ID D6RFL0_HUMAN Unreviewed; 43 AA. AC D6RFL0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-APR-2021, entry version 85. DE RecName: Full=Cell division protein kinase 7 {ECO:0000256|ARBA:ARBA00013339}; DE EC=2.7.11.22 {ECO:0000256|ARBA:ARBA00012425}; DE AltName: Full=Cyclin-dependent kinase 7 {ECO:0000256|ARBA:ARBA00013901}; GN Name=CDK7 {ECO:0000313|EMBL:ALQ33429.1, GN ECO:0000313|Ensembl:ENSP00000426561}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000426561, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000426561, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] {ECO:0007829|PubMed:18691976} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [3] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [4] {ECO:0000313|Ensembl:ENSP00000426561} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [5] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [6] {ECO:0000313|Ensembl:ENSP00000479440} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [7] {ECO:0000313|EMBL:ALQ33429.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26871637; DOI=10.1016/j.cell.2016.01.029; RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T., RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K., RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q., RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D., RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J., RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P., RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.; RT "Widespread Expansion of Protein Interaction Capabilities by Alternative RT Splicing."; RL Cell 164:805-817(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CC Evidence={ECO:0000256|ARBA:ARBA00000584}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.22; Evidence={ECO:0000256|ARBA:ARBA00000875}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC145132; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC145145; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KU177971; ALQ33429.1; -; mRNA. DR RefSeq; NP_001311007.1; NM_001324078.1. DR MaxQB; D6RFL0; -. DR ProteomicsDB; 14563; -. DR DNASU; 1022; -. DR Ensembl; ENST00000510106; ENSP00000426561; ENSG00000134058. DR Ensembl; ENST00000615854; ENSP00000479440; ENSG00000277273. DR GeneID; 1022; -. DR UCSC; uc063efs.1; human. DR CTD; 1022; -. DR HGNC; HGNC:1778; CDK7. DR OpenTargets; ENSG00000134058; -. DR VEuPathDB; HostDB:ENSG00000134058.10; -. DR GeneTree; ENSGT00940000155179; -. DR SignaLink; D6RFL0; -. DR BioGRID-ORCS; 1022; 716 hits in 1022 CRISPR screens. DR ChiTaRS; CDK7; human. DR GenomeRNAi; 1022; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000134058; Expressed in testis and 114 other tissues. DR ExpressionAtlas; D6RFL0; baseline and differential. DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0106311; F:protein threonine kinase activity; IEA:RHEA. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:InterPro. DR InterPro; IPR037770; CDK7. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR24056:SF375; PTHR24056:SF375; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000313|EMBL:ALQ33429.1}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|EPD:D6RFL0, KW ECO:0007829|MaxQB:D6RFL0, ECO:0007829|PeptideAtlas:D6RFL0, KW ECO:0007829|ProteomicsDB:D6RFL0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transferase {ECO:0000313|EMBL:ALQ33429.1}. FT DOMAIN 12..43 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 42 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 43 AA; 4945 MW; 9C40CB3CED87CE53 CRC64; MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKV //