P63_HUMAN - dbPTM
P63_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P63_HUMAN
UniProt AC Q9H3D4
Protein Name Tumor protein 63
Gene Name TP63
Organism Homo sapiens (Human).
Sequence Length 680
Subcellular Localization Nucleus .
Protein Description Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter..
Protein Sequence MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE
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
10 (in isoform 10)Phosphorylation-20.3024043423
13PhosphorylationSRCATLQYCPDPYIQ
CCCEECCCCCCHHHH
14.7322817900
13 (in isoform 10)Phosphorylation-14.7324043423
15 (in isoform 10)Phosphorylation-40.4524043423
16 (in isoform 10)Phosphorylation-45.1024043423
17 (in isoform 10)Phosphorylation-17.1724043423
18PhosphorylationLQYCPDPYIQRFVET
CCCCCCHHHHHHHCC
19.6422817900
30PhosphorylationVETPAHFSWKESYYR
HCCCCCCCHHHHHHH
27.6327067055
36PhosphorylationFSWKESYYRSTMSQS
CCHHHHHHHHCCCCC
13.8422817900
43PhosphorylationYRSTMSQSTQTNEFL
HHHCCCCCCCCCCCC
18.38-
46PhosphorylationTMSQSTQTNEFLSPE
CCCCCCCCCCCCCHH
36.48-
51PhosphorylationTQTNEFLSPEVFQHI
CCCCCCCCHHHHHHH
25.08-
66 (in isoform 2)Phosphorylation-2.46-
68 (in isoform 2)Phosphorylation-25.22-
149PhosphorylationSVTAPSPYAQPSSTF
CCCCCCCCCCCCCCC
23.3922817900
160PhosphorylationSSTFDALSPSPAIPS
CCCCCCCCCCCCCCC
25.67-
162PhosphorylationTFDALSPSPAIPSNT
CCCCCCCCCCCCCCC
24.48-
171PhosphorylationAIPSNTDYPGPHSFD
CCCCCCCCCCCCCEE
14.1922817900
202PhosphorylationSTELKKLYCQIAKTC
EHHHHHHHHHHHCCC
7.3829496907
231PhosphorylationVIRAMPVYKKAEHVT
EEEEEECCCCCHHHH
10.82-
232AcetylationIRAMPVYKKAEHVTE
EEEEECCCCCHHHHH
45.8282517801
242MethylationEHVTEVVKRCPNHEL
HHHHHHHHHCCCCHH
54.16-
281PhosphorylationQYVEDPITGRQSVLV
EEEECCCCCCEEEEE
31.53-
290PhosphorylationRQSVLVPYEPPQVGT
CEEEEEECCCCCCCC
33.3222817900
326PhosphorylationRPILIIVTLETRDGQ
CCEEEEEEEECCCCC
14.4119413330
329PhosphorylationLIIVTLETRDGQVLG
EEEEEEECCCCCEEC
36.8519413330
358PhosphorylationDRKADEDSIRKQQVS
CCCCCHHHHHHHHCC
23.42-
365PhosphorylationSIRKQQVSDSTKNGD
HHHHHHCCCCCCCCC
22.8524043423
367PhosphorylationRKQQVSDSTKNGDGT
HHHHCCCCCCCCCCC
33.5024043423
368PhosphorylationKQQVSDSTKNGDGTK
HHHCCCCCCCCCCCC
33.2524043423
374PhosphorylationSTKNGDGTKRPFRQN
CCCCCCCCCCCCCCC
28.7230631047
388PhosphorylationNTHGIQMTSIKKRRS
CCCCCCCCCEEECCC
15.7827080861
389PhosphorylationTHGIQMTSIKKRRSP
CCCCCCCCEEECCCC
27.3727080861
395PhosphorylationTSIKKRRSPDDELLY
CCEEECCCCCCCCEE
36.3925106551
397 (in isoform 8)Phosphorylation-64.3627067055
402PhosphorylationSPDDELLYLPVRGRE
CCCCCCEEEECCCHH
22.9127642862
431PhosphorylationMQYLPQHTIETYRQQ
HHHCCHHHHHHHHHH
18.4328450419
434PhosphorylationLPQHTIETYRQQQQQ
CCHHHHHHHHHHHHH
21.8328450419
435PhosphorylationPQHTIETYRQQQQQQ
CHHHHHHHHHHHHHH
8.1428450419
451PhosphorylationQHLLQKQTSIQSPSS
HHHHHHHHHCCCCCC
34.5325106551
452PhosphorylationHLLQKQTSIQSPSSY
HHHHHHHHCCCCCCC
19.0125106551
455PhosphorylationQKQTSIQSPSSYGNS
HHHHHCCCCCCCCCC
25.6923927012
457PhosphorylationQTSIQSPSSYGNSSP
HHHCCCCCCCCCCCC
41.2523927012
458PhosphorylationTSIQSPSSYGNSSPP
HHCCCCCCCCCCCCC
40.2125106551
459PhosphorylationSIQSPSSYGNSSPPL
HCCCCCCCCCCCCCH
25.3525106551
462PhosphorylationSPSSYGNSSPPLNKM
CCCCCCCCCCCHHHC
39.6023927012
463PhosphorylationPSSYGNSSPPLNKMN
CCCCCCCCCCHHHCC
34.2428731282
477PhosphorylationNSMNKLPSVSQLINP
CCCCCCCCHHHHCCH
44.8519282665
479PhosphorylationMNKLPSVSQLINPQQ
CCCCCCHHHHCCHHH
24.4922817900
491PhosphorylationPQQRNALTPTTIPDG
HHHCCCCCCCCCCCC
19.0419282665
491 (in isoform 7)Phosphorylation-19.0427067055
551PhosphorylationPTDCSIVSFLARLGC
CCCCHHHHHHHHCCC
16.9324719451
560PhosphorylationLARLGCSSCLDYFTT
HHHCCCCHHHHHHHC
23.8322817900
588SumoylationMDDLASLKIPEQFRH
HHHHHHCCCCHHHHH
54.44-
588SumoylationMDDLASLKIPEQFRH
HHHHHHCCCCHHHHH
54.44-
599UbiquitinationQFRHAIWKGILDHRQ
HHHHHHHHHHCCHHH
29.93-
611PhosphorylationHRQLHEFSSPSHLLR
HHHHHCCCCHHHHCC
38.0523927012
612PhosphorylationRQLHEFSSPSHLLRT
HHHHCCCCHHHHCCC
35.4225394399
614PhosphorylationLHEFSSPSHLLRTPS
HHCCCCHHHHCCCCC
28.8127080861
619PhosphorylationSPSHLLRTPSSASTV
CHHHHCCCCCCCCEE
27.7327794612
621PhosphorylationSHLLRTPSSASTVSV
HHHCCCCCCCCEEEC
37.6125394399
622PhosphorylationHLLRTPSSASTVSVG
HHCCCCCCCCEEECC
27.6925394399
624PhosphorylationLRTPSSASTVSVGSS
CCCCCCCCEEECCCC
31.1527794612
625PhosphorylationRTPSSASTVSVGSSE
CCCCCCCEEECCCCC
19.2727794612
627PhosphorylationPSSASTVSVGSSETR
CCCCCEEECCCCCCC
22.3527067055
645PhosphorylationVIDAVRFTLRQTISF
HHHHHHEEEEECCCC
15.5124719451
651PhosphorylationFTLRQTISFPPRDEW
EEEEECCCCCCCCCC
34.7824719451
676SumoylationRNKQQRIKEEGE---
HHHHHHHHHCCC---
52.48-
676SumoylationRNKQQRIKEEGE---
HHHHHHHHHCCC---
52.48-

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
43SPhosphorylationKinaseIKBKBO14920
GPS
46TPhosphorylationKinaseGAKO14976
PSP
51SPhosphorylationKinaseIKBKBO14920
GPS
66SPhosphorylationKinaseTGFBR1P36897
PSP
66SPhosphorylationKinaseP38AQ16539
PSP
68SPhosphorylationKinaseTGFBR1P36897
PSP
68SPhosphorylationKinaseP38AQ16539
PSP
149YPhosphorylationKinaseABL1P00519
GPS
171YPhosphorylationKinaseABL1P00519
GPS
281TPhosphorylationKinaseGAKO14976
PSP
290YPhosphorylationKinaseABL1P00519
GPS
301SPhosphorylationKinaseP38AQ16539
PSP
361SPhosphorylationKinaseP38AQ16539
PSP
385SPhosphorylationKinaseATMQ13315
GPS
397TPhosphorylationKinaseCDK2P24941
GPS
466SPhosphorylationKinaseP70-SUBFAMILY-GPS
479SPhosphorylationKinaseATMQ13315
PSP
491TPhosphorylationKinaseHIPK2Q9H2X6
PSP
491TPhosphorylationKinaseCDK2P24941
PSP
560SPhosphorylationKinaseRPS6KB1P23443
GPS
-KUbiquitinationE3 ubiquitin ligaseRCHY1Q96PM5
PMID:23235527
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:18806757
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:16861923
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:16908849
-KUbiquitinationE3 ubiquitin ligaseCRBNQ96SW2
PMID:31591562

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P63_HUMAN !!

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 P63_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RACK1_HUMANGNB2L1physical
12692135
ROAA_HUMANHNRNPABphysical
12692135
SFR15_HUMANSCAF4physical
12692135
YAP1_HUMANYAP1physical
11278685
HIPK2_HUMANHIPK2physical
11925430
FBW1A_HUMANBTRCphysical
17965458
ADHX_HUMANADH5physical
20308539
CBPC2_HUMANAGBL2physical
20308539
ASPM_HUMANASPMphysical
20308539
BRD8_HUMANBRD8physical
20308539
NPRL3_HUMANNPRL3physical
20308539
TPC11_HUMANTRAPPC11physical
20308539
CDT1_HUMANCDT1physical
20308539
DAB2P_HUMANDAB2IPphysical
20308539
DDX23_HUMANDDX23physical
20308539
DNJB6_HUMANDNAJB6physical
20308539
DPH1_HUMANDPH1physical
20308539
AGO1_HUMANAGO1physical
20308539
AGO2_HUMANAGO2physical
20308539
GAS8_HUMANGAS8physical
20308539
IF2B1_HUMANIGF2BP1physical
20308539
JPH1_HUMANJPH1physical
20308539
MTHSD_HUMANMTHFSDphysical
20308539
MYL9_HUMANMYL9physical
20308539
N4BP2_HUMANN4BP2physical
20308539
PIWL1_HUMANPIWIL1physical
20308539
RNF38_HUMANRNF38physical
20308539
SMRD2_HUMANSMARCD2physical
20308539
TRM11_HUMANTRMT11physical
20308539
MDM2_HUMANMDM2physical
21088494
MDM4_HUMANMDM4physical
21088494
TF65_HUMANRELAphysical
22020940
IKKA_HUMANCHUKphysical
20145131
IKKB_HUMANIKBKBphysical
20145131
FBXW7_HUMANFBXW7physical
20571051
RACK1_HUMANGNB2L1physical
15467455
1433S_HUMANSFNphysical
15467455
MDM2_HUMANMDM2physical
11714701
UBC9_HUMANUBE2Iphysical
15539951
UBE4B_HUMANUBE4Bphysical
18418053
DAXX_HUMANDAXXphysical
12954772
DAXX_HUMANDAXXphysical
15339933
ZN363_HUMANRCHY1physical
23235527
WWOX_HUMANWWOXphysical
23370280
ITCH_HUMANITCHphysical
23370280
TNR6_HUMANFASphysical
20085233
PYR1_HUMANCADphysical
20085233
FLNC_HUMANFLNCphysical
20085233
DHX9_HUMANDHX9physical
20085233
SC24C_HUMANSEC24Cphysical
20085233
TERA_HUMANVCPphysical
20085233
SACS_HUMANSACSphysical
20085233
PSMD2_HUMANPSMD2physical
20085233
HNRPR_HUMANHNRNPRphysical
20085233
GOGA4_HUMANGOLGA4physical
20085233
GRP78_HUMANHSPA5physical
20085233
FUS_HUMANFUSphysical
20085233
A2MG_HUMANA2Mphysical
20085233
HNRPQ_HUMANSYNCRIPphysical
20085233
ZN676_HUMANZNF676physical
20085233
P63_HUMANTP63physical
20085233
CPSF6_HUMANCPSF6physical
20085233
PLST_HUMANPLS3physical
20085233
K2C5_HUMANKRT5physical
20085233
CARM1_HUMANCARM1physical
20085233
HNRPL_HUMANHNRNPLphysical
20085233
TCPQ_HUMANCCT8physical
20085233
NONO_HUMANNONOphysical
20085233
HNRPK_HUMANHNRNPKphysical
20085233
K2C6C_HUMANKRT6Cphysical
20085233
TBA1C_HUMANTUBA1Cphysical
20085233
ATPA_HUMANATP5A1physical
20085233
RL3_HUMANRPL3physical
20085233
EF1A1_HUMANEEF1A1physical
20085233
RSSA_HUMANRPSAphysical
20085233
ZBTB4_HUMANZBTB4physical
20085233
HNRC1_HUMANHNRNPCL1physical
20085233
ROA3_HUMANHNRNPA3physical
20085233
ROAA_HUMANHNRNPABphysical
20085233
MAP1A_HUMANMAP1Aphysical
20085233
RLA0_HUMANRPLP0physical
20085233
H13_HUMANHIST1H1Dphysical
20085233
UACA_HUMANUACAphysical
20085233
SNRPA_HUMANSNRPAphysical
20085233
RENT2_HUMANUPF2physical
20085233
CENPE_HUMANCENPEphysical
20085233
SAFB1_HUMANSAFBphysical
20085233
S1PR5_HUMANS1PR5physical
20085233
RL24_HUMANRPL24physical
20085233
RL13A_HUMANRPL13Aphysical
20085233
RL12_HUMANRPL12physical
20085233
MLRS_HUMANMYLPFphysical
20085233
HS90B_HUMANHSP90AB1physical
20085233
ETV4_HUMANETV4physical
21150337
CEBPB_HUMANCEBPBphysical
21150337
NFYA_HUMANNFYAphysical
21150337
NFKB1_HUMANNFKB1physical
21150337
STK11_HUMANSTK11physical
21150337
P53_HUMANTP53physical
23687300
EP300_HUMANEP300physical
23589370
EP300_HUMANEP300physical
15965232
BRCA1_HUMANBRCA1physical
24556685
P53_HUMANTP53physical
22575646
ITCH_HUMANITCHphysical
25485500
CHK2_HUMANCHEK2physical
28514442
P73_HUMANTP73physical
28514442
SH3K1_HUMANSH3KBP1physical
28514442
RP3A_HUMANRPH3Aphysical
28514442
FOXK1_HUMANFOXK1physical
28514442
FOXK2_HUMANFOXK2physical
28514442
PEX14_HUMANPEX14physical
28514442
ATF3_HUMANATF3physical
24554706
P53_HUMANTP53physical
24554706

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
103285Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT syndrome)
106260Ankyloblepharon-ectodermal defects-cleft lip/palate (AEC)
604292Ectrodactyly, ectodermal dysplasia, and cleft lip/palate syndrome 3 (EEC3)
605289Split-hand/foot malformation 4 (SHFM4)
603543Limb-mammary syndrome (LMS)
Note=Defects in TP63 are a cause of cervical, colon, head and neck, lung and ovarian cancers.
129400
129400Non-syndromic orofacial cleft 8 (OFC8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P63_HUMAN

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Related Literatures of Post-Translational Modification

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