dbPTM

KKCC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KKCC1_HUMAN
UniProt AC	Q8N5S9
Protein Name	Calcium/calmodulin-dependent protein kinase kinase 1
Gene Name	CAMKK1
Organism	Homo sapiens (Human).
Sequence Length	505
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death..
Protein Sequence	MEGGPAVCCQDPRAELVERVAAIDVTHLEEADGGPEPTRNGVDPPPRARAASVIPGSTSRLLPARPSLSARKLSLQERPAGSYLEAQAGPYATGPASHISPRAWRRPTIESHHVAISDAEDCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQAAQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFSEEQARLYLRDVILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDFILALHRKIKNEPVVFPEEPEISEELKDLILKMLDKNPETRIGVPDIKLHPWVTKNGEEPLPSEEEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNLLVKEGFGEGGKSPELPGVQEDEAAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Phosphorylation	PPRARAASVIPGSTS CCCHHHCCCCCCCHH	21.42	23927012
57	Phosphorylation	AASVIPGSTSRLLPA HCCCCCCCHHHCCCC	20.18	23927012
58	Phosphorylation	ASVIPGSTSRLLPAR CCCCCCCHHHCCCCC	24.63	23927012
59	Phosphorylation	SVIPGSTSRLLPARP CCCCCCHHHCCCCCC	23.72	23927012
67	Phosphorylation	RLLPARPSLSARKLS HCCCCCCCCCHHHCC	29.42	25159151
69	Phosphorylation	LPARPSLSARKLSLQ CCCCCCCCHHHCCCC	30.30	25159151
72	Ubiquitination	RPSLSARKLSLQERP CCCCCHHHCCCCCCC	41.99	-
74	Phosphorylation	SLSARKLSLQERPAG CCCHHHCCCCCCCCC	30.92	23401153
78	Asymmetric dimethylarginine	RKLSLQERPAGSYLE HHCCCCCCCCCCCEE	17.26	-
78	Methylation	RKLSLQERPAGSYLE HHCCCCCCCCCCCEE	17.26	-
82	Phosphorylation	LQERPAGSYLEAQAG CCCCCCCCCEEECCC	28.75	23927012
83	Phosphorylation	QERPAGSYLEAQAGP CCCCCCCCEEECCCC	13.98	28450419
91	Phosphorylation	LEAQAGPYATGPASH EEECCCCCCCCCHHH	18.84	28450419
93	Phosphorylation	AQAGPYATGPASHIS ECCCCCCCCCHHHCC	37.54	23927012
97	Phosphorylation	PYATGPASHISPRAW CCCCCCHHHCCCCHH	25.20	23927012
100	Phosphorylation	TGPASHISPRAWRRP CCCHHHCCCCHHCCC	11.69	25159151
102	Methylation	PASHISPRAWRRPTI CHHHCCCCHHCCCCC	39.74	-
108	Phosphorylation	PRAWRRPTIESHHVA CCHHCCCCCCCCCEE	35.25	10187789
111	Phosphorylation	WRRPTIESHHVAISD HCCCCCCCCCEEECC	18.29	28348404
277	Ubiquitination	KIVHRDIKPSNLLLG EEECCCCCHHHEEEC	46.84	-
443	Phosphorylation	NSVRLIPSWTTVILV HCCEECCCHHHHHHH	30.02	20044836
446	Phosphorylation	RLIPSWTTVILVKSM EECCCHHHHHHHHHH	10.17	30576142
452	Phosphorylation	TTVILVKSMLRKRSF HHHHHHHHHHHHCCC	18.64	30576142
458	Phosphorylation	KSMLRKRSFGNPFEP HHHHHHCCCCCCCCH	40.31	23927012
469	Methylation	PFEPQARREERSMSA CCCHHHHHHHHCCCC	53.82	-
472	Methylation	PQARREERSMSAPGN HHHHHHHHCCCCCCC	32.67	-
473	Phosphorylation	QARREERSMSAPGNL HHHHHHHCCCCCCCE	21.99	30243723
475	Phosphorylation	RREERSMSAPGNLLV HHHHHCCCCCCCEEE	32.34	25159151
492	Phosphorylation	GFGEGGKSPELPGVQ CCCCCCCCCCCCCCC	27.21	25159151
496	Phosphorylation	GGKSPELPGVQEDEA CCCCCCCCCCCCCHH	38.97	27251275
505	Phosphorylation	VQEDEAAS------- CCCCHHCC-------	48.04	20068231
513	Phosphorylation	--------------- ---------------		27251275
513 (in isoform 2)	Phosphorylation	-		11574070

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
74	S	Phosphorylation	Kinase	PKACA	P17612	PSP
74	S	Phosphorylation	Kinase	PRKACA	P36887	GPS
108	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
108	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
475	S	Phosphorylation	Kinase	PKACA	P17612	PSP
475	S	Phosphorylation	Kinase	PRKACA	P36887	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
458	S	Phosphorylation		18691976
Phosphorylation of Ser-458 is blocked upon binding to Ca(2+)/calmodulin.

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 KKCC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
AAPK1_HUMAN	PRKAA1	physical	20801214
ANXA7_HUMAN	ANXA7	physical	26496610
KC1E_HUMAN	CSNK1E	physical	26496610
DDB1_HUMAN	DDB1	physical	26496610
H33_HUMAN	H3F3A	physical	26496610
NTH_HUMAN	NTHL1	physical	26496610
RS10_HUMAN	RPS10	physical	26496610
SAFB2_HUMAN	SAFB2	physical	26496610
NSA2_HUMAN	NSA2	physical	26496610
NEPRO_HUMAN	C3orf17	physical	26496610
FBXL6_HUMAN	FBXL6	physical	26496610
RNZ2_HUMAN	ELAC2	physical	26496610
K2013_HUMAN	KIAA2013	physical	26496610
BRNP1_HUMAN	BRINP1	physical	26496610
RUVB2_HUMAN	RUVBL2	physical	28514442
RUVB1_HUMAN	RUVBL1	physical	28514442

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 KKCC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-505, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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 SER-492, AND MASSSPECTROMETRY.	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-74; SER-458 AND SER-492,AND MASS SPECTROMETRY.	18691976 [Abstract]

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