Skip Header

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

CDK-activating kinase assembly factor MAT1

Gene

Mnat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. adult heart development Source: MGI
  2. DNA repair Source: GO_Central
  3. G1/S transition of mitotic cell cycle Source: Ensembl
  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: MGI
  7. protein phosphorylation Source: MGI
  8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: GO_Central
  9. regulation of transcription, DNA-templated Source: MGI
  10. regulation of transcription from RNA polymerase II promoter Source: MGI
  11. response to calcium ion Source: MGI
  12. transcription from RNA polymerase II promoter Source: UniProtKB
  13. 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_279019. Dual incision reaction in TC-NER.
REACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_289448. Cyclin D associated events in G1.
REACT_289837. RNA Polymerase I Transcription Termination.
REACT_296099. RNA Polymerase I Promoter Escape.
REACT_296420. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_296832. Dual incision reaction in GG-NER.
REACT_302527. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_308057. Formation of the Early Elongation Complex.
REACT_314261. Formation of incision complex in GG-NER.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_321479. Cyclin A:Cdk2-associated events at S phase entry.
REACT_321519. Cyclin E associated events during G1/S transition.
REACT_326102. Formation of RNA Pol II elongation complex.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_338828. mRNA Capping.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_350574. RNA Polymerase I Transcription Initiation.
REACT_354877. RNA Polymerase I Chain 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 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:106207. Mnat1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. holo TFIIH complex Source: UniProtKB
  3. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309CDK-activating kinase assembly factor MAT1PRO_0000055933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei51 – 511PhosphothreonineBy similarity
Modified residuei279 – 2791PhosphoserineBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 16120UIMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 UIM (ubiquitin-interacting motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 5045RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5220.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiP51949.
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

        10         20         30         40         50
MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG
60 70 80 90 100
TPLRKSNFRV QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE
110 120 130 140 150
EVEEIVFNLT NNVDLENTKK KMEIYQKENK DVIQKNKLKL TREQEELEEA
160 170 180 190 200
LEVERQEHEQ RRLFIQKEEE LQQALKRKNK QAFLDELESS DLPVALLLAQ
210 220 230 240 250
HKDRSTQLEM QLEKPRSMKP VTFSTGIKMG QQISLAPIQK LEEALYEYQP
260 270 280 290 300
LQIETCGPQV PEQELLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA

FSGLFWQPR
Length:309
Mass (Da):35,848
Last modified:October 18, 2001 - v2
Checksum:iC72CD43175D69499
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151R → P in BAB25483 (PubMed:16141072).Curated
Sequence conflicti74 – 741I → F in BAB25483 (PubMed:16141072).Curated
Sequence conflicti117 – 1171N → K in BAB25483 (PubMed:16141072).Curated
Sequence conflicti139 – 1402KL → NV in BAB25483 (PubMed:16141072).Curated
Sequence conflicti162 – 1621R → Q in AAA91741 (PubMed:7553872).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP51949.
SMRiP51949. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP51949.

Proteomic databases

MaxQBiP51949.
PaxDbiP51949.
PRIDEiP51949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4331.
MGIiMGI:106207. Mnat1.

Phylogenomic databases

eggNOGiCOG5220.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiP51949.
KOiK10842.
OMAiETCGPQV.
OrthoDBiEOG71VST2.
PhylomeDBiP51949.
TreeFamiTF106124.

Enzyme and pathway databases

ReactomeiREACT_279019. Dual incision reaction in TC-NER.
REACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_289448. Cyclin D associated events in G1.
REACT_289837. RNA Polymerase I Transcription Termination.
REACT_296099. RNA Polymerase I Promoter Escape.
REACT_296420. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_296832. Dual incision reaction in GG-NER.
REACT_302527. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_308057. Formation of the Early Elongation Complex.
REACT_314261. Formation of incision complex in GG-NER.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_321479. Cyclin A:Cdk2-associated events at S phase entry.
REACT_321519. Cyclin E associated events during G1/S transition.
REACT_326102. Formation of RNA Pol II elongation complex.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_338828. mRNA Capping.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_350574. RNA Polymerase I Transcription Initiation.
REACT_354877. RNA Polymerase I Chain Elongation.

Miscellaneous databases

NextBioi292038.
PROiP51949.
SOURCEiSearch...

Gene expression databases

BgeeiP51949.
CleanExiMM_MNAT1.
GenevestigatoriP51949.

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]
ProtoNetiSearch...

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(1994) [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(2004) [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(2003) [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: April 1, 2015
This is version 125 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.