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Cellular tumor antigen p53 (Tumor suppressor p53)

 P53_RAT                 Reviewed;         391 AA.
P10361; O09168; Q4KMA9; Q66HM0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
30-AUG-2017, entry version 199.
RecName: Full=Cellular tumor antigen p53;
AltName: Full=Tumor suppressor p53;
Name=Tp53; Synonyms=P53;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3060862; DOI=10.1093/nar/16.23.11384;
Soussi T.;
"Nucleotide sequence of a cDNA encoding the rat p53 nuclear
oncoprotein.";
Nucleic Acids Res. 16:11384-11384(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8441680; DOI=10.1093/nar/21.3.713;
Hulla J.E., Schneider R.P.;
"Structure of the rat p53 tumor suppressor gene.";
Nucleic Acids Res. 21:713-717(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=9278438; DOI=10.1074/jbc.272.36.22776;
Mathupala S.P., Heese C., Pedersen P.L.;
"Glucose catabolism in cancer cells. The type II hexokinase promoter
contains functionally active response elements for the tumor
suppressor p53.";
J. Biol. Chem. 272:22776-22780(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart, and Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH HSP90AB1.
TISSUE=Embryo;
PubMed=8663025; DOI=10.1074/jbc.271.25.15084;
Sepehrnia B., Paz I.B., Dasgupta G., Momand J.;
"Heat shock protein 84 forms a complex with mutant p53 protein
predominantly within a cytoplasmic compartment of the cell.";
J. Biol. Chem. 271:15084-15090(1996).
[6]
SUBCELLULAR LOCATION.
PubMed=22726440; DOI=10.1016/j.cell.2012.05.014;
Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S.,
Moll U.M.;
"p53 opens the mitochondrial permeability transition pore to trigger
necrosis.";
Cell 149:1536-1548(2012).
-!- 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 (PubMed:8663025).
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 on 'Ser-58' 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 RFWD2. 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, ECO:0000269|PubMed:8663025}.
-!- 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. Probably phosphorylated on by CDK7 in a CAK
complex in response to DNA damage. Phosphorylated by HIPK1.
Phosphorylated on Ser-390 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, leading to accumulation of p53/TP53, particularly in the
nucleus, thus inducing the transactivation of p53/TP53 target
genes. 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 and Lys-290, 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 RFWD2, which leads to proteasomal
degradation. Ubiquitination and subsequent proteasomal degradation
is negatively regulated by CCAR2 (By similarity).
{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; X13058; CAA31457.1; -; mRNA.
EMBL; L07910; AAA41788.1; -; Genomic_DNA.
EMBL; L07904; AAA41788.1; JOINED; Genomic_DNA.
EMBL; L07905; AAA41788.1; JOINED; Genomic_DNA.
EMBL; L07906; AAA41788.1; JOINED; Genomic_DNA.
EMBL; L07907; AAA41788.1; JOINED; Genomic_DNA.
EMBL; L07908; AAA41788.1; JOINED; Genomic_DNA.
EMBL; L07909; AAA41788.1; JOINED; Genomic_DNA.
EMBL; U90328; AAB80959.1; -; mRNA.
EMBL; BC081788; AAH81788.2; -; mRNA.
EMBL; BC098663; AAH98663.1; -; mRNA.
PIR; S02192; S02192.
RefSeq; NP_112251.2; NM_030989.3.
RefSeq; XP_006246656.1; XM_006246594.3.
RefSeq; XP_006246657.1; XM_006246595.3.
UniGene; Rn.54443; -.
ProteinModelPortal; P10361; -.
SMR; P10361; -.
BioGrid; 246960; 10.
DIP; DIP-46016N; -.
IntAct; P10361; 4.
MINT; MINT-4651801; -.
STRING; 10116.ENSRNOP00000047840; -.
iPTMnet; P10361; -.
PhosphoSitePlus; P10361; -.
PaxDb; P10361; -.
PRIDE; P10361; -.
Ensembl; ENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756.
Ensembl; ENSRNOT00000085115; ENSRNOP00000074031; ENSRNOG00000010756.
GeneID; 24842; -.
KEGG; rno:24842; -.
UCSC; RGD:3889; rat.
CTD; 7157; -.
RGD; 3889; Tp53.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
GeneTree; ENSGT00390000015092; -.
HOGENOM; HOG000039957; -.
HOVERGEN; HBG005201; -.
InParanoid; P10361; -.
KO; K04451; -.
OMA; SMDQSIQ; -.
PhylomeDB; P10361; -.
TreeFam; TF106101; -.
PRO; PR:P10361; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000010756; -.
ExpressionAtlas; P10361; baseline and differential.
Genevisible; P10361; RN.
GO; GO:0000785; C:chromatin; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005657; C:replication fork; IBA:GO_Central.
GO; GO:0005667; C:transcription factor complex; IDA:RGD.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:RGD.
GO; GO:0002039; F:p53 binding; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0001221; F:transcription cofactor binding; IPI:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:RGD.
GO; GO:0034644; P:cellular response to UV; IBA:GO_Central.
GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IBA:GO_Central.
GO; GO:0000733; P:DNA strand renaturation; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IBA:GO_Central.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
GO; GO:0031065; P:positive regulation of histone deacetylation; IBA:GO_Central.
GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
GO; GO:1903205; P:regulation of hydrogen peroxide-induced cell death; IMP:UniProtKB.
GO; GO:0051453; P:regulation of intracellular pH; IMP:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:RGD.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; IBA:GO_Central.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0010038; P:response to metal ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0009411; P:response to UV; IEP:RGD.
GO; GO:0010224; P:response to UV-B; IEP:RGD.
GO; GO:0033552; P:response to vitamin B3; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042060; P:wound healing; IEP:RGD.
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.
InterPro; IPR011615; p53_DNA-bd.
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.
1: Evidence at protein level;
Acetylation; Activator; Apoptosis; Biological rhythms; Cell cycle;
Complete proteome; Cytoplasm; DNA-binding; Endoplasmic reticulum;
Isopeptide bond; Metal-binding; Methylation; Mitochondrion; Necrosis;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
CHAIN 1 391 Cellular tumor antigen p53.
/FTId=PRO_0000185712.
DNA_BIND 100 290 {ECO:0000250}.
REGION 1 318 Interaction with CCAR2.
{ECO:0000250|UniProtKB:P04637}.
REGION 1 47 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 39 39 Phosphoserine; by MAPKAPK5.
{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 290 290 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}.
VARIANT 103 103 G -> S.
VARIANT 256 256 E -> G.
CONFLICT 174 174 C -> W (in Ref. 2; AAA41788).
{ECO:0000305}.
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


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