P53_MOUSE - dbPTM
P53_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P53_MOUSE
UniProt AC P02340
Protein Name Cellular tumor antigen p53
Gene Name Tp53
Organism Mus musculus (Mouse).
Sequence Length 387
Subcellular Localization Cytoplasm . Nucleus . Nucleus, PML body . Endoplasmic reticulum . Mitochondrion matrix . Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Transloca
Protein Description Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2. [PubMed: 24051492]
Protein Sequence MEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPLDGEYFTLKIRGRKRFEMFRELNEALELKDAHATEESGDSRAHSSYLKTKKGQSTSRHKKTMVKKVGPDSD
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
4Phosphorylation----MEESQSDISLE
----CCCCCCCCEEE
22.981584757
6Phosphorylation--MEESQSDISLELP
--CCCCCCCCEEECC
46.311584757
9PhosphorylationEESQSDISLELPLSQ
CCCCCCCEEECCCCC
22.3026643407
12PhosphorylationQSDISLELPLSQETF
CCCCEEECCCCCHHH
6.6618022393
15PhosphorylationISLELPLSQETFSGL
CEEECCCCCHHHCCH
24.8321151168
18PhosphorylationELPLSQETFSGLWKL
ECCCCCHHHCCHHHH
18.5715195100
20PhosphorylationPLSQETFSGLWKLLP
CCCCHHHCCHHHHCC
40.1618519674
21PhosphorylationLSQETFSGLWKLLPP
CCCHHHCCHHHHCCH
31.22-
23PhosphorylationQETFSGLWKLLPPED
CHHHCCHHHHCCHHH
7.87-
34PhosphorylationPPEDILPSPHCMDDL
CHHHCCCCCCCHHCC
24.671584757
37PhosphorylationDILPSPHCMDDLLLP
HCCCCCCCHHCCCCC
3.4817254968
55PhosphorylationEEFFEGPSEALRVSG
HHHHHCCHHHHHHCC
46.4919118006
114AcetylationFLQSGTAKSVMCTYS
EECCCCCCEEEEECC
43.34128765
117AcetylationSGTAKSVMCTYSPPL
CCCCCEEEEECCCCH
1.50-
126AcetylationTYSPPLNKLFCQLAK
ECCCCHHHHHHHHHC
51.1022826441
142PhosphorylationCPVQLWVSATPPAGS
CCEEEEEECCCCCCC
18.1626643407
144PhosphorylationVQLWVSATPPAGSRV
EEEEEECCCCCCCHH
23.4626643407
149PhosphorylationSATPPAGSRVRAMAI
ECCCCCCCHHHEEEE
29.7016964247
177PhosphorylationCPHHERCSDGDGLAP
CCCCCCCCCCCCCCC
51.34-
180PhosphorylationHERCSDGDGLAPPQH
CCCCCCCCCCCCCHH
54.65-
221PhosphorylationYEPPEAGSEYTTIHY
CCCCCCCCCCEEEEE
34.1822499769
223PhosphorylationPPEAGSEYTTIHYKY
CCCCCCCCEEEEEEE
15.7522499769
224PhosphorylationPEAGSEYTTIHYKYM
CCCCCCCEEEEEEEE
18.4122499769
225PhosphorylationEAGSEYTTIHYKYMC
CCCCCCEEEEEEEEC
12.5922499769
228PhosphorylationSEYTTIHYKYMCNSS
CCCEEEEEEEECCCC
10.4422499769
230PhosphorylationYTTIHYKYMCNSSCM
CEEEEEEEECCCCCC
10.3428576409
263PhosphorylationGNLLGRDSFEVRVCA
CCCCCCCCEEEEEEE
23.19-
266PhosphorylationLGRDSFEVRVCACPG
CCCCCEEEEEEECCC
5.39-
278PhosphorylationCPGRDRRTEEENFRK
CCCCCCCCHHHCCCC
48.95-
281PhosphorylationRDRRTEEENFRKKEV
CCCCCHHHCCCCCCC
56.27-
286UbiquitinationEEENFRKKEVLCPEL
HHHCCCCCCCCCCCC
49.12-
297PhosphorylationCPELPPGSAKRALPT
CCCCCCCCHHHHCCC
36.0727149854
299AcetylationELPPGSAKRALPTCT
CCCCCCHHHHCCCCC
39.6423806337
299UbiquitinationELPPGSAKRALPTCT
CCCCCCHHHHCCCCC
39.64-
302AcetylationPGSAKRALPTCTSAS
CCCHHHHCCCCCCCC
4.13-
304PhosphorylationSAKRALPTCTSASPP
CHHHHCCCCCCCCCC
29.3025619855
306PhosphorylationKRALPTCTSASPPQK
HHHCCCCCCCCCCCC
29.7925619855
307PhosphorylationRALPTCTSASPPQKK
HHCCCCCCCCCCCCC
28.9722942356
309PhosphorylationLPTCTSASPPQKKKP
CCCCCCCCCCCCCCC
36.563006031
312PhosphorylationCTSASPPQKKKPLDG
CCCCCCCCCCCCCCC
73.853006031
313AcetylationTSASPPQKKKPLDGE
CCCCCCCCCCCCCCC
69.4160803
314UbiquitinationSASPPQKKKPLDGEY
CCCCCCCCCCCCCCC
55.14-
314AcetylationSASPPQKKKPLDGEY
CCCCCCCCCCCCCCC
55.1422826441
315UbiquitinationASPPQKKKPLDGEYF
CCCCCCCCCCCCCCE
58.82-
315AcetylationASPPQKKKPLDGEYF
CCCCCCCCCCCCCCE
58.8223806337
318AcetylationPQKKKPLDGEYFTLK
CCCCCCCCCCCEEEE
57.3023806337
321PhosphorylationKKPLDGEYFTLKIRG
CCCCCCCCEEEEECC
13.85-
325AcetylationDGEYFTLKIRGRKRF
CCCCEEEEECCCHHH
27.5723806337
330MethylationTLKIRGRKRFEMFRE
EEEECCCHHHHHHHH
65.35-
332MethylationKIRGRKRFEMFRELN
EECCCHHHHHHHHHH
10.02-
334MethylationRGRKRFEMFRELNEA
CCCHHHHHHHHHHHH
3.36-
360PhosphorylationSGDSRAHSSYLKTKK
CCCCCHHHHHCCCCC
21.509183006
361PhosphorylationGDSRAHSSYLKTKKG
CCCCHHHHHCCCCCC
25.3128418008
363PhosphorylationSRAHSSYLKTKKGQS
CCHHHHHCCCCCCCC
6.499183006
364"N6,N6-dimethyllysine"RAHSSYLKTKKGQST
CHHHHHCCCCCCCCC
50.49-
364MethylationRAHSSYLKTKKGQST
CHHHHHCCCCCCCCC
50.49-
364AcetylationRAHSSYLKTKKGQST
CHHHHHCCCCCCCCC
50.4923806337
364UbiquitinationRAHSSYLKTKKGQST
CHHHHHCCCCCCCCC
50.49-
365PhosphorylationAHSSYLKTKKGQSTS
HHHHHCCCCCCCCCC
35.089183006
366MethylationHSSYLKTKKGQSTSR
HHHHCCCCCCCCCCH
54.01-
366AcetylationHSSYLKTKKGQSTSR
HHHHCCCCCCCCCCH
54.0122826441
366UbiquitinationHSSYLKTKKGQSTSR
HHHHCCCCCCCCCCH
54.01-
367UbiquitinationSSYLKTKKGQSTSRH
HHHCCCCCCCCCCHH
68.37-
367"N6,N6-dimethyllysine"SSYLKTKKGQSTSRH
HHHCCCCCCCCCCHH
68.37-
367AcetylationSSYLKTKKGQSTSRH
HHHCCCCCCCCCCHH
68.3722826441
367MethylationSSYLKTKKGQSTSRH
HHHCCCCCCCCCCHH
68.37-
368PhosphorylationSYLKTKKGQSTSRHK
HHCCCCCCCCCCHHC
28.389183006
369MethylationYLKTKKGQSTSRHKK
HCCCCCCCCCCHHCC
53.03-
370PhosphorylationLKTKKGQSTSRHKKT
CCCCCCCCCCHHCCC
36.709183006
370MethylationLKTKKGQSTSRHKKT
CCCCCCCCCCHHCCC
36.70-
370AcetylationLKTKKGQSTSRHKKT
CCCCCCCCCCHHCCC
36.70-
372PhosphorylationTKKGQSTSRHKKTMV
CCCCCCCCHHCCCCC
37.329739174
373PhosphorylationKKGQSTSRHKKTMVK
CCCCCCCHHCCCCCC
45.819183006
375UbiquitinationGQSTSRHKKTMVKKV
CCCCCHHCCCCCCCC
49.15-
375AcetylationGQSTSRHKKTMVKKV
CCCCCHHCCCCCCCC
49.1523806337
376MethylationQSTSRHKKTMVKKVG
CCCCHHCCCCCCCCC
35.41-
376UbiquitinationQSTSRHKKTMVKKVG
CCCCHHCCCCCCCCC
35.41-
376"N6,N6-dimethyllysine"QSTSRHKKTMVKKVG
CCCCHHCCCCCCCCC
35.41-
376AcetylationQSTSRHKKTMVKKVG
CCCCHHCCCCCCCCC
35.4123806337
377PhosphorylationSTSRHKKTMVKKVGP
CCCHHCCCCCCCCCC
31.819183006
378AcetylationTSRHKKTMVKKVGPD
CCHHCCCCCCCCCCC
5.97-
379AcetylationSRHKKTMVKKVGPDS
CHHCCCCCCCCCCCC
7.03-
379MethylationSRHKKTMVKKVGPDS
CHHCCCCCCCCCCCC
7.03-
380AcetylationRHKKTMVKKVGPDSD
HHCCCCCCCCCCCCC
30.8022826441
380PhosphorylationRHKKTMVKKVGPDSD
HHCCCCCCCCCCCCC
30.809183006
380UbiquitinationRHKKTMVKKVGPDSD
HHCCCCCCCCCCCCC
30.80-
381UbiquitinationHKKTMVKKVGPDSD-
HCCCCCCCCCCCCC-
40.80-
386PhosphorylationVKKVGPDSD------
CCCCCCCCC------
48.643006031
389PhosphorylationVGPDSD---------
CCCCCC---------
3006031

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
7SPhosphorylationKinaseCSNK1EP49674
GPS
7SPhosphorylationKinaseCSNK1DP48730
GPS
7SPhosphorylationKinasePRKDCP78527
GPS
7SPhosphorylationKinaseCSNK1A1P48729
GPS
9SPhosphorylationKinaseHIPK4Q3V016
GPS
9SPhosphorylationKinaseCSNK1EP49674
GPS
9SPhosphorylationKinaseCSNK1DP48730
GPS
9SPhosphorylationKinaseCSNK1A1P48729
GPS
12SPhosphorylationKinaseCSNK1EP49674
GPS
12SPhosphorylationKinaseHIPK4Q3V016
Uniprot
12SPhosphorylationKinaseCSNK1A1P48729
GPS
12SPhosphorylationKinaseCSNK1DP48730
GPS
15SPhosphorylationKinaseNUAK1Q641K5
GPS
15SPhosphorylationKinaseCDK5P49615
GPS
15SPhosphorylationKinaseTP53RKQ99PW4
GPS
15SPhosphorylationKinaseATMQ62388
GPS
15SPhosphorylationKinaseAMPK-FAMILY-GPS
18SPhosphorylationKinaseMAPK1P63085
GPS
18SPhosphorylationKinasePRKCDP28867
GPS
18SPhosphorylationKinaseAMPKA2P54646
PSP
18SPhosphorylationKinaseMELKQ61846
PSP
18SPhosphorylationKinaseMAPK3Q63844
GPS
18SPhosphorylationKinaseMAPK14P47811
GPS
18SPhosphorylationKinaseNUAK1Q641K5
Uniprot
18SPhosphorylationKinasePRKDCP78527
GPS
18SPhosphorylationKinasePRPKQ61136
Uniprot
18SPhosphorylationKinaseVRK2Q86Y07-2
GPS
18SPhosphorylationKinaseAMPK-Uniprot
18SPhosphorylationKinasePRKAA2Q8BRK8
GPS
18SPhosphorylationKinaseATRQ9JKK8
PSP
18SPhosphorylationKinaseCDK5P49615
Uniprot
18SPhosphorylationKinaseATMQ62388
Uniprot
20SPhosphorylationKinaseMAPKAPK2P49138
GPS
20SPhosphorylationKinaseJNK-SUBFAMILY-GPS
21TPhosphorylationKinaseCSNK1A1P48729
GPS
21TPhosphorylationKinaseVRK1Q99986
PSP
21TPhosphorylationKinaseVRK1Q80X41
Uniprot
21TPhosphorylationKinaseVRK2Q86Y07
PSP
21TPhosphorylationKinaseVRK2 ISO2Q86Y07-2
PSP
21TPhosphorylationKinaseVRK2Q8BN21
Uniprot
21TPhosphorylationKinaseCK1-Uniprot
23SPhosphorylationKinasePLK3Q60806
Uniprot
23SPhosphorylationKinaseCHEK2Q9Z265
Uniprot
23SPhosphorylationKinaseCK1-Uniprot
34SPhosphorylationKinaseMAPK10Q61831
GPS
34SPhosphorylationKinaseMAPK9Q9WTU6
GPS
34SPhosphorylationKinaseMAPK8Q91Y86
GPS
34SPhosphorylationKinaseMAPKAPK5O54992
GPS
37SPhosphorylationKinaseMAPKAPK5O54992
Uniprot
58SPhosphorylationKinaseHIPK2Q9H2X6
PSP
73TPhosphorylationKinaseMAPK-FAMILY-GPS
83TPhosphorylationKinaseMAPK-FAMILY-GPS
180SPhosphorylationKinaseAURKBO70126
Uniprot
266SPhosphorylationKinaseAURKBO70126
Uniprot
281TPhosphorylationKinaseAURKBO70126
Uniprot
312SPhosphorylationKinaseCDK1P11440
Uniprot
312SPhosphorylationKinaseCDK2P97377
Uniprot
312SPhosphorylationKinaseAURKAP97477
Uniprot
365TPhosphorylationKinasePKC-FAMILY-GPS
370SPhosphorylationKinasePKC-FAMILY-GPS
371TPhosphorylationKinasePKC-FAMILY-GPS
372SPhosphorylationKinasePKC-FAMILY-GPS
377TPhosphorylationKinasePKC-FAMILY-GPS
386SPhosphorylationKinaseCK2-FAMILY-GPS
389SPhosphorylationKinaseNUAK1Q641K5
Uniprot
389SPhosphorylationKinaseCDK2P97377
Uniprot
389SPhosphorylationKinaseCK2A1Q60737
PSP
389SPhosphorylationKinaseCK2-Uniprot
389SPhosphorylationKinaseCSNK2A1P19139
GPS
-KUbiquitinationE3 ubiquitin ligaseE4f1Q8CCE9
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseFbxo11Q7TPD1
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseHuwe1Q7TMY8
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseMdm2P23804
PMID:31847675
-KUbiquitinationE3 ubiquitin ligaseMkrn1Q9QXP6
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRfflQ6ZQM0
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRfwd3Q8CIK8
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSyvn1Q9DBY1
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseUbe3aO08759
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseWwp1Q8BZZ3
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
12SPhosphorylation

2145148
18SPhosphorylation

2145148
18SPhosphorylation

2145148
18SPhosphorylation

2145148
18SOxidation

2145148
21TPhosphorylation

2145148
23Subiquitylation

2145148
23SPhosphorylation

2145148
23SPhosphorylation

2145148
27Kubiquitylation

-
288Kubiquitylation

25732823
289Kubiquitylation

25732823
330RMethylation

-
332RMethylation

-
334RMethylation

-
367KMethylation

-
367KMethylation

-
367KMethylation

-
369KMethylation

-
369KMethylation

-
370KMethylation

-
379KMethylation

-
383KSumoylation

-
389SPhosphorylation

2145148

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 P53_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOPRS_HUMANTOPORSphysical
10415337
MDM2_MOUSEMdm2physical
18309296
MDM2_MOUSEMdm2physical
17936560
ING4_HUMANING4physical
17325660
UBE2N_MOUSEUbe2nphysical
17000756
P53_MOUSETrp53physical
20211142
P63_MOUSETrp63physical
20211142
P73_MOUSETrp73physical
20211142
ZN292_MOUSEZfp292physical
20211142
MED16_MOUSEMed16physical
20211142
KMT2E_MOUSEKmt2ephysical
21423215
NPM_MOUSENpm1physical
17277230
PIAS4_MOUSEPias4physical
16816390
PIAS1_MOUSEPias1physical
16816390
PIAS2_MOUSEPias2physical
16816390
MDM2_MOUSEMdm2physical
17086174
SIR1_MOUSESirt1physical
20157588
SP1_MOUSESp1physical
20157588
MDM4_MOUSEMdm4physical
20697359
MDM2_MOUSEMdm2physical
20697359
FAK2_MOUSEPtk2bphysical
19880522
MDM2_MOUSEMdm2physical
22216266
PAX3_MOUSEPax3physical
22216266
MDM2_MOUSEMdm2physical
20818388
CDN1A_MOUSECdkn1aphysical
22666487
MDM2_MOUSEMdm2physical
22666487
EP300_MOUSEEp300physical
22666487
SMCA4_MOUSESmarca4physical
18303029
SMRD1_MOUSESmarcd1physical
18303029
KMT5A_MOUSESetd8genetic
22117221
MCM4_MOUSEMcm4genetic
21611832
SKIL_MOUSESkilphysical
22805162
MDM2_MOUSEMdm2physical
22805162
NUMB_HUMANNUMBphysical
9632782
CCNG1_MOUSECcng1physical
11983168
MDM2_MOUSEMdm2physical
8058315
PARK7_MOUSEPark7physical
19680261
HUWE1_MOUSEHuwe1genetic
22213803
EP300_MOUSEEp300physical
21057544
MDM2_MOUSEMdm2physical
10205143
TOPRS_MOUSEToporsphysical
15735665
HS71B_MOUSEHspa1bphysical
23251530
P63_MOUSETrp63physical
23251530
P73_MOUSETrp73physical
23251530
MDM2_MOUSEMdm2physical
10706102
MK08_MOUSEMapk8physical
10706102
EP300_MOUSEEp300physical
10706102
CDN2A_MOUSECdkn2aphysical
10706102
ARF_MOUSECdkn2aphysical
10706102
AXIN1_MOUSEAxin1physical
15526030
HIPK2_MOUSEHipk2physical
15526030
BARD1_MOUSEBard1physical
11779501
PTEN_MOUSEPtenphysical
18332125
WWOX_MOUSEWwoxphysical
15580310
MK08_MOUSEMapk8physical
15580310
CDN2A_MOUSECdkn2aphysical
15989966
ARF_MOUSECdkn2aphysical
15989966
RL11_MOUSERpl11physical
15989966
B2CL1_MOUSEBcl2l1physical
14963330
RS26_MOUSERps26physical
23728348
NECD_MOUSENdnphysical
24911587
RN128_MOUSERnf128physical
23370271
MK14_MOUSEMapk14physical
21050851
MDM2_MOUSEMdm2physical
9732264
MDM2_MOUSEMdm2physical
11953423
MDM4_MOUSEMdm4physical
11953423
REV1_MOUSERev1physical
25614517
BRNP1_MOUSEBrinp1physical
25732823
MDM2_MOUSEMdm2physical
25732823
P53_MOUSETrp53physical
8035799
LT_SV40SV40gp6physical
21502952
KCMA1_MOUSEKcnma1physical
25581503
MDM2_MOUSEMdm2genetic
21437245
OLIG2_MOUSEOlig2genetic
21397859
PALB2_MOUSEPalb2genetic
23657012
XRCC2_MOUSEXrcc2genetic
23435420
SPO11_MOUSESpo11genetic
23435420
TREX2_MOUSETrex2genetic
23435420
MD2L2_MOUSEMad2l2genetic
23435420
PALB2_MOUSEPalb2genetic
23435420
ACACA_MOUSEAcacagenetic
23435420
PLM_MOUSEFxyd1genetic
23435420
XPF_MOUSEErcc4genetic
23435420
PAXI1_MOUSEPaxip1genetic
23435420
RDM1_MOUSERdm1genetic
23435420
HM20B_MOUSEHmg20bgenetic
23435420
DPOE1_MOUSEPolegenetic
23435420
POLK_MOUSEPolkgenetic
23435420
FANCB_MOUSEFancbgenetic
23435420
BLM_MOUSEBlmgenetic
23435420
POLH_MOUSEPolhgenetic
23435420
EXO1_MOUSEExo1genetic
23435420
REV3L_MOUSERev3lgenetic
23435420
RECQ1_MOUSERecqlgenetic
23435420
DPOE3_MOUSEPole3genetic
23435420
UBP1_MOUSEUsp1genetic
23435420
REV1_MOUSERev1genetic
23435420
XRCC3_MOUSEXrcc3genetic
23435420
MDM2_MOUSEMdm2physical
14555661
EP300_MOUSEEp300physical
14555661
MDM2_HUMANMDM2physical
14555661
PRKN_MOUSEPark2physical
28395174

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P53_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Novel homeodomain-interacting protein kinase family member, HIPK4,phosphorylates human p53 at serine 9.";
Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.;
FEBS Lett. 581:5649-5657(2007).
Cited for: PHOSPHORYLATION AT SER-9.
"PRAK is essential for ras-induced senescence and tumor suppression.";
Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C.,Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III,Wright P.E., Han J.;
Cell 128:295-308(2007).
Cited for: PHOSPHORYLATION AT SER-34.
"PML regulates p53 stability by sequestering Mdm2 to the nucleolus.";
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H.,Pandolfi P.P.;
Nat. Cell Biol. 6:665-672(2004).
Cited for: PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, ANDSUBCELLULAR LOCATION.

TOP