wanglab/bioreason-pro-rl-reasoning-data huggingface dataset:
Protein: Cyclin-dependent kinase-like 2 (EC 2.7.11.22) (J3KNE8)
Organism: Homo sapiens (Human)
Function: Not known
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Sequence: MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAERFSQELQLKVQKDARNVSLSKKSQNRKKEKEKDDSLVEERKTLVVQDTNADPKIKDYKLFKIKGSKIDGEKAEKGNRASNASCLHDSRTSHNKIVPSTSLKDCSNVSVDHTRNPSVAIPPLTHNLSAVAPSINSGMGTETIPIQGYRVDEKTKKCSIPFVKPNRHSPSGIYNINVTTLVSSEKNLFWASKKRREYSRTDVRLPELNYNHLPELRALGGIARNSRLTKKESKILSESRIPSLAAIDLHTPSITLHQVSGPPLSDDSGADLPQMEHQH
InterPro domains: - IPR011009: Protein kinase-like domain superfamily (homologous_superfamily) [1-288]
- IPR008271: Serine/threonine-protein kinase, active site (active_site) [122-134]
- IPR050108: Cyclin-dependent kinase (family) [2-289]
- IPR017441: Protein kinase, ATP binding site (binding_site) [10-34]
- IPR000719: Protein kinase domain (domain) [4-287]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0140096 (catalytic activity, acting on a protein), GO:0004672 (protein kinase activity), GO:0016772 (transferase activity, transferring phosphorus-containing groups), GO:0016773 (phosphotransferase activity, alcohol group as acceptor), GO:0016301 (kinase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0032502 (developmental process), GO:0009987 (cellular process), GO:0023052 (signaling), GO:0065007 (biological regulation), GO:0050896 (response to stimulus), GO:0050789 (regulation of biological process), GO:0000003 (reproduction), GO:0022414 (reproductive process), GO:0051716 (cellular response to stimulus), GO:0003006 (developmental process involved in reproduction), GO:0007154 (cell communication), GO:0007165 (signal transduction), GO:0050794 (regulation of cellular process), GO:0007548 (sex differentiation)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005815 (microtubule organizing center), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0042995 (cell projection), GO:0043229 (intracellular organelle), GO:0036064 (ciliary basal body), GO:0043227 (membrane-bounded organelle), GO:0120025 (plasma membrane bounded cell projection), GO:0043228 (non-membrane-bounded organelle), GO:0005929 (cilium), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0005856 (cytoskeleton), GO:0015630 (microtubule cytoskeleton)
Protein: Cartilage matrix protein (Matrilin-1) (P21941)
Organism: Homo sapiens (Human)
Function: Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Sequence: MRVLSGTSLMLCSLLLLLQALCSPGLAPQSRGHLCRTRPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGMVNYASTVKQEFSLRAHVSKAALLQAVRRIQPLSTGTMTGLAIQFAITKAFGDAEGGRSRSPDISKVVIVVTDGRPQDSVQDVSARARASGVELFAIGVGSVDKATLRQIASEPQDEHVDYVESYSVIEKLSRKFQEAFCVVSDLCATGDHDCEQVCISSPGSYTCACHEGFTLNSDGKTCNVCSGGGGSSATDLVFLIDGSKSVRPENFELVKKFISQIVDTLDVSDKLAQVGLVQYSSSVRQEFPLGRFHTKKDIKAAVRNMSYMEKGTMTGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAAKKAKDLGFKMFAVGVGNAVEDELREIASEPVAEHYFYTADFKTINQIGKKLQKKICVEEDPCACESLVKFQAKVEGLLQALTRKLEAVSKRLAILENTVV
InterPro domains: - IPR019466: Matrilin, coiled-coil trimerisation domain (domain) [450-496]
- IPR002035: von Willebrand factor, type A (domain) [39-452]
- IPR001881: EGF-like calcium-binding domain (domain) [231-263]
- IPR000742: EGF-like domain (domain) [226-263]
- IPR050525: Extracellular Matrix Assembly and Organization (family) [35-259]
- IPR036465: von Willebrand factor A-like domain superfamily (homologous_superfamily) [31-454]
- IPR036337: Matrilin, coiled-coil domain superfamily (homologous_superfamily) [453-496]
Interaction partners: - Aggrecan core protein
- Matrilin-4
- Collagen alpha-1
- Cartilage oligomeric matrix protein
- Collagen alpha-1
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0032502 (developmental process), GO:0065007 (biological regulation), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0032501 (multicellular organismal process), GO:0048583 (regulation of response to stimulus), GO:0023051 (regulation of signaling), GO:0023056 (positive regulation of signaling), GO:0048856 (anatomical structure development), GO:0007275 (multicellular organism development), GO:0048584 (positive regulation of response to stimulus), GO:0050794 (regulation of cellular process), GO:0048522 (positive regulation of cellular process), GO:0090287 (regulation of cellular response to growth factor stimulus), GO:0009967 (positive regulation of signal transduction), GO:0010647 (positive regulation of cell communication), GO:0009966 (regulation of signal transduction), GO:0010646 (regulation of cell communication), GO:0090092 (regulation of transmembrane receptor protein serine/threonine kinase signaling pathway), GO:0030510 (regulation of BMP signaling pathway), GO:0090100 (positive regulation of transmembrane receptor protein serine/threonine kinase signaling pathway), GO:0030513 (positive regulation of BMP signaling pathway)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0071944 (cell periphery), GO:0030312 (external encapsulating structure), GO:0031012 (extracellular matrix)
Protein: Periplasmic/secreted acid trehalase ATH1 (cgATH1) (EC 3.2.1.28) (M1RNJ8)
Organism: Candida glabrata (Yeast) (Torulopsis glabrata)
Function: Periplasmic/secreted acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Growth on trehalose is not restricted to respiration.
Subcellular location: Secreted {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:33146242}. Periplasm {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:33146242}. Membrane {ECO:0000250|UniProtKB:P48016}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P48016}.
Sequence: MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE
InterPro domains: - IPR011013: Galactose mutarotase-like domain superfamily (homologous_superfamily) [222-447]
- IPR012341: Six-hairpin glycosidase-like superfamily (homologous_superfamily) [503-823]
- IPR005194: Glycoside hydrolase family 65, C-terminal (domain) [886-933]
- IPR037018: Glycoside hydrolase family 65, N-terminal domain (homologous_superfamily) [174-449]
- IPR005196: Glycoside hydrolase, family 65, N-terminal (domain) [177-448]
- IPR005195: Glycoside hydrolase, family 65, central catalytic (domain) [509-728]
- IPR008928: Six-hairpin glycosidase superfamily (homologous_superfamily) [462-931]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016787 (hydrolase activity), GO:0016798 (hydrolase activity, acting on glycosyl bonds), GO:0004553 (hydrolase activity, hydrolyzing O-glycosyl compounds), GO:0015927 (trehalase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0050896 (response to stimulus), GO:0009605 (response to external stimulus), GO:0009991 (response to extracellular stimulus), GO:0031667 (response to nutrient levels), GO:0015976 (carbon utilization)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0042597 (periplasmic space)
Protein: Transcription factor LATE FLOWERING (OsLF) (Basic helix-loop-helix protein 119) (OsbHLH119) (A0A0P0WQ90)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor involved in the negative regulation of flowering. May be involved in the repression of the flowering factor GI and HD1 by interacting with PIL13 and PIL15 and competing with PRR1. Possesses transactivation activity in yeast.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21549224}.
Sequence: MYMDAFGWSAPAAPCQPSCGPGGDDDDDVLLAAVLGASFELHSLVDGGGNGAAGAVRSDDAYGLDVDLPSHQMSLLRCQDGLSALHGDASPTAAAAAFLDSVDVLPVPAIAGATHDDGGLLDRFAFPNVAETTTVQAAASNTAFSGYSSNTTGGGNISSGESNTYTEVASTPCAVSTTTTTTALPPSKRKLPEKYPVVGTSPTTKTTTTSETAAERRSTKRGAGGSSSITFGGGCHGAGAAAALLGYGRGYEPDTEAIAQVKEMIYRAAAMRPVTLGGPASASDPSSRPPPPPQRPRRKNVRISSDPQTVAARLRRERVSERLRVLQRLVPGGSKMDTATMLDEAASYLKFLKSQLEALETLGNGNGNGNLLHHGYYTGSRNATATAATGSSNSTVLAFGRDGLAGFVKSNRNLQL
InterPro domains: - IPR011598: Myc-type, basic helix-loop-helix (bHLH) domain (domain) [303-358]
- IPR045843: Transcription factor IND-like (family) [156-380]
- IPR036638: Helix-loop-helix DNA-binding domain superfamily (homologous_superfamily) [308-362]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0050789 (regulation of biological process), GO:0019222 (regulation of metabolic process), GO:0050794 (regulation of cellular process), GO:0060255 (regulation of macromolecule metabolic process), GO:0031323 (regulation of cellular metabolic process), GO:0080090 (regulation of primary metabolic process), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0019219 (regulation of nucleobase-containing compound metabolic process), GO:0051252 (regulation of RNA metabolic process), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0010468 (regulation of gene expression), GO:0031326 (regulation of cellular biosynthetic process), GO:2001141 (regulation of RNA biosynthetic process), GO:0006355 (regulation of DNA-templated transcription), GO:1903506 (regulation of nucleic acid-templated transcription)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus)
Protein: Glycosyltransferase WbpL (G3XD50)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Not known
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Sequence: MMIWMIACLVVLLFSFVATWGLRRYALATKLMDVPNARSSHSQPTPRGGGVAIVLVFLAALVWMLSAGSISGGWGGAMLGAGSGVALLGFLDDHGHIAARWRLLGHFSAAIWILLWTGGFPPLDVVGHAVDLGWLGHVLAVFYLVWVLNLYNFMDGIDGIASVEAIGVCVGGALIYWLTGHVAMVGIPLLLACAVAGFLIWNFPPARIFMGDAGSGFLGMVIGALAIQAAWTAPSLFWCWLILLGVFIVDATYTLIRRIARGEKFYEAHRSHAYQFASRRYASHLRVTLGVLAINTLWLLPLALMVALGWISGFIGILVAYAPLCLLAVGYKAGSLEKS
InterPro domains: - IPR000715: Glycosyl transferase, family 4 (family) [2-301]
Interaction partners: - Probable NAD-dependent epimerase/dehydratase WbpK
- O-antigen polymerase
- UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase
- O-antigen chain length regulator
- Probable glycosyl transferase WbpJ
- O-antigen translocase
- UDP-N-acetyl-D-glucosamine 6-dehydrogenase
- LPS biosynthesis protein WbpG
- Probable glycosyltransferase WbpH
- UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016757 (glycosyltransferase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006629 (lipid metabolic process), GO:0044255 (cellular lipid metabolic process), GO:0044249 (cellular biosynthetic process), GO:0005975 (carbohydrate metabolic process), GO:0044260 (cellular macromolecule metabolic process), GO:0043170 (macromolecule metabolic process), GO:1901135 (carbohydrate derivative metabolic process), GO:0044262 (cellular carbohydrate metabolic process), GO:0009059 (macromolecule biosynthetic process), GO:0016051 (carbohydrate biosynthetic process), GO:0005976 (polysaccharide metabolic process), GO:0034637 (cellular carbohydrate biosynthetic process), GO:1903509 (liposaccharide metabolic process), GO:0034645 (cellular macromolecule biosynthetic process), GO:1901137 (carbohydrate derivative biosynthetic process), GO:0008610 (lipid biosynthetic process), GO:0008653 (lipopolysaccharide metabolic process), GO:0044264 (cellular polysaccharide metabolic process), GO:0046402 (O antigen metabolic process), GO:0009103 (lipopolysaccharide biosynthetic process), GO:0033692 (cellular polysaccharide biosynthetic process), GO:0000271 (polysaccharide biosynthetic process), GO:0009243 (O antigen biosynthetic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0031975 (envelope), GO:0071944 (cell periphery), GO:0030312 (external encapsulating structure), GO:0005618 (cell wall), GO:0030313 (cell envelope), GO:0009274 (peptidoglycan-based cell wall)
Protein: Nosiheptide precursor [Cleaved into: Nosiheptide (NOS) (Antibiotic 9671-RP) (Multhiomycin)] (C6FX52)
Organism: Streptomyces actuosus
Function: Inhibits bacterial protein biosynthesis by binding to ribosomes. Specifically, binds to the complex of 23S rRNA and ribosomal protein L11 (RPLK) in the 50S ribosomal subunit. While allowing a weak binding of elongation factor G (EF-G) to the ribosome and subsequent GTP-hydrolysis, probably impairs conformational changes in both the ribosome and EF-G which are necessary for translocation. In vitro, inhibits Gram-positive bacteria S.aureus strain 209P (MIC=0.0009 ug/ml), S.aureus strain 133 (MIC=0.0019 ug/ml), S.aureus strain B3 (MIC=0.003 ug/ml), S.aureus strain Hb (MIC=0.003 ug/ml), M.citreus strain ATCC 8411 (MIC=0.0038 ug/ml), M.lysodeikticus strain ATCC 4698 (MIC=0.003 ug/ml), S.lutea strain ATCC 9341 (MIC=0.0011 ug/ml), S.faecalis strain ATCC 9790 (MIC=0.0007 ug/ml), S.viridans (MIC=0.0065 ug/ml), S.pyogenes hemolyticus strain Dig7 (MIC=0.00028 ug/ml), D.pneumoniae strain Til (MIC=0.00015 ug/ml), N.catrrhalis (MIC=0.0017 ug/ml), L.casei strain ATCC 6633 (MIC=0.003 ug/ml), B.cereus strain ATCC 6630 (MIC=0.0071 ug/ml) and various isolates of L.monocytogenes. In vitro, inhibits Gram-negative bacterium P.multocida strain A125 (MIC=0.0024 ug/ml) but not M.smegmatis strain ATCC 6630, S.typhimurium, A.aerogenes strain ATCC 8308, P.vulgaris, K.pneumoniae strain ATCC 10031, S.marcescens strain A476, P.aeruginosa strain Bass or B.bronchiseptica strain CN387. Does not inhibit Gram-negative bacterium E.coli strain ATCC 9637 but does inhibit purified ribosomes from E.coli. In vivo, has no systemic effect in mice infected with staphylococci or streptococci when applied orally or subcutaneously. Has a local effect in mice infected subcutaneously or intraperitoneally with staphylococci when applied immediately afterwards. Is not toxic to mice.
Sequence: MDAAHLSDLDIDALEISEFLDESRLEDSEVVAKVMSASCTTCECCCSCSS
InterPro domains: - IPR023895: Thiazolylpeptide-type bacteriocin precursor (family) [6-48]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding), GO:0042802 (identical protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0050896 (response to stimulus), GO:0044419 (biological process involved in interspecies interaction between organisms), GO:0009605 (response to external stimulus), GO:0051707 (response to other organism), GO:0009607 (response to biotic stimulus), GO:0006950 (response to stress), GO:0006952 (defense response), GO:0009617 (response to bacterium), GO:0043207 (response to external biotic stimulus), GO:0098542 (defense response to other organism), GO:0042742 (defense response to bacterium), GO:0050830 (defense response to Gram-positive bacterium)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005576 (extracellular region)
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (P75391)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Sequence: MSKTIQANNIEALGNAMDLALERDPNVVLYGQDAGFEGGVFRATKGLQKKYGEERVWDCPIAEAAMAGIGVGAAIGGLKPIVEIQFSGFSFPAMFQIFTHAARIRNRSRGVYTCPIIVRMPMGGGIKALEHHSETLEAIYGQIAGLKTVMPSNPYDTKGLFLAAVESPDPVVFFEPKKLYRAFRQEIPADYYTVPIGQANLISQGNNLTIVSYGPTMFDLINMVYGGELKDKGIELIDLRTISPWDKETVFNSVKKTGRLLVVTEAAKTFTTSGEIIASVTEELFSYLKAAPQRVTGWDIVVPLARGEHYQFNLNARILEAVNQLLK
InterPro domains: - IPR005475: Transketolase-like, pyrimidine-binding domain (domain) [7-182]
- IPR009014: Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II (homologous_superfamily) [192-327]
- IPR029061: Thiamin diphosphate-binding fold (homologous_superfamily) [8-196]
- IPR033248: Transketolase, C-terminal domain (domain) [197-311]
Interaction partners: - Pyruvate dehydrogenase E1 component subunit alpha
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Ribose-phosphate pyrophosphokinase
- L-lactate dehydrogenase
- Probable lipoate-protein ligase A
- Pyruvate kinase
- Transketolase
- Fructose-bisphosphate aldolase
- NADH oxidase
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0044238 (primary metabolic process), GO:0044255 (cellular lipid metabolic process), GO:0044249 (cellular biosynthetic process), GO:1901576 (organic substance biosynthetic process), GO:0006629 (lipid metabolic process), GO:0044283 (small molecule biosynthetic process), GO:0006082 (organic acid metabolic process), GO:0006631 (fatty acid metabolic process), GO:0043436 (oxoacid metabolic process), GO:0016053 (organic acid biosynthetic process), GO:0008610 (lipid biosynthetic process), GO:0006633 (fatty acid biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0046394 (carboxylic acid biosynthetic process), GO:0072330 (monocarboxylic acid biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:1990204 (oxidoreductase complex)
Protein: Early E1A protein (Early E1A 28 kDa protein) (P10407)
Organism: Human adenovirus E serotype 4 (HAdV-4) (Human adenovirus 4)
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03255}.
Sequence: MRHLRDLPDEEIIIASGSEILELVVNATMGDDHPEPPTPFGTPSLHDLYDLEVDVPEDDPNEKAVNDLFSDAALLAAEEASSPSSDSDSSLHTPRHDRGEKEIPGLKWEKMDLRCYEECLPPSDDEDEQAIQNAASHGVQAVSESFALDCPPLPGHGCKSCEFHRINTGDKAVLCALCYMRAYNHCVYSPVSDADDETPTTESTLSPPEIGTSPSDNIVRPVPVRATGRRAAVECLDDLLQGGDEPLDLCTRKRPRH
InterPro domains: - IPR014410: Adenovirus early E1A protein (family) [1-257]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0016032 (viral process), GO:0019080 (viral gene expression), GO:0019083 (viral transcription)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0043657 (host cell), GO:0033643 (host cell part), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0033647 (host intracellular organelle), GO:0033648 (host intracellular membrane-bounded organelle), GO:0042025 (host cell nucleus)