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Cellular tumor antigen p53 (Tumor suppressor p53)

 P53_MARMO               Reviewed;         391 AA.
O36006;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
20-JUN-2018, entry version 162.
RecName: Full=Cellular tumor antigen p53;
AltName: Full=Tumor suppressor p53;
Name=TP53;
Marmota monax (Woodchuck).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
Sciuridae; Xerinae; Marmotini; Marmota.
NCBI_TaxID=9995;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9233767; DOI=10.1038/sj.onc.1201203;
Feitelson M.A., Ranganathan P.N., Clayton M.M., Zhang S.M.;
"Partial characterization of the woodchuck tumor suppressor, p53, and
its interaction with woodchuck hepatitis virus X antigen in
hepatocarcinogenesis.";
Oncogene 15:327-336(1997).
-!- FUNCTION: 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. 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 and seem to have to effect on
cell-cycle regulation. Regulates the circadian clock by repressing
CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2.
{ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Binds DNA as a homotetramer. Interacts with AXIN1.
Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By
similarity). Interacts with histone acetyltransferases EP300 and
methyltransferases HRMT1L2 and CARM1, and recruits them to
promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part
of the TFIID complex. Interacts with ING4; this interaction may be
indirect. Found in a complex with CABLES1 and TP73. Interacts with
HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. Interacts with
USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8;
leading to recruit histone H1 and prevent transactivation activity
(By similarity). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1,
STK11/LKB1, UHRF2 and E4F1. Interacts with YWHAZ; the interaction
enhances TP53 transcriptional activity. Phosphorylation of YWHAZ
inhibits this interaction. Interacts (via DNA-binding domain) with
MAML1 (via N-terminus). Interacts with MKRN1. Interacts with PML
(via C-terminus). Interacts with MDM2; leading to ubiquitination
and proteasomal degradation of TP53. Directly interacts with
FBXO42; leading to ubiquitination and degradation of TP53.
Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase
PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent
inhibition of cell proliferation. Interacts with PPP2R2A.
Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when
monomethylated at Lys-380) with L3MBTL1. Interacts with GRK5.
Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to
DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB,
SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1;
this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2;
this promotes ubiquitination by MDM2. Interacts with PRKCG.
Interacts with PPIF; the association implicates preferentially
tetrameric TP53, is induced by oxidative stress and is impaired by
cyclosporin A (CsA). Interacts with SNAI1; the interaction induces
SNAI1 degradation via MDM2-mediated ubiquitination and inhibits
SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with
UBC9. Interacts with ZNF385B; the interaction is direct. Interacts
(via DNA-binding domain) with ZNF385A; the interaction is direct
and enhances p53/TP53 transactivation functions on cell-cycle
arrest target genes, resulting in growth arrest. Interacts with
ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53
ubiquitination. Interacts with MTA1 and COP1. Interacts with CCAR2
(via N-terminus). Interacts with MORC3. Interacts (via C-terminus)
with POU4F2 (via C-terminus). Interacts (via oligomerization
region) with NOP53; the interaction is direct and may prevent the
MDM2-mediated proteasomal degradation of TP53. Interacts with
AFG1L; mediates mitochondrial translocation of TP53. Interacts
with UBD (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P04637}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}.
Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body
{ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix
{ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP
promotes nuclear localization. Recruited into PML bodies together
with CHEK2. Translocates to mitochondria upon oxidative stress.
Translocates to mitochondria in response to mitomycin C treatment
(By similarity). {ECO:0000250|UniProtKB:P04637}.
-!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the
SETD7 methyltransferase. {ECO:0000250}.
-!- PTM: Phosphorylation on Ser residues mediates transcriptional
activation. Phosphorylation at Ser-9 by HIPK4 increases repression
activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-
18 by VRK1, which may prevent the interaction with MDM2.
Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which
prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3
in response to reactive oxygen species (ROS), promoting p53/TP53-
mediated apoptosis. Phosphorylated on Ser-33 by CDK7 in a CAK
complex in response to DNA damage. Phosphorylated by HIPK1.
Phosphorylated on Ser-46 by HIPK2 upon UV irradiation.
Phosphorylation on Ser-46 is required for acetylation by CREBBP.
Phosphorylated by CK2 following UV but not gamma irradiation.
Phosphorylated on Ser-15 upon ultraviolet irradiation; which is
enhanced by interaction with BANP. Stabilized by CDK5-mediated
phosphorylation in response to genotoxic and oxidative stresses at
Ser-15, Ser-33 and Ser-46, leading to accumulation of p53,
particularly in the nucleus, thus inducing the transactivation of
p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in
response to genotoxic stress. Phosphorylated at Ser-313 and Ser-
390 by CDK2 in response to DNA-damage (By similarity).
{ECO:0000250}.
-!- PTM: Acetylated. Its deacetylation by SIRT1 impairs its ability to
induce proapoptotic program and modulate cell senescence.
Deacetylation by SIRT2 impairs its ability to induce transcription
activation in a AKT-dependent manner (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal
degradation. Ubiquitinated by RFWD3, which works in cooperation
with MDM2 and may catalyze the formation of short polyubiquitin
chains on p53/TP53 that are not targeted to the proteasome.
Ubiquitinated by MKRN1 at Lys-289, which leads to proteasomal
degradation. Deubiquitinated by USP10, leading to stabilize it.
Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to
proteasomal degradation. Ubiquitination by TOPORS induces
degradation. Deubiquitination by USP7, leading to stabilize it.
Ubiquitinated by COP1, which leads to proteasomal degradation (By
similarity). Ubiquitination and subsequent proteasomal degradation
is negatively regulated by CCAR2 (By similarity).
{ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.
-!- PTM: Monomethylated at Lys-370 by SETD7, leading to stabilization
and increased transcriptional activation. Monomethylated at Lys-
368 by SMYD2, leading to decreased DNA-binding activity and
subsequent transcriptional regulation activity. Lys-370
monomethylation prevents interaction with SMYD2 and subsequent
monomethylation at Lys-368. Dimethylated at Lys-371 by EHMT1 and
EHMT2. Monomethylated at Lys-380 by KMT5A, promoting interaction
with L3MBTL1 and leading to repress transcriptional activity.
Demethylation of dimethylated Lys-368 by KDM1A prevents
interaction with TP53BP1 and represses TP53-mediated
transcriptional activation (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=p53 is found in increased amounts in a wide variety
of transformed cells. p53 is frequently mutated or inactivated in
many types of cancer.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ001022; CAA04478.1; -; mRNA.
ProteinModelPortal; O36006; -.
SMR; O36006; -.
HOVERGEN; HBG005201; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
GO; GO:0000733; P:DNA strand renaturation; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd08367; P53; 1.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.170.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR036674; p53_tetramer_sf.
InterPro; IPR010991; p53_tetrameristn.
InterPro; IPR013872; p53_transactivation_domain.
InterPro; IPR002117; p53_tumour_suppressor.
PANTHER; PTHR11447; PTHR11447; 1.
Pfam; PF00870; P53; 1.
Pfam; PF08563; P53_TAD; 1.
Pfam; PF07710; P53_tetramer; 1.
PRINTS; PR00386; P53SUPPRESSR.
SUPFAM; SSF47719; SSF47719; 1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS00348; P53; 1.
2: Evidence at transcript level;
Acetylation; Activator; Apoptosis; Biological rhythms; Cell cycle;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond;
Metal-binding; Methylation; Mitochondrion; Necrosis; Nucleus;
Phosphoprotein; Repressor; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation; Zinc.
CHAIN 1 391 Cellular tumor antigen p53.
/FTId=PRO_0000185707.
DNA_BIND 100 290 {ECO:0000250}.
REGION 1 318 Interaction with CCAR2.
{ECO:0000250|UniProtKB:P04637}.
REGION 1 44 Transcription activation (acidic).
REGION 64 108 Interaction with WWOX. {ECO:0000250}.
REGION 98 368 Interaction with HIPK1. {ECO:0000250}.
REGION 98 298 Required for interaction with ZNF385A.
{ECO:0000250}.
REGION 111 234 Required for interaction with FBXO42.
{ECO:0000250}.
REGION 114 290 Interaction with AXIN1. {ECO:0000250}.
REGION 254 292 Interaction with E4F1. {ECO:0000250}.
REGION 271 278 Interaction with DNA. {ECO:0000250}.
REGION 317 358 Interaction with HIPK2. {ECO:0000250}.
REGION 323 354 Oligomerization.
REGION 357 361 Interaction with USP7. {ECO:0000250}.
REGION 366 385 Basic (repression of DNA-binding).
MOTIF 303 319 Bipartite nuclear localization signal.
{ECO:0000250}.
MOTIF 337 348 Nuclear export signal. {ECO:0000250}.
MOTIF 368 370 [KR]-[STA]-K motif.
METAL 174 174 Zinc. {ECO:0000250}.
METAL 177 177 Zinc. {ECO:0000250}.
METAL 236 236 Zinc. {ECO:0000250}.
METAL 240 240 Zinc. {ECO:0000250}.
SITE 118 118 Interaction with DNA. {ECO:0000250}.
MOD_RES 9 9 Phosphoserine; by HIPK4.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 15 15 Phosphoserine; by CDK5, PRPK, AMPK, NUAK1
and ATM. {ECO:0000250|UniProtKB:P04637}.
MOD_RES 18 18 Phosphothreonine; by CK1, VRK1 and VRK2.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 20 20 Phosphoserine; by CHEK2, CK1 and PLK3.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 33 33 Phosphoserine; by CDK5 and CDK7.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 37 37 Phosphoserine; by MAPKAPK5.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 46 46 Phosphoserine; by CDK5, DYRK2, HIPK2 and
PKC/PRKCG.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 118 118 N6-acetyllysine; by KAT6A.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 181 181 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 267 267 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 282 282 Phosphothreonine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 303 303 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 313 313 Phosphoserine; by AURKA, CDK1 and CDK2.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 319 319 N6-acetyllysine.
{ECO:0000250|UniProtKB:P02340}.
MOD_RES 368 368 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 368 368 N6-methyllysine; by SMYD2; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 370 370 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 371 371 N6,N6-dimethyllysine; by EHMT1 and EHMT2;
alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 371 371 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 379 379 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 380 380 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 380 380 N6-acetyllysine; by KAT6A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 380 380 N6-methyllysine; by KMT5A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 390 390 Phosphoserine; by CK2, CDK2 and NUAK1.
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 384 384 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
SEQUENCE 391 AA; 43468 MW; E1DE5DB84BA40182 CRC64;
MEEAQSDLSI EPPLSQETFS DLWNLLPENN VLSPVLSPPM DDLLLSSEDV ENWFDKGPDE
ALQMSAAPAP KAPTPAASTL AAPSPATSWP LSSSVPSQNT YPGVYGFRLG FLHSGTAKSV
TCTYSPSLNK LFCQLAKTCP VQLWVDSTPP PGTRVRAMAI YKKSQHMTEV VRRCPHHERC
SDSDGLAPPQ HLIRVEGNLR AEYLDDRNTF RHSVVVPYEP PEVGSECTTI HYNYMCNSSC
MGGMNRRPIL TIITLEGSSG NLLGRNSFEV RVCACPGRDR RTEEENFRKR GEPCPEPPPR
STKRALPNGT SSSPQPKKKP LDGEYFTLKI RGRARFEMFQ ELNEALELKD AQAEKEPGES
RPHPSYLKSK KGQSTSRHKK IIFKREGPDS D


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