UniProt ID | SKP2_HUMAN | |
---|---|---|
UniProt AC | Q13309 | |
Protein Name | S-phase kinase-associated protein 2 | |
Gene Name | SKP2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 424 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration.. | |
Protein Sequence | MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL | |
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 |
---|---|---|---|---|---|
29 | Phosphorylation | WGWDSSKTSELLSGM CCCCCHHHHHHHCCC | 29.40 | 24144214 | |
30 | Phosphorylation | GWDSSKTSELLSGMG CCCCHHHHHHHCCCC | 29.95 | 24144214 | |
34 | Phosphorylation | SKTSELLSGMGVSAL HHHHHHHCCCCCCHH | 39.08 | 24144214 | |
39 | Phosphorylation | LLSGMGVSALEKEEP HHCCCCCCHHCCCCC | 22.77 | 24144214 | |
43 | Sumoylation | MGVSALEKEEPDSEN CCCCHHCCCCCCCCC | 69.13 | - | |
48 (in isoform 2) | Phosphorylation | - | 43.17 | - | |
48 | Phosphorylation | LEKEEPDSENIPQEL HCCCCCCCCCCCHHH | 43.17 | 25159151 | |
57 (in isoform 2) | Phosphorylation | - | 42.50 | - | |
57 | Phosphorylation | NIPQELLSNLGHPES CCCHHHHHHCCCCCC | 42.50 | 22167270 | |
64 | Phosphorylation | SNLGHPESPPRKRLK HHCCCCCCCCCHHCC | 44.66 | 22167270 | |
64 (in isoform 2) | Phosphorylation | - | 44.66 | - | |
68 | Acetylation | HPESPPRKRLKSKGS CCCCCCCHHCCCCCC | 68.78 | 22770219 | |
71 | Acetylation | SPPRKRLKSKGSDKD CCCCHHCCCCCCCCC | 54.90 | 22770219 | |
72 | Phosphorylation | PPRKRLKSKGSDKDF CCCHHCCCCCCCCCE | 47.01 | 23927012 | |
73 | Ubiquitination | PRKRLKSKGSDKDFV CCHHCCCCCCCCCEE | 61.93 | - | |
75 | Phosphorylation | KRLKSKGSDKDFVIV HHCCCCCCCCCEEEE | 45.27 | 23927012 | |
77 | Ubiquitination | LKSKGSDKDFVIVRR CCCCCCCCCEEEEEC | 55.55 | - | |
77 | Acetylation | LKSKGSDKDFVIVRR CCCCCCCCCEEEEEC | 55.55 | 25953088 | |
125 | Ubiquitination | LKVSGVCKRWYRLAS HHHHCCCHHHHHHCC | 43.49 | - | |
145 | Ubiquitination | QTLDLTGKNLHPDVT HHHCCCCCCCCCCHH | 51.61 | 21890473 | |
145 (in isoform 1) | Ubiquitination | - | 51.61 | 21890473 | |
145 (in isoform 2) | Ubiquitination | - | 51.61 | 21890473 | |
145 | Ubiquitination | QTLDLTGKNLHPDVT HHHCCCCCCCCCCHH | 51.61 | 21890473 | |
179 | Phosphorylation | QPLAEHFSPFRVQHM CHHHHHCCCCEEEEC | 25.66 | 30266825 | |
206 | Phosphorylation | HGILSQCSKLQNLSL HHHHHHHHHHCCCCC | 28.85 | 24719451 | |
207 | Ubiquitination | GILSQCSKLQNLSLE HHHHHHHHHCCCCCC | 62.81 | - | |
212 | Phosphorylation | CSKLQNLSLEGLRLS HHHHCCCCCCCCCCC | 31.74 | 21406692 | |
219 | Phosphorylation | SLEGLRLSDPIVNTL CCCCCCCCCHHHHHH | 34.60 | 27461979 | |
225 | Phosphorylation | LSDPIVNTLAKNSNL CCCHHHHHHHHCCCE | 19.73 | 27461979 | |
228 (in isoform 2) | Ubiquitination | - | 65.11 | 21890473 | |
228 (in isoform 1) | Ubiquitination | - | 65.11 | 21890473 | |
228 | Ubiquitination | PIVNTLAKNSNLVRL HHHHHHHHCCCEEEE | 65.11 | 2190698 | |
256 | Phosphorylation | QTLLSSCSRLDELNL HHHHHHCCCCHHCCC | 37.51 | - | |
299 | Ubiquitination | GYRKNLQKSDLSTLV HHHHHCCHHCHHHHH | 49.45 | - | |
303 | Phosphorylation | NLQKSDLSTLVRRCP HCCHHCHHHHHHHCC | 25.37 | - | |
341 | Phosphorylation | LNYLQHLSLSRCYDI HHHHHHHCHHHHHHC | 23.36 | 24719451 | |
343 | Phosphorylation | YLQHLSLSRCYDIIP HHHHHCHHHHHHCCH | 19.54 | 17081983 | |
367 (in isoform 2) | Phosphorylation | - | 5.51 | 30631047 | |
405 | Ubiquitination | RPTIGNKKNQEIWGI CCCCCCCCCCEEEEE | 68.79 | - | |
413 | Ubiquitination | NQEIWGIKCRLTLQK CCEEEEEEEEEEECC | 14.90 | - | |
417 | Phosphorylation | WGIKCRLTLQKPSCL EEEEEEEEECCCCCC | 14.06 | 20663873 | |
420 | Ubiquitination | KCRLTLQKPSCL--- EEEEEECCCCCC--- | 41.85 | - | |
420 | Acetylation | KCRLTLQKPSCL--- EEEEEECCCCCC--- | 41.85 | 25953088 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
64 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
64 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
64 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
64 | S | Phosphorylation | Kinase | PIM1 | P26794 | PSP |
72 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
72 | S | Phosphorylation | Kinase | PIM1 | P26794 | PSP |
256 | S | Phosphorylation | Kinase | AMPKB1 | Q9Y478 | PSP |
256 | S | Phosphorylation | Kinase | AMPKG2 | Q9UGJ0 | PSP |
256 | S | Phosphorylation | Kinase | AMPKA1 | Q13131 | PSP |
417 | T | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
417 | T | Phosphorylation | Kinase | PIM1 | P26794 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | FZR1 | Q9UM11 | PMID:15014502 |
- | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:12813041 |
- | K | Ubiquitination | E3 ubiquitin ligase | VHL | P40337 | PMID:21358672 |
* 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 SKP2_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 |
"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-64, AND MASSSPECTROMETRY. | |
"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-64, 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-64, AND MASSSPECTROMETRY. | |
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASSSPECTROMETRY. | |
"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-64, AND MASSSPECTROMETRY. |