P53_CANLF
ID P53_CANLF Reviewed; 381 AA.
AC Q29537; Q9TV78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=TP53; Synonyms=P53;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukocyte;
RX PubMed=9519881; DOI=10.1038/sj.onc.1201863;
RA Veldhoen N., Milner J.;
RT "Isolation of canine p53 cDNA and detailed characterization of the full
RT length canine p53 protein.";
RL Oncogene 16:1077-1084(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RA Setoguchi A., Sakai T., Okuda M., Minehata K., Yazawa M., Ishizaka T.,
RA Watari T., Hasagawa A., Tsujimoto H.;
RT "Aberrations of p53 tumor suppressor gene in various spontaneous tumors in
RT the dog.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-300.
RC STRAIN=Beagle;
RX PubMed=7600529; DOI=10.1016/0304-3835(95)03779-v;
RA Kraegel S.A., Pazzi K.A., Madewell B.R.;
RT "Sequence analysis of canine p53 in the region of exons 3-8.";
RL Cancer Lett. 92:181-186(1995).
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. 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-370) 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 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: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. Phosphorylated on Thr-18 by VRK1, which may prevent the
CC interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to
CC DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on
CC Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting
CC p53/TP53-mediated apoptosis. Phosphorylated on Ser-33 by CDK7 in a CAK
CC complex in response to DNA damage. Phosphorylated by HIPK1. Stabilized
CC by CDK5-mediated phosphorylation in response to genotoxic and oxidative
CC stresses at Ser-15 and Ser-33, leading to accumulation of p53/TP53,
CC particularly in the nucleus, thus inducing the transactivation of
CC p53/TP53 target genes. Phosphorylated at Ser-303 and Ser-380 by CDK2 in
CC response to DNA-damage. Phosphorylated on Ser-380 following UV but not
CC gamma irradiation (By similarity). Phosphorylation at Ser-15 is
CC required for interaction with DDX3X and gamma-tubulin (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Monomethylated at Lys-360 by SETD7, leading to stabilization and
CC increased transcriptional activation. Monomethylated at Lys-358 by
CC SMYD2, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity. Lys-360 monomethylation prevents
CC interaction with SMYD2 and subsequent monomethylation at Lys-358.
CC Dimethylated at Lys-361 by EHMT1 and EHMT2. Monomethylated at Lys-370
CC by KMT5A, promoting interaction with L3MBTL1 and leading to repress
CC transcriptional activity. Demethylation of dimethylated Lys-358 by
CC KDM1A prevents interaction with TP53BP1 and represses TP53-mediated
CC transcriptional activation (By similarity). Monomethylated at Arg-321
CC and dimethylated at Arg-323 and Arg-325 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-374 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). {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Acetylation of Lys-370 by CREBBP enhances transcriptional
CC activity. Acetylation of Lys-370 by EP300. Deacetylation of Lys-370 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 369 increases stability. Deacetylation at Lys-369 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF060514; AAC16909.1; -; mRNA.
DR EMBL; AB020761; BAA78379.1; -; Genomic_DNA.
DR EMBL; S77819; AAB42022.1; -; mRNA.
DR RefSeq; NP_001003210.1; NM_001003210.1.
DR AlphaFoldDB; Q29537; -.
DR SMR; Q29537; -.
DR BioGRID; 139788; 1.
DR STRING; 9612.ENSCAFP00000024579; -.
DR iPTMnet; Q29537; -.
DR PaxDb; Q29537; -.
DR GeneID; 403869; -.
DR CTD; 7157; -.
DR eggNOG; ENOG502QVY3; Eukaryota.
DR InParanoid; Q29537; -.
DR OrthoDB; 257530at2759; -.
DR Proteomes; UP000002254; Unplaced.
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; IDA:CACAO.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 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; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
FT CHAIN 1..381
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185695"
FT DNA_BIND 89..280
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..308
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..44
FT /note="Transcription activation (acidic)"
FT REGION 55..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..97
FT /note="Interaction with WWOX"
FT /evidence="ECO:0000250"
FT REGION 87..358
FT /note="Interaction with HIPK1"
FT /evidence="ECO:0000250"
FT REGION 87..288
FT /note="Required for interaction with ZNF385A"
FT /evidence="ECO:0000250"
FT REGION 100..224
FT /note="Required for interaction with FBXO42"
FT /evidence="ECO:0000250"
FT REGION 103..280
FT /note="Interaction with AXIN1"
FT /evidence="ECO:0000250"
FT REGION 244..282
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 261..268
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 270..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..348
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT REGION 313..344
FT /note="Oligomerization"
FT REGION 338..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..351
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 356..375
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 293..309
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 327..338
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 358..360
FT /note="[KR]-[STA]-K motif"
FT COMPBIAS 67..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT SITE 107
FT /note="Interaction with DNA"
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 107
FT /note="N6-acetyllysine; by KAT6A"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 170
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 257
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 272
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 303
FT /note="Phosphoserine; by AURKA, CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02340"
FT MOD_RES 321
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 323
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 325
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 358
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 358
FT /note="N6-methyllysine; by SMYD2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 360
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 361
FT /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 361
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 369
FT /note="N6-acetyllysine"
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-acetyllysine; by KAT6A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 370
FT /note="N6-methyllysine; by KMT5A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="Phosphoserine; by CK2, CDK2 and NUAK1"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 1..4
FT /note="MEES -> MQEP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="L -> P (in Ref. 2; BAA78379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42486 MW; 761A718FDC93DA59 CRC64;
MEESQSELNI DPPLSQETFS ELWNLLPENN VLSSELCPAV DELLLPESVV NWLDEDSDDA
PRMPATSAPT APGPAPSWPL SSSVPSPKTY PGTYGFRLGF LHSGTAKSVT WTYSPLLNKL
FCQLAKTCPV QLWVSSPPPP NTCVRAMAIY KKSEFVTEVV RRCPHHERCS DSSDGLAPPQ
HLIRVEGNLR AKYLDDRNTF RHSVVVPYEP PEVGSDYTTI HYNYMCNSSC MGGMNRRPIL
TIITLEDSSG NVLGRNSFEV RVCACPGRDR RTEEENFHKK GEPCPEPPPG STKRALPPST
SSSPPQKKKP LDGEYFTLQI RGRERYEMFR NLNEALELKD AQSGKEPGGS RAHSSHLKAK
KGQSTSRHKK LMFKREGLDS D
