dbPTM

CEP55_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEP55_HUMAN
UniProt AC	Q53EZ4
Protein Name	Centrosomal protein of 55 kDa {ECO:0000312\|HGNC:HGNC:1161}
Gene Name	CEP55 {ECO:0000312\|HGNC:HGNC:1161}
Organism	Homo sapiens (Human).
Sequence Length	464
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cleavage furrow . Midbody, Midbody ring . Present at the centrosomes at interphase. A sma
Protein Description	Plays a role in mitotic exit and cytokinesis. [PubMed: 16198290]
Protein Sequence	MSSRSTKDLIKSKWGSKPSNSKSETTLEKLKGEIAHLKTSVDEITSGKGKLTDKERHRLLEKIRVLEAEKEKNAYQLTEKDKEIQRLRDQLKARYSTTTLLEQLEETTREGERREQVLKALSEEKDVLKQQLSAATSRIAELESKTNTLRLSQTVAPNCFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLPQQTKKPESEGYLQEEKQKCYNDLLASAKKDLEVERQTITQLSFELSEFRRKYEETQKEVHNLNQLLYSQRRADVQHLEDDRHKTEKIQKLREENDIARGKLEEEKKRSEELLSQVQFLYTSLLKQQEEQTRVALLEQQMQACTLDFENEKLDRQHVQHQLHVILKELRKARNQITQLESLKQLHEFAITEPLVTFQGETENREKVAASPKSPTAALNESLVECPKCNIQYPATEHRDLLVHVEYCSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MSSRSTKDLIKS ---CCCCCHHHHHHH	41.58	24719451
6	Ubiquitination	--MSSRSTKDLIKSK --CCCCCHHHHHHHH	27.71	22817900
11	Ubiquitination	RSTKDLIKSKWGSKP CCHHHHHHHHCCCCC	53.96	21890473
13	Ubiquitination	TKDLIKSKWGSKPSN HHHHHHHHCCCCCCC	51.04	29967540
16	Phosphorylation	LIKSKWGSKPSNSKS HHHHHCCCCCCCCCC	40.03	27470641
17	Ubiquitination	IKSKWGSKPSNSKSE HHHHCCCCCCCCCCH	48.83	29967540
19	Phosphorylation	SKWGSKPSNSKSETT HHCCCCCCCCCCHHH	58.43	25002506
21	Phosphorylation	WGSKPSNSKSETTLE CCCCCCCCCCHHHHH	41.73	25002506
22	Ubiquitination	GSKPSNSKSETTLEK CCCCCCCCCHHHHHH	57.47	33845483
23	Phosphorylation	SKPSNSKSETTLEKL CCCCCCCCHHHHHHH	39.74	30576142
25	Phosphorylation	PSNSKSETTLEKLKG CCCCCCHHHHHHHHH	43.71	25002506
26	Phosphorylation	SNSKSETTLEKLKGE CCCCCHHHHHHHHHH	28.94	25002506
27	Ubiquitination	NSKSETTLEKLKGEI CCCCHHHHHHHHHHH	7.73	21890473
29	Ubiquitination	KSETTLEKLKGEIAH CCHHHHHHHHHHHHH	59.62	33845483
31	Ubiquitination	ETTLEKLKGEIAHLK HHHHHHHHHHHHHHH	66.61	21906983
31 (in isoform 1)	Ubiquitination	-	66.61	21890473
31 (in isoform 2)	Ubiquitination	-	66.61	21890473
32	Ubiquitination	TTLEKLKGEIAHLKT HHHHHHHHHHHHHHC	41.81	22817900
38	Ubiquitination	KGEIAHLKTSVDEIT HHHHHHHHCCHHHHH	28.96	29967540
39	Phosphorylation	GEIAHLKTSVDEITS HHHHHHHCCHHHHHC	40.10	23312004
40	Phosphorylation	EIAHLKTSVDEITSG HHHHHHCCHHHHHCC	26.45	23312004
45	Phosphorylation	KTSVDEITSGKGKLT HCCHHHHHCCCCCCC	29.40	27470641
48	Acetylation	VDEITSGKGKLTDKE HHHHHCCCCCCCHHH	53.27	26051181
48	Ubiquitination	VDEITSGKGKLTDKE HHHHHCCCCCCCHHH	53.27	32015554
52	Phosphorylation	TSGKGKLTDKERHRL HCCCCCCCHHHHHHH	48.81	-
64	Ubiquitination	HRLLEKIRVLEAEKE HHHHHHHHHHHHHHH	37.73	22817900
66	Ubiquitination	LLEKIRVLEAEKEKN HHHHHHHHHHHHHHC	3.56	22817900
72	Ubiquitination	VLEAEKEKNAYQLTE HHHHHHHHCHHHCCH	58.93	33845483
75	Phosphorylation	AEKEKNAYQLTEKDK HHHHHCHHHCCHHHH	17.28	28060719
92	Ubiquitination	QRLRDQLKARYSTTT HHHHHHHHHHHHHHH	25.78	-
95	Phosphorylation	RDQLKARYSTTTLLE HHHHHHHHHHHHHHH	18.41	30576142
96	Phosphorylation	DQLKARYSTTTLLEQ HHHHHHHHHHHHHHH	17.45	24719451
97	Phosphorylation	QLKARYSTTTLLEQL HHHHHHHHHHHHHHH	18.18	27251275
98	Phosphorylation	LKARYSTTTLLEQLE HHHHHHHHHHHHHHH	14.98	30576142
99	Phosphorylation	KARYSTTTLLEQLEE HHHHHHHHHHHHHHH	29.45	30576142
119	Ubiquitination	ERREQVLKALSEEKD HHHHHHHHHHHHCHH	48.72	29967540
125	Ubiquitination	LKALSEEKDVLKQQL HHHHHHCHHHHHHHH	49.43	22817900
129	Ubiquitination	SEEKDVLKQQLSAAT HHCHHHHHHHHHHHH	35.53	-
129	Ubiquitination	SEEKDVLKQQLSAAT HHCHHHHHHHHHHHH	35.53	22817900
129 (in isoform 1)	Ubiquitination	-	35.53	21890473
129 (in isoform 2)	Ubiquitination	-	35.53	21890473
133	Phosphorylation	DVLKQQLSAATSRIA HHHHHHHHHHHHHHH	16.12	29514088
136	Phosphorylation	KQQLSAATSRIAELE HHHHHHHHHHHHHHH	20.46	29514088
137	Phosphorylation	QQLSAATSRIAELES HHHHHHHHHHHHHHH	19.57	29514088
144	Phosphorylation	SRIAELESKTNTLRL HHHHHHHHHCCCEEH	58.36	29514088
145	Ubiquitination	RIAELESKTNTLRLS HHHHHHHHCCCEEHH	36.10	-
145	Ubiquitination	RIAELESKTNTLRLS HHHHHHHHCCCEEHH	36.10	22817900
145 (in isoform 1)	Ubiquitination	-	36.10	21890473
145 (in isoform 2)	Ubiquitination	-	36.10	21890473
146	Phosphorylation	IAELESKTNTLRLSQ HHHHHHHCCCEEHHC	42.59	-
148	Phosphorylation	ELESKTNTLRLSQTV HHHHHCCCEEHHCCC	20.63	-
152	Phosphorylation	KTNTLRLSQTVAPNC HCCCEEHHCCCCCCC	19.85	27080861
154	Phosphorylation	NTLRLSQTVAPNCFN CCEEHHCCCCCCCCC	18.43	25159151
162	Phosphorylation	VAPNCFNSSINNIHE CCCCCCCCCCCCHHE	16.61	27080861
163	Phosphorylation	APNCFNSSINNIHEM CCCCCCCCCCCHHEE	30.36	27080861
175	Ubiquitination	HEMEIQLKDALEKNQ HEEEEHHHHHHHHHC	25.28	22817900
180	Ubiquitination	QLKDALEKNQQWLVY HHHHHHHHHCCEEEE	61.99	-
180	Ubiquitination	QLKDALEKNQQWLVY HHHHHHHHHCCEEEE	61.99	22817900
180 (in isoform 1)	Ubiquitination	-	61.99	21890473
180 (in isoform 2)	Ubiquitination	-	61.99	21890473
187	Phosphorylation	KNQQWLVYDQQREVY HHCCEEEEHHHHHHH	13.08	27642862
196	Ubiquitination	QQREVYVKGLLAKIF HHHHHHHHHHHHHHH	26.59	-
196	Ubiquitination	QQREVYVKGLLAKIF HHHHHHHHHHHHHHH	26.59	21890473
196 (in isoform 1)	Ubiquitination	-	26.59	21890473
196 (in isoform 2)	Ubiquitination	-	26.59	21890473
198	Ubiquitination	REVYVKGLLAKIFEL HHHHHHHHHHHHHHH	3.31	22505724
201	Ubiquitination	YVKGLLAKIFELEKK HHHHHHHHHHHHHHH	48.15	21906983
201 (in isoform 1)	Ubiquitination	-	48.15	21890473
201 (in isoform 2)	Ubiquitination	-	48.15	21890473
207	2-Hydroxyisobutyrylation	AKIFELEKKTETAAH HHHHHHHHHHHHHHH	77.08	-
207	Ubiquitination	AKIFELEKKTETAAH HHHHHHHHHHHHHHH	77.08	32015554
208	Ubiquitination	KIFELEKKTETAAHS HHHHHHHHHHHHHHC	42.07	29967540
215	Phosphorylation	KTETAAHSLPQQTKK HHHHHHHCCCCCCCC	36.70	30576142
220	Phosphorylation	AHSLPQQTKKPESEG HHCCCCCCCCCCCCC	35.47	30576142
221	Ubiquitination	HSLPQQTKKPESEGY HCCCCCCCCCCCCCC	63.09	32015554
222	Ubiquitination	SLPQQTKKPESEGYL CCCCCCCCCCCCCCC	58.36	32015554
225	Phosphorylation	QQTKKPESEGYLQEE CCCCCCCCCCCCHHH	44.86	28851738
228	Phosphorylation	KKPESEGYLQEEKQK CCCCCCCCCHHHHHH	10.93	29978859
229	Ubiquitination	KPESEGYLQEEKQKC CCCCCCCCHHHHHHH	8.32	22817900
233	Acetylation	EGYLQEEKQKCYNDL CCCCHHHHHHHHHHH	55.06	26051181
233	Ubiquitination	EGYLQEEKQKCYNDL CCCCHHHHHHHHHHH	55.06	21906983
233 (in isoform 1)	Ubiquitination	-	55.06	21890473
233 (in isoform 2)	Ubiquitination	-	55.06	21890473
235	Ubiquitination	YLQEEKQKCYNDLLA CCHHHHHHHHHHHHH	50.16	22817900
237	Phosphorylation	QEEKQKCYNDLLASA HHHHHHHHHHHHHHH	20.81	27642862
243	Phosphorylation	CYNDLLASAKKDLEV HHHHHHHHHHHCHHH	40.36	21815630
245	Ubiquitination	NDLLASAKKDLEVER HHHHHHHHHCHHHHH	44.30	32015554
246	Ubiquitination	DLLASAKKDLEVERQ HHHHHHHHCHHHHHH	68.23	-
268	Ubiquitination	ELSEFRRKYEETQKE HHHHHHHHHHHHHHH	53.40	29967540
269	Phosphorylation	LSEFRRKYEETQKEV HHHHHHHHHHHHHHH	19.72	23403867
272	Phosphorylation	FRRKYEETQKEVHNL HHHHHHHHHHHHHHH	32.76	23403867
274	Ubiquitination	RKYEETQKEVHNLNQ HHHHHHHHHHHHHHH	69.95	29967540
284	Phosphorylation	HNLNQLLYSQRRADV HHHHHHHHHHHHHHH	16.02	29978859
285	Phosphorylation	NLNQLLYSQRRADVQ HHHHHHHHHHHHHHH	19.72	29978859
300	Ubiquitination	HLEDDRHKTEKIQKL HHHCCHHHHHHHHHH	60.31	29967540
303	Ubiquitination	DDRHKTEKIQKLREE CCHHHHHHHHHHHHH	56.52	29967540
306	Ubiquitination	HKTEKIQKLREENDI HHHHHHHHHHHHCCH	53.65	29967540
317	Ubiquitination	ENDIARGKLEEEKKR HCCHHHCHHHHHHHH	47.36	29967540
336	Phosphorylation	LSQVQFLYTSLLKQQ HHHHHHHHHHHHHHH	8.79	22461510
337	Phosphorylation	SQVQFLYTSLLKQQE HHHHHHHHHHHHHHH	18.29	22461510
338	Phosphorylation	QVQFLYTSLLKQQEE HHHHHHHHHHHHHHH	20.39	24719451
341	Ubiquitination	FLYTSLLKQQEEQTR HHHHHHHHHHHHHHH	56.05	-
360	Phosphorylation	EQQMQACTLDFENEK HHHHHHHCCCCCCCH	32.17	-
367	Ubiquitination	TLDFENEKLDRQHVQ CCCCCCCHHHHHHHH	68.23	32015554
396	Phosphorylation	NQITQLESLKQLHEF HHHHHHHHHHHHHHH	49.84	27067055
398	Ubiquitination	ITQLESLKQLHEFAI HHHHHHHHHHHHHHC	61.16	22817900
398 (in isoform 1)	Ubiquitination	-	61.16	21890473
425	Phosphorylation	NREKVAASPKSPTAA CHHHHCCCCCCCCHH	24.11	25159151
427	Ubiquitination	EKVAASPKSPTAALN HHHCCCCCCCCHHHC	67.58	29967540
428	Phosphorylation	KVAASPKSPTAALNE HHCCCCCCCCHHHCH	30.76	19664994
430	Phosphorylation	AASPKSPTAALNESL CCCCCCCCHHHCHHH	31.49	22167270
436	Phosphorylation	PTAALNESLVECPKC CCHHHCHHHCCCCCC	36.32	19664994
442	Ubiquitination	ESLVECPKCNIQYPA HHHCCCCCCCCCCCC	52.12	29967540
461	Phosphorylation	DLLVHVEYCSK---- CEEEEHHCCCC----	10.84	29978859
463	Phosphorylation	LVHVEYCSK------ EEEHHCCCC------	40.26	29978859

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
425	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
425	S	Phosphorylation	Kinase	ERK2	P28482	PSP
428	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
428	S	Phosphorylation	Kinase	ERK2	P28482	PSP
436	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
425	S	Phosphorylation	16198290
Phosphorylation at Ser-425 and Ser-428 is required for dissociation from the centrosome at the G2/M boundary.
425	S	Phosphorylation	16198290
Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully.
425	S	Phosphorylation	16198290
There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436.
428	S	Phosphorylation	16198290
Phosphorylation at Ser-425 and Ser-428 is required for dissociation from the centrosome at the G2/M boundary.
428	S	Phosphorylation	16198290
Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully.
428	S	Phosphorylation	16198290
There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436.
436	S	Phosphorylation	16198290
Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully.
436	S	Phosphorylation	16198290
There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436.

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 CEP55_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TS101_HUMAN	TSG101	physical	17853893
VP37B_HUMAN	VPS37B	physical	17853893
VP37C_HUMAN	VPS37C	physical	17853893
PDC6I_HUMAN	PDCD6IP	physical	17853893
TS101_HUMAN	TSG101	physical	17556548
PDC6I_HUMAN	PDCD6IP	physical	17556548
CEP55_HUMAN	CEP55	physical	17556548
PDC6I_HUMAN	PDCD6IP	physical	18948538
TS101_HUMAN	TSG101	physical	18948538
NBR1_HUMAN	NBR1	physical	21909099
CEP55_HUMAN	CEP55	physical	25416956
PKHG6_HUMAN	PLEKHG6	physical	25416956
RBM22_HUMAN	RBM22	physical	25416956
RCOR3_HUMAN	RCOR3	physical	25416956
EIF1A_HUMAN	EIF1AD	physical	25416956
MUM1_HUMAN	MUM1	physical	25416956
SPF45_HUMAN	RBM17	physical	25416956
FBF1_HUMAN	FBF1	physical	25416956
MISSL_HUMAN	MAPK1IP1L	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
CCBE1_HUMAN	CCBE1	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
TGO1_HUMAN	MIA3	physical	25416956
PEF1_HUMAN	PEF1	physical	25416956
TEAD4_HUMAN	TEAD4	physical	21516116
MTMR4_HUMAN	MTMR4	physical	27432908

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 CEP55_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-425; SER-428; THR-430AND SER-436, AND MASS 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-425; SER-428; THR-430AND SER-436, AND MASS SPECTROMETRY.	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-428, AND MASSSPECTROMETRY.	18691976 [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-425 AND SER-428, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosomeprotein, Cep55, is required for its recruitment to midbody andcytokinesis."; Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E.,Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.; Dev. Cell 9:477-488(2005). Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITHPLK1; AKAP9 AND PCNT, PHOSPHORYLATION AT SER-425; SER-428 AND SER-436,MUTAGENESIS OF SER-396; SER-425; SER-428 AND SER-436, AND MASSSPECTROMETRY.	16198290 [Abstract]

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