dbPTM

CENPR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CENPR_HUMAN
UniProt AC	Q13352
Protein Name	Centromere protein R
Gene Name	ITGB3BP
Organism	Homo sapiens (Human).
Sequence Length	177
Subcellular Localization	Isoform 1: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Isoform 2: Nucleus. Isoform 3: Nucleus. Cytoplasm. Isoform 3 is predominantly nuclear and weakly cytoplasmic. Isoform 4: Cytoplasm.
Protein Description	Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1, but not other isoforms, is involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex..
Protein Sequence	MPVKRSLKLDGLLEENSFDPSKITRKKSVITYSPTTGTCQMSLFASPTSSEEQKHRNGLSNEKRKKLNHPSLTESKESTTKDNDEFMMLLSKVEKLSEEIMEIMQNLSSIQALEGSRELENLIGISCASHFLKREMQKTKELMTKVNKQKLFEKSTGLPHKASRHLDSYEFLKAILN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPVKRSLKLDGLL --CCCCCCCCCCCHH	24.92	21712546
8	Sumoylation	MPVKRSLKLDGLLEE CCCCCCCCCCCHHCC	45.86	-
8	Ubiquitination	MPVKRSLKLDGLLEE CCCCCCCCCCCHHCC	45.86	-
8	Sumoylation	MPVKRSLKLDGLLEE CCCCCCCCCCCHHCC	45.86	28112733
17	Phosphorylation	DGLLEENSFDPSKIT CCHHCCCCCCHHHCC	34.01	25159151
18 (in isoform 5)	Phosphorylation	-	27.82	24719451
18	Phosphorylation	GLLEENSFDPSKITR CHHCCCCCCHHHCCC	27.82	24719451
21	Phosphorylation	EENSFDPSKITRKKS CCCCCCHHHCCCCCE	38.24	26074081
22	Sumoylation	ENSFDPSKITRKKSV CCCCCHHHCCCCCEE	54.18	28112733
22	Ubiquitination	ENSFDPSKITRKKSV CCCCCHHHCCCCCEE	54.18	-
27	Methylation	PSKITRKKSVITYSP HHHCCCCCEEEEECC	46.82	-
28	Phosphorylation	SKITRKKSVITYSPT HHCCCCCEEEEECCC	23.06	30266825
31	Phosphorylation	TRKKSVITYSPTTGT CCCCEEEEECCCCCE	18.78	30266825
32	Phosphorylation	RKKSVITYSPTTGTC CCCEEEEECCCCCEE	11.09	30266825
33	Phosphorylation	KKSVITYSPTTGTCQ CCEEEEECCCCCEEE	13.71	30266825
35	Phosphorylation	SVITYSPTTGTCQMS EEEEECCCCCEEEEE	31.73	30266825
36	Phosphorylation	VITYSPTTGTCQMSL EEEECCCCCEEEEEE	33.60	30266825
38	Phosphorylation	TYSPTTGTCQMSLFA EECCCCCEEEEEEEE	9.47	30266825
42	Phosphorylation	TTGTCQMSLFASPTS CCCEEEEEEEECCCC	8.41	30266825
46	Phosphorylation	CQMSLFASPTSSEEQ EEEEEEECCCCHHHH	22.75	30266825
48	Phosphorylation	MSLFASPTSSEEQKH EEEEECCCCHHHHHH	42.25	30266825
49	Phosphorylation	SLFASPTSSEEQKHR EEEECCCCHHHHHHH	38.85	30266825
50	Phosphorylation	LFASPTSSEEQKHRN EEECCCCHHHHHHHC	47.86	30266825
56	Phosphorylation	SSEEQKHRNGLSNEK CHHHHHHHCCCCHHH	46.04	27251275
60	Phosphorylation	QKHRNGLSNEKRKKL HHHHCCCCHHHHHHC	44.32	20860994
66	Sumoylation	LSNEKRKKLNHPSLT CCHHHHHHCCCCCCC	59.56	-
66	Ubiquitination	LSNEKRKKLNHPSLT CCHHHHHHCCCCCCC	59.56	-
66	Sumoylation	LSNEKRKKLNHPSLT CCHHHHHHCCCCCCC	59.56	-
71	Phosphorylation	RKKLNHPSLTESKES HHHCCCCCCCCCCCC	40.13	10490654
72	Phosphorylation	KKLNHPSLTESKEST HHCCCCCCCCCCCCC	7.89	24719451
73	Phosphorylation	KLNHPSLTESKESTT HCCCCCCCCCCCCCC	42.42	28450419
74	Phosphorylation	LNHPSLTESKESTTK CCCCCCCCCCCCCCC	66.17	27251275
75	Phosphorylation	NHPSLTESKESTTKD CCCCCCCCCCCCCCC	36.17	23186163
76	Ubiquitination	HPSLTESKESTTKDN CCCCCCCCCCCCCCH	49.83	-
81	Ubiquitination	ESKESTTKDNDEFMM CCCCCCCCCHHHHHH	55.40	-
92	Sumoylation	EFMMLLSKVEKLSEE HHHHHHHHHHHHHHH	55.15	-
92	Ubiquitination	EFMMLLSKVEKLSEE HHHHHHHHHHHHHHH	55.15	-
92	Sumoylation	EFMMLLSKVEKLSEE HHHHHHHHHHHHHHH	55.15	-
126	Phosphorylation	LENLIGISCASHFLK HHHHHHHHHHHHHHH	9.83	20068231
129	Phosphorylation	LIGISCASHFLKREM HHHHHHHHHHHHHHH	21.06	20068231
133	Ubiquitination	SCASHFLKREMQKTK HHHHHHHHHHHHHHH	45.42	-
154	Ubiquitination	NKQKLFEKSTGLPHK HHHHHHHHHHCCCCH	46.08	-
155	Phosphorylation	KQKLFEKSTGLPHKA HHHHHHHHHCCCCHH	22.10	27251275
156	Phosphorylation	QKLFEKSTGLPHKAS HHHHHHHHCCCCHHH	54.53	27251275
161	Ubiquitination	KSTGLPHKASRHLDS HHHCCCCHHHHCCCH	46.23	-
163	Phosphorylation	TGLPHKASRHLDSYE HCCCCHHHHCCCHHH	25.65	27251275
168	Phosphorylation	KASRHLDSYEFLKAI HHHHCCCHHHHHHHH	32.68	20068231
169	Phosphorylation	ASRHLDSYEFLKAIL HHHCCCHHHHHHHHH	15.46	29496907
172 (in isoform 5)	Ubiquitination	-	2.15	-
173	Ubiquitination	LDSYEFLKAILN--- CCHHHHHHHHHC---	38.41	-
195	Phosphorylation	------------------------- -------------------------		27251275
207	Phosphorylation	------------------------------------- -------------------------------------		27251275
208	Phosphorylation	-------------------------------------- --------------------------------------		27251275

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
28	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
33	S	Phosphorylation	Kinase	CDK2	P24941	PSP
46	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:16252010

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARFP2_HUMAN	ARFIP2	physical	16189514
THA_HUMAN	THRA	physical	11713274
RXRG_HUMAN	RXRG	physical	11713274
CENPR_HUMAN	ITGB3BP	physical	11713274
NFKB1_HUMAN	NFKB1	physical	12244126
TF65_HUMAN	RELA	physical	12244126
CCNA2_HUMAN	CCNA2	physical	10673397
RXRA_HUMAN	RXRA	physical	10490654
THA_HUMAN	THRA	physical	10490654
ITB5_HUMAN	ITGB5	physical	10579726
MTA1_HUMAN	MTA1	physical	15254226
ACTN2_HUMAN	ACTN2	physical	15604093
A4_HUMAN	APP	physical	21832049
KDM1A_HUMAN	KDM1A	physical	23455924
ARFP2_HUMAN	ARFIP2	physical	25416956
UBR7_HUMAN	UBR7	physical	25416956
PIHD2_HUMAN	PIH1D2	physical	25416956
CENPU_HUMAN	CENPU	physical	26186194
CENPQ_HUMAN	CENPQ	physical	26186194
ATP5J_HUMAN	ATP5J	physical	26496610
FACD2_HUMAN	FANCD2	physical	26496610
FLNB_HUMAN	FLNB	physical	26496610
CENPI_HUMAN	CENPI	physical	26496610
MCM5_HUMAN	MCM5	physical	26496610
COG1_HUMAN	COG1	physical	26496610
ATPK_HUMAN	ATP5J2	physical	26496610
C2CD5_HUMAN	C2CD5	physical	26496610
C43BP_HUMAN	COL4A3BP	physical	26496610
COBL1_HUMAN	COBLL1	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
CAB45_HUMAN	SDF4	physical	26496610
PPHLN_HUMAN	PPHLN1	physical	26496610
CENPN_HUMAN	CENPN	physical	26496610
UBE2O_HUMAN	UBE2O	physical	26496610
CENPK_HUMAN	CENPK	physical	26496610
CENPO_HUMAN	CENPO	physical	26496610
CENPU_HUMAN	CENPU	physical	26496610
CENPT_HUMAN	CENPT	physical	26496610
CENPP_HUMAN	CENPP	physical	26496610
CENPQ_HUMAN	CENPQ	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 CENPR_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-17, 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-17, AND MASSSPECTROMETRY.	18691976 [Abstract]