P53_MACFU
ID P53_MACFU Reviewed; 393 AA.
AC P61260;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=TP53; Synonyms=P53;
OS Macaca fuscata fuscata (Japanese macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9543;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=12099687; DOI=10.1016/s0006-291x(02)00730-1;
RA Shimizu Y., Ishida T.;
RT "Somatic mutations in the p53 gene account for the extension of replicative
RT life span of macaque cells.";
RL Biochem. Biophys. Res. Commun. 295:644-650(2002).
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. In cooperation with mitochondrial PPIF
CC is involved in activating oxidative stress-induced necrosis; the
CC function is largely independent of transcription. Prevents CDK7 kinase
CC activity when associated to CAK complex in response to DNA damage, thus
CC stopping cell cycle progression. Induces the transcription of long
CC intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-
CC p21 participates in TP53-dependent transcriptional repression leading
CC to 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. 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-15 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-382) 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). When
CC phosphorylated at Ser-15, interacts with DDX3X and gamma-tubulin (By
CC similarity). Interacts with KAT7/HBO1; leading to inhibit histone
CC acetyltransferase activity of KAT7/HBO1 (By similarity). Interacts (via
CC N-terminus) with E3 ubiquitin-protein ligase MUL1; the interaction
CC results in ubiquitination of cytoplasmic TP53 at Lys-24 and subsequent
CC proteasomal degradation (By similarity). Interacts with S100A4; this
CC interaction promotes TP53 degradation (By similarity). Interacts with
CC TTC5/STRAP; the interaction may result in increased mitochondrial-
CC dependent apoptosis (By similarity). Interacts with NQO1; this
CC interaction is NADH-dependent, stabilizes TP53 in response to oxidative
CC stress and protects it from ubiquitin-independent degradation by the
CC 20S proteasome. {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637, ECO:0000250|UniProtKB:P10361}.
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 Phosphorylated on Ser-392 following UV but not gamma irradiation.
CC Phosphorylated on Thr-55 by TAF1 which promotes MDM2-mediated TP53
CC degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in
CC response to DNA damage. Stabilized by CDK5-mediated phosphorylation in
CC response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-
CC 46, leading to accumulation of p53/TP53, particularly in the nucleus,
CC thus inducing the transactivation of p53/TP53 target genes.
CC Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress.
CC Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage
CC (By similarity). Phosphorylation at Ser-15 is required for interaction
CC with DDX3X and gamma-tubulin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Monomethylated at Lys-372 by SETD7, leading to stabilization and
CC increased transcriptional activation. Monomethylated at Lys-370 by
CC SMYD2, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity. Lys-372 monomethylation prevents
CC interaction with SMYD2 and subsequent monomethylation at Lys-370.
CC Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382
CC by KMT5A, promoting interaction with L3MBTL1 and leading to repress
CC transcriptional activity. Demethylation of dimethylated Lys-370 by
CC KDM1A prevents interaction with TP53BP1 and represses TP53-mediated
CC transcriptional activation (By similarity). Monomethylated at Arg-333
CC and dimethylated at Arg-335 and Arg-337 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-386 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-382 by CREBBP enhances transcriptional
CC activity. Acetylation of Lys-382 by EP300. Deacetylation of Lys-382 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 381 increases stability. Deacetylation at Lys-381 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; AF456344; AAN64028.1; -; mRNA.
DR AlphaFoldDB; P61260; -.
DR BMRB; P61260; -.
DR SMR; P61260; -.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
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; IPR040926; p53_TAD2.
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 Pfam; PF18521; TAD2; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript 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; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
FT CHAIN 1..393
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185705"
FT DNA_BIND 102..292
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..320
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..83
FT /note="Interaction with HRMT1L2"
FT /evidence="ECO:0000250"
FT REGION 1..44
FT /note="Transcription activation (acidic)"
FT REGION 48..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..110
FT /note="Interaction with WWOX"
FT /evidence="ECO:0000250"
FT REGION 100..300
FT /note="Required for interaction with ZNF385A"
FT /evidence="ECO:0000250"
FT REGION 113..236
FT /note="Required for interaction with FBXO42"
FT /evidence="ECO:0000250"
FT REGION 256..294
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 273..280
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 283..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..393
FT /note="Interaction with CARM1"
FT /evidence="ECO:0000250"
FT REGION 325..356
FT /note="Oligomerization"
FT REGION 352..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..363
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 368..387
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 305..321
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 339..350
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 370..372
FT /note="[KR]-[STA]-K motif"
FT COMPBIAS 70..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT SITE 120
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 33
FT /note="Phosphoserine; by CDK5 and CDK7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 37
FT /note="Phosphoserine; by MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 46
FT /note="Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 55
FT /note="Phosphothreonine; by TAF1"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Phosphothreonine; by TAF1 and GRK5"
FT /evidence="ECO:0000250"
FT MOD_RES 120
FT /note="N6-acetyllysine; by KAT6A"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 183
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 269
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 284
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 315
FT /note="Phosphoserine; by AURKA, CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02340"
FT MOD_RES 333
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 335
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 337
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 370
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 370
FT /note="N6-methyllysine; by SMYD2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 372
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 373
FT /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 373
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 381
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 382
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 382
FT /note="N6-acetyllysine; by KAT6A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 382
FT /note="N6-methyllysine; by KMT5A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 392
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 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 393 AA; 43655 MW; E212E5E4FE650103 CRC64;
MEEPQSDPSI EPPLSQETFS DLWKLLPENN VLSPLPSQAV DDLMLSPDDL AQWLTEDPGP
DEAPRMSEAA PPMAPTPAAP TPAAPAPAPS WPLSSSVPSQ KTYHGSYGFR LGFLHSGTAK
SVTCTYSPDL NKMFCQLAKT CPVQLWVDST PPPGSRVRAM AIYKQSQHMT EVVRRCPHHE
RCSDSDGLAP PQHLIRVEGN LRVEYSDDRN TFRHSVVVPY EPPEVGSDCT TIHYNYMCNS
SCMGGMNRRP ILTIITLEDS SGNLLGRNSF EVRVCACPGR DRRTEEENFR KKGEPCHQLP
PGSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPA
GSRAHSSHLK SKKGQSTSRH KKFMFKTEGP DSD
