CC14A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CC14A_HUMAN
• UniProt AC: Q9UNH5
• Protein Name: Dual specificity protein phosphatase CDC14A
• Gene Name: CDC14A
• Organism: Homo sapiens (Human).
• Sequence Length: 594
• Subcellular Localization: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, spindle . Cell projection, kinocilium . Centrosomal during interphase, released into the cytoplasm at the
• Protein Description: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis..
• Protein Sequence: MAAESGELIGACEFMKDRLYFATLRNRPKSTVNTHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTCFDQRKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSNPPYLPFRDASFGNCTYNLTILDCLQGIRKGLQHGFFDFETFDVDEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKHNVTAVVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEEKQASLWVQGDIFRSKLKNRPSSEGSINKILSGLDDMSIGGNLSKTQNMERFGEDNLEDDDVEMKNGITQGDKLRALKSQRQPRTSPSCAFRSDDTKGHPRAVSQPFRLSSSLQGSAVTLKTSKMALSPSATAKRINRTSLSSGATVRSFSINSRLASSLGNLNAATDDPENKKTSSSSKAGFTASPFTNLLNGSSQPTTRNYPELNNNQYNRSSNSNGGNLNSPPGPHSAKTEEHTTILRPSYTGLSSSSARFLSRSIPSLQSEYVHY

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
20	Phosphorylation	EFMKDRLYFATLRNR HHHHHCEEEEECCCC	7.64	23612710
69	Ubiquitination	RYCCKLNKKLKSYSL HHHHHHCHHHHHCCC	70.67	-
72	Ubiquitination	CKLNKKLKSYSLSRK HHHCHHHHHCCCCCC	57.11	-
77	Phosphorylation	KLKSYSLSRKKIVHY HHHHCCCCCCCEEEE	35.79	24260401
84	Phosphorylation	SRKKIVHYTCFDQRK CCCCEEEEECCCHHH	8.36	24719451
85	Phosphorylation	RKKIVHYTCFDQRKR CCCEEEEECCCHHHH	7.57	24719451
192	Phosphorylation	PGKFLAFSGPHPKSK CCCEEEECCCCCHHH	45.89	26074081
198	Phosphorylation	FSGPHPKSKIENGYP ECCCCCHHHCCCCCC	43.23	26074081
222	Phosphorylation	YFKKHNVTAVVRLNK HHHHCCEEEEEEECH	21.03	27794612
347	Phosphorylation	SKLKNRPSSEGSINK HHHCCCCCCCCHHHH	37.47	27251275
348 (in isoform 2)	Phosphorylation	-	48.97	27251275
348	Phosphorylation	KLKNRPSSEGSINKI HHCCCCCCCCHHHHH	48.97	23312004
351	Phosphorylation	NRPSSEGSINKILSG CCCCCCCHHHHHHHC	20.95	27251275
357	Phosphorylation	GSINKILSGLDDMSI CHHHHHHHCCCCCCC	40.56	23403867
363	Phosphorylation	LSGLDDMSIGGNLSK HHCCCCCCCCCCCCC	25.69	23403867
369 (in isoform 3)	Phosphorylation	-	37.34	24719451
371 (in isoform 3)	Phosphorylation	-	23.07	24719451
381 (in isoform 3)	Phosphorylation	-	40.82	24719451
411	Phosphorylation	SQRQPRTSPSCAFRS HCCCCCCCCCCCCCC	18.98	-
422	Methylation	AFRSDDTKGHPRAVS CCCCCCCCCCCCCCC	63.32	-
429	Phosphorylation	KGHPRAVSQPFRLSS CCCCCCCCCCEECCH	31.02	-
435	Phosphorylation	VSQPFRLSSSLQGSA CCCCEECCHHCCCCE	17.39	27732954
436	Phosphorylation	SQPFRLSSSLQGSAV CCCEECCHHCCCCEE	39.39	29978859
437	Phosphorylation	QPFRLSSSLQGSAVT CCEECCHHCCCCEEE	22.72	29978859
441	Phosphorylation	LSSSLQGSAVTLKTS CCHHCCCCEEEEECC	13.45	27732954
444	Phosphorylation	SLQGSAVTLKTSKMA HCCCCEEEEECCCCC	23.43	27732954
447	Phosphorylation	GSAVTLKTSKMALSP CCEEEEECCCCCCCC	36.37	23403867
448	Phosphorylation	SAVTLKTSKMALSPS CEEEEECCCCCCCCC	20.88	23403867
453	Phosphorylation	KTSKMALSPSATAKR ECCCCCCCCCHHCHH	13.79	23186163
455	Phosphorylation	SKMALSPSATAKRIN CCCCCCCCHHCHHCC	34.57	23186163
457	Phosphorylation	MALSPSATAKRINRT CCCCCCHHCHHCCCC	36.73	23186163
465	Phosphorylation	AKRINRTSLSSGATV CHHCCCCCCCCCCEE	24.02	27251275
465 (in isoform 2)	Phosphorylation	-	24.02	27251275
474	Phosphorylation	SSGATVRSFSINSRL CCCCEEEEEEHHHHH	21.00	27251275
476	Phosphorylation	GATVRSFSINSRLAS CCEEEEEEHHHHHHH	23.31	27251275
476 (in isoform 2)	Phosphorylation	-	23.31	27251275
483	Phosphorylation	SINSRLASSLGNLNA EHHHHHHHHHCCCCC	30.59	23401153
484 (in isoform 2)	Phosphorylation	-	34.39	27251275
484	Phosphorylation	INSRLASSLGNLNAA HHHHHHHHHCCCCCC	34.39	30266825
492	Phosphorylation	LGNLNAATDDPENKK HCCCCCCCCCCCCCC	38.23	30266825
499	Acetylation	TDDPENKKTSSSSKA CCCCCCCCCCCCCCC	66.28	21339330
500	Phosphorylation	DDPENKKTSSSSKAG CCCCCCCCCCCCCCC	35.14	23312004
501	Phosphorylation	DPENKKTSSSSKAGF CCCCCCCCCCCCCCC	36.78	23312004
502	Phosphorylation	PENKKTSSSSKAGFT CCCCCCCCCCCCCCC	43.81	23312004
503	Phosphorylation	ENKKTSSSSKAGFTA CCCCCCCCCCCCCCC	35.31	23312004
504	Phosphorylation	NKKTSSSSKAGFTAS CCCCCCCCCCCCCCC	28.59	23312004
505	Acetylation	KKTSSSSKAGFTASP CCCCCCCCCCCCCCC	55.25	21339330
542	Phosphorylation	QYNRSSNSNGGNLNS CCCCCCCCCCCCCCC	38.51	28348404
549	Phosphorylation	SNGGNLNSPPGPHSA CCCCCCCCCCCCCCC	35.32	-
583	Phosphorylation	SARFLSRSIPSLQSE HHHHHHHCCHHHHCC	35.16	23401153
586	Phosphorylation	FLSRSIPSLQSEYVH HHHHCCHHHHCCCCC	37.05	23403867
589	Phosphorylation	RSIPSLQSEYVHY-- HCCHHHHCCCCCC--	35.87	23403867
591	Phosphorylation	IPSLQSEYVHY---- CHHHHCCCCCC----	9.58	23403867
594	Phosphorylation	LQSEYVHY------- HHCCCCCC-------	15.37	23186163

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
411	S	Phosphorylation	Kinase	CDK1	P06493	PSP
453	S	Phosphorylation	Kinase	CDK1	P06493	PSP
549	S	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BRAP	Q7Z569	PMID:19152073

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CC14A_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CC14A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FZR1_HUMAN	FZR1	physical	11598127
BRAP_HUMAN	BRAP	physical	19152073
KI20A_HUMAN	KIF20A	physical	15263015
RPB1_HUMAN	POLR2A	physical	22020438
MPIP2_HUMAN	CDC25B	physical	20956543
ACM1_HUMAN	CHRM1	physical	22117071
CDC6_HUMAN	CDC6	physical	22117071
PLK1_HUMAN	PLK1	physical	19390576
CUL7_HUMAN	CUL7	physical	27880917
DAPK3_HUMAN	DAPK3	physical	27880917
TRI36_HUMAN	TRIM36	physical	27880917
CP135_HUMAN	CEP135	physical	27880917
C2CD3_HUMAN	C2CD3	physical	27880917
CKAP2_HUMAN	CKAP2	physical	27880917
IFT57_HUMAN	IFT57	physical	27880917
JCAD_HUMAN	KIAA1462	physical	27880917
POC5_HUMAN	POC5	physical	27880917
EFL1_HUMAN	EFTUD1	physical	27880917
MTUS1_HUMAN	MTUS1	physical	27880917
CE290_HUMAN	CEP290	physical	27880917
CSPP1_HUMAN	CSPP1	physical	27880917
NIN_HUMAN	NIN	physical	27880917
SPICE_HUMAN	SPICE1	physical	27880917
CE162_HUMAN	CEP162	physical	27880917
IF2B2_HUMAN	IGF2BP2	physical	27880917
K1328_HUMAN	KIAA1328	physical	27880917
ODFP2_HUMAN	ODF2	physical	27880917
LUZP1_HUMAN	LUZP1	physical	27880917
TDRD3_HUMAN	TDRD3	physical	27880917
CNTRB_HUMAN	CNTROB	physical	27880917
PKHA7_HUMAN	PLEKHA7	physical	27880917
TOP3B_HUMAN	TOP3B	physical	27880917
MARE2_HUMAN	MAPRE2	physical	27880917
CE350_HUMAN	CEP350	physical	27880917
CCD61_HUMAN	CCDC61	physical	27880917
NFL_HUMAN	NEFL	physical	27880917
CCD77_HUMAN	CCDC77	physical	27880917
MYCB2_HUMAN	MYCBP2	physical	27880917
PRC2A_HUMAN	PRRC2A	physical	27880917
K1C18_HUMAN	KRT18	physical	27880917
MPP9_HUMAN	MPHOSPH9	physical	27880917
PP6R1_HUMAN	PPP6R1	physical	27880917
CP131_HUMAN	CEP131	physical	27880917
TBC31_HUMAN	TBC1D31	physical	27880917
ZO1_HUMAN	TJP1	physical	27880917

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.