protein CLBA1
- Gametogenetin-binding protein 2
Sequence:
MPCTRSRPSLYSLSYIKRGKTRNCLYPFWSPYAYYLYCYKYRITLREKMLPCCYRSITYKEQEDLTLRPHCCLPCSCLPYSCLPCSESLEGLQVGRSTAQEKDHSQLKELYSAGNLTVLSADPLLHQDPVQLDFHFRLTPHSSAHWHGLLCDHQLFLDIPFQALEQGNRESLTATLEYVEEKTNVDSVFVNFQSNHKDRGALLRAFSYMGFEVVRPDHPALPPWDNVIFMVYPLERDLGQPGQ