ID   MAT1_MOUSE              Reviewed;         309 AA.
AC   P51949; Q14BS9; Q3TZP0; Q9D8A0; Q9D8D2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=CDK-activating kinase assembly factor MAT1;
DE   AltName: Full=CDK7/cyclin-H assembly factor;
DE   AltName: Full=Menage a trois;
DE   AltName: Full=RING finger protein MAT1;
DE   AltName: Full=p35;
DE   AltName: Full=p36;
GN   Name=Mnat1; Synonyms=Mat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7553872; DOI=10.1016/0092-8674(95)90233-3;
RA   Fisher R.P., Jin P., Chamberlin H.M., Morgan D.O.;
RT   "Alternative mechanisms of CAK assembly require an assembly factor or an
RT   activating kinase.";
RL   Cell 83:47-57(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; U35249; AAA91741.1; -; mRNA.
DR   EMBL; AK008134; BAB25483.1; -; mRNA.
DR   EMBL; AK008249; BAB25556.1; -; mRNA.
DR   EMBL; AK155859; BAE33464.1; -; mRNA.
DR   EMBL; AK157721; BAE34168.1; -; mRNA.
DR   EMBL; BC089023; AAH89023.1; -; mRNA.
DR   EMBL; BC115630; AAI15631.1; -; mRNA.
DR   CCDS; CCDS49087.1; -.
DR   PIR; A57235; A57235.
DR   RefSeq; NP_032638.2; NM_008612.2.
DR   AlphaFoldDB; P51949; -.
DR   SMR; P51949; -.
DR   BioGRID; 201456; 2.
DR   ComplexPortal; CPX-3268; Cyclin-dependent protein kinase-activating kinase complex.
DR   IntAct; P51949; 1.
DR   STRING; 10090.ENSMUSP00000021523; -.
DR   iPTMnet; P51949; -.
DR   PhosphoSitePlus; P51949; -.
DR   SwissPalm; P51949; -.
DR   EPD; P51949; -.
DR   jPOST; P51949; -.
DR   MaxQB; P51949; -.
DR   PaxDb; 10090-ENSMUSP00000021523; -.
DR   PeptideAtlas; P51949; -.
DR   ProteomicsDB; 295698; -.
DR   Pumba; P51949; -.
DR   Antibodypedia; 34; 301 antibodies from 35 providers.
DR   DNASU; 17420; -.
DR   Ensembl; ENSMUST00000021523.7; ENSMUSP00000021523.7; ENSMUSG00000021103.13.
DR   GeneID; 17420; -.
DR   KEGG; mmu:17420; -.
DR   UCSC; uc007nwe.1; mouse.
DR   AGR; MGI:106207; -.
DR   CTD; 4331; -.
DR   MGI; MGI:106207; Mnat1.
DR   VEuPathDB; HostDB:ENSMUSG00000021103; -.
DR   eggNOG; KOG3800; Eukaryota.
DR   GeneTree; ENSGT00390000002319; -.
DR   HOGENOM; CLU_048466_0_1_1; -.
DR   InParanoid; P51949; -.
DR   OMA; QGLYYTA; -.
DR   OrthoDB; 9088at2759; -.
DR   PhylomeDB; P51949; -.
DR   TreeFam; TF106124; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   BioGRID-ORCS; 17420; 22 hits in 119 CRISPR screens.
DR   ChiTaRS; Mnat1; mouse.
DR   PRO; PR:P51949; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P51949; Protein.
DR   Bgee; ENSMUSG00000021103; Expressed in hindlimb bud and 259 other cell types or tissues.
DR   ExpressionAtlas; P51949; baseline and differential.
DR   GO; GO:0070516; C:CAK-ERCC2 complex; ISO:MGI.
DR   GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; ISO:MGI.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007512; P:adult heart development; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:MGI.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR   CDD; cd16517; RING-HC_MAT1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   NCBIfam; TIGR00570; cdk7; 1.
DR   PANTHER; PTHR12683; CDK-ACTIVATING KINASE ASSEMBLY FACTOR MAT1; 1.
DR   PANTHER; PTHR12683:SF13; CDK-ACTIVATING KINASE ASSEMBLY FACTOR MAT1; 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   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; P51949; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; 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_0000055933"
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:0000250|UniProtKB:P51948"
FT   MOD_RES         51
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P51948"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        15
FT                   /note="R -> P (in Ref. 2; BAB25483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="I -> F (in Ref. 2; BAB25483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="N -> K (in Ref. 2; BAB25483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139..140
FT                   /note="KL -> NV (in Ref. 2; BAB25483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="R -> Q (in Ref. 1; AAA91741)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  35848 MW;  C72CD43175D69499 CRC64;
     MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG TPLRKSNFRV
     QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE EVEEIVFNLT NNVDLENTKK
     KMEIYQKENK DVIQKNKLKL TREQEELEEA LEVERQEHEQ RRLFIQKEEE LQQALKRKNK
     QAFLDELESS DLPVALLLAQ HKDRSTQLEM QLEKPRSMKP VTFSTGIKMG QQISLAPIQK
     LEEALYEYQP LQIETCGPQV PEQELLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA
     FSGLFWQPR
//