wanglab/gogpt-training-data huggingface dataset:
Protein: Aldehyde dehydrogenase family 3 member A2 (EC 1.2.1.3) (EC 1.2.1.94) (Aldehyde dehydrogenase 10) (Fatty aldehyde dehydrogenase) (Microsomal aldehyde dehydrogenase) (P51648)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of medium and long chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:9133646}; Single-pass membrane protein {ECO:0000305|PubMed:25047030, ECO:0000305|PubMed:9133646}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:9133646}; Single-pass membrane protein {ECO:0000305|PubMed:25047030, ECO:0000305|PubMed:9133646}; Cytoplasmic side {ECO:0000250|UniProtKB:P30839}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Peroxisomal bifunctional enzyme
- Aldo-keto reductase family 1 member B1
- Amine oxidase [flavin-containing] A
- Aldo-keto reductase family 1 member A1
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Alkylglycerol monooxygenase
- Aldo-keto reductase family 1 member B10
- 4-aminobutyrate aminotransferase, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
Sequence:
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLVKAEYY
Protein: Rhodomycin D methylesterase DauP (EC 3.1.1.-) (10-carbomethoxy-13-deoxycarminomycin esterase) (4-O-methylrhodomycin D methylesterase) (Q55217)
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. Catalyzes the removal of methyl group from the carbomethoxy group of rhodomycin D (10-carbomethoxy-13-deoxycarminomycin) and 4-O-methylrhodomycin D to yield 10-carboxy-13-deoxycarminomycin and 10-carboxy-13-deoxydaunorubicin, respectively. Could be also involved in the decarboxylation of 10-carboxy-13-deoxycarminomycin and 10-carboxy-13-deoxydaunorubicin to yield 13-deoxycarminomycin and 13-deoxydaunorubicin, respectively. It seems that DauK may influence the ability of DauP to carry out the decarboxylation.
Interaction partners:
Sequence:
MPTRMITKDEVTLWSEGIGDPADAPLLLIAGGNLSARSWPDEFVERLAAAGHFVIRYDHRDTGRSSRYDFALHPYGFDELATDALAVLDAWQVRAAHVVGMSLGNTIGQLLALDAPERLLTLTVMLGGALDVDFDADLEAALKGEPSVSGLPVPSRRFLDMMMLLQQPAGTDEELLERRVEKWRLLNGEGVPFDSDEFRRRELLAAGHAGTFDEPIVHHMIPQPPVSRGAELARITTPVLAIQAMCDPAAPPPHARHLADRIPGARVVEIENMGHALPLAVHEPLAAAICAHTRAATV
Protein: ETS domain-containing protein Elk-1 (A4GTP4)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2 (By similarity). Induces target gene transcription upon JNK-signaling pathway stimulation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P19419}.
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Serum response factor
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 12
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 13
Sequence:
MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSAVAMAPATVHSGPGDNATGKPGTPKGAGMTGQGGLARSSRNEYMRSGLYSTFTIQSLQPQPPLHPRPASVLPNTTPAGVPAPPSGSRSTSPNPLEACLEAEEAGLPLQVILTPPEAPNQKSEELSLNPGFGRPQPPEVKVEGPKEELEVTEVGGFSPEAVKAEQEVSPSEGLLARLPAILTENTAQVCGLSTSTTEITQPQKGRKPRDLELPLSPSLLGGQGPERTPGSGTSSGLQAQGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP
Protein: 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC 1.1.1.141) (EC 1.1.1.232) (Eicosanoid/docosanoid dehydrogenase [NAD(+)]) (Prostaglandin dehydrogenase 1) (G1TBB5)
Organism: Oryctolagus cuniculus (Rabbit)
Interaction partners:
Sequence:
MHVNGKVALVTGAAQGIGRAFAEALLHKGAKVALVDWNLEAGVKCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSMAGLMPVAQQPVYCASKHGIIGFTRSAAMAANLMNSGVRLNAICPAFVNTPILESIEKEENMGQYIEYKDHIKAMMKYYGILDPSMIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTFPSP
Protein: Alpha-ketoglutarate permease (P0AEX3)
Organism: Escherichia coli (strain K12)
Function: Uptake of alpha-ketoglutarate across the boundary membrane with the concomitant import of a cation (symport system).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
Sequence:
MAESTVTADSKLTSSDTRRRIWAIVGASSGNLVEWFDFYVYSFCSLYFAHIFFPSGNTTTQLLQTAGVFAAGFLMRPIGGWLFGRIADKHGRKKSMLLSVCMMCFGSLVIACLPGYETIGTWAPALLLLARLFQGLSVGGEYGTSATYMSEVAVEGRKGFYASFQYVTLIGGQLLALLVVVVLQHTMEDAALREWGWRIPFALGAVLAVVALWLRRQLDETSQQETRALKEAGSLKGLWRNRRAFIMVLGFTAAGSLCFYTFTTYMQKYLVNTAGMHANVASGIMTAALFVFMLIQPLIGALSDKIGRRTSMLCFGSLAAIFTVPILSALQNVSSPYAAFGLVMCALLIVSFYTSISGILKAEMFPAQVRALGVGLSYAVANAIFGGSAEYVALSLKSIGMETAFFWYVTLMAVVAFLVSLMLHRKGKGMRL
Protein: Uncharacterized ABC transporter ATP-binding protein/permease YOL075C (Q08234)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Topoisomerase I damage affected protein 4
Sequence:
MSQQENGDVATELIENRLSFSRIPRISLHVRDLSIVASKTNTTLVNTFSMDLPSGSVMAVMGGSGSGKTTLLNVLASKISGGLTHNGSIRYVLEDTGSEPNETEPKRAHLDGQDHPIQKHVIMAYLPQQDVLSPRLTCRETLKFAADLKLNSSERTKKLMVEQLIEELGLKDCADTLVGDNSHRGLSGGEKRRLSIGTQMISNPSIMFLDEPTTGLDAYSAFLVIKTLKKLAKEDGRTFIMSIHQPRSDILFLLDQVCILSKGNVVYCDKMDNTIPYFESIGYHVPQLVNPADYFIDLSSVDSRSDKEEAATQSRLNSLIDHWHDYERTHLQLQAESYISNATEIQIQNMTTRLPFWKQVTVLTRRNFKLNFSDYVTLISTFAEPLIIGTVCGWIYYKPDKSSIGGLRTTTACLYASTILQCYLYLLFDTYRLCEQDIALYDRERAEGSVTPLAFIVARKISLFLSDDFAMTMIFVSITYFMFGLEADARKFFYQFAVVFLCQLSCSGLSMLSVAVSRDFSKASLVGNMTFTVLSMGCGFFVNAKVMPVYVRWIKYIAFTWYSFGTLMSSTFTNSYCTTDNLDECLGNQILEVYGFPRNWITVPAVVLLCWSVGYFVVGAIILYLHKIDITLQNEVKSKQKKIKKKSPTGMKPEIQLLDDVYHQKDLEAEKGKNIHITIKLEDIDLRVIFSAPFSNWKEGNFHHETKEILQSVNAIFKPGMINAIMGPSGSGKSSLLNLISGRLKSSVFAKFDTSGSIMFNDIQVSELMFKNVCSYVSQDDDHLLAALTVKETLKYAAALRLHHLTEAERMERTDNLIRSLGLKHCENNIIGNEFVKGISGGEKRRVTMGVQLLNDPPILLLDEPTSGLDSFTSATILEILEKLCREQGKTIIITIHQPRSELFKRFGNVLLLAKSGRTAFNGSPDEMIAYFTELGYNCPSFTNVADFFLDLISVNTQNEQNEISSRARVEKILSAWKANMDNESLSPTPISEKQQYSQESFFTEYSEFVRKPANLVLAYIVNVKRQFTTTRRSFDSLMARIAQIPGLGVIFALFFAPVKHNYTSISNRLGLAQESTALYFVGMLGNLACYPTERDYFYEEYNDNVYGIAPFFLAYMTLELPLSALASVLYAVFTVLACGLPRTAGNFFATVYCSFIVTCCGEALGIMTNTFFERPGFVVNCISIILSIGTQMSGLMSLGMSRVLKGFNYLNPVGYTSMIIINFAFPGNLKLTCEDGGKNSDGTCEFANGHDVLVSYGLVRNTQKYLGIIVCVAIIYRLIAFFILKAKLEWIKW
Protein: Regulator of G-protein signaling 7 (RGS7) (O54829)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS7/GNB5 dimer enhances GNAO1 GTPase activity. May play a role in synaptic vesicle exocytosis. Modulates the activity of potassium channels that are activated by GNAO1 in response to muscarinic acetylcholine receptor M2/CHRM2 signaling.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49802}. Cytoplasm {ECO:0000250|UniProtKB:P49802}. Cell membrane {ECO:0000269|PubMed:22689652, ECO:0000269|PubMed:25792749, ECO:0000269|PubMed:30546127}. Membrane {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49802}; Cytoplasmic side {ECO:0000250|UniProtKB:P49802}. Note=Interaction with PKD1 promotes location at the cell membrane. Interaction with RGS7BP promotes location at the cell membrane. {ECO:0000250|UniProtKB:P49802}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein G
- T-complex protein 1 subunit epsilon
- Metabotropic glycine receptor
- Guanine nucleotide-binding protein G
- G-protein coupled receptor 179
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 9-binding protein
- Guanine nucleotide-binding protein G
Sequence:
MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELHQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYVEYDPFLVPPDPSNPWLSDDTTFWELEASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKRRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKRKGKTLTSKRLTSLVQSY
Protein: Partitioning defective 6 homolog beta (PAR-6 beta) (PAR-6B) (Q9JK83)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins.
Subcellular location: Cytoplasm. Cell membrane. Cell junction, tight junction. Note=Colocalizes with active form of CDC42 or RAC1 at membrane ruffles. Also localizes to tight junctions.
Interaction partners:
- Cell division control protein 42 homolog
- Partitioning defective 3 homolog
- Protein kinase C zeta type
- Protein kinase C iota type
- Ras-related C3 botulinum toxin substrate 2
- Protein PALS1
- Ras-related C3 botulinum toxin substrate 3
- Partitioning defective 6 homolog gamma
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Glycogen synthase kinase-3 beta
Sequence:
MNRGHRHGASSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLVGYADIHGDLLPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIRKKNMLSNVLRPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLYKYGTEKPLGFYIRDGSSVRVTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSRNLIITVRPANQRNNVVRNSRTSGSSSQSTDNSLLGFPQQVEASFEPEDQDSDEDDIIIEDSGEPQQIPKATPAQSLESLTQIELSFESGQNGFSPPQDTSLVPVPGSLDTELESRAPDQKLLEEDGTIITL
Protein: Probable inactive receptor kinase At1g27190 (O04567)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Somatic embryogenesis receptor kinase 1
- Somatic embryogenesis receptor kinase 2
- Putative F-box/kelch-repeat protein At4g22430
- At5g19340
- RING-type E3 ubiquitin transferase
- Transmembrane protein
- AT1G11360 protein
- Membrane-anchored ubiquitin-fold protein 3
- SAP domain-containing protein
- Protein IQ-DOMAIN 32
Sequence:
MKKIFITLLWLLFISSFLCSSSSAEDDVLCLQGLKNSLIDPSSRLSSWSFPNSSASSICKLTGVSCWNEKENRIISLQLQSMQLAGEIPESLKLCRSLQSLDLSGNDLSGSIPSQICSWLPYLVTLDLSGNKLGGSIPTQIVECKFLNALILSDNKLSGSIPSQLSRLDRLRRLSLAGNDLSGTIPSELARFGGDDFSGNNGLCGKPLSRCGALNGRNLSIIIVAGVLGAVGSLCVGLVIFWWFFIREGSRKKKGYGAGKSKDDSDWIGLLRSHKLVQVTLFQKPIVKIKLGDLMAATNNFSSGNIDVSSRTGVSYKADLPDGSALAVKRLSACGFGEKQFRSEMNKLGELRHPNLVPLLGYCVVEDERLLVYKHMVNGTLFSQLHNGGLCDAVLDWPTRRAIGVGAAKGLAWLHHGCQPPYLHQFISSNVILLDDDFDARITDYGLAKLVGSRDSNDSSFNNGDLGELGYVAPEYSSTMVASLKGDVYGFGIVLLELVTGQKPLSVINGVEGFKGSLVDWVSQYLGTGRSKDAIDRSICDKGHDEEILQFLKIACSCVVSRPKERPTMIQVYESLKNMADKHGVSEHYDEFPLVFNKQEA
Protein: Interleukin-12 subunit alpha (IL-12A) (Cytotoxic lymphocyte maturation factor 35 kDa subunit) (CLMF p35) (IL-12 subunit p35) (NK cell stimulatory factor chain 1) (NKSF1) (P29459)
Organism: Homo sapiens (Human)
Function: Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity. Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits. Binding to the receptor results in the rapid tyrosine phosphorylation of a number of cellular substrates including the JAK family kinases TYK2 and JAK2. In turn, recruited STAT4 gets phosphorylated and translocates to the nucleus where it regulates cytokine/growth factor responsive genes. As part of IL-35, plays essential roles in maintaining the immune homeostasis of the liver microenvironment and functions also as an immune-suppressive cytokine (By similarity). Mediates biological events through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers. Signaling requires the transcription factors STAT1 and STAT4, which form a unique heterodimer that binds to distinct DNA sites.
Subcellular location: Secreted {ECO:0000269|PubMed:1674604, ECO:0000269|PubMed:9342359}.
Interaction partners:
- Interleukin-12 subunit beta
- Interleukin-27 subunit beta
- Interleukin-12 receptor subunit beta-1
- Interleukin-12 receptor subunit beta-2
- Leptin receptor
- Signal transducer and activator of transcription 4
- Protein disulfide-isomerase
- Vesicle-associated membrane protein 7
- Signal transducer and activator of transcription 1-alpha/beta
- Granulocyte colony-stimulating factor receptor
Sequence:
MCPARSLLLVATLVLLDHLSLARNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS
Protein: ATP-dependent 6-phosphofructokinase subunit alpha (EC 2.7.1.11) (ATP-dependent 6-phosphofructokinase 1) (ATP-PFK 1) (Phosphofructokinase 1) (Glucose-induced selective autophagy 1 protein) (Phosphohexokinase 1) (Q92448)
Organism: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Involved in the modulation of glucose-induced microautophagy of peroxisomes independent of its ability to metabolize glucose intermediates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase subunit beta
- Glucose-6-phosphate isomerase
- Fructose-1,6-bisphosphatase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase
- Transaldolase
- Transaldolase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
Sequence:
MPEPSISALSFTSFVTNDDKLFEETFNFYTKLGFHATRSYVKDNRSDFELTGISTDSIKEIWLESFPLSEVVETSAGRELRKPLQESVGYQSEALLGYSPYQSDGVVIKLRLSNHDLQKNKDLPGEVTFFTASIDKLRAKLIEIGAEIIPSEIDLVEFSTKDPMGDVISFSSYPSLSSKKITSPDFFLHPKKEVRSQESIVEQVKSEEGKKKIAIITSGGDAPGMNAAVRAVTRAGIFYGCKVYACYEGYTGLVKGGDMLKELQWQDVRGLLSIGGTIIGTARSKEFRERWGRLQACYNMVSNGIDALVVCGGDGSLTGADLFRNEWPELIKELLGEGKITKEQYETHRNLTIVGLVGSIDNDMCGTDSTIGAYSSLERIIELVDYIDATAASHSRAFVVEVMGRHCGWLGLMSGIATGADYIFIPERPPSETNWKDDLKKVCLRHREKGRRKTTVIVAEGAIDDQLNPITSEEVKDVLVEIGLDTRITRLGHVQRGGAPCAFDRFLATVQGVDAVRAVLESTPAIPSPVISILENKIVRQPLVESVAQTKTVSDAIEAKDFDKALKLRDQEFATSYESFLSVSKYDDGSYLVPESSRLNIAIIHVGAPTSALNPATRVATLNSLAKGHRVFAIRNGFAGLIRHGAVRELNWIDVEDWHNTGGSEIGTNRSLPSDDMGTVAYYFQQYKFDGLIIIGGFEAFTALYQLDAARAQYPIFNIPMCCLPATVSNNVPGTEYSLGSDTCLNTLSGYCDAVKQSASASRRRTFVVEVQGGYSGYLASYAGLITGALAVYTPENPINLQTVQEDIELLTRTYEEDDGKNRSGKIFIHNEKASKVYTTDLIAAIIGEAGKGRFESRTAVPGHVQQGKSPSSIDRVNACRLAIKCCNFIEDANFQVKHNANLSADERHLRFFYDDGVKTSAVSGKSSVIDDNTSVVIGIQGSEVTFTPVKQLWEKETHHKWRKGKNVHWEQLNIVSDLLSGRLSIRTT
Protein: Rho guanine nucleotide exchange factor 12 (Leukemia-associated RhoGEF) (Q8R4H2)
Organism: Mus musculus (Mouse)
Function: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13 (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}. Note=Translocated to the membrane upon stimulation. {ECO:0000305}.
Interaction partners:
- Transforming protein RhoA
- Guanine nucleotide-binding protein subunit alpha-12
- Plexin-B1
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Plexin-B2
- CD44 antigen
- Plexin-B3
- RIKEN cDNA 4930544G11 gene
- Rho guanine nucleotide exchange factor 7
Sequence:
MSGTQSTITDRFPLKKPIRHGSILNRESPTDKKQKVERSSSHDFDPTDSSSKKTKSSSEESRSEIYGLVQRCVIIQKDDNGFGLTVSGDNPVFVQSVKEDGAAMRAGVQTGDRIIKVNGTLVTHSNHLEVVKLIRSGSYVALTVQGRPPGSPQIPLADSEVEPSVTGHMSPIMTSPHSPGAAGNMERITSPVLVGEENNVVHNQKVEILRKMLQKEQERLQLLQEDYNRTATQRLLKEIQEAKKHIPQLQEQLSKATGSAQDGAVIAPSRPLGDALTLSEAEADPGDGLCRTDWSSGDASRPSSDSADSPKSSLRERSYLEEAPERSEGVQDAEPQSLVGSPSTRGAPHIIGAEDDDFGTEHEQINGQCSCFQSIELLKSRPAHLAVFLHHVVSQFDPATLLCYLYSDLYKQTNSKETRRVFLEFHQFFLDRSAHLKVPVPEEISVDLEKRRPELIPEDLHRLYIQTMQERVHPEVQRHLEDFRQKRSMGLTLAESELTKLDAERDKDRGTLEKERACAEQIVTKIEEVLMTAQAVEEERSSTMQYVILMYMKYLGVKVKEPRNLEHKRGRIGFLPKIKQSMKKDREGEEKGKRRGFPSILGPPRRPSRHDNSAIGRAMEIQKSRHPKHLSTPSSVSPEPQDPAKLRQSGVANEGTDTGYLPASSMSSATSGTALSQEGGRENDTGTKQVGEASAPGDCLDSTPRVPTTVFDFPPPLLDQVQEEECEVERVAEHGTPKPFRKFDSIAFGESQSEDEQFENDLETDPPNWQQLVSREVLLGLKPSEIKRQEVINELFYTERAHVRTLKVLDQVFYQRVSREGILSPSELRKIFSNLEDILQLHVGLNEQMKAVRKRNETSVIDHIGEDLLIWFSGPGEEKLKHAAATFCSNQPFALEMIKSRQKKDSRFHTFVQDAESNPLCRRLQLKDIIPTQMQRLTKYPLLLDNIAKYTEWPPEREKVKKAADHCRQILNYVNQAVREAENKQRLEDYQRRLDTSNLKLSEYPNVDELRNLDLTKRKMIHEGPLVWKVNRDKSIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKHTFSPVIKLSTVLVRQVATDNKALFVISMSDNGAQIYELVAQTVSEKTVWQDLICRMAASVKEQSTKPIPLPQPPPCEGDNDEEEPAKLKVEHHDLSVAGLQSPDRVLGLESPLISSKPQSHSLNTPGKSAAEHLFVTATQFAKEQHANGALKEGDGGYPVTIPGPHLPVSEERWALDALRNLGLLKQLLVQQLGLTEKSTQEDWQSFSRYGPASEEVQADSGIRDLENVKACHAREGQMSFKTGTGDIATCDSPRTSTESCAAQDSVILASQDSQASNVLVMDHMILTPEMPPAEPEGGLDESGEHFFDAREAHSDDNPSEGDGAVKKEEKDVNLRISGNCLILDGYDAVQESSTDEEVASSFPLQPVTGIPAVDSSHQQQHSPQNVHPEGPVSPFTPEFLVQRHWRAMEDTCFEIQSPSCTDSQSQILEYIHKIEADLEHLKKVEESYALLCQRLAGSALPDKLSDKS
Protein: AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein) (Q9UHB7)
Organism: Homo sapiens (Human)
Function: Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:12065898}. Note=Associates to transcriptionally active chromatin but not at snRNA genes. {ECO:0000250}.
Interaction partners:
- Cyclin-T1
- AF4/FMR2 family member 1
- Cyclin-T2
- RNA polymerase II elongation factor ELL2
- Cyclin-dependent kinase 9
- Protein ENL
- RNA polymerase II elongation factor ELL
- Protein AF-9
- RNA polymerase II elongation factor ELL3
- ELL-associated factor 1
Sequence:
MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPKLVAIPKPTVPPSADEKSNPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRTSAGSSSGTNSSGQRHDRESYNNSGSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLNSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSTQSFPPSLMSKSNSMLQKPTAYVRPMDGQESMEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSQPLDASASGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGTGEQKRYNPSKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQGYKKEGREQGTGNSYTDTSGPKETSSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKAEKAAAEEPRGGLKIESETPVDLASSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSTSKSSQKSREIIETDTSSSDSDESESLPPSSQTPKYPESNRTPVKPSSVEEEDSFFRQRMFSPMEEKELLSPLSEPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHTREAQKQASEKVSNKGKRKHKNEDDNRASESKKPKTEDKNSAGHKPSSNRESSKQSAAKEKDLLPSPAGPVPSKDPKTEHGSRKRTISQSSSLKSSSNSNKETSGSSKNSSSTSKQKKTEGKTSSSSKEVKEKAPSSSSNCPPSAPTLDSSKPRRTKLVFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSETVDLIKYTMKLKNYLAPDATAADKRLTVLCLRCESLLYLRLFKLKKENALKYSKTLTEHLKNSYNNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGNYSSGASSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLVRYTRQGLHWLRQDAKLIS
Protein: Serine-palmitoyl-CoA transferase, putative (EC 2.3.1.50) (Q580D0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- serine C-palmitoyltransferase
- 3-dehydrosphinganine reductase
- Cystathionine beta-synthase, putative
- Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase
- Phosphatidylcholine:ceramide cholinephosphotransferase 4
- Phosphatidylcholine:ceramide cholinephosphotransferase 3
- Sphingomyelin phosphodiesterase, putative
- Phosphatidylinositol:ceramide inositolphosphotransferase
Sequence:
MVGFKTLSSTAPLAFSEFSHLLLEALLAAALAVALALHFIRRRNTSKIVEPELPPLEEQQRRIAAFRSQMFRADAKPNANTQLPNRTGMSEVEARNSCYITLRDESDSSSREYLDLVTEDFHSFSTHPTVVDVAKKIVVAYGVGSCGPRGFYGTIKPHMVLEEDIAKFLGVEDSLIFSFSFATISTLIPCHASRGDYLIVDDGVSLPVHEGCTLSRANLLKYRHNDMAHLEEILREVQIKEMKEKKLSRRFVVTEGVFKNLGDVCKLPQVLELCEKYKFRIILDDSCGFGCMGPTGRGTHEHYGIPTTRIDLYVGSLSQAMGGVGGFCAGEHAIIEYQRLTAAAYVFSASLAPYITAGVSAVLKLLDEDHSFPEKLQRNAGLFRGAIRSAGMNPEKITLVECAGDVSPIVILRPTDAYVKCHHQKVEEELQQVVEAARRKGVLLTRHLFSKEEACSNFSALRILVKGTATEDELLRAAKVITEAVKSVFV
Protein: Basic helix-loop-helix (BHLH)-like (Q6K8Y4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQPNARQMRGGGGGGGGGQDDFFDQMLSTLPAVWSELGSGKPAWDLTAGAVGGGGGASDDHSAAAFDDSALLASRLRQHQIDGGGDKPIMLQLSDLHRHHGLAAGDDSGGAAGFLPLSLFADRSQDDIDAAFKSPNGARGDHALYNGFGAAGMHGAAAMQPPPFGQGGSMPAQSFGGGAAASGGGGGGSASAAAAAGASSGGGAAAPPRQRQRARRGQATDPHSIAERVYHSPTTFPFSPPFFIASMPCCLRRERIAERMKALQELVPNANKTDKASMLDEIIDYVKFLQLQVKVLSMSRLGGASAVAPLVANMSSESNGNGNATSSSGNGEAANGSSNGDNNGGGTLRVTEQQVAKLMEEDMGSAMQYLQGKGLCLMPISLATAISSATSSSLLPRTGGGAGGSLHEGGNGTSPPLVNGTATGCDDAGVFFSVKFVVELSFLLLNEDCRGKEESKLLVQKGP
Protein: Thioredoxin (Trx) (MPT46) (P9WG67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Interaction partners:
- Thioredoxin reductase
- N-acetylmuramoyl-L-alanine amidase CwlM
- Anti-sigma-M factor RsmA
- Chaperone protein DnaK
- Alkyl hydroperoxide reductase C
- Putative peroxiredoxin Rv2521
- ECF RNA polymerase sigma factor SigM
- Superoxide dismutase
- Dihydrolipoyl dehydrogenase
Sequence:
MTDSEKSATIKVTDASFATDVLSSNKPVLVDFWATWCGPCKMVAPVLEEIATERATDLTVAKLDVDTNPETARNFQVVSIPTLILFKDGQPVKRIVGAKGKAALLRELSDVVPNLN