SKP2_HUMAN - dbPTM
SKP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
29PhosphorylationWGWDSSKTSELLSGM
CCCCCHHHHHHHCCC
29.4024144214
30PhosphorylationGWDSSKTSELLSGMG
CCCCHHHHHHHCCCC
29.9524144214
34PhosphorylationSKTSELLSGMGVSAL
HHHHHHHCCCCCCHH
39.0824144214
39PhosphorylationLLSGMGVSALEKEEP
HHCCCCCCHHCCCCC
22.7724144214
43SumoylationMGVSALEKEEPDSEN
CCCCHHCCCCCCCCC
69.13-
48 (in isoform 2)Phosphorylation-43.17-
48PhosphorylationLEKEEPDSENIPQEL
HCCCCCCCCCCCHHH
43.1725159151
57 (in isoform 2)Phosphorylation-42.50-
57PhosphorylationNIPQELLSNLGHPES
CCCHHHHHHCCCCCC
42.5022167270
64PhosphorylationSNLGHPESPPRKRLK
HHCCCCCCCCCHHCC
44.6622167270
64 (in isoform 2)Phosphorylation-44.66-
68AcetylationHPESPPRKRLKSKGS
CCCCCCCHHCCCCCC
68.7822770219
71AcetylationSPPRKRLKSKGSDKD
CCCCHHCCCCCCCCC
54.9022770219
72PhosphorylationPPRKRLKSKGSDKDF
CCCHHCCCCCCCCCE
47.0123927012
73UbiquitinationPRKRLKSKGSDKDFV
CCHHCCCCCCCCCEE
61.93-
75PhosphorylationKRLKSKGSDKDFVIV
HHCCCCCCCCCEEEE
45.2723927012
77UbiquitinationLKSKGSDKDFVIVRR
CCCCCCCCCEEEEEC
55.55-
77AcetylationLKSKGSDKDFVIVRR
CCCCCCCCCEEEEEC
55.5525953088
125UbiquitinationLKVSGVCKRWYRLAS
HHHHCCCHHHHHHCC
43.49-
145UbiquitinationQTLDLTGKNLHPDVT
HHHCCCCCCCCCCHH
51.6121890473
145 (in isoform 1)Ubiquitination-51.6121890473
145 (in isoform 2)Ubiquitination-51.6121890473
145UbiquitinationQTLDLTGKNLHPDVT
HHHCCCCCCCCCCHH
51.6121890473
179PhosphorylationQPLAEHFSPFRVQHM
CHHHHHCCCCEEEEC
25.6630266825
206PhosphorylationHGILSQCSKLQNLSL
HHHHHHHHHHCCCCC
28.8524719451
207UbiquitinationGILSQCSKLQNLSLE
HHHHHHHHHCCCCCC
62.81-
212PhosphorylationCSKLQNLSLEGLRLS
HHHHCCCCCCCCCCC
31.7421406692
219PhosphorylationSLEGLRLSDPIVNTL
CCCCCCCCCHHHHHH
34.6027461979
225PhosphorylationLSDPIVNTLAKNSNL
CCCHHHHHHHHCCCE
19.7327461979
228 (in isoform 2)Ubiquitination-65.1121890473
228 (in isoform 1)Ubiquitination-65.1121890473
228UbiquitinationPIVNTLAKNSNLVRL
HHHHHHHHCCCEEEE
65.112190698
256PhosphorylationQTLLSSCSRLDELNL
HHHHHHCCCCHHCCC
37.51-
299UbiquitinationGYRKNLQKSDLSTLV
HHHHHCCHHCHHHHH
49.45-
303PhosphorylationNLQKSDLSTLVRRCP
HCCHHCHHHHHHHCC
25.37-
341PhosphorylationLNYLQHLSLSRCYDI
HHHHHHHCHHHHHHC
23.3624719451
343PhosphorylationYLQHLSLSRCYDIIP
HHHHHCHHHHHHCCH
19.5417081983
367 (in isoform 2)Phosphorylation-5.5130631047
405UbiquitinationRPTIGNKKNQEIWGI
CCCCCCCCCCEEEEE
68.79-
413UbiquitinationNQEIWGIKCRLTLQK
CCEEEEEEEEEEECC
14.90-
417PhosphorylationWGIKCRLTLQKPSCL
EEEEEEEEECCCCCC
14.0620663873
420UbiquitinationKCRLTLQKPSCL---
EEEEEECCCCCC---
41.85-
420AcetylationKCRLTLQKPSCL---
EEEEEECCCCCC---
41.8525953088

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
64SPhosphorylationKinaseCDK2P24941
PSP
64SPhosphorylationKinaseMAPK14Q16539
GPS
64SPhosphorylationKinasePIM1P11309
PSP
64SPhosphorylationKinasePIM1P26794
PSP
72SPhosphorylationKinasePIM1P11309
PSP
72SPhosphorylationKinasePIM1P26794
PSP
256SPhosphorylationKinaseAMPKB1Q9Y478
PSP
256SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
256SPhosphorylationKinaseAMPKA1Q13131
PSP
417TPhosphorylationKinasePIM1P11309
PSP
417TPhosphorylationKinasePIM1P26794
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:15014502
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:12813041
-KUbiquitinationE3 ubiquitin ligaseVHLP40337
PMID:21358672

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

22770219
71KAcetylation

22770219

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFE2_HUMANTCF3physical
14592976
CUL1_HUMANCUL1physical
12840033
CDT1_HUMANCDT1physical
12840033
CKS1_HUMANCKS1Bphysical
12813041
CDN1B_HUMANCDKN1Bphysical
12813041
CUL1_HUMANCUL1physical
12609982
SKP1_HUMANSKP1physical
12609982
CKS1_HUMANCKS1Bphysical
12140288
CDN1B_HUMANCDKN1Bphysical
12140288
CKS1_HUMANCKS1Bphysical
11231585
CUL1_HUMANCUL1physical
9430629
SKP1_HUMANSKP1physical
10918611
ORC1_HUMANORC1physical
11931757
CUL1_HUMANCUL1physical
10559858
CCNA2_HUMANCCNA2physical
10559858
CDK2_HUMANCDK2physical
10559858
SKP1_HUMANSKP1physical
10559858
E2F1_HUMANE2F1physical
10559858
MYBB_HUMANMYBL2physical
10871850
CKS1_HUMANCKS1Bphysical
18519678
TAL1_HUMANTAL1physical
17962192
CDN1A_HUMANCDKN1Aphysical
17679094
CUL1_HUMANCUL1physical
17439941
CKS1_HUMANCKS1Bphysical
17409098
CCNA1_HUMANCCNA1physical
16774918
CUL1_HUMANCUL1physical
16774918
CDN1B_HUMANCDKN1Bphysical
16774918
TOB1_HUMANTOB1physical
16951159
CUL1_HUMANCUL1physical
16880511
RO52_HUMANTRIM21physical
16880511
SKP1_HUMANSKP1physical
16880511
ELF4_HUMANELF4physical
16581786
RAG2_HUMANRAG2physical
15949444
FOXO1_HUMANFOXO1physical
15668399
RB_HUMANRB1physical
15469821
SKP1_HUMANSKP1physical
15469821
SKP1_HUMANSKP1physical
15342634
UBP18_HUMANUSP18physical
15342634
SMAD4_HUMANSMAD4physical
15314162
WEE1_HUMANWEE1physical
15070733
SKP1_HUMANSKP1physical
15070733
CDT1_HUMANCDT1physical
15004027
E2F1_HUMANE2F1physical
12097298
MYC_HUMANMYCphysical
12769844
RASF1_HUMANRASSF1physical
18071316
UBP13_HUMANUSP13physical
21571647
UFD1_HUMANUFD1Lphysical
21571647
KMT2A_HUMANKMT2Aphysical
20818375
PIM1_HUMANPIM1physical
20663873
UB2R1_HUMANCDC34physical
20663873
CDC20_HUMANCDC20physical
20663873
ING3_HUMANING3physical
19935701
CDN1A_HUMANCDKN1Aphysical
19686743
CDN1B_HUMANCDKN1Bphysical
19686743
CDN1C_HUMANCDKN1Cphysical
19686743
RASF1_HUMANRASSF1physical
19686743
FOXO1_HUMANFOXO1physical
19686743
FZR1_HUMANFZR1physical
19686743
CDK2_HUMANCDK2physical
19686743
CC14B_HUMANCDC14Bphysical
19686743
BTG2_HUMANBTG2physical
19615363
AKT1_HUMANAKT1physical
19270694
SKP1_HUMANSKP1physical
19270694
CUL1_HUMANCUL1physical
19270694
1433B_HUMANYWHABphysical
19270694
JAK3_MOUSEJak3physical
21969365
SKP1_HUMANSKP1physical
20041211
FOXO3_HUMANFOXO3physical
21841822
JAK2_HUMANJAK2physical
21119685
ASB2_HUMANASB2physical
21119685
CUL1_HUMANCUL1physical
21119685
CUL5_HUMANCUL5physical
21119685
PHB_HUMANPHBphysical
20134482
VHL_HUMANVHLphysical
21358672
AKT1_HUMANAKT1physical
21358672
FZR1_HUMANFZR1physical
20663873
CUL1_HUMANCUL1physical
15456869
SKP1_HUMANSKP1physical
15456869
TFE2_HUMANTCF3physical
15456869
CHIP_HUMANSTUB1physical
15456869
DNJB5_HUMANDNAJB5physical
15456869
CKS1_HUMANCKS1Bphysical
11463388
CDN1B_HUMANCDKN1Bphysical
11463388
ATM_HUMANATMphysical
22464731
RAD50_HUMANRAD50physical
22464731
MRE11_HUMANMRE11Aphysical
22464731
CUL1_HUMANCUL1physical
22464731
SKP1_HUMANSKP1physical
22464731
NBN_HUMANNBNphysical
22464731
TYY1_HUMANYY1physical
22440256
CUL1_HUMANCUL1physical
17704768
ELOC_HUMANTCEB1physical
17786314
MYC_HUMANMYCphysical
12963825
CCNG2_HUMANCCNG2physical
18784254
CDN1A_HUMANCDKN1Aphysical
13678583
AKT1_HUMANAKT1physical
19270695
CDK2_HUMANCDK2physical
19270695
CCNA1_HUMANCCNA1physical
19270695
IMA5_HUMANKPNA1physical
19270695
IMA7_HUMANKPNA6physical
19270695
SPDYA_HUMANSPDYAphysical
19622356
CUL1_HUMANCUL1physical
20160477
SKP1_HUMANSKP1physical
20160477
CDN1B_HUMANCDKN1Bphysical
20160477
CCNB1_HUMANCCNB1physical
20160477
CDK2_HUMANCDK2physical
20160477
CCNA2_HUMANCCNA2physical
20160477
CDN1B_HUMANCDKN1Bphysical
15075339
SKP1_HUMANSKP1physical
19398581
RBX1_HUMANRBX1physical
19398581
CUL1_HUMANCUL1physical
19398581
CCNA2_HUMANCCNA2physical
18604603
CDK2_HUMANCDK2physical
18604603
CUL1_HUMANCUL1physical
22013077
CUL1_HUMANCUL1physical
17438373
RBL2_HUMANRBL2physical
12435635
CDN1B_HUMANCDKN1Bphysical
15355997
CCNA2_HUMANCCNA2physical
15355997
SKP1_HUMANSKP1physical
16275325
RBX2_HUMANRNF7physical
11255262
CDN1B_HUMANCDKN1Bphysical
10559916
CUL1_HUMANCUL1physical
10559916
SKP1_HUMANSKP1physical
10559916
CKS1_HUMANCKS1Bphysical
16338391
CUL1_HUMANCUL1physical
9636170
CDN1B_HUMANCDKN1Bphysical
22310285
SKP1_HUMANSKP1physical
22310285
CUL1_HUMANCUL1physical
22310285
FOXO3_HUMANFOXO3physical
22310285
E2F1_HUMANE2F1physical
17471231
RIR2_HUMANRRM2physical
18820369
BTG1_HUMANBTG1physical
22975506
BTG2_HUMANBTG2physical
22975506
SIR3_HUMANSIRT3physical
23045395
CDN1B_HUMANCDKN1Bphysical
11565034
UB2R1_HUMANCDC34physical
16774918
BRCA1_HUMANBRCA1physical
23086937
BARD1_HUMANBARD1physical
23086937
FBW1A_HUMANBTRCphysical
23071779
SKP1_HUMANSKP1physical
23261596
CDN1A_HUMANCDKN1Aphysical
23261596
CUL1_HUMANCUL1physical
18239684
SKP1_HUMANSKP1physical
18239684
RBX1_HUMANRBX1physical
18239684
CKS1_HUMANCKS1Bphysical
18239684
CDN1B_HUMANCDKN1Bphysical
18239684
SIR3_HUMANSIRT3physical
22770219
SIR4_HUMANSIRT4physical
22770219
SIR6_HUMANSIRT6physical
22770219
CDK2_HUMANCDK2physical
22770219
IMA5_HUMANKPNA1physical
22770219
IMA7_HUMANKPNA6physical
22770219
EP300_HUMANEP300physical
22770219
CDN1B_MOUSECdkn1bphysical
23589337
E2F1_HUMANE2F1physical
23868976
SKP1_HUMANSKP1physical
23868976
CUL1_HUMANCUL1physical
23868976
KMT2A_HUMANKMT2Aphysical
23868976
CDN1B_HUMANCDKN1Bphysical
23910095
FZR1_HUMANFZR1physical
23972993
CUL1_HUMANCUL1physical
24085301
SKP1_HUMANSKP1physical
24085301
CDN1B_HUMANCDKN1Bphysical
24085301
RND3_HUMANRND3physical
24045951
ANDR_HUMANARphysical
24347472
CUL1_HUMANCUL1physical
25143387
CDN1A_HUMANCDKN1Aphysical
18794347
ESR1_HUMANESR1physical
23770852
SKP1_HUMANSKP1physical
23770852
CUL1_HUMANCUL1physical
23770852
RBX1_HUMANRBX1physical
23770852
CDN1C_HUMANCDKN1Cphysical
12925736
CDN1B_HUMANCDKN1Bphysical
20663873
FZR1_HUMANFZR1physical
19270695
FZR1_HUMANFZR1physical
22770219
CDN1B_HUMANCDKN1Bphysical
22959436
CCNE1_HUMANCCNE1physical
22959436
CADH1_HUMANCDH1physical
20717963
CDN1B_MOUSECdkn1bphysical
15980415
CDN1A_HUMANCDKN1Aphysical
15980415
MEF2D_HUMANMEF2Dphysical
25733682
MEF2C_HUMANMEF2Cphysical
25733682
CDN1B_HUMANCDKN1Bphysical
22524983
SKP1_HUMANSKP1physical
22524983
CUL1_HUMANCUL1physical
22524983
NHRF1_HUMANSLC9A3R1physical
25492869
SK2L2_HUMANSKIV2L2physical
26344197
TP4AP_HUMANTRPC4APphysical
26038816
MYC_HUMANMYCphysical
26038816
EP300_HUMANEP300physical
26593157
SKP1_HUMANSKP1physical
26087183
AURKB_HUMANAURKBphysical
26697838
SKP1_HUMANSKP1physical
26474281
CADH1_HUMANCDH1physical
26474281
BRCA1_HUMANBRCA1physical
25659039
SKP2_HUMANSKP2physical
17254749
CUL1_HUMANCUL1physical
27542266
DCNL3_HUMANDCUN1D3physical
27542266
FBXW2_HUMANFBXW2physical
28090088
IFI27_HUMANIFI27physical
27194766
RICTR_HUMANRICTORphysical
28514442
CDK1_HUMANCDK1physical
28514442
LRCH2_HUMANLRCH2physical
28514442
LRC58_HUMANLRRC58physical
28514442
AP5B1_HUMANAP5B1physical
28514442
TTC9C_HUMANTTC9Cphysical
28514442
LRC40_HUMANLRRC40physical
28514442
DDX11_HUMANDDX11physical
28514442
OFD1_HUMANOFD1physical
28514442
FA83H_HUMANFAM83Hphysical
28514442
ATG2B_HUMANATG2Bphysical
28514442
IMDH2_HUMANIMPDH2physical
28514442
CDC20_HUMANCDC20physical
28514442
DISC1_HUMANDISC1physical
28514442
GFAP_HUMANGFAPphysical
28514442
SGT1_HUMANSUGT1physical
28514442
GRDN_HUMANCCDC88Aphysical
28514442
KDM5C_HUMANKDM5Cphysical
28514442
KPCD2_HUMANPRKD2physical
28514442
MFR1L_HUMANMTFR1Lphysical
28514442
UBB_HUMANUBBphysical
28514442
APC1_HUMANANAPC1physical
28514442
IQEC1_HUMANIQSEC1physical
28514442
ALMS1_HUMANALMS1physical
28514442
CUL1_HUMANCUL1physical
28514442
KIRR1_HUMANKIRRELphysical
28514442
FXL18_HUMANFBXL18physical
28514442
STIL_HUMANSTILphysical
28514442
STK3_HUMANSTK3physical
28514442
SAMD1_HUMANSAMD1physical
28514442
PHLP1_HUMANPHLPP1physical
28514442
WDR59_HUMANWDR59physical
28514442
MCM8_HUMANMCM8physical
28514442
UBP19_HUMANUSP19physical
28514442
CSN2_HUMANCOPS2physical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
TBB3_HUMANTUBB3physical
28514442
K1671_HUMANKIAA1671physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
DPYL4_HUMANDPYSL4physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
KANK2_HUMANKANK2physical
28514442
ZN507_HUMANZNF507physical
28514442
SENP1_HUMANSENP1physical
28514442
CSN6_HUMANCOPS6physical
28514442
P73_HUMANTP73physical
28514442
CDN1B_HUMANCDKN1Bphysical
19112177
SKP1_HUMANSKP1physical
28614300
CUL1_HUMANCUL1physical
28614300
MTOR_HUMANMTORphysical
28446188

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 SKP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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