UniProt ID | CENPA_HUMAN | |
---|---|---|
UniProt AC | P49450 | |
Protein Name | Histone H3-like centromeric protein A | |
Gene Name | CENPA | |
Organism | Homo sapiens (Human). | |
Sequence Length | 140 | |
Subcellular Localization | Nucleus . Chromosome, centromere, kinetochore . Chromosome, centromere . Localizes exclusively in the kinetochore domain of centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constric | |
Protein Description | Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. [PubMed: 7962047] | |
Protein Sequence | MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Methylation | ------MGPRRRSRK ------CCCCCCCCC | 25.15 | 26543159 | |
7 | Phosphorylation | -MGPRRRSRKPEAPR -CCCCCCCCCCCCCC | 42.73 | 26055452 | |
17 | Phosphorylation | PEAPRRRSPSPTPTP CCCCCCCCCCCCCCC | 28.11 | 29255136 | |
17 (in isoform 2) | Phosphorylation | - | 28.11 | - | |
19 (in isoform 2) | Phosphorylation | - | 42.52 | - | |
19 | Phosphorylation | APRRRSPSPTPTPGP CCCCCCCCCCCCCCC | 42.52 | 29255136 | |
21 | Phosphorylation | RRRSPSPTPTPGPSR CCCCCCCCCCCCCCC | 44.10 | 29255136 | |
21 (in isoform 2) | Phosphorylation | - | 44.10 | - | |
23 | Phosphorylation | RSPSPTPTPGPSRRG CCCCCCCCCCCCCCC | 43.27 | 30266825 | |
23 (in isoform 2) | Phosphorylation | - | 43.27 | - | |
27 | Phosphorylation | PTPTPGPSRRGPSLG CCCCCCCCCCCCCCC | 40.29 | 22167270 | |
27 (in isoform 2) | Phosphorylation | - | 40.29 | - | |
32 | Phosphorylation | GPSRRGPSLGASSHQ CCCCCCCCCCCCCHH | 42.11 | 30576142 | |
36 | Phosphorylation | RGPSLGASSHQHSRR CCCCCCCCCHHHHHH | 26.93 | 30576142 | |
37 | Phosphorylation | GPSLGASSHQHSRRR CCCCCCCCHHHHHHH | 26.99 | 23927012 | |
41 | Phosphorylation | GASSHQHSRRRQGWL CCCCHHHHHHHHHHH | 22.40 | 23927012 | |
42 | Methylation | ASSHQHSRRRQGWLK CCCHHHHHHHHHHHH | 35.36 | - | |
68 | Phosphorylation | LIRKLPFSRLAREIC HHHHCCHHHHHHHHH | 25.17 | 11756469 | |
124 | Ubiquitination | GRVTLFPKDVQLARR CCEEECHHHHHHHHH | 64.30 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
7 | S | Phosphorylation | Kinase | AURA | O14965 | PSP |
7 | S | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
19 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
68 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | ICP0 | P08393 | PMID:22199232 |
* 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 CENPA_HUMAN !! |
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. |
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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; SER-19; THR-23 ANDSER-27, AND MASS SPECTROMETRY. | |
"Aurora-C and Aurora-B share phosphorylation and regulation of CENP-Aand Borealin during mitosis."; Slattery S.D., Moore R.V., Brinkley B.R., Hall R.M.; Cell Cycle 7:787-795(2008). Cited for: PHOSPHORYLATION AT SER-7. | |
"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-17 AND SER-19, AND MASSSPECTROMETRY. | |
"CENP-A phosphorylation by Aurora-A in prophase is required forenrichment of Aurora-B at inner centromeres and for kinetochorefunction."; Kunitoku N., Sasayama T., Marumoto T., Zhang D., Honda S.,Kobayashi O., Hatakeyama K., Ushio Y., Saya H., Hirota T.; Dev. Cell 5:853-864(2003). Cited for: PHOSPHORYLATION AT SER-7, AND MUTAGENESIS OF SER-7. | |
"CENP-A is phosphorylated by Aurora B kinase and plays an unexpectedrole in completion of cytokinesis."; Zeitlin S.G., Shelby R.D., Sullivan K.F.; J. Cell Biol. 155:1147-1157(2001). Cited for: PHOSPHORYLATION AT SER-7, AND MUTAGENESIS OF SER-7. |