dbPTM

CEP76_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEP76_HUMAN
UniProt AC	Q8TAP6
Protein Name	Centrosomal protein of 76 kDa
Gene Name	CEP76
Organism	Homo sapiens (Human).
Sequence Length	659
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Does not localize along the ciliary axoneme.
Protein Description	Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication..
Protein Sequence	MSLPPEKASELKQLIHQQLSKMDVHGRIREILAETIREELAPDQQHLSTEDLIKALRRRGIIDDVMKELNFVTDSVEQELPSSPKQPICFDRQSTLKKTNIDPTRRYLYLQVLGGKAFLEHLQEPEPLPGQVCSTFTLCLHYRNQRFRSKPVPCACEPDFHDGFLLEVHRESLGDGTRMADSTTMLSISDPIHMVLIKTDIFGETTLVASYFLEWRSVLGSENGVTSLTVELMGVGTESKVSVGILNIKLEMYPPLNQTLSQEVVNTQLALERQKTAEKERLFLVYAKQWWREYLQIRPSHNSRLVKIFAQDENGINRPVCSYVKPLRAGRLLDTPRQAARFVNVLGYERAPVIGGGGKQEQWCTLLAFLCRNKGDCEDHANLLCSLLLGYGLEAFVCVGTKAKGVPHAWVMTCGTDGAITFWESLTGHRYIHKPTNPDEPPVAEQPKPLYPYRTIGCVFNHQMFLGNCQPSDAVETCVFDLNDESKWKPMSEEAIKSVCAPGATTSLPPFPPLCASTIDASVTSNEIEMQLRLLVSEHRKDLGLTTVWEDQLSYLLSPALASYEFERTTSISAGNEEFQDAIRRAVPDGHTFKGFPIHFVYRNARRAFATCLRSPFCEEIICCRGDQVRLAVRVRVFTYPESACAVWIMFACKYRSVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLPPEKAS ------CCCCHHHHH	49.97	28270605
9	Phosphorylation	SLPPEKASELKQLIH CCCHHHHHHHHHHHH	55.30	28270605
12	Ubiquitination	PEKASELKQLIHQQL HHHHHHHHHHHHHHH	38.72	-
20	Phosphorylation	QLIHQQLSKMDVHGR HHHHHHHHCCCHHHH	22.92	30622161
21	Ubiquitination	LIHQQLSKMDVHGRI HHHHHHHCCCHHHHH	47.95	-
48	Phosphorylation	APDQQHLSTEDLIKA CCCCCCCCHHHHHHH	27.85	30622161
49	Phosphorylation	PDQQHLSTEDLIKAL CCCCCCCHHHHHHHH	39.62	30622161
54	Ubiquitination	LSTEDLIKALRRRGI CCHHHHHHHHHHCCC	48.98	-
73	Phosphorylation	MKELNFVTDSVEQEL HHHCCCCCCCHHHCC	20.58	29396449
75	Phosphorylation	ELNFVTDSVEQELPS HCCCCCCCHHHCCCC	20.42	29255136
82	Phosphorylation	SVEQELPSSPKQPIC CHHHCCCCCCCCCCE	72.41	30266825
83	Phosphorylation	VEQELPSSPKQPICF HHHCCCCCCCCCCEE	33.89	19664994
85	Ubiquitination	QELPSSPKQPICFDR HCCCCCCCCCCEECC	71.32	-
94	Phosphorylation	PICFDRQSTLKKTNI CCEECCCCCCCCCCC	36.28	23882029
95	Phosphorylation	ICFDRQSTLKKTNID CEECCCCCCCCCCCC	33.97	23882029
279	Acetylation	ERQKTAEKERLFLVY HHHHHHHHHHHHHHH	45.75	20167786
322	Phosphorylation	GINRPVCSYVKPLRA CCCCCCHHHCCCCCC	32.94	-
323	Phosphorylation	INRPVCSYVKPLRAG CCCCCHHHCCCCCCC	13.84	-
325	Ubiquitination	RPVCSYVKPLRAGRL CCCHHHCCCCCCCCC	30.06	-
335	Phosphorylation	RAGRLLDTPRQAARF CCCCCCCCHHHHHHH	21.97	22210691
434	Ubiquitination	TGHRYIHKPTNPDEP CCCCEECCCCCCCCC	43.93	-
489	Ubiquitination	LNDESKWKPMSEEAI CCCCCCCEECCHHHH	34.28	21139048
537	Phosphorylation	MQLRLLVSEHRKDLG HHHHHHHHHHHHHCC	27.88	22496350
571	Phosphorylation	YEFERTTSISAGNEE CEEEECCCCCCCCHH	17.59	28555341
594	Ubiquitination	VPDGHTFKGFPIHFV CCCCCCCCCCCEEEE	61.88	-

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
83	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CEP76_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 CEP76_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP97_HUMAN	CEP97	physical	22441691
CE290_HUMAN	CEP290	physical	22441691
CP110_HUMAN	CCP110	physical	22441691
ABR_HUMAN	ABR	physical	23443559
AMOT_HUMAN	AMOT	physical	23443559
PRC2C_HUMAN	PRRC2C	physical	23443559
NDUF3_HUMAN	NDUFAF3	physical	23443559
UQCC2_HUMAN	UQCC2	physical	23443559
CALU_HUMAN	CALU	physical	23443559
KCC2D_HUMAN	CAMK2D	physical	23443559
CE290_HUMAN	CEP290	physical	23443559
CEP55_HUMAN	CEP55	physical	23443559
CEP97_HUMAN	CEP97	physical	23443559
YBOX3_HUMAN	YBX3	physical	23443559
TBB5_HUMAN	TUBB	physical	23443559
DSG1_HUMAN	DSG1	physical	23443559
EF1A2_HUMAN	EEF1A2	physical	23443559
CSK21_HUMAN	CSNK2A1	physical	23443559
DSC1_HUMAN	DSC1	physical	23443559
RCN1_HUMAN	RCN1	physical	23443559
RCN2_HUMAN	RCN2	physical	23443559
RL17_HUMAN	RPL17	physical	23443559
RL24_HUMAN	RPL24	physical	23443559
RL23_HUMAN	RPL23	physical	23443559
FA7_HUMAN	F7	physical	23443559
F90A1_HUMAN	FAM90A1	physical	23443559
MIP18_HUMAN	FAM96B	physical	23443559
MOGS_HUMAN	MOGS	physical	23443559
GGYF2_HUMAN	GIGYF2	physical	23443559
GRWD1_HUMAN	GRWD1	physical	23443559
HNRH1_HUMAN	HNRNPH1	physical	23443559
HNRPU_HUMAN	HNRNPU	physical	23443559
HPCL1_HUMAN	HPCAL1	physical	23443559
HORN_HUMAN	HRNR	physical	23443559
HS90A_HUMAN	HSP90AA1	physical	23443559
HS90B_HUMAN	HSP90AB1	physical	23443559
HSP72_HUMAN	HSPA2	physical	23443559
GRP78_HUMAN	HSPA5	physical	23443559
GRP75_HUMAN	HSPA9	physical	23443559
IQGA1_HUMAN	IQGAP1	physical	23443559
IRS4_HUMAN	IRS4	physical	23443559
LPPRC_HUMAN	LRPPRC	physical	23443559
RT11_HUMAN	MRPS11	physical	23443559
RT16_HUMAN	MRPS16	physical	23443559
RT23_HUMAN	MRPS23	physical	23443559
RT25_HUMAN	MRPS25	physical	23443559
RT26_HUMAN	MRPS26	physical	23443559
RT27_HUMAN	MRPS27	physical	23443559
RT07_HUMAN	MRPS7	physical	23443559
MYL6B_HUMAN	MYL6B	physical	23443559
LIPB1_HUMAN	PPFIBP1	physical	23443559
PP2BA_HUMAN	PPP3CA	physical	23443559
PP2BB_HUMAN	PPP3CB	physical	23443559
PRP19_HUMAN	PRPF19	physical	23443559
RD23A_HUMAN	RAD23A	physical	23443559
RAVR1_HUMAN	RAVER1	physical	23443559
RBBP4_HUMAN	RBBP4	physical	23443559
RFC2_HUMAN	RFC2	physical	23443559
MRRP1_HUMAN	TRMT10C	physical	23443559
RL10L_HUMAN	RPL10L	physical	23443559
RL21_HUMAN	RPL21	physical	23443559
RL22_HUMAN	RPL22	physical	23443559
RL23A_HUMAN	RPL23A	physical	23443559
RL26_HUMAN	RPL26	physical	23443559
RL30_HUMAN	RPL30	physical	23443559
RL31_HUMAN	RPL31	physical	23443559
RL38_HUMAN	RPL38	physical	23443559
RS11_HUMAN	RPS11	physical	23443559
RS14_HUMAN	RPS14	physical	23443559
RS15_HUMAN	RPS15	physical	23443559
RS15A_HUMAN	RPS15A	physical	23443559
RS16_HUMAN	RPS16	physical	23443559
RS17_HUMAN	RPS17	physical	23443559
RS23_HUMAN	RPS23	physical	23443559
RS25_HUMAN	RPS25	physical	23443559
RS3A_HUMAN	RPS3A	physical	23443559
RS4X_HUMAN	RPS4X	physical	23443559
RS7_HUMAN	RPS7	physical	23443559
RS9_HUMAN	RPS9	physical	23443559
S10A4_HUMAN	S100A4	physical	23443559
SMCE1_HUMAN	SMARCE1	physical	23443559
SMD3_HUMAN	SNRPD3	physical	23443559
SPTN1_HUMAN	SPTAN1	physical	23443559
SPT6H_HUMAN	SUPT6H	physical	23443559
TCRG1_HUMAN	TCERG1	physical	23443559
TBA1B_HUMAN	TUBA1B	physical	23443559
TBA4A_HUMAN	TUBA4A	physical	23443559
TBB2A_HUMAN	TUBB2A	physical	23443559
TBB4B_HUMAN	TUBB4B	physical	23443559
UBB_HUMAN	UBB	physical	23443559
QCR7_HUMAN	UQCRB	physical	23443559
DCAF7_HUMAN	DCAF7	physical	23443559
Z804B_HUMAN	ZNF804B	physical	23443559
CCD92_HUMAN	CCDC92	physical	25416956
PAR6B_HUMAN	PARD6B	physical	25416956
EAF1_HUMAN	EAF1	physical	25416956
CV039_HUMAN	C22orf39	physical	25416956
ZMAT2_HUMAN	ZMAT2	physical	25416956
DZI1L_HUMAN	DZIP1L	physical	25416956
TT21A_HUMAN	TTC21A	physical	25416956
NHLC2_HUMAN	NHLRC2	physical	25416956
AKA7A_HUMAN	AKAP7	physical	21516116
AKA7G_HUMAN	AKAP7	physical	21516116
BACD3_HUMAN	KCTD10	physical	28514442
URFB1_HUMAN	UHRF1BP1	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 CEP76_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-83, AND MASSSPECTROMETRY.	19690332 [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-83, AND MASSSPECTROMETRY.	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-83, AND MASSSPECTROMETRY.	18691976 [Abstract]