MAT1_HUMAN - dbPTM
MAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAT1_HUMAN
UniProt AC P51948
Protein Name CDK-activating kinase assembly factor MAT1
Gene Name MNAT1
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Nucleus.
Protein Description 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..
Protein Sequence MDDQGCPRCKTTKYRNPSLKLMVNVCGHTLCESCVDLLFVRGAGNCPECGTPLRKSNFRVQLFEDPTVDKEVEIRKKVLKIYNKREEDFPSLREYNDFLEEVEEIVFNLTNNVDLDNTKKKMEIYQKENKDVIQKNKLKLTREQEELEEALEVERQENEQRRLFIQKEEQLQQILKRKNKQAFLDELESSDLPVALLLAQHKDRSTQLEMQLEKPKPVKPVTFSTGIKMGQHISLAPIHKLEEALYEYQPLQIETYGPHVPELEMLGRLGYLNHVRAASPQDLAGGYTSSLACHRALQDAFSGLFWQPS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MDDQGCPR
-------CCCCCCCC		13.3019413330
11PhosphorylationQGCPRCKTTKYRNPS
CCCCCCCCCCCCCCC		31.9525072903
12PhosphorylationGCPRCKTTKYRNPSL
CCCCCCCCCCCCCCH		16.1525072903
14PhosphorylationPRCKTTKYRNPSLKL
CCCCCCCCCCCCHHH		17.33-
18PhosphorylationTTKYRNPSLKLMVNV
CCCCCCCCHHHHEEC		41.50-
51PhosphorylationGNCPECGTPLRKSNF
CCCCCCCCCCCCCCC		30.7025159151
70UbiquitinationFEDPTVDKEVEIRKK
CCCCCCCHHHHHHHH		60.36-
80MalonylationEIRKKVLKIYNKREE
HHHHHHHHHHHHCHH		46.2426320211
167UbiquitinationQRRLFIQKEEQLQQI
HHHHHHCHHHHHHHH		59.4021890473
167UbiquitinationQRRLFIQKEEQLQQI
HHHHHHCHHHHHHHH		59.4021890473
176UbiquitinationEQLQQILKRKNKQAF
HHHHHHHHHHCHHHH		64.06-
180UbiquitinationQILKRKNKQAFLDEL
HHHHHHCHHHHHHHH		46.14-
189PhosphorylationAFLDELESSDLPVAL
HHHHHHHHCCHHHHH		41.6025627689
190PhosphorylationFLDELESSDLPVALL
HHHHHHHCCHHHHHH		33.5225627689
202UbiquitinationALLLAQHKDRSTQLE
HHHHHHCCCCCCHHH		42.64-
205PhosphorylationLAQHKDRSTQLEMQL
HHHCCCCCCHHHHHH		30.5517192257
219UbiquitinationLEKPKPVKPVTFSTG
HCCCCCCCCEEECCC		42.15-
219AcetylationLEKPKPVKPVTFSTG
HCCCCCCCCEEECCC		42.1526051181
222PhosphorylationPKPVKPVTFSTGIKM
CCCCCCEEECCCCCC		22.0120068231
224PhosphorylationPVKPVTFSTGIKMGQ
CCCCEEECCCCCCCC		19.1620068231
225PhosphorylationVKPVTFSTGIKMGQH
CCCEEECCCCCCCCC		38.4420068231
234PhosphorylationIKMGQHISLAPIHKL
CCCCCCEECCCCHHH		19.1625159151
279PhosphorylationLNHVRAASPQDLAGG
CHHHCCCCHHHHCCC		23.3123927012
287PhosphorylationPQDLAGGYTSSLACH
HHHHCCCHHHHHHHH		11.5228464451
288PhosphorylationQDLAGGYTSSLACHR
HHHCCCHHHHHHHHH		18.3423403867
289PhosphorylationDLAGGYTSSLACHRA
HHCCCHHHHHHHHHH		18.1823403867
290PhosphorylationLAGGYTSSLACHRAL
HCCCHHHHHHHHHHH		16.5223403867
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MAT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MAT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTA1_HUMANMTA1physical
12527756
ESR1_HUMANESR1physical
12527756
HPS6_HUMANHPS6physical
16169070
CSN6_HUMANCOPS6physical
16169070
RBM48_HUMANRBM48physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
MCM7_HUMANMCM7physical
11056214
ERCC3_HUMANERCC3physical
8692842
TF2H2_HUMANGTF2H2physical
8692842
BRCA1_HUMANBRCA1physical
15282296
TF2H3_HUMANGTF2H3physical
22939629
TF2H1_HUMANGTF2H1physical
22939629
TF2H4_HUMANGTF2H4physical
22939629
RPB1_HUMANPOLR2Aphysical
16327805
SPT5H_HUMANSUPT5Hphysical
16327805
TRIM2_HUMANTRIM2physical
22493164
TRIM9_HUMANTRIM9physical
22493164
TRIML_HUMANTRIML1physical
22493164
MKRN3_HUMANMKRN3physical
22493164
TRI31_HUMANTRIM31physical
22493164
TRI34_HUMANTRIM34physical
22493164
BRCA1_HUMANBRCA1physical
22493164
RNF32_HUMANRNF32physical
22493164
TRI17_HUMANTRIM17physical
22493164
RBX2_HUMANRNF7physical
22493164
RNF41_HUMANRNF41physical
22493164
RO52_HUMANTRIM21physical
22493164
TRI39_HUMANTRIM39physical
22493164
TRIM5_HUMANTRIM5physical
22493164
MDM4_HUMANMDM4physical
22493164
TRI26_HUMANTRIM26physical
22493164
BEX3_HUMANNGFRAP1physical
21988832
CDK7_HUMANCDK7physical
26186194
ERCC2_HUMANERCC2physical
26186194
CCNH_HUMANCCNHphysical
26186194
CDK7_HUMANCDK7physical
26344197
SFR1_HUMANSFR1physical
26344197
RPB1_HUMANPOLR2Aphysical
15530371
CCNH_HUMANCCNHphysical
28514442
CDK7_HUMANCDK7physical
28514442
ERCC2_HUMANERCC2physical
28514442
ERCC2_HUMANERCC2physical
26340423
TF2H2_HUMANGTF2H2physical
26340423
CDK7_HUMANCDK7physical
26340423
TF2H1_HUMANGTF2H1physical
26340423
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-205 AND SER-279,AND MASS SPECTROMETRY.

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