P53_RAT
ID P53_RAT Reviewed; 391 AA.
AC P10361; O09168; Q4KMA9; Q66HM0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=Tp53; Synonyms=P53;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3060862; DOI=10.1093/nar/16.23.11384;
RA Soussi T.;
RT "Nucleotide sequence of a cDNA encoding the rat p53 nuclear oncoprotein.";
RL Nucleic Acids Res. 16:11384-11384(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8441680; DOI=10.1093/nar/21.3.713;
RA Hulla J.E., Schneider R.P.;
RT "Structure of the rat p53 tumor suppressor gene.";
RL Nucleic Acids Res. 21:713-717(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9278438; DOI=10.1074/jbc.272.36.22776;
RA Mathupala S.P., Heese C., Pedersen P.L.;
RT "Glucose catabolism in cancer cells. The type II hexokinase promoter
RT contains functionally active response elements for the tumor suppressor
RT p53.";
RL J. Biol. Chem. 272:22776-22780(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH HSP90AB1.
RC TISSUE=Embryo;
RX PubMed=8663025; DOI=10.1074/jbc.271.25.15084;
RA Sepehrnia B., Paz I.B., Dasgupta G., Momand J.;
RT "Heat shock protein 84 forms a complex with mutant p53 protein
RT predominantly within a cytoplasmic compartment of the cell.";
RL J. Biol. Chem. 271:15084-15090(1996).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=22726440; DOI=10.1016/j.cell.2012.05.014;
RA Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.;
RT "p53 opens the mitochondrial permeability transition pore to trigger
RT necrosis.";
RL Cell 149:1536-1548(2012).
CC -!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
CC growth arrest or apoptosis depending on the physiological circumstances
CC and cell type. Involved in cell cycle regulation as a trans-activator
CC that acts to negatively regulate cell division by controlling a set of
CC genes required for this process. One of the activated genes is an
CC inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be
CC mediated either by stimulation of BAX and FAS antigen expression, or by
CC repression of Bcl-2 expression. Its pro-apoptotic activity is activated
CC via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By
CC similarity). However, this activity is inhibited when the interaction
CC with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By
CC similarity). In cooperation with mitochondrial PPIF is involved in
CC activating oxidative stress-induced necrosis; the function is largely
CC independent of transcription. Prevents CDK7 kinase activity when
CC associated to CAK complex in response to DNA damage, thus stopping cell
CC cycle progression. Induces the transcription of long intergenic non-
CC coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21
CC participates in TP53-dependent transcriptional repression leading to
CC apoptosis and seems to have an effect on cell-cycle regulation.
CC Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated
CC transcriptional activation of PER2. {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Forms homodimers and homotetramers (By similarity). Binds DNA
CC as a homotetramer. Interacts with AXIN1. Probably part of a complex
CC consisting of TP53, HIPK2 and AXIN1 (By similarity). Interacts with
CC histone acetyltransferases EP300 and methyltransferases HRMT1L2 and
CC CARM1, and recruits them to promoters. Interacts (via C-terminus) with
CC TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this
CC interaction may be indirect. Found in a complex with CABLES1 and TP73.
CC Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX.
CC Interacts with USP7 and SYVN1. Interacts with HSP90AB1
CC (PubMed:8663025). Interacts with CHD8; leading to recruit histone H1
CC and prevent transactivation activity (By similarity). Interacts with
CC ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F1. Interacts
CC with YWHAZ; the interaction enhances TP53 transcriptional activity.
CC Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction.
CC Interacts (via DNA-binding domain) with MAML1 (via N-terminus).
CC Interacts with MKRN1. Interacts with PML (via C-terminus). Interacts
CC with MDM2; leading to ubiquitination and proteasomal degradation of
CC TP53. Directly interacts with FBXO42; leading to ubiquitination and
CC degradation of TP53. Interacts (phosphorylated at Ser-15 by ATM) with
CC the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-
CC dependent inhibition of cell proliferation. Interacts with PPP2R2A.
CC Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when
CC monomethylated at Lys-380) with L3MBTL1. Interacts with GRK5. Binds to
CC the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage.
CC Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and
CC NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes
CC ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes
CC ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the
CC association implicates preferentially tetrameric TP53, is induced by
CC oxidative stress and is impaired by cyclosporin A (CsA). Interacts with
CC SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated
CC ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with
CC KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is
CC direct. Interacts (via DNA-binding domain) with ZNF385A; the
CC interaction is direct and enhances p53/TP53 transactivation functions
CC on cell-cycle arrest target genes, resulting in growth arrest.
CC Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in
CC p53/TP53 ubiquitination. Interacts with MTA1 and COP1. Interacts with
CC CCAR2 (via N-terminus). Interacts with MORC3. Interacts (via C-
CC terminus) with POU4F2 (via C-terminus). Interacts (via oligomerization
CC region) with NOP53; the interaction is direct and may prevent the MDM2-
CC mediated proteasomal degradation of TP53. Interacts with AFG1L;
CC mediates mitochondrial translocation of TP53. Interacts with UBD (By
CC similarity). Interacts with TAF6 (By similarity). Binds DNA as a
CC homotetramer. Interacts with AXIN1. Probably part of a complex
CC consisting of TP53, HIPK2 and AXIN1. Interacts with histone
CC acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and
CC recruits them to promoters. Interacts (via C-terminus) with TAF1; when
CC TAF1 is part of the TFIID complex. Interacts with ING4; this
CC interaction may be indirect. Found in a complex with CABLES1 and TP73.
CC Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX.
CC Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with
CC CHD8; leading to recruit histone H1 and prevent transactivation
CC activity. Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1,
CC UHRF2 and E4F. Interacts with YWHAZ; the interaction enhances TP53
CC transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits
CC this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-
CC terminus). Interacts with MKRN1. Interacts with PML (via C-terminus).
CC Interacts with MDM2; leading to ubiquitination and proteasomal
CC degradation of TP53. Directly interacts with FBXO42; leading to
CC ubiquitination and degradation of TP53. Interacts (phosphorylated at
CC Ser-18 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates
CC stress-induced TP53-dependent inhibition of cell proliferation.
CC Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24.
CC Interacts (when monomethylated at Lys-379) with L3MBTL1. Interacts with
CC GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to
CC DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB,
CC SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this
CC promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this
CC promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with
CC PPIF; the association implicates preferentially tetrameric TP53, is
CC induced by oxidative stress and is impaired by cyclosporin A (CsA).
CC Interacts with SNAI1; the interaction induces SNAI1 degradation via
CC MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion.
CC Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the
CC interaction is direct. Interacts (via DNA-binding domain) with ZNF385A;
CC the interaction is direct and enhances p53/TP53 transactivation
CC functions on cell-cycle arrest target genes, resulting in growth arrest
CC (By similarity). Interacts with ANKRD2. Interacts with RFFL and RNF34;
CC involved in p53/TP53 ubiquitination. Interacts with MTA1 and COP1.
CC Interacts with CCAR2 (via N-terminus). Interacts with MORC3. Interacts
CC (via C-terminus) with POU4F2 (via C-terminus). Interacts (via
CC oligomerization region) with NOP53; the interaction is direct and may
CC prevent the MDM2-mediated proteasomal degradation of TP53. Interacts
CC with AFG1L; mediates mitochondrial translocation of TP53. Interacts
CC with UBD (By similarity). Interacts with TAF6 (By similarity).
CC Interacts with C10orf90/FATS; the interaction inhibits binding of TP53
CC and MDM2 (By similarity). Interacts with NUPR1; interaction is stress-
CC dependent. Forms a complex with EP300 and NUPR1; this complex binds
CC CDKN1A promoter leading to transcriptional induction of CDKN1A (By
CC similarity). Interacts with PRMT5 in response to DNA damage; the
CC interaction is TTC5/STRAP dependent (By similarity). Interacts with
CC PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits
CC pro-apoptotic activity of p53/TP53 (By similarity). Interacts with
CC PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-
CC apoptotic activity (By similarity). When phosphorylated at Ser-15,
CC interacts with DDX3X and gamma-tubulin (By similarity). Interacts with
CC KAT7/HBO1; leading to inhibit histone acetyltransferase activity of
CC KAT7/HBO1 (By similarity). Interacts (via N-terminus) with E3
CC ubiquitin-protein ligase MUL1; the interaction results in
CC ubiquitination of cytoplasmic TP53 at Lys-24 and subsequent proteasomal
CC degradation (By similarity). Interacts with S100A4; this interaction
CC promotes TP53 degradation (By similarity). Interacts with TTC5/STRAP;
CC the interaction may result in increased mitochondrial-dependent
CC apoptosis (By similarity). Interacts with NQO1; this interaction is
CC NADH-dependent, stabilizes TP53 in response to oxidative stress and
CC protects it from ubiquitin-independent degradation by the 20S
CC proteasome. {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:8663025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus
CC {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P04637}.
CC Note=Interaction with BANP promotes nuclear localization. Recruited
CC into PML bodies together with CHEK2. Translocates to mitochondria upon
CC oxidative stress. Translocates to mitochondria in response to mitomycin
CC C treatment (By similarity). {ECO:0000250|UniProtKB:P04637}.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser residues mediates transcriptional
CC activation. Phosphorylation at Ser-9 by HIPK4 increases repression
CC activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by
CC VRK1, which may prevent the interaction with MDM2. Phosphorylated on
CC Ser-20 by CHEK2 in response to DNA damage, which prevents
CC ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to
CC reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis.
CC Probably phosphorylated on by CDK7 in a CAK complex in response to DNA
CC damage. Phosphorylated by HIPK1. Phosphorylated on Ser-390 following UV
CC but not gamma irradiation. Stabilized by CDK5-mediated phosphorylation
CC in response to genotoxic and oxidative stresses at Ser-15, leading to
CC accumulation of p53/TP53, particularly in the nucleus, thus inducing
CC the transactivation of p53/TP53 target genes. Phosphorylated at Ser-313
CC and Ser-390 by CDK2 in response to DNA-damage (By similarity).
CC Phosphorylation at Ser-15 is required for interaction with DDX3X and
CC gamma-tubulin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Monomethylated at Lys-370 by SETD7, leading to stabilization and
CC increased transcriptional activation. Monomethylated at Lys-368 by
CC SMYD2, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity. Lys-370 monomethylation prevents
CC interaction with SMYD2 and subsequent monomethylation at Lys-368.
CC Dimethylated at Lys-371 by EHMT1 and EHMT2. Monomethylated at Lys-380
CC by KMT5A, promoting interaction with L3MBTL1 and leading to repress
CC transcriptional activity. Demethylation of dimethylated Lys-368 by
CC KDM1A prevents interaction with TP53BP1 and represses TP53-mediated
CC transcriptional activation (By similarity). Monomethylated at Arg-331
CC and dimethylated at Arg-333 and Arg-335 by PRMT5; methylation is
CC increased after DNA damage and might possibly affect TP53 target gene
CC specificity (By similarity). {ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal
CC degradation. Ubiquitinated by RFWD3, which works in cooperation with
CC MDM2 and may catalyze the formation of short polyubiquitin chains on
CC p53/TP53 that are not targeted to the proteasome. Ubiquitinated by
CC MKRN1, which leads to proteasomal degradation. Deubiquitinated by
CC USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34
CC and RNF125, which leads to proteasomal degradation. Ubiquitination by
CC TOPORS induces degradation. Deubiquitination by USP7, leading to
CC stabilize it. Ubiquitinated by COP1, which leads to proteasomal
CC degradation (By similarity). Ubiquitination and subsequent proteasomal
CC degradation is negatively regulated by CCAR2 (By similarity).
CC Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-
CC linkage independent and non-proteolytic, leading to TP53 stabilization
CC (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to
CC proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Acetylation of Lys-380 by CREBBP enhances transcriptional
CC activity. Acetylation of Lys-380 by EP300. Deacetylation of Lys-380 by
CC SIRT1 impairs its ability to induce proapoptotic program and modulate
CC cell senescence. Deacetylation by SIRT2 impairs its ability to induce
CC transcription activation in a AKT-dependent manner. Acetylation at Lys-
CC 379 increases stability. Deacetylation at Lys-379 by SIRT6 decreases
CC its stability, thereby regulating cell senescence.
CC {ECO:0000250|UniProtKB:P04637}.
CC -!- DISEASE: Note=p53 is found in increased amounts in a wide variety of
CC transformed cells. p53 is frequently mutated or inactivated in many
CC types of cancer.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; X13058; CAA31457.1; -; mRNA.
DR EMBL; L07910; AAA41788.1; -; Genomic_DNA.
DR EMBL; L07904; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; L07905; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; L07906; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; L07907; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; L07908; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; L07909; AAA41788.1; JOINED; Genomic_DNA.
DR EMBL; U90328; AAB80959.1; -; mRNA.
DR EMBL; BC081788; AAH81788.2; -; mRNA.
DR EMBL; BC098663; AAH98663.1; -; mRNA.
DR PIR; S02192; S02192.
DR RefSeq; NP_112251.2; NM_030989.3.
DR RefSeq; XP_006246656.1; XM_006246594.3.
DR RefSeq; XP_006246657.1; XM_006246595.3.
DR AlphaFoldDB; P10361; -.
DR SMR; P10361; -.
DR BioGRID; 246960; 11.
DR DIP; DIP-46016N; -.
DR IntAct; P10361; 5.
DR MINT; P10361; -.
DR STRING; 10116.ENSRNOP00000047840; -.
DR iPTMnet; P10361; -.
DR PhosphoSitePlus; P10361; -.
DR PaxDb; P10361; -.
DR PRIDE; P10361; -.
DR Ensembl; ENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756.
DR GeneID; 24842; -.
DR KEGG; rno:24842; -.
DR UCSC; RGD:3889; rat.
DR CTD; 7157; -.
DR RGD; 3889; Tp53.
DR eggNOG; ENOG502QVY3; Eukaryota.
DR GeneTree; ENSGT00950000183153; -.
DR HOGENOM; CLU_019621_0_0_1; -.
DR InParanoid; P10361; -.
DR OMA; VVSTRIC; -.
DR OrthoDB; 257530at2759; -.
DR PhylomeDB; P10361; -.
DR TreeFam; TF106101; -.
DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-RNO-2559585; Oncogene Induced Senescence.
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-6804754; Regulation of TP53 Expression.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69541; Stabilization of p53.
DR Reactome; R-RNO-69895; Transcriptional activation of cell cycle inhibitor p21.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8941855; RUNX3 regulates CDKN1A transcription.
DR PRO; PR:P10361; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000010756; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; P10361; baseline and differential.
DR Genevisible; P10361; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016605; C:PML body; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005657; C:replication fork; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ARUK-UCL.
DR GO; GO:0035861; C:site of double-strand break; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IDA:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:RGD.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0035033; F:histone deacetylase regulator activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0002326; P:B cell lineage commitment; ISO:RGD.
DR GO; GO:0048539; P:bone marrow development; ISO:RGD.
DR GO; GO:0060411; P:cardiac septum morphogenesis; ISO:RGD.
DR GO; GO:0072717; P:cellular response to actinomycin D; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0071494; P:cellular response to UV-C; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0031497; P:chromatin assembly; ISO:RGD.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:RGD.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:RGD.
DR GO; GO:0006302; P:double-strand break repair; ISO:RGD.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISO:RGD.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0006983; P:ER overload response; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISO:RGD.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; ISO:RGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO:RGD.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0009299; P:mRNA transcription; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0070266; P:necroptotic process; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:RGD.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:1903451; P:negative regulation of G1 to G0 transition; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1904024; P:negative regulation of glucose catabolic process to lactate via pyruvate; ISO:RGD.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISO:RGD.
DR GO; GO:1901525; P:negative regulation of mitophagy; ISO:RGD.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISO:RGD.
DR GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; ISO:RGD.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0090403; P:oxidative stress-induced premature senescence; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:2000774; P:positive regulation of cellular senescence; ISO:RGD.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0062100; P:positive regulation of programmed necrotic cell death; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; ISO:RGD.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:RGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ARUK-UCL.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000772; P:regulation of cellular senescence; ISO:RGD.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:2000269; P:regulation of fibroblast apoptotic process; ISO:RGD.
DR GO; GO:1903205; P:regulation of hydrogen peroxide-induced cell death; IMP:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:RGD.
DR GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0070243; P:regulation of thymocyte apoptotic process; ISO:RGD.
DR GO; GO:0034103; P:regulation of tissue remodeling; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1990248; P:regulation of transcription from RNA polymerase II promoter in response to DNA damage; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0090399; P:replicative senescence; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009651; P:response to salt stress; ISO:RGD.
DR GO; GO:0009411; P:response to UV; IEP:RGD.
DR GO; GO:0010224; P:response to UV-B; IEP:RGD.
DR GO; GO:0033552; P:response to vitamin B3; IEP:RGD.
DR GO; GO:0010165; P:response to X-ray; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0009303; P:rRNA transcription; ISO:RGD.
DR GO; GO:0072331; P:signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0002360; P:T cell lineage commitment; ISO:RGD.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0016032; P:viral process; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR013872; p53_transactivation_domain.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF08563; P53_TAD; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Apoptosis; Biological rhythms; Cell cycle;
KW Cytoplasm; Cytoskeleton; DNA-binding; Endoplasmic reticulum;
KW Isopeptide bond; Metal-binding; Methylation; Mitochondrion; Necrosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
FT CHAIN 1..391
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185712"
FT DNA_BIND 100..290
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..318
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..47
FT /note="Transcription activation (acidic)"
FT REGION 64..108
FT /note="Interaction with WWOX"
FT /evidence="ECO:0000250"
FT REGION 65..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..368
FT /note="Interaction with HIPK1"
FT /evidence="ECO:0000250"
FT REGION 98..298
FT /note="Required for interaction with ZNF385A"
FT /evidence="ECO:0000250"
FT REGION 111..234
FT /note="Required for interaction with FBXO42"
FT /evidence="ECO:0000250"
FT REGION 114..290
FT /note="Interaction with AXIN1"
FT /evidence="ECO:0000250"
FT REGION 254..292
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 271..278
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 281..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..358
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT REGION 323..354
FT /note="Oligomerization"
FT REGION 350..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..361
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 366..385
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 303..319
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 337..348
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 368..370
FT /note="[KR]-[STA]-K motif"
FT COMPBIAS 281..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT SITE 118
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 9
FT /note="Phosphoserine; by HIPK4"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 15
FT /note="Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 18
FT /note="Phosphothreonine; by CK1, VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 20
FT /note="Phosphoserine; by CHEK2, CK1 and PLK3"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 39
FT /note="Phosphoserine; by MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 118
FT /note="N6-acetyllysine; by KAT6A"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 181
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 267
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 282
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 303
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 313
FT /note="Phosphoserine; by AURKA, CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02340"
FT MOD_RES 331
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 333
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 335
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 368
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 368
FT /note="N6-methyllysine; by SMYD2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 370
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 371
FT /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 371
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6-acetyllysine; by KAT6A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6-methyllysine; by KMT5A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 390
FT /note="Phosphoserine; by CK2, CDK2 and NUAK1"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VARIANT 103
FT /note="G -> S"
FT VARIANT 256
FT /note="E -> G"
FT CONFLICT 174
FT /note="C -> W (in Ref. 2; AAA41788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43451 MW; E62522313A5C872F CRC64;
MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ DVAELLEGPE
EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT YQGNYGFHLG FLQSGTAKSV
MCTYSISLNK LFCQLAKTCP VQLWVTSTPP PGTRVRAMAI YKKSQHMTEV VRRCPHHERC
SDGDGLAPPQ HLIRVEGNPY AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC
MGGMNRRPIL TIITLEDSSG NLLGRDSFEV RVCACPGRDR RTEEENFRKK EEHCPELPPG
SAKRALPTST SSSPQQKKKP LDGEYFTLKI RGRERFEMFR ELNEALELKD ARAAEESGDS
RAHSSYPKTK KGQSTSRHKK PMIKKVGPDS D
