dbPTM

CCNH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNH_HUMAN
UniProt AC	P51946
Protein Name	Cyclin-H
Gene Name	CCNH
Organism	Homo sapiens (Human).
Sequence Length	323
Subcellular Localization	Nucleus.
Protein Description	Regulates CDK7, the catalytic subunit of the 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. Its expression and activity are constant throughout the cell cycle..
Protein Sequence	MYHNSSQKRHWTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEPHEEMTLCKYYEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFNVSSPQFVGNLRESPLGQEKALEQILEYELLLIQQLNFHLIVHNPYRPFEGFLIDLKTRYPILENPEILRKTADDFLNRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLKENRTCLSQLLDIMKSMRNLVKKYEPPRSEEVAVLKQKLERCHSAELALNVITKKRKGYEDDDYVSKKSKHEEEEWTDDDLVESL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MYHNSSQKRHWT ---CCCCCCCCCCCC	22.34	10993082
8	Ubiquitination	MYHNSSQKRHWTFSS CCCCCCCCCCCCCCC	48.45	-
8	2-Hydroxyisobutyrylation	MYHNSSQKRHWTFSS CCCCCCCCCCCCCCC	48.45	-
39	Ubiquitination	CKAVANGKVLPNDPV CEEEECCEECCCCCC	40.17	-
58	Ubiquitination	HEEMTLCKYYEKRLL CCHHHHHHHHHHHHH	54.72	29967540
72	Ubiquitination	LEFCSVFKPAMPRSV HHHHHCCCCCCCCCH	29.70	-
121	Phosphorylation	KVDEFNVSSPQFVGN CCCCCCCCCCCHHCC	37.09	23186163
122	Phosphorylation	VDEFNVSSPQFVGNL CCCCCCCCCCHHCCC	20.59	23186163
132	Phosphorylation	FVGNLRESPLGQEKA HHCCCCCCCCCHHHH	20.99	25159151
136	Ubiquitination	LRESPLGQEKALEQI CCCCCCCHHHHHHHH	57.61	33845483
189	Ubiquitination	ENPEILRKTADDFLN CCHHHHHHHHHHHHH	44.62	33845483
221	Ubiquitination	LTAILSSASRAGITM HHHHHHHHHHCCCCH	10.32	29967540
227	Phosphorylation	SASRAGITMESYLSE HHHHCCCCHHHHHHH	17.61	18767875
233	Phosphorylation	ITMESYLSESLMLKE CCHHHHHHHHHCHHC	19.53	18767875
253	Ubiquitination	SQLLDIMKSMRNLVK HHHHHHHHHHHHHHH	41.24	-
262	Phosphorylation	MRNLVKKYEPPRSEE HHHHHHHHCCCCHHH	28.13	-
274	Acetylation	SEEVAVLKQKLERCH HHHHHHHHHHHHHHH	38.50	25953088
274	Ubiquitination	SEEVAVLKQKLERCH HHHHHHHHHHHHHHH	38.50	29967540
282	Phosphorylation	QKLERCHSAELALNV HHHHHHHHHHHHHHH	27.37	23898821
297	Phosphorylation	ITKKRKGYEDDDYVS HHHHCCCCCCCCCCC	21.15	27642862
302	Phosphorylation	KGYEDDDYVSKKSKH CCCCCCCCCCCCCCC	17.39	28674419
304	Phosphorylation	YEDDDYVSKKSKHEE CCCCCCCCCCCCCCC	28.30	10993082
305	Acetylation	EDDDYVSKKSKHEEE CCCCCCCCCCCCCCC	51.53	26051181
306	Ubiquitination	DDDYVSKKSKHEEEE CCCCCCCCCCCCCCC	58.17	-
307	Phosphorylation	DDYVSKKSKHEEEEW CCCCCCCCCCCCCCC	42.87	30266825
315	Phosphorylation	KHEEEEWTDDDLVES CCCCCCCCCCHHHHC	32.60	19664994
322	Phosphorylation	TDDDLVESL------ CCCHHHHCC------	31.72	25159151

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
5	S	Phosphorylation	Kinase	CDK8	P49336	Uniprot
304	S	Phosphorylation	Kinase	CDK8	P49336	Uniprot
315	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
315	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
315	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
315	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCNH_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 CCNH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSA27_HUMAN	SSSCA1	physical	16189514
PSA1_HUMAN	PSMA1	physical	16189514
MAT1_HUMAN	MNAT1	physical	17353931
RADIL_HUMAN	RADIL	physical	17353931
MAT1_HUMAN	MNAT1	physical	12527756
MTA1_HUMAN	MTA1	physical	12527756
ESR1_HUMAN	ESR1	physical	12527756
MCM7_HUMAN	MCM7	physical	11056214
CDK7_HUMAN	CDK7	physical	8078587
P53_HUMAN	TP53	physical	9840937
CDK7_HUMAN	CDK7	physical	10958691
ERCC3_HUMAN	ERCC3	physical	8692842
ERCC2_HUMAN	ERCC2	physical	8692842
CDK2_HUMAN	CDK2	physical	10393546
RPB2_HUMAN	POLR2B	physical	9334327
CDK7_HUMAN	CDK7	physical	16782892
MAT1_HUMAN	MNAT1	physical	16782892
BRCA1_HUMAN	BRCA1	physical	15282296
CDK7_HUMAN	CDK7	physical	22939629
MAT1_HUMAN	MNAT1	physical	22939629
ERCC2_HUMAN	ERCC2	physical	22939629
TF2H4_HUMAN	GTF2H4	physical	22939629
RPB1_HUMAN	POLR2A	physical	14627702
CDK7_HUMAN	CDK7	physical	9056480
CDK7_HUMAN	CDK7	physical	11113184
CDK2_HUMAN	CDK2	physical	11113184
CDK2_HUMAN	CDK2	physical	15530371
CDK7_HUMAN	CDK7	physical	15328539
MAT1_HUMAN	MNAT1	physical	15328539
CDK8_HUMAN	CDK8	physical	10993082
CCNC_HUMAN	CCNC	physical	10993082
CTBP2_HUMAN	CTBP2	physical	21988832
TRIM8_HUMAN	TRIM8	physical	21988832
GOGA2_HUMAN	GOLGA2	physical	21988832
CSK2B_HUMAN	CSNK2B	physical	21988832
RARB_HUMAN	RARB	physical	21988832
GANAB_HUMAN	GANAB	physical	21988832
ADIP_HUMAN	SSX2IP	physical	21988832
NEDD4_HUMAN	NEDD4	physical	24141722
GOGA2_HUMAN	GOLGA2	physical	25416956
1433S_HUMAN	SFN	physical	25416956
PSA1_HUMAN	PSMA1	physical	25416956
LIPA1_HUMAN	PPFIA1	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
NDC80_HUMAN	NDC80	physical	25416956
SSA27_HUMAN	SSSCA1	physical	25416956
DUS12_HUMAN	DUSP12	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
CC170_HUMAN	CCDC170	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
KLC3_HUMAN	KLC3	physical	25416956
ERCC2_HUMAN	ERCC2	physical	26186194
CDK7_HUMAN	CDK7	physical	26186194
TBC15_HUMAN	TBC1D15	physical	26186194
ERCC3_HUMAN	ERCC3	physical	26186194
ERCC5_HUMAN	ERCC5	physical	26186194
HNRPF_HUMAN	HNRNPF	physical	26344197
MAT1_HUMAN	MNAT1	physical	26344197
RPB1_HUMAN	POLR2A	physical	15530371
CDK7_HUMAN	CDK7	physical	28514442
ERCC5_HUMAN	ERCC5	physical	28514442
ERCC2_HUMAN	ERCC2	physical	28514442
TBC15_HUMAN	TBC1D15	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CCNH_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND SER-322, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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 SER-132; SER-307; THR-315AND SER-322, AND MASS SPECTROMETRY.	18691976 [Abstract]
"TFIIH is negatively regulated by cdk8-containing mediatorcomplexes."; Akoulitchev S., Chuikov S., Reinberg D.; Nature 407:102-106(2000). Cited for: PHOSPHORYLATION AT SER-5 AND SER-304, AND MUTAGENESIS OF SER-5 ANDSER-304.	10993082 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 THR-315, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND MASSSPECTROMETRY.	17081983 [Abstract]