CDN1A_HUMAN - dbPTM
CDN1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDN1A_HUMAN
UniProt AC P38936
Protein Name Cyclin-dependent kinase inhibitor 1
Gene Name CDKN1A
Organism Homo sapiens (Human).
Sequence Length 164
Subcellular Localization Cytoplasm. Nucleus.
Protein Description May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding. [PubMed: 11595739]
Protein Sequence MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
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
2Acetylation------MSEPAGDVR
------CCCCCCCCC
52.8915574338
16UbiquitinationRQNPCGSKACRRLFG
CCCCCCCHHHHHHHC
36.4713678583
27PhosphorylationRLFGPVDSEQLSRDC
HHHCCCCHHHHHHHH
27.7227732954
31PhosphorylationPVDSEQLSRDCDALM
CCCHHHHHHHHHHHH
26.2625849741
50UbiquitinationQEARERWNFDFVTET
HHHHHHCCCCEEECC
32.60-
57PhosphorylationNFDFVTETPLEGDFA
CCCEEECCCCCCCCH
24.6522817900
65PhosphorylationPLEGDFAWERVRGLG
CCCCCCHHHHHCCCC
8.23-
75UbiquitinationVRGLGLPKLYLPTGP
HCCCCCCCEECCCCC
55.6021890473
75UbiquitinationVRGLGLPKLYLPTGP
HCCCCCCCEECCCCC
55.6021906983
77PhosphorylationGLGLPKLYLPTGPRR
CCCCCCEECCCCCCC
19.4328674419
80PhosphorylationLPKLYLPTGPRRGRD
CCCEECCCCCCCCCC
58.1725329316
91PhosphorylationRGRDELGGGRRPGTS
CCCCCCCCCCCCCCC
38.7712058028
97PhosphorylationGGGRRPGTSPALLQG
CCCCCCCCCHHHHCC
33.9328348404
98PhosphorylationGGRRPGTSPALLQGT
CCCCCCCCHHHHCCC
17.6822817900
109UbiquitinationLQGTAEEDHVDLSLS
HCCCCCCCCEEEEEE
38.32-
114PhosphorylationEEDHVDLSLSCTLVP
CCCCEEEEEEEEEEC
17.4818794347
123PhosphorylationSCTLVPRSGEQAEGS
EEEEECCCCCCCCCC
40.3823403867
130PhosphorylationSGEQAEGSPGGPGDS
CCCCCCCCCCCCCCC
16.3319664994
132PhosphorylationEQAEGSPGGPGDSQG
CCCCCCCCCCCCCHH
57.5317325029
137PhosphorylationSPGGPGDSQGRKRRQ
CCCCCCCCHHHHHCC
40.2123403867
141AcetylationPGDSQGRKRRQTSMT
CCCCHHHHHCCCCHH
59.7725231691
141UbiquitinationPGDSQGRKRRQTSMT
CCCCHHHHHCCCCHH
59.7713678583
145PhosphorylationQGRKRRQTSMTDFYH
HHHHHCCCCHHHHHH
20.7519822666
146PhosphorylationGRKRRQTSMTDFYHS
HHHHCCCCHHHHHHH
16.0211756412
148PhosphorylationKRRQTSMTDFYHSKR
HHCCCCHHHHHHHHH
23.7917283049
151PhosphorylationQTSMTDFYHSKRRLI
CCCHHHHHHHHHHHH
14.1624719451
153PhosphorylationSMTDFYHSKRRLIFS
CHHHHHHHHHHHHHC
19.2415851482
154UbiquitinationMTDFYHSKRRLIFSK
HHHHHHHHHHHHHCC
28.3813678583
154AcetylationMTDFYHSKRRLIFSK
HHHHHHHHHHHHHCC
28.3825231683
156DimethylationDFYHSKRRLIFSKRK
HHHHHHHHHHHCCCC
35.55-
156MethylationDFYHSKRRLIFSKRK
HHHHHHHHHHHCCCC
35.55101521401
157PhosphorylationFYHSKRRLIFSKRKP
HHHHHHHHHHCCCCC
5.57-
160PhosphorylationSKRRLIFSKRKP---
HHHHHHHCCCCC---
25.2618794347
161AcetylationKRRLIFSKRKP----
HHHHHHCCCCC----
54.4125231695
161UbiquitinationKRRLIFSKRKP----
HHHHHHCCCCC----
54.41-
163AcetylationRLIFSKRKP------
HHHHCCCCC------
59.8325231687
163UbiquitinationRLIFSKRKP------
HHHHCCCCC------
59.83-
164PhosphorylationLIFSKRKP-------
HHHCCCCC-------
54.1819664994
175Ubiquitination------------------
------------------
-
175Acetylation------------------
------------------
-
179Phosphorylation----------------------
----------------------
15001356
180Phosphorylation-----------------------
-----------------------
17855660
185Phosphorylation----------------------------
----------------------------
-
187Phosphorylation------------------------------
------------------------------
15851482
188Ubiquitination-------------------------------
-------------------------------
-
188Acetylation-------------------------------
-------------------------------
-
190Methylation---------------------------------
---------------------------------
-
194Phosphorylation-------------------------------------
-------------------------------------
10753973
195Acetylation--------------------------------------
--------------------------------------
-
195Ubiquitination--------------------------------------
--------------------------------------
-
197Acetylation----------------------------------------
----------------------------------------
-
197Ubiquitination----------------------------------------
----------------------------------------
-

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
55TPhosphorylationKinaseMELKQ61846
PSP
57TPhosphorylationKinaseMAPK14Q16539
GPS
57TPhosphorylationKinaseMAPK8P45983
GPS
57TPhosphorylationKinaseMAPK1P28482
GPS
57TPhosphorylationKinaseMAPK9P45984
GPS
57TPhosphorylationKinaseMAPK_GROUP-PhosphoELM
57TPhosphorylationKinaseGSK3AP49840
PSP
57TPhosphorylationKinaseGSK3BP49841
PSP
57TPhosphorylationKinaseGSK3BP49841
GPS
57TPhosphorylationKinaseMAPK-FAMILY-GPS
80TPhosphorylationKinaseLKB1Q15831
Uniprot
98SPhosphorylationKinaseMAPK3P27361
GPS
98SPhosphorylationKinaseMAPK8P45983
GPS
98SPhosphorylationKinaseMAPK1P28482
GPS
98SPhosphorylationKinaseMAP3K5Q99683
GPS
98SPhosphorylationKinaseMAPK9P45984
GPS
98SPhosphorylationKinaseMAPK10P53779
GPS
98SPhosphorylationKinaseCDK4P11802
PSP
98SPhosphorylationKinaseMAPK14Q16539
GPS
114SPhosphorylationKinaseGSK3BP49841
PSP
130SPhosphorylationKinaseMAPK9P45984
GPS
130SPhosphorylationKinaseMAPK10P53779
GPS
130SPhosphorylationKinaseP38AQ16539
PSP
130SPhosphorylationKinaseMAPK14P47811
GPS
130SPhosphorylationKinaseMAPK8P45983
GPS
130SPhosphorylationKinaseMAPK3P27361
GPS
130SPhosphorylationKinaseMAPK1P28482
GPS
130SPhosphorylationKinaseMAPK-FAMILY-GPS
130SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
130SPhosphorylationKinaseCDK6Q00534
PSP
130SPhosphorylationKinaseCDK4P11802
PSP
130SPhosphorylationKinaseCDK2P24941
PSP
130SPhosphorylationKinaseCDK1P06493
PSP
145TPhosphorylationKinaseAKT-FAMILY-GPS
145TPhosphorylationKinasePKB_GROUP-PhosphoELM
145TPhosphorylationKinasePIM2Q9P1W9
Uniprot
145TPhosphorylationKinasePKA-FAMILY-GPS
145TPhosphorylationKinasePKA-Uniprot
145TPhosphorylationKinaseAKT1P31749
Uniprot
145TPhosphorylationKinasePIM1P11309
Uniprot
145TPhosphorylationKinaseDAPK3O43293
PSP
145TPhosphorylationKinasePRKCAP17252
GPS
146SPhosphorylationKinasePKC-FAMILY-GPS
146SPhosphorylationKinaseAKT1P31749
PSP
146SPhosphorylationKinasePKB_GROUP-PhosphoELM
146SPhosphorylationKinasePKC-Uniprot
146SPhosphorylationKinasePIM1P11309
PSP
146SPhosphorylationKinasePRKCAP17252
GPS
146SPhosphorylationKinaseLATS2Q9NRM7
PSP
146SPhosphorylationKinaseAKT-FAMILY-GPS
146SPhosphorylationKinaseNUAK1O60285
Uniprot
146SPhosphorylationKinasePIM2Q9P1W9
PSP
153SPhosphorylationKinasePRKCAP17252
GPS
153SPhosphorylationKinaseDYR1BQ9Y463
PhosphoELM
160SPhosphorylationKinasePKC-FAMILY-GPS
160SPhosphorylationKinasePKC-Uniprot
-KUbiquitinationE3 ubiquitin ligaseRNF126Q9BV68
PMID:23026136
-KUbiquitinationE3 ubiquitin ligaseDTLQ9NZJ0
PMID:18703516
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:12393444
-KUbiquitinationE3 ubiquitin ligaseCDC20Q12834
PMID:17679094
-KUbiquitinationE3 ubiquitin ligaseCDCA3Q99618
PMID:14761977
-KUbiquitinationE3 ubiquitin ligaseMDM4O15151
PMID:18086887
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:10698510
-KUbiquitinationE3 ubiquitin ligaseMKRN1Q9UHC7
PMID:19536131
-KUbiquitinationE3 ubiquitin ligaseRNF144BQ7Z419
PMID:12853982
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:31831018

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2Subiquitylation

15574338
80TPhosphorylation

25329316
114SPhosphorylation

18794347
114Subiquitylation

18794347
141KAcetylation

-
145TPhosphorylation

10753973
145TPhosphorylation

10753973
145TPhosphorylation

10753973
146SPhosphorylation

10753973
146SPhosphorylation

10753973
154KAcetylation

23213251
161KAcetylation

-
163KAcetylation

-

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 CDN1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEX11_HUMANTEX11physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
PCNA_HUMANPCNAphysical
16189514
CDK2_HUMANCDK2physical
10878006
GA45A_HUMANGADD45Aphysical
10973963
BCCIP_HUMANBCCIPphysical
10878006
PARP1_HUMANPARP1physical
12930846
PCNA_HUMANPCNAphysical
12930846
CDK2_HUMANCDK2physical
12839982
CCNE1_HUMANCCNE1physical
12839982
RACK1_HUMANGNB2L1physical
16169070
HDA11_HUMANHDAC11physical
16169070
PCNA_HUMANPCNAphysical
9465025
M3K5_HUMANMAP3K5physical
12820963
TS101_HUMANTSG101physical
11943869
PCNA_HUMANPCNAphysical
8861913
CIZ1_HUMANCIZ1physical
10529385
SET_HUMANSETphysical
12407107
CUL4A_HUMANCUL4Aphysical
18794347
DDB1_HUMANDDB1physical
18794347
DTL_HUMANDTLphysical
18794347
PCNA_HUMANPCNAphysical
11313979
PSME3_HUMANPSME3physical
17588519
PCNA_HUMANPCNAphysical
17588519
SKP2_HUMANSKP2physical
17477906
HDAC1_HUMANHDAC1physical
20154723
CDK2_HUMANCDK2physical
20102411
CDK4_HUMANCDK4physical
20102411
CDK6_HUMANCDK6physical
20102411
MK08_HUMANMAPK8physical
20102411
JUN_HUMANJUNphysical
20102411
DTL_HUMANDTLphysical
18703516
DDB1_HUMANDDB1physical
18703516
G3P_HUMANGAPDHphysical
16474839
SET_HUMANSETphysical
16474839
PCNA_HUMANPCNAphysical
16474839
MDM2_HUMANMDM2physical
14761977
PCNA_HUMANPCNAphysical
16082198
CCNB1_HUMANCCNB1physical
16082198
HDAC1_HUMANHDAC1physical
16082198
HDAC4_HUMANHDAC4physical
16082198
HDAC6_HUMANHDAC6physical
16082198
CCND1_HUMANCCND1physical
16082198
HDAC2_HUMANHDAC2physical
16082198
R144B_HUMANRNF144Bphysical
12853982
EP300_HUMANEP300physical
18263614
MDM4_HUMANMDM4physical
18086887
PRS8_HUMANPSMC5physical
18086887
PCNA_HUMANPCNAphysical
18086887
DTL_HUMANDTLphysical
20606006
CDK4_HUMANCDK4physical
17556661
CCND1_HUMANCCND1physical
17556661
NEMO_HUMANIKBKGphysical
19609363
OPTN_HUMANOPTNphysical
19609363
NPM_HUMANNPM1physical
19221506
MDM4_HUMANMDM4physical
21148311
SPRE1_HUMANSPRED1physical
21900206
ATX3_HUMANATXN3physical
21900206
VATA_HUMANATP6V1Aphysical
21900206
HMGX3_HUMANHMGXB3physical
21900206
P53_HUMANTP53physical
21900206
CSAD_HUMANCSADphysical
21900206
S10A8_HUMANS100A8physical
21900206
CPNE6_HUMANCPNE6physical
21900206
GBB2_HUMANGNB2physical
21900206
EXT2_HUMANEXT2physical
21900206
CAB45_HUMANSDF4physical
21900206
FAD1_HUMANFLAD1physical
21900206
CPNE2_HUMANCPNE2physical
21900206
OTUB1_HUMANOTUB1physical
21900206
ECHB_HUMANHADHBphysical
21900206
WIZ_HUMANWIZphysical
21900206
TAF5L_HUMANTAF5Lphysical
21900206
TCPH_HUMANCCT7physical
21900206
BAG6_HUMANBAG6physical
21900206
UB2D1_HUMANUBE2D1physical
21900206
RBM48_HUMANRBM48physical
21900206
GDF9_HUMANGDF9physical
21900206
DEAF1_HUMANDEAF1physical
21900206
TZAP_HUMANZBTB48physical
21900206
ZBT16_HUMANZBTB16physical
21900206
TBA1A_HUMANTUBA1Aphysical
21900206
KLH23_HUMANKLHL23physical
21900206
F13A_HUMANF13A1physical
21900206
SUMO3_HUMANSUMO3physical
21900206
VIME_HUMANVIMphysical
21900206
ODPB_HUMANPDHBphysical
21900206
TYB4_HUMANTMSB4Xphysical
21900206
DDAH2_HUMANDDAH2physical
21900206
ATS10_HUMANADAMTS10physical
21900206
WDR73_HUMANWDR73physical
21900206
HEM1_HUMANALAS1physical
21900206
TLE1_HUMANTLE1physical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
ACTB_HUMANACTBphysical
21900206
CSN6_HUMANCOPS6physical
21900206
UBP4_HUMANUSP4physical
21900206
RS2_HUMANRPS2physical
21900206
CATB_HUMANCTSBphysical
21900206
A2MG_HUMANA2Mphysical
21900206
MED31_HUMANMED31physical
21900206
CENPB_HUMANCENPBphysical
21900206
SP110_HUMANSP110physical
21900206
A1BG_HUMANA1BGphysical
21900206
CO4A5_HUMANCOL4A5physical
21900206
RAI1_HUMANRAI1physical
21900206
ATPB_HUMANATP5Bphysical
21900206
DC1I1_HUMANDYNC1I1physical
21900206
EF1A1_HUMANEEF1A1physical
21900206
FBN3_HUMANFBN3physical
21900206
NPRL2_HUMANNPRL2physical
21900206
APLP1_HUMANAPLP1physical
21900206
INP5K_HUMANINPP5Kphysical
21900206
U119A_HUMANUNC119physical
21900206
CELF3_HUMANCELF3physical
21900206
GNB5_HUMANGNB5physical
21900206
MSH2_HUMANMSH2physical
21900206
LRIF1_HUMANLRIF1physical
21900206
ANGP2_HUMANANGPT2physical
21900206
TBB3_HUMANTUBB3physical
21900206
SCG1_HUMANCHGBphysical
21900206
ZN431_HUMANZNF431physical
21900206
MYOME_HUMANPDE4DIPphysical
21900206
ACL6B_HUMANACTL6Bphysical
21900206
KPYM_HUMANPKMphysical
21900206
TNR16_HUMANNGFRphysical
21900206
DOCK7_HUMANDOCK7physical
21900206
SYQ_HUMANQARSphysical
21900206
ING5_HUMANING5physical
21900206
ZN135_HUMANZNF135physical
21900206
KMT2B_HUMANKMT2Bphysical
21900206
TBB2B_HUMANTUBB2Bphysical
21900206
FIBB_HUMANFGBphysical
21900206
RBBP4_HUMANRBBP4physical
21900206
HXD8_HUMANHOXD8physical
21900206
TETN_HUMANCLEC3Bphysical
21900206
NRBP_HUMANNRBP1physical
21900206
FAF1_HUMANFAF1physical
21900206
SETB1_HUMANSETDB1physical
21900206
ESR1_HUMANESR1physical
17911387
PCNA_HUMANPCNAphysical
11559705
CDK1_HUMANCDK1physical
11559705
CCNB1_HUMANCCNB1physical
11559705
NF2L2_HUMANNFE2L2physical
19560419
PCNA_HUMANPCNAphysical
20605778
FKBPL_HUMANFKBPLphysical
15664193
MDM2_HUMANMDM2physical
14633995
CDN1B_HUMANCDKN1Bgenetic
18850315
CCND2_HUMANCCND2physical
15169570
CDK4_HUMANCDK4physical
15169570
CDK2_HUMANCDK2physical
12800980
CDK2_HUMANCDK2physical
11477082
CCNE1_HUMANCCNE1physical
11477082
PCNA_HUMANPCNAphysical
22383522
CCNE1_HUMANCCNE1physical
8891332
BRAP_HUMANBRAPphysical
15340083
1433T_HUMANYWHAQphysical
20086099
MDM2_HUMANMDM2physical
20086099
PSA3_HUMANPSMA3physical
20086099
MDM2_HUMANMDM2physical
20308078
P63_HUMANTP63genetic
21511729
CCNA1_HUMANCCNA1physical
12383116
CDK2_HUMANCDK2physical
12383116
CCND1_HUMANCCND1physical
12383116
CDK4_HUMANCDK4physical
12383116
RN126_HUMANRNF126physical
23026136
A4_HUMANAPPphysical
21832049
CCNE1_HUMANCCNE1physical
16765349
CDK2_HUMANCDK2physical
16765349
CCND2_HUMANCCND2physical
16765349
PCNA_HUMANPCNAphysical
11302688
BCCIP_HUMANBCCIPphysical
14726710
CDK14_HUMANCDK14physical
17517622
PCNA_HUMANPCNAphysical
7911228
CCNE1_HUMANCCNE1physical
8756624
NOV_HUMANNOVphysical
8756624
CCND1_HUMANCCND1physical
8756624
CDK2_HUMANCDK2physical
8756624
CDK4_HUMANCDK4physical
8756624
CEBPA_HUMANCEBPAphysical
9372966
CDK2_HUMANCDK2physical
9660939
CCNA2_HUMANCCNA2physical
8662825
CCNB1_HUMANCCNB1physical
8662825
CCND1_HUMANCCND1physical
8662825
PCNA_HUMANPCNAphysical
8662825
CCNE1_HUMANCCNE1physical
8662825
H15_HUMANHIST1H1Bphysical
8662825
CCNE2_HUMANCCNE2physical
9840943
TRI39_HUMANTRIM39physical
23213251
MKRN1_HUMANMKRN1physical
19536131
CDK5_HUMANCDK5physical
15890360
CDK2_HUMANCDK2physical
15890360
CCNE1_HUMANCCNE1physical
9472014
CDK2_HUMANCDK2physical
9472014
PCNA_HUMANPCNAphysical
10022118
CDK2_HUMANCDK2physical
10022118
PCNA_HUMANPCNAphysical
9546435
RN114_HUMANRNF114genetic
23645206
TNIP2_HUMANTNIP2physical
21988832
HNRPK_HUMANHNRNPKphysical
21988832
THIO_HUMANTXNphysical
21988832
RL35_HUMANRPL35physical
21988832
FAD1_HUMANFLAD1physical
21988832
GCKR_HUMANGCKRphysical
21988832
HPPD_HUMANHPDphysical
21988832
PCNA_HUMANPCNAphysical
21988832
RL18_HUMANRPL18physical
21988832
SIPA1_HUMANSIPA1physical
21988832
NR1H2_HUMANNR1H2physical
21988832
TNIP1_HUMANTNIP1physical
21988832
TXD11_HUMANTXNDC11physical
21988832
NKD2_HUMANNKD2physical
21988832
CXL13_HUMANCXCL13physical
24027428
CDK2_HUMANCDK2physical
8622677
CDK4_HUMANCDK4physical
8622677
GRP78_HUMANHSPA5physical
23443559
CDK4_HUMANCDK4physical
23443559
RBL2_HUMANRBL2physical
23443559
RAVR1_HUMANRAVER1physical
23443559
GRP75_HUMANHSPA9physical
23443559
CDK5_HUMANCDK5physical
23443559
CCND2_HUMANCCND2physical
23443559
CCND3_HUMANCCND3physical
23443559
MOGS_HUMANMOGSphysical
23443559
UBP11_HUMANUSP11physical
23443559
TBB5_HUMANTUBBphysical
23443559
CCNE2_HUMANCCNE2physical
23443559
CCND1_HUMANCCND1physical
23443559
CCNA2_HUMANCCNA2physical
23443559
UBR4_HUMANUBR4physical
23443559
GGYF2_HUMANGIGYF2physical
23443559
IRS4_HUMANIRS4physical
23443559
TBCD4_HUMANTBC1D4physical
23443559
HSP7C_HUMANHSPA8physical
23443559
LPPRC_HUMANLRPPRCphysical
23443559
CKS2_HUMANCKS2physical
23443559
CCNE1_HUMANCCNE1physical
23443559
PUM1_HUMANPUM1physical
23443559
UBR5_HUMANUBR5physical
23443559
TBA1A_HUMANTUBA1Aphysical
23443559
CRTC2_HUMANCRTC2physical
23443559
AMOT_HUMANAMOTphysical
23443559
ANR17_HUMANANKRD17physical
23443559
YTHD1_HUMANYTHDF1physical
23443559
EPN4_HUMANCLINT1physical
23443559
DDB1_HUMANDDB1physical
23443559
CPVL_HUMANCPVLphysical
23443559
FBX21_HUMANFBXO21physical
23443559
NUCL_HUMANNCLphysical
23443559
CDK2_HUMANCDK2physical
23443559
4EBP3_HUMANEIF4EBP3physical
23443559
HSP72_HUMANHSPA2physical
23443559
ROA2_HUMANHNRNPA2B1physical
23443559
DOCK7_HUMANDOCK7physical
23443559
MARK2_HUMANMARK2physical
23443559
CCNB1_HUMANCCNB1physical
23443559
LIPB1_HUMANPPFIBP1physical
23443559
CCNO_HUMANCCNOphysical
23443559
MTMR5_HUMANSBF1physical
23443559
PCNA_HUMANPCNAphysical
23443559
ABR_HUMANABRphysical
23443559
RS16_HUMANRPS16physical
23443559
U520_HUMANSNRNP200physical
23443559
CDC20_HUMANCDC20physical
23443559
PRP8_HUMANPRPF8physical
23443559
CKS1_HUMANCKS1Bphysical
23443559
SPT6H_HUMANSUPT6Hphysical
23443559
IF2B1_HUMANIGF2BP1physical
23443559
KPB1_HUMANPHKA1physical
23443559
LIPA1_HUMANPPFIA1physical
23443559
KCC2D_HUMANCAMK2Dphysical
23443559
PHKG2_HUMANPHKG2physical
23443559
CE290_HUMANCEP290physical
23443559
CDK3_HUMANCDK3physical
23443559
RS4X_HUMANRPS4Xphysical
23443559
EPIPL_HUMANEPPK1physical
23443559
ODPX_HUMANPDHXphysical
23443559
PUF60_HUMANPUF60physical
23443559
RS25_HUMANRPS25physical
23443559
U5S1_HUMANEFTUD2physical
23443559
UBB_HUMANUBBphysical
23443559
NET4_HUMANNTN4physical
23443559
SNTB2_HUMANSNTB2physical
23443559
RS9_HUMANRPS9physical
23443559
K1H1_HUMANKRT31physical
25416956
PCNA_HUMANPCNAphysical
25416956
ITF2_HUMANTCF4physical
25416956
TRAF1_HUMANTRAF1physical
25416956
IKZF3_HUMANIKZF3physical
25416956
TEX11_HUMANTEX11physical
25416956
TRI54_HUMANTRIM54physical
25416956
PCNA_HUMANPCNAphysical
25411249
PCNA_HUMANPCNAphysical
23223023
PCNA_HUMANPCNAphysical
20606006
AKT2_HUMANAKT2physical
16982699
CCNA1_HUMANCCNA1physical
16982699
CDK2_HUMANCDK2physical
25483090
CCND1_HUMANCCND1physical
21516116
CCNA2_HUMANCCNA2physical
26496610
CCND3_HUMANCCND3physical
26496610
CDK1_HUMANCDK1physical
26496610
CDK2_HUMANCDK2physical
26496610
PCNA_HUMANPCNAphysical
26496610
SSXT_HUMANSS18physical
26496610
CCNE2_HUMANCCNE2physical
26496610
RUSC2_HUMANRUSC2physical
26496610
CCNA1_HUMANCCNA1physical
25241761
STAT3_HUMANSTAT3physical
25241761
CDN1B_HUMANCDKN1Bphysical
25241761
SMAD4_HUMANSMAD4physical
25241761
MDM2_HUMANMDM2physical
25241761
FOXO1_HUMANFOXO1physical
25241761
SKP2_HUMANSKP2physical
25241761
HDAC1_HUMANHDAC1physical
25241761
CBP_HUMANCREBBPphysical
25241761
PCNA_HUMANPCNAphysical
26272819
SMAD3_HUMANSMAD3physical
22995475
KAT2B_HUMANKAT2Bphysical
22995475
CCND1_HUMANCCND1physical
23007395
CDK4_HUMANCDK4physical
23007395
CDK2_HUMANCDK2physical
23007395
CHIP_HUMANSTUB1physical
28232384
PCNA_HUMANPCNAphysical
11463845
CDK2_HUMANCDK2physical
11463845
CDK4_HUMANCDK4physical
11463845

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 CDN1A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"N-acetylation and ubiquitin-independent proteasomal degradation ofp21(Cip1).";
Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E.,Roberts J.M.;
Mol. Cell 16:839-847(2004).
Cited for: PROTEIN SEQUENCE OF 2-16, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-130, AND MASSSPECTROMETRY.
"PCNA-dependent regulation of p21 ubiquitylation and degradation viathe CRL4Cdt2 ubiquitin ligase complex.";
Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.;
Genes Dev. 22:2496-2506(2008).
Cited for: UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA,MUTAGENESIS OF SER-114 AND 144-GLN--PHE-150, AND PHOSPHORYLATION ATSER-114.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
"Reversible phosphorylation at the C-terminal regulatory domain ofp21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding.";
Scott M.T., Morrice N., Ball K.L.;
J. Biol. Chem. 275:11529-11537(2000).
Cited for: PROTEIN SEQUENCE OF 136-148, PHOSPHORYLATION AT THR-145; SER-146 ANDSER-160, AND MASS SPECTROMETRY.
"Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability andinhibits cell proliferation in HCT116 cells.";
Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.;
Int. J. Biochem. Cell Biol. 42:1030-1038(2010).
Cited for: PHOSPHORYLATION AT THR-145 BY PIM2.
"Only Akt1 is required for proliferation, while Akt2 promotes cellcycle exit through p21 binding.";
Heron-Milhavet L., Franckhauser C., Rana V., Berthenet C., Fisher D.,Hemmings B.A., Fernandez A., Lamb N.J.;
Mol. Cell. Biol. 26:8267-8280(2006).
Cited for: PHOSPHORYLATION AT THR-145.
"Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1kinase.";
Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J.,Magnuson N.S.;
Biochim. Biophys. Acta 1593:45-55(2002).
Cited for: PHOSPHORYLATION AT THR-145 BY PIM1, SUBCELLULAR LOCATION, ANDINTERACTION WITH PIM1.
"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding andproliferation of endothelial cells.";
Roessig L., Jadidi A.S., Urbich C., Badorff C., Zeiher A.M.,Dimmeler S.;
Mol. Cell. Biol. 21:5644-5657(2001).
Cited for: PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145 AND SER-146, ANDSUBCELLULAR LOCATION.

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