MAT1_HUMAN
ID MAT1_HUMAN Reviewed; 309 AA.
AC P51948; G3V1U8; Q15817; Q6ICQ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=CDK-activating kinase assembly factor MAT1;
DE AltName: Full=CDK7/cyclin-H assembly factor;
DE AltName: Full=Cyclin-G1-interacting protein;
DE AltName: Full=Menage a trois;
DE AltName: Full=RING finger protein 66;
DE AltName: Full=RING finger protein MAT1;
DE AltName: Full=p35;
DE AltName: Full=p36;
GN Name=MNAT1; Synonyms=CAP35, MAT1, RNF66;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-48 AND
RP 123-147.
RC TISSUE=Placenta;
RX PubMed=8521818; DOI=10.1002/j.1460-2075.1995.tb00248.x;
RA Tassan J.-P., Jaquenoud M., Fry A.M., Frutiger S., Hughes G.J., Nigg E.A.;
RT "In vitro assembly of a functional human CDK7-cyclin H complex requires
RT MAT1, a novel 36 kDa RING finger protein.";
RL EMBO J. 14:5608-5617(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=8521393;
RA Yee A., Nichols M., Wu L., Hall F.L., Kobayashi R., Xiong Y.;
RT "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent
RT kinase-activating kinase (CAK) assembly factor.";
RL Cancer Res. 55:6058-6062(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Xu F., Hall F.L., Starnes V., Wu L.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [10]
RP FUNCTION.
RX PubMed=10024882; DOI=10.1016/s1097-2765(00)80177-x;
RA Tirode F., Busso D., Coin F., Egly J.-M.;
RT "Reconstitution of the transcription factor TFIIH: assignment of functions
RT for the three enzymatic subunits, XPB, XPD, and cdk7.";
RL Mol. Cell 3:87-95(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
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., Buerckstuemmer 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP STRUCTURE BY NMR OF 1-65.
RX PubMed=11056162; DOI=10.1074/jbc.m007963200;
RA Gervais V., Busso D., Wasielewski E., Poterszman A., Egly J.-M.,
RA Thierry J.-C., Kieffer B.;
RT "Solution structure of the N-terminal domain of the human TFIIH MAT1
RT subunit: new insights into the RING finger family.";
RL J. Biol. Chem. 276:7457-7464(2001).
CC -!- FUNCTION: Stabilizes the cyclin H-CDK7 complex to form a functional
CC CDK-activating kinase (CAK) enzymatic complex. CAK activates the
CC cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine
CC phosphorylation. CAK complexed to the core-TFIIH basal transcription
CC factor activates RNA polymerase II by serine phosphorylation of the
CC repetitive C-terminal domain (CTD) of its large subunit (POLR2A),
CC allowing its escape from the promoter and elongation of the
CC transcripts. Involved in cell cycle control and in RNA transcription by
CC RNA polymerase II. {ECO:0000269|PubMed:10024882}.
CC -!- SUBUNIT: Associates primarily with CDK7 and cyclin H to form the CAK
CC complex. CAK can further associate with the core-TFIIH to form the
CC TFIIH basal transcription factor. {ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P51948; Q08379: GOLGA2; NbExp=3; IntAct=EBI-716139, EBI-618309;
CC P51948; P42858: HTT; NbExp=9; IntAct=EBI-716139, EBI-466029;
CC P51948; O60260-5: PRKN; NbExp=3; IntAct=EBI-716139, EBI-21251460;
CC P51948; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-716139, EBI-396669;
CC P51948; Q13148: TARDBP; NbExp=3; IntAct=EBI-716139, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51948-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51948-2; Sequence=VSP_046772;
CC -!- TISSUE SPECIFICITY: Highest levels in colon and testis. Moderate levels
CC are present thymus, prostate, ovary, and small intestine. The lowest
CC levels are found in spleen and leukocytes.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mnat1/";
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DR EMBL; X87843; CAA61112.1; -; mRNA.
DR EMBL; X92669; CAA63356.1; -; mRNA.
DR EMBL; U61835; AAB05248.1; -; mRNA.
DR EMBL; AY165512; AAN47195.1; -; Genomic_DNA.
DR EMBL; AL132777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80788.1; -; Genomic_DNA.
DR EMBL; CR450336; CAG29332.1; -; mRNA.
DR EMBL; CH471061; EAW80787.1; -; Genomic_DNA.
DR EMBL; BC000820; AAH00820.1; -; mRNA.
DR CCDS; CCDS53899.1; -. [P51948-2]
DR CCDS; CCDS9750.1; -. [P51948-1]
DR PIR; G02764; G02764.
DR PIR; S60157; S60157.
DR RefSeq; NP_001171434.1; NM_001177963.1. [P51948-2]
DR RefSeq; NP_002422.1; NM_002431.3. [P51948-1]
DR RefSeq; XP_005267744.1; XM_005267687.2. [P51948-1]
DR PDB; 1G25; NMR; -; A=1-65.
DR PDB; 6NMI; EM; 3.70 A; H=1-309.
DR PDB; 6O9L; EM; 7.20 A; 3=1-309.
DR PDB; 6O9M; EM; 4.40 A; 3=1-309.
DR PDB; 6TUN; X-ray; 2.07 A; C/D=66-141.
DR PDB; 6XBZ; EM; 2.80 A; H=1-309.
DR PDB; 6XD3; EM; 3.30 A; H=220-309.
DR PDB; 7B5O; EM; 2.50 A; H=1-309.
DR PDB; 7B5Q; EM; 2.50 A; H=1-309.
DR PDB; 7EGB; EM; 3.30 A; 0=1-309.
DR PDB; 7EGC; EM; 3.90 A; 0=1-309.
DR PDB; 7ENA; EM; 4.07 A; 0=1-309.
DR PDB; 7ENC; EM; 4.13 A; 0=1-309.
DR PDB; 7LBM; EM; 4.80 A; d=1-309.
DR PDB; 7NVR; EM; 4.50 A; 3=1-309.
DR PDB; 7NVW; EM; 4.30 A; 3=1-309.
DR PDB; 7NVX; EM; 3.90 A; 3=1-309.
DR PDB; 7NVY; EM; 7.30 A; 3=1-309.
DR PDB; 7NVZ; EM; 7.20 A; 3=1-309.
DR PDB; 7NW0; EM; 6.60 A; 3=1-309.
DR PDBsum; 1G25; -.
DR PDBsum; 6NMI; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6O9M; -.
DR PDBsum; 6TUN; -.
DR PDBsum; 6XBZ; -.
DR PDBsum; 6XD3; -.
DR PDBsum; 7B5O; -.
DR PDBsum; 7B5Q; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVW; -.
DR PDBsum; 7NVX; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P51948; -.
DR SMR; P51948; -.
DR BioGRID; 110474; 108.
DR ComplexPortal; CPX-578; Cyclin-dependent protein kinase-activating kinase complex.
DR CORUM; P51948; -.
DR IntAct; P51948; 48.
DR MINT; P51948; -.
DR STRING; 9606.ENSP00000261245; -.
DR BindingDB; P51948; -.
DR ChEMBL; CHEMBL3038473; -.
DR MoonDB; P51948; Predicted.
DR iPTMnet; P51948; -.
DR PhosphoSitePlus; P51948; -.
DR BioMuta; MNAT1; -.
DR DMDM; 1708932; -.
DR EPD; P51948; -.
DR jPOST; P51948; -.
DR MassIVE; P51948; -.
DR MaxQB; P51948; -.
DR PaxDb; P51948; -.
DR PeptideAtlas; P51948; -.
DR PRIDE; P51948; -.
DR ProteomicsDB; 32447; -.
DR ProteomicsDB; 56452; -. [P51948-1]
DR Antibodypedia; 34; 257 antibodies from 35 providers.
DR DNASU; 4331; -.
DR Ensembl; ENST00000261245.9; ENSP00000261245.4; ENSG00000020426.11. [P51948-1]
DR Ensembl; ENST00000539616.6; ENSP00000446437.2; ENSG00000020426.11. [P51948-2]
DR GeneID; 4331; -.
DR KEGG; hsa:4331; -.
DR MANE-Select; ENST00000261245.9; ENSP00000261245.4; NM_002431.4; NP_002422.1.
DR UCSC; uc001xfd.4; human. [P51948-1]
DR CTD; 4331; -.
DR DisGeNET; 4331; -.
DR GeneCards; MNAT1; -.
DR HGNC; HGNC:7181; MNAT1.
DR HPA; ENSG00000020426; Low tissue specificity.
DR MIM; 602659; gene.
DR neXtProt; NX_P51948; -.
DR OpenTargets; ENSG00000020426; -.
DR PharmGKB; PA30894; -.
DR VEuPathDB; HostDB:ENSG00000020426; -.
DR eggNOG; KOG3800; Eukaryota.
DR GeneTree; ENSGT00390000002319; -.
DR HOGENOM; CLU_048466_0_1_1; -.
DR InParanoid; P51948; -.
DR OMA; FSGLFWH; -.
DR PhylomeDB; P51948; -.
DR TreeFam; TF106124; -.
DR PathwayCommons; P51948; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR SignaLink; P51948; -.
DR SIGNOR; P51948; -.
DR BioGRID-ORCS; 4331; 486 hits in 1146 CRISPR screens.
DR ChiTaRS; MNAT1; human.
DR EvolutionaryTrace; P51948; -.
DR GeneWiki; MNAT1; -.
DR GenomeRNAi; 4331; -.
DR Pharos; P51948; Tbio.
DR PRO; PR:P51948; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P51948; protein.
DR Bgee; ENSG00000020426; Expressed in calcaneal tendon and 143 other tissues.
DR ExpressionAtlas; P51948; baseline and differential.
DR Genevisible; P51948; HS.
DR GO; GO:0070516; C:CAK-ERCC2 complex; IDA:UniProtKB.
DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:UniProtKB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:UniProtKB.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015877; Cdk-activating_kinase_MAT1_cen.
DR InterPro; IPR004575; MAT1/Tfb3.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12683:SF13; PTHR12683:SF13; 1.
DR Pfam; PF06391; MAT1; 1.
DR Pfam; PF17121; zf-C3HC4_5; 1.
DR PIRSF; PIRSF003338; MAT1_metazoa; 1.
DR SMART; SM00184; RING; 1.
DR TIGRFAMs; TIGR00570; cdk7; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..309
FT /note="CDK-activating kinase assembly factor MAT1"
FT /id="PRO_0000055932"
FT DOMAIN 142..161
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 6..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 188..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046772"
FT VARIANT 282
FT /note="D -> A (in dbSNP:rs35188899)"
FT /id="VAR_052084"
FT CONFLICT 247..248
FT /note="EY -> DN (in Ref. 3; AAB05248)"
FT /evidence="ECO:0000305"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1G25"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:1G25"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1G25"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1G25"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1G25"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1G25"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1G25"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:6TUN"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6TUN"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6TUN"
FT HELIX 92..110
FT /evidence="ECO:0007829|PDB:6TUN"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:6TUN"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7B5Q"
FT TURN 263..270
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:7B5O"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:7B5O"
SQ SEQUENCE 309 AA; 35823 MW; 6818DDE230E81A97 CRC64;
MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG TPLRKSNFRV
QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE EVEEIVFNLT NNVDLDNTKK
KMEIYQKENK DVIQKNKLKL TREQEELEEA LEVERQENEQ RRLFIQKEEQ LQQILKRKNK
QAFLDELESS DLPVALLLAQ HKDRSTQLEM QLEKPKPVKP VTFSTGIKMG QHISLAPIHK
LEEALYEYQP LQIETYGPHV PELEMLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA
FSGLFWQPS
