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P51949 (MAT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Mnat1
Synonyms:Mat1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 RING-type zinc finger.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

adult heart development

Inferred from mutant phenotype PubMed 17276355. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: GOC

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 17276355. Source: MGI

response to calcium ion

Inferred from mutant phenotype PubMed 17276355. Source: MGI

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

ventricular system development

Inferred from mutant phenotype PubMed 17276355. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

holo TFIIH complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA-dependent ATPase activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 17276355. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309CDK-activating kinase assembly factor MAT1
PRO_0000055933

Regions

Repeat142 – 16120UIM
Zinc finger6 – 5045RING-type

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue511Phosphothreonine By similarity
Modified residue2791Phosphoserine By similarity

Experimental info

Sequence conflict151R → P in BAB25483. Ref.2
Sequence conflict741I → F in BAB25483. Ref.2
Sequence conflict1171N → K in BAB25483. Ref.2
Sequence conflict139 – 1402KL → NV in BAB25483. Ref.2
Sequence conflict1621R → Q in AAA91741. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51949 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: C72CD43175D69499

FASTA30935,848
        10         20         30         40         50         60 
MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG TPLRKSNFRV 

        70         80         90        100        110        120 
QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE EVEEIVFNLT NNVDLENTKK 

       130        140        150        160        170        180 
KMEIYQKENK DVIQKNKLKL TREQEELEEA LEVERQEHEQ RRLFIQKEEE LQQALKRKNK 

       190        200        210        220        230        240 
QAFLDELESS DLPVALLLAQ HKDRSTQLEM QLEKPRSMKP VTFSTGIKMG QQISLAPIQK 

       250        260        270        280        290        300 
LEEALYEYQP LQIETCGPQV PEQELLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA 


FSGLFWQPR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS49087.1.
PIRA57235.
RefSeqNP_032638.2. NM_008612.2.
UniGeneMm.246750.

3D structure databases

ProteinModelPortalP51949.
SMRP51949. Positions 1-65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP51949. 2 interactions.
MINTMINT-4101287.
STRING10090.ENSMUSP00000021523.

PTM databases

PhosphoSiteP51949.

Proteomic databases

MaxQBP51949.
PaxDbP51949.
PRIDEP51949.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021523; ENSMUSP00000021523; ENSMUSG00000021103.
GeneID17420.
KEGGmmu:17420.
UCSCuc007nwe.1. mouse.

Organism-specific databases

CTD4331.
MGIMGI:106207. Mnat1.

Phylogenomic databases

eggNOGCOG5220.
GeneTreeENSGT00390000002319.
HOGENOMHOG000189680.
HOVERGENHBG001144.
InParanoidQ14BS9.
KOK10842.
OMAETCGPQV.
OrthoDBEOG71VST2.
PhylomeDBP51949.
TreeFamTF106124.

Gene expression databases

BgeeP51949.
CleanExMM_MNAT1.
GenevestigatorP51949.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR015877. 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]
PANTHERPTHR12683. PTHR12683. 1 hit.
PfamPF06391. MAT1. 1 hit.
[Graphical view]
PIRSFPIRSF003338. MAT1_metazoa. 1 hit.
SMARTSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsTIGR00570. cdk7. 1 hit.
PROSITEPS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292038.
PROP51949.
SOURCESearch...

Entry information

Entry nameMAT1_MOUSE
AccessionPrimary (citable) accession number: P51949
Secondary accession number(s): Q14BS9 expand/collapse secondary AC list , Q3TZP0, Q9D8A0, Q9D8D2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot