CENPV_HUMAN - dbPTM
CENPV_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPV_HUMAN
UniProt AC Q7Z7K6
Protein Name Centromere protein V
Gene Name CENPV
Organism Homo sapiens (Human).
Sequence Length 275
Subcellular Localization Chromosome, centromere, kinetochore . Nucleus . Cytoplasm, cytoskeleton, spindle . Enriched at the nuclear periphery and around the nucleolus (PubMed:12196509). In mitotic cells, localizes to kinetochores from prometaphase to metaphase (PubMed:187728
Protein Description Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis..
Protein Sequence MRRSRSSAAAKLRGQKRSGASGASAAPAASAAAALAPSATRTRRSASQAGSKSQAVEKPPSEKPRLRRSSPRAQEEGPGEPPPPELALLPPPPPPPPTPATPTSSASNLDLGEQRERWETFQKRQKLTSEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFKLLKGAEHITTYTFNTHKAQHTFCKRCGVQSFYTPRSNPGGFGIAPHCLDEGTVRSMVTEEFNGSDWEKAMKEHKTIKNMSKE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MRRSRSSAAAKLR
--CCCCHHHHHHHHH		26.1026546556
11AcetylationSRSSAAAKLRGQKRS
CHHHHHHHHHCCCCC		33.7125953088
18 (in isoform 3)Phosphorylation-45.8325159151
18PhosphorylationKLRGQKRSGASGASA
HHHCCCCCCCCCCCH		45.8325159151
21 (in isoform 3)Phosphorylation-38.1218669648
21PhosphorylationGQKRSGASGASAAPA
CCCCCCCCCCCHHHH		38.1225159151
24PhosphorylationRSGASGASAAPAASA
CCCCCCCCHHHHHHH		28.6125159151
27 (in isoform 3)Phosphorylation-28.2422210691
30PhosphorylationASAAPAASAAAALAP
CCHHHHHHHHHHHCC		22.1324732914
35 (in isoform 3)Phosphorylation-6.5421406692
37 (in isoform 3)Phosphorylation-25.9121406692
38PhosphorylationAAAALAPSATRTRRS
HHHHHCCCHHHHHHH		36.3424732914
40PhosphorylationAALAPSATRTRRSAS
HHHCCCHHHHHHHHH		36.5924732914
42PhosphorylationLAPSATRTRRSASQA
HCCCHHHHHHHHHHC		26.5320068231
43MethylationAPSATRTRRSASQAG
CCCHHHHHHHHHHCC		27.54-
44PhosphorylationPSATRTRRSASQAGS
CCHHHHHHHHHHCCC		35.6433259812
45PhosphorylationSATRTRRSASQAGSK
CHHHHHHHHHHCCCH		29.0523312004
47PhosphorylationTRTRRSASQAGSKSQ
HHHHHHHHHCCCHHH		23.0828985074
51PhosphorylationRSASQAGSKSQAVEK
HHHHHCCCHHHCCCC		31.9523312004
52AcetylationSASQAGSKSQAVEKP
HHHHCCCHHHCCCCC		45.7426051181
53PhosphorylationASQAGSKSQAVEKPP
HHHCCCHHHCCCCCC		25.6823312004
60UbiquitinationSQAVEKPPSEKPRLR
HHCCCCCCCCCCCCC		67.2129967540
61PhosphorylationQAVEKPPSEKPRLRR
HCCCCCCCCCCCCCC		67.7729116813
63AcetylationVEKPPSEKPRLRRSS
CCCCCCCCCCCCCCC		39.5123749302
69PhosphorylationEKPRLRRSSPRAQEE
CCCCCCCCCCCHHHC		37.9617081983
70PhosphorylationKPRLRRSSPRAQEEG
CCCCCCCCCCHHHCC		19.3217081983
98O-linked_GlycosylationPPPPPPPTPATPTSS
CCCCCCCCCCCCCCC		31.1832119511
98PhosphorylationPPPPPPPTPATPTSS
CCCCCCCCCCCCCCC		31.1827499020
101O-linked_GlycosylationPPPPTPATPTSSASN
CCCCCCCCCCCCCCC		28.4432119511
101PhosphorylationPPPPTPATPTSSASN
CCCCCCCCCCCCCCC		28.4425159151
103O-linked_GlycosylationPPTPATPTSSASNLD
CCCCCCCCCCCCCCC		30.8432119511
103PhosphorylationPPTPATPTSSASNLD
CCCCCCCCCCCCCCC		30.8430177828
104PhosphorylationPTPATPTSSASNLDL
CCCCCCCCCCCCCCH		25.7220068231
104O-linked_GlycosylationPTPATPTSSASNLDL
CCCCCCCCCCCCCCH		25.7232119511
105PhosphorylationTPATPTSSASNLDLG
CCCCCCCCCCCCCHH		37.8920068231
107O-linked_GlycosylationATPTSSASNLDLGEQ
CCCCCCCCCCCHHHH		39.6132119511
107PhosphorylationATPTSSASNLDLGEQ
CCCCCCCCCCCHHHH		39.6120068231
120UbiquitinationEQRERWETFQKRQKL
HHHHHHHHHHHHHHC		25.1432015554
1232-HydroxyisobutyrylationERWETFQKRQKLTSE
HHHHHHHHHHHCCHH		53.24-
123UbiquitinationERWETFQKRQKLTSE
HHHHHHHHHHHCCHH		53.2429967540
131UbiquitinationRQKLTSEGAAKLLLD
HHHCCHHHHHHHHHH		30.5129967540
134UbiquitinationLTSEGAAKLLLDTFE
CCHHHHHHHHHHHHH		38.85-
147UbiquitinationFEYQGLVKHTGGCHC
HHHCCEEECCCCCCC		40.26-
190PhosphorylationRHFIVPASRFKLLKG
CCEEEEHHHHHHCCC		31.9829449344
193UbiquitinationIVPASRFKLLKGAEH
EEEHHHHHHCCCCCE		52.3729967540
202PhosphorylationLKGAEHITTYTFNTH
CCCCCEEEEEECCCH		18.6921406692
203PhosphorylationKGAEHITTYTFNTHK
CCCCEEEEEECCCHH		21.6921406692
204PhosphorylationGAEHITTYTFNTHKA
CCCEEEEEECCCHHC		10.7321406692
205PhosphorylationAEHITTYTFNTHKAQ
CCEEEEEECCCHHCC		14.3321406692
207UbiquitinationHITTYTFNTHKAQHT
EEEEEECCCHHCCCE		33.2129967540
208PhosphorylationITTYTFNTHKAQHTF
EEEEECCCHHCCCEE		22.1421406692
210AcetylationTYTFNTHKAQHTFCK
EEECCCHHCCCEEHH		47.9426051181
214UbiquitinationNTHKAQHTFCKRCGV
CCHHCCCEEHHHCCC		20.7429967540
217AcetylationKAQHTFCKRCGVQSF
HCCCEEHHHCCCCEE		46.6725953088
257PhosphorylationVTEEFNGSDWEKAMK
HCCHHCCHHHHHHHH		40.4320873877
258UbiquitinationTEEFNGSDWEKAMKE
CCHHCCHHHHHHHHH		59.9832015554
267UbiquitinationEKAMKEHKTIKNMSK
HHHHHHHHHHHHCCC		53.7029967540
267AcetylationEKAMKEHKTIKNMSK
HHHHHHHHHHHHCCC		53.707695369
270AcetylationMKEHKTIKNMSKE--
HHHHHHHHHCCCC--		52.4025953088
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 CENPV_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPV_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 CENPV_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYN_HUMANLYNphysical
19930468
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 CENPV_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-21, AND MASSSPECTROMETRY.

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