dbPTM

CCNY_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNY_HUMAN
UniProt AC	Q8ND76
Protein Name	Cyclin-Y
Gene Name	CCNY
Organism	Homo sapiens (Human).
Sequence Length	341
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Isoform 3: Nucleus.
Protein Description	Positive regulatory subunit of the cyclin-dependent kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway. Recruits CDK16 to the plasma membrane. Isoform 3 might play a role in the activation of MYC-mediated transcription..
Protein Sequence	MGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNMEFNPSDHPRASTIFLSKSQTDVREKRKSLFINHHPPGQIARKYSSCSTIFLDDSTVSQPNLKYTIKCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLSRERAHKLEAISRLCEDKYKDLRRSARKRSASADNLTLPRWSPAIIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGNTTSCCV ------CCCCCCCCC	39.94	-
2	Myristoylation	------MGNTTSCCV ------CCCCCCCCC	39.94	19524571
10	Phosphorylation	NTTSCCVSSSPKLRR CCCCCCCCCCHHHHH	15.93	27251275
11	Phosphorylation	TTSCCVSSSPKLRRN CCCCCCCCCHHHHHC	30.20	28985074
12 (in isoform 3)	Phosphorylation	-	20.67	30153514
12	Phosphorylation	TSCCVSSSPKLRRNA CCCCCCCCHHHHHCH	20.67	27251275
18 (in isoform 3)	Ubiquitination	-	35.25	21890473
18	Ubiquitination	SSPKLRRNAHSRLES CCHHHHHCHHHHHHH	35.25	21890473
19 (in isoform 3)	Phosphorylation	-	10.54	-
21	Phosphorylation	KLRRNAHSRLESYRP HHHHCHHHHHHHHCC	35.83	21955146
25	Phosphorylation	NAHSRLESYRPDTDL CHHHHHHHHCCCCCC	30.91	29255136
26	Phosphorylation	AHSRLESYRPDTDLS HHHHHHHHCCCCCCC	19.45	29255136
30	Phosphorylation	LESYRPDTDLSREDT HHHHCCCCCCCCCCC	41.33	21955146
33	Phosphorylation	YRPDTDLSREDTGCN HCCCCCCCCCCCCCC	36.11	21955146
37	Phosphorylation	TDLSREDTGCNLQHI CCCCCCCCCCCCCCC	38.59	26657352
45	Phosphorylation	GCNLQHISDRENIDD CCCCCCCCCCCCCCC	28.61	30266825
46 (in isoform 3)	Phosphorylation	-	62.40	-
48 (in isoform 3)	Phosphorylation	-	64.62	-
66	Phosphorylation	PSDHPRASTIFLSKS CCCCCCCCEEEEECC	24.26	30266825
67	Phosphorylation	SDHPRASTIFLSKSQ CCCCCCCEEEEECCC	18.11	30266825
71	Phosphorylation	RASTIFLSKSQTDVR CCCEEEEECCCCHHH	21.36	23401153
72 (in isoform 1)	Ubiquitination	-	49.05	21890473
72	Ubiquitination	ASTIFLSKSQTDVRE CCEEEEECCCCHHHH	49.05	-
73	Phosphorylation	STIFLSKSQTDVREK CEEEEECCCCHHHHH	34.63	23401153
75	Phosphorylation	IFLSKSQTDVREKRK EEEECCCCHHHHHHH	43.48	26846344
83	Phosphorylation	DVREKRKSLFINHHP HHHHHHHHHHHCCCC	32.33	29255136
98	Phosphorylation	PGQIARKYSSCSTIF CCHHHHHHCCCCEEE	10.56	30266825
99	Phosphorylation	GQIARKYSSCSTIFL CHHHHHHCCCCEEEE	28.09	23401153
99 (in isoform 3)	Phosphorylation	-	28.09	-
100	Phosphorylation	QIARKYSSCSTIFLD HHHHHHCCCCEEEEC	14.70	30266825
102	Phosphorylation	ARKYSSCSTIFLDDS HHHHCCCCEEEECCC	26.87	23401153
103	Phosphorylation	RKYSSCSTIFLDDST HHHCCCCEEEECCCC	21.78	30266825
109	Phosphorylation	STIFLDDSTVSQPNL CEEEECCCCCCCCCH	30.30	23927012
110	Phosphorylation	TIFLDDSTVSQPNLK EEEECCCCCCCCCHH	31.04	23927012
112	Phosphorylation	FLDDSTVSQPNLKYT EECCCCCCCCCHHHH	39.75	23403867
118	Phosphorylation	VSQPNLKYTIKCVAL CCCCCHHHHHHHHHH	19.50	28270605
119	Phosphorylation	SQPNLKYTIKCVALA CCCCHHHHHHHHHHH	16.63	28270605
153	Phosphorylation	DENLHPLSKSEVPPD CCCCCCCCCCCCCCC	38.29	20068231
161	Phosphorylation	KSEVPPDYDKHNPEQ CCCCCCCCCCCCHHH	32.44	27642862
169	Malonylation	DKHNPEQKQIYRFVR CCCCHHHHHHHHHHH	36.68	26320211
237	Phosphorylation	QAVWNVDYCQILKDI CCCCCCCHHHHHCCC	5.08	28796482
268	Phosphorylation	QFNINVPSSVYAKYY CCCCCCCCHHHHHHE	28.31	24043423
269	Phosphorylation	FNINVPSSVYAKYYF CCCCCCCHHHHHHEE	17.05	24043423
270 (in isoform 3)	Phosphorylation	-	6.72	-
271	Phosphorylation	INVPSSVYAKYYFDL CCCCCHHHHHHEEEH	10.18	24043423
272 (in isoform 3)	Phosphorylation	-	7.39	-
277 (in isoform 3)	Phosphorylation	-	25.67	-
280	Phosphorylation	KYYFDLRSLAEANNL HHEEEHHHHHHHCCC	38.95	25850435
288	Phosphorylation	LAEANNLSFPLEPLS HHHHCCCCCCCCCCC	27.26	24794231
295	Phosphorylation	SFPLEPLSRERAHKL CCCCCCCCHHHHHHH	42.69	24794231
301	Ubiquitination	LSRERAHKLEAISRL CCHHHHHHHHHHHHH	47.22	-
312	Acetylation	ISRLCEDKYKDLRRS HHHHHHHHHHHHHHH	31.72	27452117
319	Phosphorylation	KYKDLRRSARKRSAS HHHHHHHHHHHHHCC	26.45	27282143
324	Phosphorylation	RRSARKRSASADNLT HHHHHHHHCCCCCCC	29.61	22167270
326	Phosphorylation	SARKRSASADNLTLP HHHHHHCCCCCCCCC	37.08	19664994
331	Phosphorylation	SASADNLTLPRWSPA HCCCCCCCCCCCCCC	40.76	29255136
336	Phosphorylation	NLTLPRWSPAIIS-- CCCCCCCCCCCCC--	13.01	22199227
341	Phosphorylation	RWSPAIIS------- CCCCCCCC-------	28.23	29514088

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
67	T	Phosphorylation	Kinase	CDK14	O94921	Uniprot
71	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
73	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
83	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
288	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
295	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
326	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
336	S	Phosphorylation	Kinase	CDK16	Q00536	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
71	S	Phosphorylation	24794231
Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination.
71	S	ubiquitylation	24794231
Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination.
73	S	Phosphorylation	24794231
Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination.
73	S	ubiquitylation	24794231
Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination.

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 CCNY_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK14_HUMAN	CDK14	physical	19524571
CUL1_HUMAN	CUL1	physical	24794231
CDK14_HUMAN	CDK14	physical	24794231

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 CCNY_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Cell cycle control of wnt receptor activation."; Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.; Dev. Cell 17:788-799(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITHCDK14 AND LRP6, UBIQUITINATION, MYRISTOYLATION AT GLY-2, ANDMUTAGENESIS OF GLY-2.	20059949 [Abstract]
"Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1."; Jiang M., Gao Y., Yang T., Zhu X., Chen J.; FEBS Lett. 583:2171-2178(2009). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULARLOCATION, INTERACTION WITH CDK14, MYRISTOYLATION AT GLY-2, ANDMUTAGENESIS OF GLY-2 AND ASN-3.	19524571 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-326, 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 SER-326, AND MASSSPECTROMETRY.	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-102 AND SER-326, ANDMASS SPECTROMETRY.	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-25, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASSSPECTROMETRY.	18088087 [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-326, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASSSPECTROMETRY.	15302935 [Abstract]

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