dbPTM

CEP72_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEP72_HUMAN
UniProt AC	Q9P209
Protein Name	Centrosomal protein of 72 kDa
Gene Name	CEP72
Organism	Homo sapiens (Human).
Sequence Length	647
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Localizes to the centrosome and centrosome-surrounding particles throughout the cell cycle
Protein Description	Involved in the recruitment of key centrosomal proteins to the centrosome. Provides centrosomal microtubule-nucleation activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles in forming a focused bipolar spindle, which is needed for proper tension generation between sister chromatids. Required for localization of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs). [PubMed: 19536135 Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2]
Protein Sequence	MARAGPRLVLSEEAVRAKSGLGPHRDLAELQSLSIPGTYQEKITHLGHSLMSLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTELVDVDFRLNPVVKVEPDYRLFVVHLLPKLQQLDDRPVRASERKASRLHFASEDSLDSKESVPASLKEGRPHHPRAKCTEALAKQSLVMDADDEAVLNLIAECEWDLGRPPGSTSFSQKGREADSRGSQESRHLLSPQLVQYQCGDSGKQGRETRRSSCRGCCLEKMPWSQLCGELPPLYGAEPEASRAPRPHTYFTPHPDSMDTEDSASSQKLDLSGEMVPGPLPAPGKCRKRRMPVGRFQTFSDQEGLGCPERTHGSSVPKESLSRQDSSESRNGRTLSQPEASETEEQRSRGVTDTREPSPGSHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQSRLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVKSADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQMHWSYQELKKTMALFPHSSASHGGCQAC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Ubiquitination	SEEAVRAKSGLGPHR CHHHHHHHCCCCCCC	34.20	29967540
32	Phosphorylation	RDLAELQSLSIPGTY CCHHHHHHCCCCCCH	36.39	28450419
34	Phosphorylation	LAELQSLSIPGTYQE HHHHHHCCCCCCHHH	31.80	28450419
38	Phosphorylation	QSLSIPGTYQEKITH HHCCCCCCHHHHHHH	19.37	28450419
39	Phosphorylation	SLSIPGTYQEKITHL HCCCCCCHHHHHHHH	22.16	28450419
44	Phosphorylation	GTYQEKITHLGHSLM CCHHHHHHHHHHHHH	23.32	-
49	Phosphorylation	KITHLGHSLMSLTGL HHHHHHHHHHHHHCC	24.78	22210691
57	Ubiquitination	LMSLTGLKSLDLSRN HHHHHCCCCCCCCCC	50.77	-
58	Phosphorylation	MSLTGLKSLDLSRNS HHHHCCCCCCCCCCC	31.96	22210691
62	Phosphorylation	GLKSLDLSRNSLVSL CCCCCCCCCCCCCHH	29.14	-
65	Ubiquitination	SLDLSRNSLVSLEGI CCCCCCCCCCHHHHH	29.10	21890473
78	Ubiquitination	GIQYLTALESLNLYY HHHHHHHHHHHHHHH	3.75	21963094
115 (in isoform 1)	Ubiquitination	-	40.91	21890473
115	Ubiquitination	FRLNPVVKVEPDYRL CCCCCCCEECCCCEE	40.91	27667366
115 (in isoform 2)	Ubiquitination	-	40.91	21890473
130	Ubiquitination	FVVHLLPKLQQLDDR EEHHHHHHHHHCCCC	59.92	-
142	Phosphorylation	DDRPVRASERKASRL CCCCCCHHHHHHHHC	27.63	25159151
153	Phosphorylation	ASRLHFASEDSLDSK HHHCCCCCCCCCCCC	40.78	20873877
156	Phosphorylation	LHFASEDSLDSKESV CCCCCCCCCCCCCCC	29.99	25159151
159	Phosphorylation	ASEDSLDSKESVPAS CCCCCCCCCCCCCCH	43.55	20873877
160	Sumoylation	SEDSLDSKESVPASL CCCCCCCCCCCCCHH	54.39	-
160	Ubiquitination	SEDSLDSKESVPASL CCCCCCCCCCCCCHH	54.39	29967540
160	Sumoylation	SEDSLDSKESVPASL CCCCCCCCCCCCCHH	54.39	-
162	Phosphorylation	DSLDSKESVPASLKE CCCCCCCCCCCHHHC	36.82	20873877
166	Phosphorylation	SKESVPASLKEGRPH CCCCCCCHHHCCCCC	33.63	29083192
168	Ubiquitination	ESVPASLKEGRPHHP CCCCCHHHCCCCCCC	56.48	29967540
178	Ubiquitination	RPHHPRAKCTEALAK CCCCCHHHHHHHHHH	42.86	29967540
217	Ubiquitination	RPPGSTSFSQKGREA CCCCCCCHHHCCCCC	10.19	21963094
226	Phosphorylation	QKGREADSRGSQESR HCCCCCCCCCCHHHH	45.66	26074081
229	Phosphorylation	READSRGSQESRHLL CCCCCCCCHHHHHHC	29.66	26074081
232	Phosphorylation	DSRGSQESRHLLSPQ CCCCCHHHHHHCCHH	19.84	26074081
237	Phosphorylation	QESRHLLSPQLVQYQ HHHHHHCCHHHEEEE	19.57	25159151
243	Phosphorylation	LSPQLVQYQCGDSGK CCHHHEEEECCCCCC	9.78	29632367
248	Phosphorylation	VQYQCGDSGKQGRET EEEECCCCCCCCHHH	32.92	24732914
250	Ubiquitination	YQCGDSGKQGRETRR EECCCCCCCCHHHHH	54.23	29967540
255	Phosphorylation	SGKQGRETRRSSCRG CCCCCHHHHHHCCCC	29.98	23882029
258	Phosphorylation	QGRETRRSSCRGCCL CCHHHHHHCCCCCCC	30.42	23882029
259	Phosphorylation	GRETRRSSCRGCCLE CHHHHHHCCCCCCCC	13.16	23882029
267	Ubiquitination	CRGCCLEKMPWSQLC CCCCCCCCCCHHHHC	37.00	21963094
293	Ubiquitination	EASRAPRPHTYFTPH CHHCCCCCCCCCCCC	24.10	21963094
303	Phosphorylation	YFTPHPDSMDTEDSA CCCCCCCCCCCCCCC	24.02	28555341
309	Phosphorylation	DSMDTEDSASSQKLD CCCCCCCCCCCCCCC	24.66	28555341
314	Ubiquitination	EDSASSQKLDLSGEM CCCCCCCCCCCCCCC	46.01	-
318	Phosphorylation	SSQKLDLSGEMVPGP CCCCCCCCCCCCCCC	32.16	25159151
331	Acetylation	GPLPAPGKCRKRRMP CCCCCCCCCCCCCCC	29.79	25953088
344	Phosphorylation	MPVGRFQTFSDQEGL CCCCCEEECCCCCCC	23.53	28450419
346	Phosphorylation	VGRFQTFSDQEGLGC CCCEEECCCCCCCCC	41.60	22617229
364	Ubiquitination	THGSSVPKESLSRQD CCCCCCCHHHCCCCC	58.75	29967540
364	Sumoylation	THGSSVPKESLSRQD CCCCCCCHHHCCCCC	58.75	-
364	Sumoylation	THGSSVPKESLSRQD CCCCCCCHHHCCCCC	58.75	-
366	Phosphorylation	GSSVPKESLSRQDSS CCCCCHHHCCCCCCC	37.46	28555341
368	Phosphorylation	SVPKESLSRQDSSES CCCHHHCCCCCCCCC	36.86	28102081
372	Phosphorylation	ESLSRQDSSESRNGR HHCCCCCCCCCCCCC	27.89	30576142
373	Phosphorylation	SLSRQDSSESRNGRT HCCCCCCCCCCCCCC	48.13	25159151
375	Phosphorylation	SRQDSSESRNGRTLS CCCCCCCCCCCCCCC	32.75	28102081
380	Phosphorylation	SESRNGRTLSQPEAS CCCCCCCCCCCCCHH	31.96	30108239
382	Phosphorylation	SRNGRTLSQPEASET CCCCCCCCCCCHHHC	42.97	25159151
387	Phosphorylation	TLSQPEASETEEQRS CCCCCCHHHCHHHHH	43.31	30108239
389	Phosphorylation	SQPEASETEEQRSRG CCCCHHHCHHHHHCC	42.18	30576142
394	Phosphorylation	SETEEQRSRGVTDTR HHCHHHHHCCCCCCC	32.83	26074081
398	Phosphorylation	EQRSRGVTDTREPSP HHHHCCCCCCCCCCC	34.18	24732914
400	Phosphorylation	RSRGVTDTREPSPGS HHCCCCCCCCCCCCC	27.80	25159151
404	Phosphorylation	VTDTREPSPGSHSAL CCCCCCCCCCCCCCC	36.82	25159151
407	Phosphorylation	TREPSPGSHSALPGK CCCCCCCCCCCCCCH	20.04	25159151
409	Phosphorylation	EPSPGSHSALPGKKT CCCCCCCCCCCCHHH	32.95	25159151
414	Ubiquitination	SHSALPGKKTALQAA CCCCCCCHHHHHHHH	45.04	29967540
415	Ubiquitination	HSALPGKKTALQAAL CCCCCCHHHHHHHHH	44.97	-
416	Phosphorylation	SALPGKKTALQAALL CCCCCHHHHHHHHHH	35.77	26074081
432	Ubiquitination	TLLDLVDRSWGGCRS HHHHHHHHCCCCHHH	27.16	21963094
439	Phosphorylation	RSWGGCRSLHSNEAF HCCCCHHHCCCCHHH	34.21	20873877
439	Ubiquitination	RSWGGCRSLHSNEAF HCCCCHHHCCCCHHH	34.21	21963094
440	Ubiquitination	SWGGCRSLHSNEAFL CCCCHHHCCCCHHHH	2.38	21963094
442	Phosphorylation	GGCRSLHSNEAFLAQ CCHHHCCCCHHHHHH	41.48	20873877
482	Ubiquitination	GSLALESKSLQSRLA HHHHHHCHHHHHHHH	45.90	21963094
522	Ubiquitination	DLRQHLDKSLEENSR HHHHHHHHHHHHHHH	64.40	29967540
523	Phosphorylation	LRQHLDKSLEENSRL HHHHHHHHHHHHHHH	40.45	22985185
531	Ubiquitination	LEENSRLKSLLLSMK HHHHHHHHHHHHHHH	37.64	29967540
532	Phosphorylation	EENSRLKSLLLSMKK HHHHHHHHHHHHHHH	28.92	-
536	Phosphorylation	RLKSLLLSMKKEVKS HHHHHHHHHHHHHHC	28.64	-
538	Acetylation	KSLLLSMKKEVKSAD HHHHHHHHHHHHCCC	42.26	25953088
538	Ubiquitination	KSLLLSMKKEVKSAD HHHHHHHHHHHHCCC	42.26	29967540
539	Ubiquitination	SLLLSMKKEVKSADT HHHHHHHHHHHCCCH	60.13	-
542	Ubiquitination	LSMKKEVKSADTAAT HHHHHHHHCCCHHHH	40.80	-
543	Phosphorylation	SMKKEVKSADTAATL HHHHHHHCCCHHHHH	36.23	22199227
546	Phosphorylation	KEVKSADTAATLNLQ HHHHCCCHHHHHHHH	20.22	22199227
549	Phosphorylation	KSADTAATLNLQIAG HCCCHHHHHHHHHHH	17.45	25311616
559	Phosphorylation	LQIAGLQTSVKRLCG HHHHHHHHHHHHHHH	40.30	25311616
560	Phosphorylation	QIAGLQTSVKRLCGE HHHHHHHHHHHHHHH	16.81	25311616
562	Ubiquitination	AGLQTSVKRLCGEIV HHHHHHHHHHHHHHH	39.15	29967540
572	Ubiquitination	CGEIVELKQHLEHYD HHHHHHHHHHHHHHH	23.36	29967540
578	Ubiquitination	LKQHLEHYDKIQELT HHHHHHHHHHHHHHH	15.00	21963094
579	Ubiquitination	KQHLEHYDKIQELTQ HHHHHHHHHHHHHHH	43.41	21963094
585	Phosphorylation	YDKIQELTQMLQESH HHHHHHHHHHHHHHH	15.92	24275569
591	Phosphorylation	LTQMLQESHSSLVST HHHHHHHHHHHHCCC	18.73	24275569
623	Phosphorylation	EVEQMHWSYQELKKT HHHHHHCCHHHHHHH	11.40	30576142
628	Ubiquitination	HWSYQELKKTMALFP HCCHHHHHHHHHHCC	45.50	21963094
629	Ubiquitination	WSYQELKKTMALFPH CCHHHHHHHHHHCCC	57.04	21963094

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
Oops, there are no upstream regulatory protein records of CEP72_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CEP72_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 CEP72_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LNX1_HUMAN	LNX1	physical	16189514
ZN417_HUMAN	ZNF417	physical	16189514
DDB1_HUMAN	DDB1	physical	23443559
TRAP1_HUMAN	TRAP1	physical	23443559
PCM1_HUMAN	PCM1	physical	23443559
AGRG4_HUMAN	GPR112	physical	23443559
PCLO_HUMAN	PCLO	physical	23443559
RAVR1_HUMAN	RAVER1	physical	23443559
S4A10_HUMAN	SLC4A10	physical	23443559
TBCD4_HUMAN	TBC1D4	physical	23443559
TBA1C_HUMAN	TUBA1C	physical	23443559
STALP_HUMAN	STAMBPL1	physical	25416956
SPA24_HUMAN	SPATA24	physical	25416956
CATIP_HUMAN	CATIP	physical	25416956
SPA24_HUMAN	SPATA24	physical	28514442
SAHH3_HUMAN	AHCYL2	physical	28514442
ZKSC1_HUMAN	ZKSCAN1	physical	28514442
HOME1_HUMAN	HOMER1	physical	28514442
SAHH2_HUMAN	AHCYL1	physical	28514442
CTU2_HUMAN	CTU2	physical	28514442
CAF1B_HUMAN	CHAF1B	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 CEP72_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-237, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, AND MASSSPECTROMETRY.	19007248 [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-237, AND MASSSPECTROMETRY.	17081983 [Abstract]