dbPTM

CDK16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDK16_HUMAN
UniProt AC	Q00536
Protein Name	Cyclin-dependent kinase 16
Gene Name	CDK16
Organism	Homo sapiens (Human).
Sequence Length	496
Subcellular Localization	Cytoplasm. Cytoplasmic vesicle, secretory vesicle. Cell membrane Peripheral membrane protein Cytoplasmic side. Cell junction, synapse, synaptosome. Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY.
Protein Description	Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro)..
Protein Sequence	MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	KKIKRQLSMTLRGGR HHHHHHHHCHHCCCC	11.03	30266825
14	Phosphorylation	IKRQLSMTLRGGRGI HHHHHHCHHCCCCCC	15.21	30266825
19	Methylation	SMTLRGGRGIDKTNG HCHHCCCCCCCCCCC	41.54	-
24	Phosphorylation	GGRGIDKTNGAPEQI CCCCCCCCCCCCCCC	34.83	30624053
30 (in isoform 2)	Phosphorylation	-	33.71	-
30	Phosphorylation	KTNGAPEQIGLDESG CCCCCCCCCCCCCCC	33.71	-
36	Phosphorylation	EQIGLDESGGGGGSD CCCCCCCCCCCCCCC	42.26	25159151
42	Phosphorylation	ESGGGGGSDPGEAPT CCCCCCCCCCCCCCC	43.86	25159151
58	Phosphorylation	AAPGELRSARGPLSS CCCCCHHHCCCCCCC	34.64	19369195
64	Phosphorylation	RSARGPLSSAPEIVH HHCCCCCCCCCCHHC	27.82	30266825
65	Phosphorylation	SARGPLSSAPEIVHE HCCCCCCCCCCHHCC	56.37	30266825
78	Phosphorylation	HEDLKMGSDGESDQA CCHHCCCCCCCCCCC	38.66	22167270
82	Phosphorylation	KMGSDGESDQASATS CCCCCCCCCCCCCCC	40.32	22167270
86	Phosphorylation	DGESDQASATSSDEV CCCCCCCCCCCCCCC	26.84	22167270
88	Phosphorylation	ESDQASATSSDEVQS CCCCCCCCCCCCCCC	26.69	22167270
89	Phosphorylation	SDQASATSSDEVQSP CCCCCCCCCCCCCCC	35.19	22167270
90	Phosphorylation	DQASATSSDEVQSPV CCCCCCCCCCCCCCC	33.17	22167270
95	Phosphorylation	TSSDEVQSPVRVRMR CCCCCCCCCCCHHCC	30.45	29255136
108	Acetylation	MRNHPPRKISTEDIN CCCCCCCCCCHHHHH	46.94	19828321
110	Phosphorylation	NHPPRKISTEDINKR CCCCCCCCHHHHHHH	28.87	27273156
111	Phosphorylation	HPPRKISTEDINKRL CCCCCCCHHHHHHHH	40.94	23401153
116	Ubiquitination	ISTEDINKRLSLPAD CCHHHHHHHHCCCCC	55.86	-
116	Phosphorylation	ISTEDINKRLSLPAD CCHHHHHHHHCCCCC	55.86	27251275
116	Acetylation	ISTEDINKRLSLPAD CCHHHHHHHHCCCCC	55.86	19828331
119	Phosphorylation	EDINKRLSLPADIRL HHHHHHHCCCCCCCC	36.02	29255136
130	Phosphorylation	DIRLPEGYLEKLTLN CCCCCCCHHHHHCCC	15.27	28152594
133	Ubiquitination	LPEGYLEKLTLNSPI CCCCHHHHHCCCCCC	44.15	21890473
135	Phosphorylation	EGYLEKLTLNSPIFD CCHHHHHCCCCCCCC	34.65	30266825
138	Phosphorylation	LEKLTLNSPIFDKPL HHHHCCCCCCCCCCH	23.61	22322096
139	Phosphorylation	EKLTLNSPIFDKPLS HHHCCCCCCCCCCHH	30.14	27251275
143	Ubiquitination	LNSPIFDKPLSRRLR CCCCCCCCCHHHHHH	36.79	21890473
146	Phosphorylation	PIFDKPLSRRLRRVS CCCCCCHHHHHHHCC	24.71	30266825
152	Phosphorylation	LSRRLRRVSLSEIGF HHHHHHHCCHHHHCC	5.66	27251275
153	Phosphorylation	SRRLRRVSLSEIGFG HHHHHHCCHHHHCCC	25.11	29255136
155	Phosphorylation	RLRRVSLSEIGFGKL HHHHCCHHHHCCCCH	21.47	29255136
164	Phosphorylation	IGFGKLETYIKLDKL HCCCCHHEEEEEEEC	40.77	24719451
167	Ubiquitination	GKLETYIKLDKLGEG CCHHEEEEEEECCCC	39.97	21890473
169	Phosphorylation	LETYIKLDKLGEGTY HHEEEEEEECCCCEE	38.85	24719451
175	Phosphorylation	LDKLGEGTYATVYKG EEECCCCEEEEEECC	12.99	29255136
176	Phosphorylation	DKLGEGTYATVYKGK EECCCCEEEEEECCC	15.90	27273156
178	Phosphorylation	LGEGTYATVYKGKSK CCCCEEEEEECCCCC	17.60	29255136
180	Phosphorylation	EGTYATVYKGKSKLT CCEEEEEECCCCCCC	15.07	29255136
183	Acetylation	YATVYKGKSKLTDNL EEEEECCCCCCCCCE	40.02	25953088
184	Phosphorylation	ATVYKGKSKLTDNLV EEEECCCCCCCCCEE	41.38	24719451
185	Phosphorylation	TVYKGKSKLTDNLVA EEECCCCCCCCCEEE	59.91	27251275
185	Acetylation	TVYKGKSKLTDNLVA EEECCCCCCCCCEEE	59.91	25953088
193	Phosphorylation	LTDNLVALKEIRLEH CCCCEEEEEHHHCCC	3.89	24719451
194	Ubiquitination	TDNLVALKEIRLEHE CCCEEEEEHHHCCCC	41.16	21890473
207	Ubiquitination	HEEGAPCTAIREVSL CCCCCCCCHHHHHHH	24.86	21890473
207	Phosphorylation	HEEGAPCTAIREVSL CCCCCCCCHHHHHHH	24.86	28857561
212	Phosphorylation	PCTAIREVSLLKDLK CCCHHHHHHHHHHHH	3.34	24719451
213	Phosphorylation	CTAIREVSLLKDLKH CCHHHHHHHHHHHHC	24.19	24719451
216	Ubiquitination	IREVSLLKDLKHANI HHHHHHHHHHHCCCE	67.33	-
217	Ubiquitination	REVSLLKDLKHANIV HHHHHHHHHHCCCEE	62.00	21890473
227	Phosphorylation	HANIVTLHDIIHTEK CCCEEEHHHHHHCCC	18.17	24719451
229	Phosphorylation	NIVTLHDIIHTEKSL CEEEHHHHHHCCCHH	1.41	24719451
238	Phosphorylation	HTEKSLTLVFEYLDK HCCCHHHHHHHHHCH	5.15	24719451
241	Ubiquitination	KSLTLVFEYLDKDLK CHHHHHHHHHCHHHH	37.39	21890473
250	Phosphorylation	LDKDLKQYLDDCGNI HCHHHHHHHHHHCCC	15.54	24719451
268	Ubiquitination	HNVKLFLFQLLRGLA HHHHHHHHHHHHHHH	3.64	21890473
288	Ubiquitination	KVLHRDLKPQNLLIN CHHCCCCCHHCEEEC	49.17	-
301	Ubiquitination	INERGELKLADFGLA ECCCCCEEEHHHHCC	37.01	21890473
319	Phosphorylation	SIPTKTYSNEVVTLW CCCCCCCCCCEEEEE	31.57	12154078
380	Phosphorylation	FIFRILGTPTEETWP HHHHHHCCCCCCCCC	24.48	-
391	Phosphorylation	ETWPGILSNEEFKTY CCCCCCCCCHHHHHC	40.03	-
425	Ubiquitination	DGADLLTKLLQFEGR CHHHHHHHHHHHCCC	47.36	-
455	Ubiquitination	SLGERIHKLPDTTSI HHHHHHHHCCCCCEE	60.38	21890473
466	Ubiquitination	TTSIFALKEIQLQKE CCEEEEEEEHHHHHH	49.71	21890473
472	Ubiquitination	LKEIQLQKEASLRSS EEEHHHHHHHHHHCC	64.93	-
478	Phosphorylation	QKEASLRSSSMPDSG HHHHHHHCCCCCCCC	31.87	23186163
479	Phosphorylation	KEASLRSSSMPDSGR HHHHHHCCCCCCCCC	24.99	23186163
480	Phosphorylation	EASLRSSSMPDSGRP HHHHHCCCCCCCCCC	35.26	25159151
529	Ubiquitination	---------------------------------------- ----------------------------------------		21890473
540	Ubiquitination	--------------------------------------------------- ---------------------------------------------------		21890473
553	Phosphorylation	---------------------------------------------------------------- ----------------------------------------------------------------		27251275
554	Phosphorylation	----------------------------------------------------------------- -----------------------------------------------------------------		24719451

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
12	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
12	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
12	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
12	S	Phosphorylation	Kinase	BRSK2	Q8IWQ3	Uniprot
95	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
95	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
95	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
110	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
110	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
110	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
119	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
119	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
119	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
138	S	Phosphorylation	Kinase	CDK2	P24941	PSP
153	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
153	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
153	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
153	S	Phosphorylation		18669648
Phosphorylation at Ser-153 inhibits kinase activity.

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 CDK16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD5R1_HUMAN	CDK5R1	physical	12084709
S10AA_HUMAN	S100A10	physical	9197417
1433Z_HUMAN	YWHAZ	physical	9197417
1433F_HUMAN	YWHAH	physical	9197417
1433T_HUMAN	YWHAQ	physical	9197417
A4_HUMAN	APP	physical	21832049
CSK22_HUMAN	CSNK2A2	physical	23602568
PP2AB_HUMAN	PPP2CB	physical	23602568
2ABA_HUMAN	PPP2R2A	physical	23602568
CSK2B_HUMAN	CSNK2B	physical	23602568
ZBT14_HUMAN	ZBTB14	physical	25416956
APBP2_HUMAN	APPBP2	physical	25416956
ATRIP_HUMAN	ATRIP	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
CCYL1_HUMAN	CCNYL1	physical	25852190
KPYM_HUMAN	PKM	physical	25852190
1433E_HUMAN	YWHAE	physical	25852190
1433Z_HUMAN	YWHAZ	physical	25852190
CCYL1_HUMAN	CCNYL1	physical	26186194
CDK17_HUMAN	CDK17	physical	26186194
CDK18_HUMAN	CDK18	physical	26186194
2ABD_HUMAN	PPP2R2D	physical	26186194
ICK_HUMAN	ICK	physical	26186194
BRCA1_HUMAN	BRCA1	physical	26186194
SNX27_HUMAN	SNX27	physical	26186194
I20L2_HUMAN	ISG20L2	physical	26496610
CCYL1_HUMAN	CCNYL1	physical	26496610
CDK17_HUMAN	CDK17	physical	28514442
CDK18_HUMAN	CDK18	physical	28514442
CCYL1_HUMAN	CCNYL1	physical	28514442
ICK_HUMAN	ICK	physical	28514442
CCNY_HUMAN	CCNY	physical	28514442
CSK22_HUMAN	CSNK2A2	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
T2FA_HUMAN	GTF2F1	physical	28514442
MCMBP_HUMAN	MCMBP	physical	28514442
KCTD3_HUMAN	KCTD3	physical	27173435
KI13B_HUMAN	KIF13B	physical	27173435
ZBT21_HUMAN	ZBTB21	physical	27173435
GGYF1_HUMAN	GIGYF1	physical	27173435
LRFN1_HUMAN	LRFN1	physical	27173435
SRGP2_HUMAN	SRGAP2	physical	27173435
SI1L1_HUMAN	SIPA1L1	physical	27173435
LIMA1_HUMAN	LIMA1	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
TESK2_HUMAN	TESK2	physical	27173435
DCLK1_HUMAN	DCLK1	physical	27173435
SRS12_HUMAN	SRSF12	physical	27173435
SYDE1_HUMAN	SYDE1	physical	27173435
AGAP1_HUMAN	AGAP1	physical	27173435
F110B_HUMAN	FAM110B	physical	27173435
UBP21_HUMAN	USP21	physical	27173435
AN34A_HUMAN	ANKRD34A	physical	27173435
FA53C_HUMAN	FAM53C	physical	27173435
F110A_HUMAN	FAM110A	physical	27173435
TBC25_HUMAN	TBC1D25	physical	27173435
MAST3_HUMAN	MAST3	physical	27173435
HDAC4_HUMAN	HDAC4	physical	27173435
RAB3I_HUMAN	RAB3IP	physical	27173435
TIAM1_HUMAN	TIAM1	physical	27173435
NADK_HUMAN	NADK	physical	27173435
M3K21_HUMAN	KIAA1804	physical	27173435
NF1_HUMAN	NF1	physical	27173435
CBY1_HUMAN	CBY1	physical	27173435
NGAP_HUMAN	RASAL2	physical	27173435
MELK_HUMAN	MELK	physical	27173435
CING_HUMAN	CGN	physical	27173435
PKHA7_HUMAN	PLEKHA7	physical	27173435
AFAD_HUMAN	MLLT4	physical	27173435
DEP1B_HUMAN	DEPDC1B	physical	27173435
SH3B4_HUMAN	SH3BP4	physical	27173435
KIF1C_HUMAN	KIF1C	physical	27173435
PKHA5_HUMAN	PLEKHA5	physical	27173435

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 CDK16_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-12; THR-14; SER-36;SER-42; SER-65; SER-78; SER-82; SER-86; THR-88; SER-89; SER-90;SER-95; SER-110; SER-119; THR-135; SER-138; SER-153; SER-155; SER-478AND SER-480, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.	19413330 [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-138; SER-153 ANDSER-155, AND MASS 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-12; SER-36; SER-42;SER-65; SER-78; SER-82; SER-95; SER-110; SER-119; SER-138; SER-153 ANDSER-480, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-138 ANDSER-153, AND MASS SPECTROMETRY.	17192257 [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 SER-119 AND SER-153, ANDMASS SPECTROMETRY.	17081983 [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-175, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-176, AND MASSSPECTROMETRY.	18083107 [Abstract]

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