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Overview

Uniprot IDP51948
Protein NameCDK-activating kinase assembly factor MAT1
Gene NameMNAT1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
135 ENKDVIQKNKLKLTR
137 KDVIQKNKLKLTREQ
176 EQLQQILKRKNKQAF
180 QILKRKNKQAFLDEL
80 EIRKKVLKIYNKREE

Function

Component of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). Binds and activates CDK7, the catalytic subunit of CAK (PubMed:41100585). CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression (PubMed:41100585). 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 (PubMed:10024882). Involved in cell cycle control and in RNA transcription by RNA polymerase II (PubMed:10024882)

Protein Sequence

10 MDDQGCPRCK 20 TTKYRNPSLK 30 LMVNVCGHTL 40 CESCVDLLFV 50 RGAGNCPECG 60 TPLRKSNFRV 70 QLFEDPTVDK 80 EVEIRKKVLK 90 IYNKREEDFP 100 SLREYNDFLE 110 EVEEIVFNLT 120 NNVDLDNTKK 130 KMEIYQKENK 140 DVIQKNKLKL 150 TREQEELEEA 160 LEVERQENEQ 170 RRLFIQKEEQ 180 LQQILKRKNK 190 QAFLDELESS 200 DLPVALLLAQ 210 HKDRSTQLEM 220 QLEKPKPVKP 230 VTFSTGIKMG 240 QHISLAPIHK 250 LEEALYEYQP 260 LQIETYGPHV 270 PELEMLGRLG 280 YLNHVRAASP 290 QDLAGGYTSS 300 LACHRALQDA FSGLFWQPS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070516 CAK-ERCC2 complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0000439 transcription factor TFIIH core complex
Cellular Component GO:0005675 transcription factor TFIIH holo complex
Cellular Component GO:0070985 transcription factor TFIIK complex
Molecular Function GO:0061575 cyclin-dependent protein serine/threonine kinase activator activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0000082 G1/S transition of mitotic cell cycle
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0048661 positive regulation of smooth muscle cell proliferation
Biological Process GO:2000045 regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0006367 transcription initiation at RNA polymerase II promoter

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.