UniProt ID | SKA2_HUMAN | |
---|---|---|
UniProt AC | Q8WVK7 | |
Protein Name | Spindle and kinetochore-associated protein 2 | |
Gene Name | SKA2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 121 | |
Subcellular Localization | Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. Localizes to both the mitotic spindle and kinetochore-associated | |
Protein Description | Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. [PubMed: 17093495] | |
Protein Sequence | MEAEVDKLELMFQKAESDLDYIQYRLEYEIKTNHPDSASEKNPVTLLKELSVIKSRYQTLYARFKPVAVEQKESKSRICATVKKTMNMIQKLQKQTDLELSPLTKEEKTAAEQFKFHMPDL | |
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 |
---|---|---|---|---|---|
21 | Phosphorylation | KAESDLDYIQYRLEY HHHHCCHHHHHHHHE | 9.38 | 27642862 | |
24 | Phosphorylation | SDLDYIQYRLEYEIK HCCHHHHHHHHEEHH | 13.96 | 27642862 | |
31 | Ubiquitination | YRLEYEIKTNHPDSA HHHHEEHHCCCCCCC | 31.19 | - | |
41 | Ubiquitination | HPDSASEKNPVTLLK CCCCCCCCCCCHHHH | 65.15 | - | |
62 (in isoform 2) | Phosphorylation | - | 17.34 | - | |
65 | Ubiquitination | QTLYARFKPVAVEQK HHHHHHHCCEEEECC | 32.79 | - | |
72 | Ubiquitination | KPVAVEQKESKSRIC CCEEEECCCCCCHHH | 50.91 | - | |
83 | Acetylation | SRICATVKKTMNMIQ CHHHHHHHHHHHHHH | 37.87 | 25953088 | |
85 | Phosphorylation | ICATVKKTMNMIQKL HHHHHHHHHHHHHHH | 14.20 | 30631047 | |
94 | Ubiquitination | NMIQKLQKQTDLELS HHHHHHHHHCCCCCC | 66.65 | - | |
96 | Phosphorylation | IQKLQKQTDLELSPL HHHHHHHCCCCCCCC | 49.97 | 23403867 | |
101 | Phosphorylation | KQTDLELSPLTKEEK HHCCCCCCCCCHHHH | 14.42 | 30266825 | |
104 | Phosphorylation | DLELSPLTKEEKTAA CCCCCCCCHHHHHHH | 39.53 | 30266825 | |
105 | Ubiquitination | LELSPLTKEEKTAAE CCCCCCCHHHHHHHH | 72.12 | - | |
115 | Ubiquitination | KTAAEQFKFHMPDL- HHHHHHHCCCCCCC- | 33.77 | - |
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 SKA2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SKA2_HUMAN !! |
* 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 SKA2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DSN1_HUMAN | DSN1 | physical | 22371557 | |
SPC24_HUMAN | SPC24 | physical | 22371557 | |
SKA1_HUMAN | SKA1 | physical | 17093495 |
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 |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASSSPECTROMETRY. | |
"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-101, AND MASSSPECTROMETRY. | |
"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-101, AND MASSSPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASSSPECTROMETRY. |