dbPTM

CP110_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CP110_HUMAN
UniProt AC	O43303
Protein Name	Centriolar coiled-coil protein of 110 kDa
Gene Name	CCP110
Organism	Homo sapiens (Human).
Sequence Length	1012
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body . Recruited early and then associates with the growing dis
Protein Description	Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation. [PubMed: 17719545 17681131]
Protein Sequence	MEEYEKFCEKSLARIQEASLSTESFLPAQSESISLIRFHGVAILSPLLNIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQVRKAPNASDFDQWEMETVYSNSEVRNLNVPATFPNSFPSHTEHSTAAKLDKIAGILPLDNEDQCKTDGIDLARDSEGFNSPKQCDSSNISHVENEAFPKTSSATPQETLISDGPFSVNEQQDLPLLAEVIPDPYVMSLQNLMKKSKEYIEREQSRRSLRGSINRIVNESHLDKEHDAVEVADCVKEKGQLTGKHCVSVIPDKPSLNKSNVLLQGASTQASSMSMPVLASFSKVDIPIRTGHPTVLESNSDFKVIPTFVTENNVIKSLTGSYAKLPSPEPSMSPKMHRRRSRTSSACHILINNPINACELSPKGKEQAMDLIIQDTDENTNVPEIMPKLPTDLAGVCSSKVYVGKNTSEVKEDVVLGKSNQVCQSSGNHLENKVTHGLVTVEGQLTSDERGAHIMNSTCAAMPKLHEPYASSQCIASPNFGTVSGLKPASMLEKNCSLQTELNKSYDVKNPSPLLMQNQNTRQQMDTPMVSCGNEQFLDNSFEKVKRRLDLDIDGLQKENCPYVITSGITEQERQHLPEKRYPKGSGFVNKNKMLGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKEIEEQEKMLKEKKAMTAEASELDINNAVELEWRKISDSSLLETMLSQADSLHTSNSNSSGFTNSAMQYSFVSANEAPFYLWGSSTSGLTKLSVTRPFGRAKTRWSQVFSLEIQAKFNKITAVAKGFLTRRLMQTDKLKQLRQTVKDTMEFIRSFQSEAPLKRGIVSAQDASLQERVLAQLRAALYGIHDIFFVMDAAERMSILHHDREVRKEKMLRQMDKMKSPRVALSAATQKSLDRKKYMKAAEMGMPNKKFLVKQNPSETRVLQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Ubiquitination	EYEKFCEKSLARIQE HHHHHHHHHHHHHHH	52.53	-
19	Phosphorylation	LARIQEASLSTESFL HHHHHHHHCCCCCCC	23.31	27251275
21	Phosphorylation	RIQEASLSTESFLPA HHHHHHCCCCCCCCC	27.86	27251275
22	Phosphorylation	IQEASLSTESFLPAQ HHHHHCCCCCCCCCC	40.73	27251275
24	Phosphorylation	EASLSTESFLPAQSE HHHCCCCCCCCCCCC	31.97	27251275
45	Phosphorylation	FHGVAILSPLLNIEK ECHHHHHHHHHCHHH	13.85	28450419
62	Ubiquitination	EMQQEKQKALDVEAR HHHHHHHHHHHHHHH	63.08	24816145
98	Phosphorylation	VRKAPNASDFDQWEM CCCCCCCCCCCCCCE	45.51	-
107	Phosphorylation	FDQWEMETVYSNSEV CCCCCEEEECCCHHH	24.35	29978859
109	Phosphorylation	QWEMETVYSNSEVRN CCCEEEECCCHHHCC	15.00	28796482
110	Phosphorylation	WEMETVYSNSEVRNL CCEEEECCCHHHCCC	29.55	28796482
112	Phosphorylation	METVYSNSEVRNLNV EEEECCCHHHCCCCC	31.37	29978859
138	Ubiquitination	TEHSTAAKLDKIAGI CCCCHHHHHHHHCCC	55.55	29967540
141	Ubiquitination	STAAKLDKIAGILPL CHHHHHHHHCCCCCC	44.91	29967540
155	Ubiquitination	LDNEDQCKTDGIDLA CCCCHHHCCCCCCCC	43.98	29967540
165	Phosphorylation	GIDLARDSEGFNSPK CCCCCCCCCCCCCCC	33.78	23401153
170	Phosphorylation	RDSEGFNSPKQCDSS CCCCCCCCCCCCCCC	31.08	25159151
176	Phosphorylation	NSPKQCDSSNISHVE CCCCCCCCCCCCCCC	32.67	28450419
177	Phosphorylation	SPKQCDSSNISHVEN CCCCCCCCCCCCCCC	25.57	28450419
180	Phosphorylation	QCDSSNISHVENEAF CCCCCCCCCCCCCCC	26.23	23312004
194	Phosphorylation	FPKTSSATPQETLIS CCCCCCCCCCCEEEC	27.70	12361598
247	Phosphorylation	EREQSRRSLRGSINR HHHHHHHHHHHHHHH	22.70	-
251	Phosphorylation	SRRSLRGSINRIVNE HHHHHHHHHHHHHCH	15.40	-
259	Phosphorylation	INRIVNESHLDKEHD HHHHHCHHHCCCCCC	24.93	-
263	Ubiquitination	VNESHLDKEHDAVEV HCHHHCCCCCCHHHH	64.41	29967540
292	Ubiquitination	CVSVIPDKPSLNKSN EEEECCCCCCCCCCC	31.02	29967540
297	Ubiquitination	PDKPSLNKSNVLLQG CCCCCCCCCCEEECC	49.02	29967540
319	Phosphorylation	MSMPVLASFSKVDIP CCCCEEECCCCCCCC	26.37	24719451
337	Phosphorylation	GHPTVLESNSDFKVI CCCCEECCCCCCEEE	37.16	24247654
342	Ubiquitination	LESNSDFKVIPTFVT ECCCCCCEEECEEEC	44.22	32015554
346	Phosphorylation	SDFKVIPTFVTENNV CCCEEECEEECCCCE	21.44	28555341
349	O-linked_Glycosylation	KVIPTFVTENNVIKS EEECEEECCCCEEHH	28.89	28657654
349	Phosphorylation	KVIPTFVTENNVIKS EEECEEECCCCEEHH	28.89	28555341
355	Ubiquitination	VTENNVIKSLTGSYA ECCCCEEHHHHCCCC	34.82	29967540
356	Phosphorylation	TENNVIKSLTGSYAK CCCCEEHHHHCCCCC	21.75	26074081
358	Phosphorylation	NNVIKSLTGSYAKLP CCEEHHHHCCCCCCC	31.04	26074081
360	Phosphorylation	VIKSLTGSYAKLPSP EEHHHHCCCCCCCCC	19.38	26074081
361	Phosphorylation	IKSLTGSYAKLPSPE EHHHHCCCCCCCCCC	14.75	26074081
363	Ubiquitination	SLTGSYAKLPSPEPS HHHCCCCCCCCCCCC	53.34	29967540
366	Phosphorylation	GSYAKLPSPEPSMSP CCCCCCCCCCCCCCH	52.94	29255136
370	Phosphorylation	KLPSPEPSMSPKMHR CCCCCCCCCCHHHHH	30.17	29255136
372	Phosphorylation	PSPEPSMSPKMHRRR CCCCCCCCHHHHHHC	26.21	29255136
380	Phosphorylation	PKMHRRRSRTSSACH HHHHHHCCCCCCCHH	37.79	28450419
382	Phosphorylation	MHRRRSRTSSACHIL HHHHCCCCCCCHHHH	28.42	27794612
383	Phosphorylation	HRRRSRTSSACHILI HHHCCCCCCCHHHHH	18.15	27794612
384	Phosphorylation	RRRSRTSSACHILIN HHCCCCCCCHHHHHC	34.01	27794612
400	Phosphorylation	PINACELSPKGKEQA CCCCCCCCCCCHHHH	11.41	23401153
437	Phosphorylation	TDLAGVCSSKVYVGK CCCCCCCCCEEEECC	30.68	28348404
438	Phosphorylation	DLAGVCSSKVYVGKN CCCCCCCCEEEECCC	22.48	28348404
439	Ubiquitination	LAGVCSSKVYVGKNT CCCCCCCEEEECCCH	22.69	29967540
441	Phosphorylation	GVCSSKVYVGKNTSE CCCCCEEEECCCHHH	13.76	-
444	Ubiquitination	SSKVYVGKNTSEVKE CCEEEECCCHHHCCC	47.19	29967540
446	Phosphorylation	KVYVGKNTSEVKEDV EEEECCCHHHCCCCE	29.74	20860994
450	Ubiquitination	GKNTSEVKEDVVLGK CCCHHHCCCCEEECC	44.11	32015554
457	Ubiquitination	KEDVVLGKSNQVCQS CCCEEECCCCCCCCC	41.91	29967540
464	Phosphorylation	KSNQVCQSSGNHLEN CCCCCCCCCCCHHCC	34.78	28348404
465	Phosphorylation	SNQVCQSSGNHLENK CCCCCCCCCCHHCCC	20.10	28348404
508	Phosphorylation	MPKLHEPYASSQCIA CCCCCCCCCCCCEEE	19.01	-
510	Phosphorylation	KLHEPYASSQCIASP CCCCCCCCCCEEECC	18.33	29978859
511	Phosphorylation	LHEPYASSQCIASPN CCCCCCCCCEEECCC	22.39	29978859
516	Phosphorylation	ASSQCIASPNFGTVS CCCCEEECCCCCCCC	10.64	29978859
521	Phosphorylation	IASPNFGTVSGLKPA EECCCCCCCCCCCHH	13.83	29978859
526	Ubiquitination	FGTVSGLKPASMLEK CCCCCCCCHHHHHHH	41.90	29967540
533	Ubiquitination	KPASMLEKNCSLQTE CHHHHHHHHCCCCCC	60.33	29967540
536	Phosphorylation	SMLEKNCSLQTELNK HHHHHHCCCCCCCCC	32.67	24247654
543	Ubiquitination	SLQTELNKSYDVKNP CCCCCCCCCCCCCCC	64.12	29967540
544	Phosphorylation	LQTELNKSYDVKNPS CCCCCCCCCCCCCCC	26.03	29116813
548	Ubiquitination	LNKSYDVKNPSPLLM CCCCCCCCCCCCCCC	61.31	32015554
551	Phosphorylation	SYDVKNPSPLLMQNQ CCCCCCCCCCCCCCC	37.26	25159151
566	Phosphorylation	NTRQQMDTPMVSCGN CCCCCCCCCCCCCCC	14.13	12361598
570	Phosphorylation	QMDTPMVSCGNEQFL CCCCCCCCCCCHHHC	15.28	28102081
580	Phosphorylation	NEQFLDNSFEKVKRR CHHHCCCCHHHHHHH	34.15	22199227
583	Ubiquitination	FLDNSFEKVKRRLDL HCCCCHHHHHHHHCC	51.55	-
597	Ubiquitination	LDIDGLQKENCPYVI CCCCCCCCCCCCEEE	56.81	29967540
602	Phosphorylation	LQKENCPYVITSGIT CCCCCCCEEEECCCC	13.49	23403867
605	Phosphorylation	ENCPYVITSGITEQE CCCCEEEECCCCHHH	15.74	23403867
606	Phosphorylation	NCPYVITSGITEQER CCCEEEECCCCHHHH	19.64	23403867
609	Phosphorylation	YVITSGITEQERQHL EEEECCCCHHHHCCC	34.83	23403867
623	Ubiquitination	LPEKRYPKGSGFVNK CCCCCCCCCCCCCCC	57.69	29967540
625	Phosphorylation	EKRYPKGSGFVNKNK CCCCCCCCCCCCCCC	34.87	17494752
630	Ubiquitination	KGSGFVNKNKMLGTS CCCCCCCCCCCCCCC	53.28	29967540
636	Phosphorylation	NKNKMLGTSSKESEE CCCCCCCCCCHHHHH	26.35	29759185
637	Phosphorylation	KNKMLGTSSKESEEL CCCCCCCCCHHHHHH	37.30	29759185
638	Phosphorylation	NKMLGTSSKESEELL CCCCCCCCHHHHHHH	40.04	23403867
639	Ubiquitination	KMLGTSSKESEELLK CCCCCCCHHHHHHHH	66.09	29967540
641	Phosphorylation	LGTSSKESEELLKSK CCCCCHHHHHHHHHH	39.86	30278072
646	Ubiquitination	KESEELLKSKMLAFE HHHHHHHHHHHHHHH	61.73	-
648	Acetylation	SEELLKSKMLAFEEM HHHHHHHHHHHHHHH	36.02	25953088
648	Ubiquitination	SEELLKSKMLAFEEM HHHHHHHHHHHHHHH	36.02	29967540
668	Phosphorylation	EQHAQQLSLLIAEQE HHHHHHHHHHHHHHH	19.45	28555341
683	Ubiquitination	REQERLQKEIEEQEK HHHHHHHHHHHHHHH	66.31	-
690	Ubiquitination	KEIEEQEKMLKEKKA HHHHHHHHHHHHHHC	49.58	29967540
699	Phosphorylation	LKEKKAMTAEASELD HHHHHCCCCCHHHCC	26.63	25693802
703	Phosphorylation	KAMTAEASELDINNA HCCCCCHHHCCCCCC	30.14	25693802
785	Phosphorylation	RPFGRAKTRWSQVFS CCCCCCCCCHHHEEE	36.06	24719451
788	Phosphorylation	GRAKTRWSQVFSLEI CCCCCCHHHEEEEEH	17.11	27251275
792	Phosphorylation	TRWSQVFSLEIQAKF CCHHHEEEEEHHHHH	26.66	-
801	Ubiquitination	EIQAKFNKITAVAKG EHHHHHHHHHHHHHH	44.56	29967540
819	Ubiquitination	RRLMQTDKLKQLRQT HHHHCHHHHHHHHHH	62.06	-
821	"N6,N6-dimethyllysine"	LMQTDKLKQLRQTVK HHCHHHHHHHHHHHH	53.69	-
821	Methylation	LMQTDKLKQLRQTVK HHCHHHHHHHHHHHH	53.69	23644510
828	Ubiquitination	KQLRQTVKDTMEFIR HHHHHHHHHHHHHHH	51.36	29967540
836	Phosphorylation	DTMEFIRSFQSEAPL HHHHHHHHHCCCCCC	23.87	28348404
839	Phosphorylation	EFIRSFQSEAPLKRG HHHHHHCCCCCCCCC	33.44	28348404
844	Ubiquitination	FQSEAPLKRGIVSAQ HCCCCCCCCCCCCHH	47.74	33845483
854	Phosphorylation	IVSAQDASLQERVLA CCCHHCCCHHHHHHH	38.58	26471730
906	Phosphorylation	RQMDKMKSPRVALSA HHHHHCCCHHHHHHH	17.91	28258704
912	Phosphorylation	KSPRVALSAATQKSL CCHHHHHHHHHHHHH	13.20	28258704
915	Phosphorylation	RVALSAATQKSLDRK HHHHHHHHHHHHCHH	35.92	29978859
917	Ubiquitination	ALSAATQKSLDRKKY HHHHHHHHHHCHHHH	48.94	32015554
918	Phosphorylation	LSAATQKSLDRKKYM HHHHHHHHHCHHHHH	26.19	24719451
926	Ubiquitination	LDRKKYMKAAEMGMP HCHHHHHHHHHCCCC	41.16	29967540
935	Ubiquitination	AEMGMPNKKFLVKQN HHCCCCCCCEEEECC	38.75	32015554
940	Ubiquitination	PNKKFLVKQNPSETR CCCCEEEECCCCCCC	46.64	33845483
972	Phosphorylation	RQGTPKTSVKGVVQN CCCCCCCCHHHHHCC	28.14	26657352
995	Phosphorylation	VPNRVPVSGVYAGKI CCCCCCCCCEECCCC	19.23	28555341
998	Phosphorylation	RVPVSGVYAGKIQRK CCCCCCEECCCCCCC	17.11	27642862
1001	Acetylation	VSGVYAGKIQRKRPN CCCEECCCCCCCCCC	27.74	25953088
1011	Phosphorylation	RKRPNVATI------ CCCCCCCCC------	23.96	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
45	S	Phosphorylation	Kinase	CDK2	P24941	PSP
98	S	Phosphorylation	Kinase	PLK4	O00444	PSP
170	S	Phosphorylation	Kinase	CDK2	P24941	PSP
194	T	Phosphorylation	Kinase	CDK2	P24941	PSP
366	S	Phosphorylation	Kinase	CDK2	P24941	PSP
372	S	Phosphorylation	Kinase	CDK2	P24941	PSP
400	S	Phosphorylation	Kinase	CDK2	P24941	PSP
516	S	Phosphorylation	Kinase	CDK2	P24941	PSP
566	T	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CCNF	P41002	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CP110_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 CP110_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP97_HUMAN	CEP97	physical	17719545
NEUL4_HUMAN	NEURL4	physical	22441691
CEP76_HUMAN	CEP76	physical	22441691
CEP97_HUMAN	CEP97	physical	22441691
CE290_HUMAN	CEP290	physical	22441691
CEP97_HUMAN	CEP97	physical	22261722
HERC2_HUMAN	HERC2	physical	22261722
ARPC2_HUMAN	ARPC2	physical	22261722
CE290_HUMAN	CEP290	physical	22261722
SNP23_HUMAN	SNAP23	physical	22261722
LYN_HUMAN	LYN	physical	22261722
ARP3_HUMAN	ACTR3	physical	22261722
NEUL4_HUMAN	NEURL4	physical	22261722
FLOT2_HUMAN	FLOT2	physical	22261722
SSA27_HUMAN	SSSCA1	physical	22261722
CAND1_HUMAN	CAND1	physical	22261722
CEP76_HUMAN	CEP76	physical	22261722
G6PI_HUMAN	GPI	physical	22261722
CETN1_HUMAN	CETN1	physical	16760425
UBP33_HUMAN	USP33	physical	23486064
UBP20_HUMAN	USP20	physical	23486064
NEUL4_HUMAN	NEURL4	physical	23486064
CCNF_HUMAN	CCNF	physical	23486064
CEP97_HUMAN	CEP97	physical	23486064
CEP76_HUMAN	CEP76	physical	26638075
CEP97_HUMAN	CEP97	physical	26638075
CRK_HUMAN	CRK	physical	26638075
DVL1_HUMAN	DVL1	physical	26638075
WAC2A_HUMAN	FAM21A	physical	26638075
HAUS6_HUMAN	HAUS6	physical	26638075
IF2B2_HUMAN	IGF2BP2	physical	26638075
MA7D3_HUMAN	MAP7D3	physical	26638075
CND2_HUMAN	NCAPH	physical	26638075
NEDD1_HUMAN	NEDD1	physical	26638075
PCM1_HUMAN	PCM1	physical	26638075
UN45A_HUMAN	UNC45A	physical	26638075
CNDH2_HUMAN	NCAPH2	physical	27173435
CNDG2_HUMAN	NCAPG2	physical	27173435
NEDD1_HUMAN	NEDD1	physical	27173435
SMC2_HUMAN	SMC2	physical	27173435
DCAF1_HUMAN	VPRBP	physical	28242748
CEP78_HUMAN	CEP78	physical	28242748
UBR5_HUMAN	UBR5	physical	28242748
DDB1_HUMAN	DDB1	physical	28242748
DYRK2_HUMAN	DYRK2	physical	28242748

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 CP110_HUMAN

Related Literatures of Post-Translational Modification

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-372, 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-370, 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-366; SER-370 ANDSER-372, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	16964243 [Abstract]