dbPTM

CENPU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CENPU_HUMAN
UniProt AC	Q71F23
Protein Name	Centromere protein U
Gene Name	CENPU
Organism	Homo sapiens (Human).
Sequence Length	418
Subcellular Localization	Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates.
Protein Description	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression..
Protein Sequence	MAPRGRRRPRPHRSEGARRSKNTLERTHSMKDKAGQKCKPIDVFDFPDNSDVSSIGRLGENEKDEETYETFDPPLHSTAIYADEEEFSKHCGLSLSSTPPGKEAKRSSDTSGNEASEIESVKISAKKPGRKLRPISDDSESIEESDTRRKVKSAEKISTQRHEVIRTTASSELSEKPAESVTSKKTGPLSAQPSVEKENLAIESQSKTQKKGKISHDKRKKSRSKAIGSDTSDIVHIWCPEGMKTSDIKELNIVLPEFEKTHLEHQQRIESKVCKAAIATFYVNVKEQFIKMLKESQMLTNLKRKNAKMISDIEKKRQRMIEVQDELLRLEPQLKQLQTKYDELKERKSSLRNAAYFLSNLKQLYQDYSDVQAQEPNVKETYDSSSLPALLFKARTLLGAESHLRNINHQLEKLLDQG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18 (in isoform 2)	Ubiquitination	-	55.02	21890473
23	Phosphorylation	GARRSKNTLERTHSM HHHHCHHHHHHHHHC	33.46	29449344
27	Phosphorylation	SKNTLERTHSMKDKA CHHHHHHHHHCCCCC	14.66	29514088
29	Phosphorylation	NTLERTHSMKDKAGQ HHHHHHHHCCCCCCC	27.24	29514088
50	Phosphorylation	VFDFPDNSDVSSIGR EECCCCCCCCHHCCC	46.93	30266825
53	Phosphorylation	FPDNSDVSSIGRLGE CCCCCCCHHCCCCCC	22.64	30266825
54	Phosphorylation	PDNSDVSSIGRLGEN CCCCCCHHCCCCCCC	28.98	30266825
67	Phosphorylation	ENEKDEETYETFDPP CCCCCHHHHHCCCCC	25.30	28796482
68	Phosphorylation	NEKDEETYETFDPPL CCCCHHHHHCCCCCC	19.09	28796482
70	Phosphorylation	KDEETYETFDPPLHS CCHHHHHCCCCCCCC	23.95	27642862
77	Phosphorylation	TFDPPLHSTAIYADE CCCCCCCCCEEECCH	27.50	28450419
78	Phosphorylation	FDPPLHSTAIYADEE CCCCCCCCEEECCHH	13.31	28450419
81	Phosphorylation	PLHSTAIYADEEEFS CCCCCEEECCHHHHH	12.92	28450419
94	Phosphorylation	FSKHCGLSLSSTPPG HHHHCCCCCCCCCCC	16.10	30266825
96	Phosphorylation	KHCGLSLSSTPPGKE HHCCCCCCCCCCCCC	28.88	30266825
97	Phosphorylation	HCGLSLSSTPPGKEA HCCCCCCCCCCCCCC	50.67	30266825
98	Phosphorylation	CGLSLSSTPPGKEAK CCCCCCCCCCCCCCC	30.08	30266825
107	Phosphorylation	PGKEAKRSSDTSGNE CCCCCCCCCCCCCCC	31.68	25159151
108	Phosphorylation	GKEAKRSSDTSGNEA CCCCCCCCCCCCCCC	49.28	25159151
110	Phosphorylation	EAKRSSDTSGNEASE CCCCCCCCCCCCCHH	40.25	25159151
111	Phosphorylation	AKRSSDTSGNEASEI CCCCCCCCCCCCHHH	44.61	25159151
116	Phosphorylation	DTSGNEASEIESVKI CCCCCCCHHHEEEEE	32.69	25159151
120	Phosphorylation	NEASEIESVKISAKK CCCHHHEEEEEEECC	34.08	25159151
124	Phosphorylation	EIESVKISAKKPGRK HHEEEEEEECCCCCC	28.46	23532336
136	Phosphorylation	GRKLRPISDDSESIE CCCCCCCCCCCHHHH	37.74	30266825
139	Phosphorylation	LRPISDDSESIEESD CCCCCCCCHHHHHHH	37.93	30266825
141	Phosphorylation	PISDDSESIEESDTR CCCCCCHHHHHHHHH	38.97	29255136
145	Phosphorylation	DSESIEESDTRRKVK CCHHHHHHHHHHHHH	31.34	23663014
147	Phosphorylation	ESIEESDTRRKVKSA HHHHHHHHHHHHHHH	41.47	25850435
151 (in isoform 2)	Ubiquitination	-	5.85	21890473
153	Phosphorylation	DTRRKVKSAEKISTQ HHHHHHHHHHHHHHH	44.65	26425664
156	Acetylation	RKVKSAEKISTQRHE HHHHHHHHHHHHHHH	41.49	25953088
158	Phosphorylation	VKSAEKISTQRHEVI HHHHHHHHHHHHHHH	29.56	26425664
167	Phosphorylation	QRHEVIRTTASSELS HHHHHHHHHCCHHHC	18.65	28450419
168	Phosphorylation	RHEVIRTTASSELSE HHHHHHHHCCHHHCC	18.07	28450419
170	Phosphorylation	EVIRTTASSELSEKP HHHHHHCCHHHCCCC	23.42	25627689
171	Phosphorylation	VIRTTASSELSEKPA HHHHHCCHHHCCCCC	39.84	30108239
174	Phosphorylation	TTASSELSEKPAESV HHCCHHHCCCCCCCC	39.25	28450419
176	Ubiquitination	ASSELSEKPAESVTS CCHHHCCCCCCCCCC	46.26	33845483
180	Phosphorylation	LSEKPAESVTSKKTG HCCCCCCCCCCCCCC	32.57	28985074
182	Phosphorylation	EKPAESVTSKKTGPL CCCCCCCCCCCCCCC	44.07	26074081
183	Phosphorylation	KPAESVTSKKTGPLS CCCCCCCCCCCCCCC	29.96	26074081
184	Acetylation	PAESVTSKKTGPLSA CCCCCCCCCCCCCCC	45.01	25953088
185	Ubiquitination	AESVTSKKTGPLSAQ CCCCCCCCCCCCCCC	59.49	29967540
185	Sumoylation	AESVTSKKTGPLSAQ CCCCCCCCCCCCCCC	59.49	28112733
186	Phosphorylation	ESVTSKKTGPLSAQP CCCCCCCCCCCCCCC	48.01	17192257
190	Phosphorylation	SKKTGPLSAQPSVEK CCCCCCCCCCCCHHH	28.17	25159151
194	O-linked_Glycosylation	GPLSAQPSVEKENLA CCCCCCCCHHHHCCH	30.72	30379171
194	Phosphorylation	GPLSAQPSVEKENLA CCCCCCCCHHHHCCH	30.72	23401153
197	Ubiquitination	SAQPSVEKENLAIES CCCCCHHHHCCHHHC	50.15	29967540
204	Phosphorylation	KENLAIESQSKTQKK HHCCHHHCCCHHCCC	33.37	25159151
206	Phosphorylation	NLAIESQSKTQKKGK CCHHHCCCHHCCCCC	47.12	19691289
215	O-linked_Glycosylation	TQKKGKISHDKRKKS HCCCCCCCCCHHHHH	29.17	30379171
229	Phosphorylation	SRSKAIGSDTSDIVH HHHHHCCCCCCCEEE	31.44	30266825
231	Phosphorylation	SKAIGSDTSDIVHIW HHHCCCCCCCEEEEE	29.96	30266825
232	Phosphorylation	KAIGSDTSDIVHIWC HHCCCCCCCEEEEEC	30.26	30266825
244	Ubiquitination	IWCPEGMKTSDIKEL EECCCCCCCCCHHHH	56.59	29967540
249	Ubiquitination	GMKTSDIKELNIVLP CCCCCCHHHHHEECC	62.23	29967540
260 (in isoform 1)	Ubiquitination	-	46.71	21890473
260	Ubiquitination	IVLPEFEKTHLEHQQ EECCHHHHHHHHHHH	46.71	22817900
260	Ubiquitination	IVLPEFEKTHLEHQQ EECCHHHHHHHHHHH	46.71	21890473
272	Ubiquitination	HQQRIESKVCKAAIA HHHHHHHHHHHHHHH	38.57	33845483
290	Ubiquitination	VNVKEQFIKMLKESQ HCHHHHHHHHHHHHH	2.27	21890473
291	Acetylation	NVKEQFIKMLKESQM CHHHHHHHHHHHHHH	39.20	19827569
300	Phosphorylation	LKESQMLTNLKRKNA HHHHHHHHHHHHHCH	32.91	-
303	Acetylation	SQMLTNLKRKNAKMI HHHHHHHHHHCHHHH	64.49	19827325
303	"N6,N6-dimethyllysine"	SQMLTNLKRKNAKMI HHHHHHHHHHCHHHH	64.49	-
303	Ubiquitination	SQMLTNLKRKNAKMI HHHHHHHHHHCHHHH	64.49	29967540
303	Methylation	SQMLTNLKRKNAKMI HHHHHHHHHHCHHHH	64.49	-
308	Methylation	NLKRKNAKMISDIEK HHHHHCHHHHHHHHH	46.27	-
308	"N6,N6-dimethyllysine"	NLKRKNAKMISDIEK HHHHHCHHHHHHHHH	46.27	-
308	Acetylation	NLKRKNAKMISDIEK HHHHHCHHHHHHHHH	46.27	25953088
335	Ubiquitination	LRLEPQLKQLQTKYD HHHHHHHHHHHHHHH	43.65	29967540
340	Ubiquitination	QLKQLQTKYDELKER HHHHHHHHHHHHHHH	37.43	-
379	Ubiquitination	QAQEPNVKETYDSSS HCCCCCCCCCCCCCC	51.48	29967540
393	Ubiquitination	SLPALLFKARTLLGA CHHHHHHHHHHHHCC	36.61	22817900
393 (in isoform 1)	Ubiquitination	-	36.61	21890473
393	Ubiquitination	SLPALLFKARTLLGA CHHHHHHHHHHHHCC	36.61	21890473
413	Ubiquitination	NINHQLEKLLDQG-- HHHHHHHHHHHCC--	64.04	-
423	Ubiquitination	DQG------------ HCC------------		21890473

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
77	S	Phosphorylation	Kinase	PLK1	P53350	PSP
78	T	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
78	T	Phosphorylation		17081991
Phosphorylated by PLK1 at Thr-78, creating a self-tethering site that specifically interacts with the polo-box domain of PLK1.

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 CENPU_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4G1_HUMAN	EIF4G1	physical	21900206
LAMC1_HUMAN	LAMC1	physical	21900206
ROBO2_HUMAN	ROBO2	physical	21900206
XRCC6_HUMAN	XRCC6	physical	21900206
PGRC1_HUMAN	PGRMC1	physical	21900206
TBB2B_HUMAN	TUBB2B	physical	21900206
GIT1_HUMAN	GIT1	physical	21900206
SPTN4_HUMAN	SPTBN4	physical	21900206
PLXB2_HUMAN	PLXNB2	physical	21900206
NDUS2_HUMAN	NDUFS2	physical	21900206
CENPQ_HUMAN	CENPQ	physical	21454580
PLK1_HUMAN	PLK1	physical	21454580
CENPI_HUMAN	CENPI	physical	16622419
CENPN_HUMAN	CENPN	physical	16622419
CENPL_HUMAN	CENPL	physical	16622419
CENPO_HUMAN	CENPO	physical	16622419
CENPK_HUMAN	CENPK	physical	16622419
CENPP_HUMAN	CENPP	physical	16622419
CENPQ_HUMAN	CENPQ	physical	16622419
CENPH_HUMAN	CENPH	physical	16622419
CENPM_HUMAN	CENPM	physical	16622419
PLK1_HUMAN	PLK1	physical	19597481
CENPF_HUMAN	CENPF	physical	26496610
CENPI_HUMAN	CENPI	physical	26496610
GOGA3_HUMAN	GOLGA3	physical	26496610
RL10A_HUMAN	RPL10A	physical	26496610
NHS_HUMAN	NHS	physical	26496610
PLXB1_HUMAN	PLXNB1	physical	26496610
NS1BP_HUMAN	IVNS1ABP	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
CENPR_HUMAN	ITGB3BP	physical	26496610
IMA7_HUMAN	KPNA6	physical	26496610
SI1L1_HUMAN	SIPA1L1	physical	26496610
CENPQ_HUMAN	CENPQ	physical	26496610
MET2B_HUMAN	METTL2B	physical	26496610
CENPN_HUMAN	CENPN	physical	26496610
MIER1_HUMAN	MIER1	physical	26496610
CENPK_HUMAN	CENPK	physical	26496610
CENPH_HUMAN	CENPH	physical	26496610
CENPM_HUMAN	CENPM	physical	26496610
CENPO_HUMAN	CENPO	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
CENPT_HUMAN	CENPT	physical	26496610
MITD1_HUMAN	MITD1	physical	26496610
SPT2_HUMAN	SPTY2D1	physical	26496610
CENPX_HUMAN	STRA13	physical	26496610
CENPP_HUMAN	CENPP	physical	26496610
CENPR_HUMAN	ITGB3BP	physical	28514442
CENPQ_HUMAN	CENPQ	physical	28514442
CENPI_HUMAN	CENPI	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
CENPH_HUMAN	CENPH	physical	28514442
PLK1_HUMAN	PLK1	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 CENPU_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-111, 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-108; THR-110; SER-111;SER-136; SER-139 AND SER-141, 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 THR-186; SER-190 ANDSER-194, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-229, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1interaction is critical for proper chromosome segregation."; Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K.,Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.; Mol. Cell 24:409-422(2006). Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1,PHOSPHORYLATION AT THR-78, AND MUTAGENESIS OF SER-77 AND THR-78.	17081991 [Abstract]

show