SKP2_MOUSE - dbPTM
SKP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKP2_MOUSE
UniProt AC Q9Z0Z3
Protein Name S-phase kinase-associated protein 2
Gene Name Skp2
Organism Mus musculus (Mouse).
Sequence Length 424
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Substrate recognition component of the 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. The SCF complex provides substrate specificity and interacts with both, the E2 ubiquitin-conjugating enzyme and the substrate. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration (By similarity)..
Protein Sequence MHRKHLQEIPDQSGNVTTSFTWGWDSSKTSELLSGMGVSALEKEEVDSENIPHGLLSNLGHPQSPPRKRVKGKGSDKDFVIIRRPKLSRENFPGVSWDSLPDELLLGIFSCLCLPELLRVSGVCKRWYRLSLDESLWQSLDLAGKNLHPDVTVRLLSRGVVAFRCPRSFMEQPLGESFSSFRVQHMDLSNSVINVSNLHKILSECSKLQNLSLEGLQLSDPIVKTLAQNENLVRLNLCGCSGFSESAVATLLSSCSRLDELNLSWCFDFTEKHVQAAVAHLPNTITQLNLSGYRKNLQKTDLCTIIKRCPNLIRLDLSDSIMLKNDCFPEFFQLNYLQHLSLSRCYDIIPDTLLELGEIPTLKTLQVFGIVPEGTLQLLREALPRLQINCAYFTTIARPTMDSKKNLEIWGIKCRLTLQKPSCL
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
29PhosphorylationWGWDSSKTSELLSGM
ECCCCCHHHHHHCCC
29.4025777480
30PhosphorylationGWDSSKTSELLSGMG
CCCCCHHHHHHCCCC
29.9525777480
34PhosphorylationSKTSELLSGMGVSAL
CHHHHHHCCCCCCHH
39.0825777480
39PhosphorylationLLSGMGVSALEKEEV
HHCCCCCCHHHHHHC
22.7725777480
48PhosphorylationLEKEEVDSENIPHGL
HHHHHCCCCCCCCHH
37.4123984901
57PhosphorylationNIPHGLLSNLGHPQS
CCCCHHHHHCCCCCC
34.7421149613
64PhosphorylationSNLGHPQSPPRKRVK
HHCCCCCCCCCCCCC
41.1221149613
68AcetylationHPQSPPRKRVKGKGS
CCCCCCCCCCCCCCC
68.2851346005
71AcetylationSPPRKRVKGKGSDKD
CCCCCCCCCCCCCCC
59.9651346003
75PhosphorylationKRVKGKGSDKDFVII
CCCCCCCCCCCEEEE
45.0025338131
88PhosphorylationIIRRPKLSRENFPGV
EEECCCCCCCCCCCC
43.6128059163
179PhosphorylationQPLGESFSSFRVQHM
CCCCCCCCCEEEEEC
37.53-
224UbiquitinationQLSDPIVKTLAQNEN
CCCCHHHHHHHCCCC
38.24-

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
256SPhosphorylationKinaseAMPKB1Q9Y478
PSP
256SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
256SPhosphorylationKinaseAMPKA1Q13131
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
68KAcetylation

-
71KAcetylation

-

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 SKP2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_MOUSESrcphysical
20596523
CDN1B_MOUSECdkn1bphysical
11463388
CUL1_HUMANCUL1physical
10790373
CUL1_MOUSECul1physical
11735228
SKP1_MOUSESkp1aphysical
11735228
E2F1_MOUSEE2f1physical
23868976
SKP1_MOUSESkp1aphysical
23868976
CUL1_MOUSECul1physical
23868976
CADH1_MOUSECdh1physical
24115035
SKP1_MOUSESkp1aphysical
24390425
CUL1_MOUSECul1physical
24390425
CUL1_HUMANCUL1physical
24390425
HS90B_HUMANHSP90AB1physical
24390425
CSN4_HUMANCOPS4physical
24390425
SKP1_HUMANSKP1physical
24390425
CADH1_MOUSECdh1physical
17601983

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKP2_MOUSE

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Related Literatures of Post-Translational Modification

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