SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51949

- MAT1_MOUSE

UniProt

P51949 - MAT1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
CDK-activating kinase assembly factor MAT1
Gene
Mnat1, Mat1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 5045RING-type
Add
BLAST

GO - Molecular functioni

  1. DNA-dependent ATPase activity Source: Ensembl
  2. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl
  3. protein binding Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. G1/S transition of mitotic cell cycle Source: Ensembl
  3. adult heart development Source: MGI
  4. negative regulation of apoptotic process Source: Ensembl
  5. positive regulation of smooth muscle cell proliferation Source: Ensembl
  6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. protein phosphorylation Source: GOC
  8. regulation of transcription, DNA-templated Source: MGI
  9. response to calcium ion Source: MGI
  10. transcription from RNA polymerase II promoter Source: UniProtKB
  11. ventricular system development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_203462. Formation of the Early Elongation Complex.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
CDK-activating kinase assembly factor MAT1
Alternative name(s):
CDK7/cyclin-H assembly factor
Menage a trois
RING finger protein MAT1
p35
p36
Gene namesi
Name:Mnat1
Synonyms:Mat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:106207. Mnat1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. holo TFIIH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309CDK-activating kinase assembly factor MAT1
PRO_0000055933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei51 – 511Phosphothreonine By similarity
Modified residuei279 – 2791Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51949.
PaxDbiP51949.
PRIDEiP51949.

PTM databases

PhosphoSiteiP51949.

Expressioni

Gene expression databases

BgeeiP51949.
CleanExiMM_MNAT1.
GenevestigatoriP51949.

Interactioni

Subunit structurei

Associates primarily with CDK7 and cyclin H to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor.

Protein-protein interaction databases

IntActiP51949. 2 interactions.
MINTiMINT-4101287.
STRINGi10090.ENSMUSP00000021523.

Structurei

3D structure databases

ProteinModelPortaliP51949.
SMRiP51949. Positions 1-65.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati142 – 16120UIM
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5220.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiQ14BS9.
KOiK10842.
OMAiETCGPQV.
OrthoDBiEOG71VST2.
PhylomeDBiP51949.
TreeFamiTF106124.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR003903. Ubiquitin-int_motif.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR12683. PTHR12683. 1 hit.
PfamiPF06391. MAT1. 1 hit.
[Graphical view]
PIRSFiPIRSF003338. MAT1_metazoa. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00570. cdk7. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51949-1 [UniParc]FASTAAdd to Basket

« Hide

MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG    50
TPLRKSNFRV QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE 100
EVEEIVFNLT NNVDLENTKK KMEIYQKENK DVIQKNKLKL TREQEELEEA 150
LEVERQEHEQ RRLFIQKEEE LQQALKRKNK QAFLDELESS DLPVALLLAQ 200
HKDRSTQLEM QLEKPRSMKP VTFSTGIKMG QQISLAPIQK LEEALYEYQP 250
LQIETCGPQV PEQELLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA 300
FSGLFWQPR 309
Length:309
Mass (Da):35,848
Last modified:October 18, 2001 - v2
Checksum:iC72CD43175D69499
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151R → P in BAB25483. 1 Publication
Sequence conflicti74 – 741I → F in BAB25483. 1 Publication
Sequence conflicti117 – 1171N → K in BAB25483. 1 Publication
Sequence conflicti139 – 1402KL → NV in BAB25483. 1 Publication
Sequence conflicti162 – 1621R → Q in AAA91741. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35249 mRNA. Translation: AAA91741.1.
AK008134 mRNA. Translation: BAB25483.1.
AK008249 mRNA. Translation: BAB25556.1.
AK155859 mRNA. Translation: BAE33464.1.
AK157721 mRNA. Translation: BAE34168.1.
BC089023 mRNA. Translation: AAH89023.1.
BC115630 mRNA. Translation: AAI15631.1.
CCDSiCCDS49087.1.
PIRiA57235.
RefSeqiNP_032638.2. NM_008612.2.
UniGeneiMm.246750.

Genome annotation databases

EnsembliENSMUST00000021523; ENSMUSP00000021523; ENSMUSG00000021103.
GeneIDi17420.
KEGGimmu:17420.
UCSCiuc007nwe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35249 mRNA. Translation: AAA91741.1 .
AK008134 mRNA. Translation: BAB25483.1 .
AK008249 mRNA. Translation: BAB25556.1 .
AK155859 mRNA. Translation: BAE33464.1 .
AK157721 mRNA. Translation: BAE34168.1 .
BC089023 mRNA. Translation: AAH89023.1 .
BC115630 mRNA. Translation: AAI15631.1 .
CCDSi CCDS49087.1.
PIRi A57235.
RefSeqi NP_032638.2. NM_008612.2.
UniGenei Mm.246750.

3D structure databases

ProteinModelPortali P51949.
SMRi P51949. Positions 1-65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51949. 2 interactions.
MINTi MINT-4101287.
STRINGi 10090.ENSMUSP00000021523.

PTM databases

PhosphoSitei P51949.

Proteomic databases

MaxQBi P51949.
PaxDbi P51949.
PRIDEi P51949.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021523 ; ENSMUSP00000021523 ; ENSMUSG00000021103 .
GeneIDi 17420.
KEGGi mmu:17420.
UCSCi uc007nwe.1. mouse.

Organism-specific databases

CTDi 4331.
MGIi MGI:106207. Mnat1.

Phylogenomic databases

eggNOGi COG5220.
GeneTreei ENSGT00390000002319.
HOGENOMi HOG000189680.
HOVERGENi HBG001144.
InParanoidi Q14BS9.
KOi K10842.
OMAi ETCGPQV.
OrthoDBi EOG71VST2.
PhylomeDBi P51949.
TreeFami TF106124.

Enzyme and pathway databases

Reactomei REACT_203462. Formation of the Early Elongation Complex.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

NextBioi 292038.
PROi P51949.
SOURCEi Search...

Gene expression databases

Bgeei P51949.
CleanExi MM_MNAT1.
Genevestigatori P51949.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR003903. Ubiquitin-int_motif.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
PANTHERi PTHR12683. PTHR12683. 1 hit.
Pfami PF06391. MAT1. 1 hit.
[Graphical view ]
PIRSFi PIRSF003338. MAT1_metazoa. 1 hit.
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00570. cdk7. 1 hit.
PROSITEi PS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase."
    Fisher R.P., Jin P., Chamberlin H.M., Morgan D.O.
    Cell 83:47-57(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Small intestine.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiMAT1_MOUSE
AccessioniPrimary (citable) accession number: P51949
Secondary accession number(s): Q14BS9
, Q3TZP0, Q9D8A0, Q9D8D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: September 3, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi