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Cellular tumor antigen p53 (Tumor suppressor p53)

 P53_FELCA               Reviewed;         386 AA.
P41685;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
30-AUG-2017, entry version 166.
RecName: Full=Cellular tumor antigen p53;
AltName: Full=Tumor suppressor p53;
Name=TP53; Synonyms=TRP53;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymph node;
PubMed=8056458; DOI=10.1002/ijc.2910580425;
Okuda M., Umeda A., Sakai T., Ohashi T., Momoi Y., Youn H.Y.,
Watari T., Goitsuka R., Tsujimoto H., Hasegawa A.;
"Cloning of feline p53 tumor-suppressor gene and its aberration in
hematopoietic tumors.";
Int. J. Cancer 58:602-607(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-354.
PubMed=8286534; DOI=10.1292/jvms.55.801;
Okuda M., Umeda A., Matsumoto Y., Momoi Y., Watari T., Goitsuka R.,
O'Brien S.J., Tsujimoto H., Hasegawa A.;
"Molecular cloning and chromosomal mapping of feline p53 tumor
suppressor gene.";
J. Vet. Med. Sci. 55:801-805(1993).
-!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
growth arrest or apoptosis depending on the physiological
circumstances and cell type. Involved in cell cycle regulation as
a trans-activator that acts to negatively regulate cell division
by controlling a set of genes required for this process. One of
the activated genes is an inhibitor of cyclin-dependent kinases.
Apoptosis induction seems to be mediated either by stimulation of
BAX and FAS antigen expression, or by repression of Bcl-2
expression. In cooperation with mitochondrial PPIF is involved in
activating oxidative stress-induced necrosis; the function is
largely independent of transcription. Prevents CDK7 kinase
activity when associated to CAK complex in response to DNA damage,
thus stopping cell cycle progression. Induces the transcription of
long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-
Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional
repression leading to apoptosis and seem to have to effect on
cell-cycle regulation. Regulates the circadian clock by repressing
CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2.
{ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Binds DNA as a homotetramer. Interacts with AXIN1.
Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By
similarity). Interacts with histone acetyltransferases EP300 and
methyltransferases HRMT1L2 and CARM1, and recruits them to
promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part
of the TFIID complex. Interacts with ING4; this interaction may be
indirect. Found in a complex with CABLES1 and TP73. Interacts with
HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. Interacts with
USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8;
leading to recruit histone H1 and prevent transactivation activity
(By similarity). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1,
STK11/LKB1, UHRF2 and E4F1. Interacts with YWHAZ; the interaction
enhances TP53 transcriptional activity. Phosphorylation of YWHAZ
inhibits this interaction. Interacts (via DNA-binding domain) with
MAML1 (via N-terminus). Interacts with MKRN1. Interacts with PML
(via C-terminus). Interacts with MDM2; leading to ubiquitination
and proteasomal degradation of TP53. Directly interacts with
FBXO42; leading to ubiquitination and degradation of TP53.
Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase
PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent
inhibition of cell proliferation. Interacts with PPP2R2A.
Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when
monomethylated at Lys-375) 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}.
-!- 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 (By
similarity). 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. Phosphorylated on Thr-18 by VRK1, which may prevent
the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in
response to DNA damage, which prevents ubiquitination by MDM2.
Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen
species (ROS), promoting p53/TP53-mediated apoptosis.
Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to
DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-46 by
HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required
for acetylation by CREBBP. Phosphorylated on Ser-385 following UV
but not gamma irradiation. Phosphorylated on Ser-15 upon
ultraviolet irradiation; which is enhanced by interaction with
BANP. Stabilized by CDK5-mediated phosphorylation in response to
genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46,
leading to accumulation of p53/TP53, particularly in the nucleus,
thus inducing the transactivation of p53/TP53 target genes.
Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress.
Phosphorylated at Ser-385 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-284 and Lys-285, 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 (By similarity). Ubiquitination and subsequent
proteasomal degradation is negatively regulated by CCAR2 (By
similarity). {ECO:0000250|UniProtKB:P02340,
ECO:0000250|UniProtKB:P04637}.
-!- PTM: Monomethylated at Lys-365 by SETD7, leading to stabilization
and increased transcriptional activation. Monomethylated at Lys-
363 by SMYD2, leading to decreased DNA-binding activity and
subsequent transcriptional regulation activity. Lys-365
monomethylation prevents interaction with SMYD2 and subsequent
monomethylation at Lys-363. Dimethylated at Lys-366 by EHMT1 and
EHMT2. Monomethylated at Lys-375 by KMT5A, promoting interaction
with L3MBTL1 and leading to repress transcriptional activity.
Demethylation of dimethylated Lys-363 by KDM1A prevents
interaction with TP53BP1 and represses TP53-mediated
transcriptional activation (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-379 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; D26608; BAA05653.1; -; mRNA.
EMBL; D16460; BAA03927.1; -; mRNA.
RefSeq; NP_001009294.1; NM_001009294.1.
ProteinModelPortal; P41685; -.
SMR; P41685; -.
STRING; 9685.ENSFCAP00000008925; -.
Ensembl; ENSFCAT00000009625; ENSFCAP00000008925; ENSFCAG00000009623.
GeneID; 493847; -.
KEGG; fca:493847; -.
CTD; 7157; -.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
GeneTree; ENSGT00390000015092; -.
HOGENOM; HOG000039957; -.
HOVERGEN; HBG005201; -.
InParanoid; P41685; -.
KO; K04451; -.
OMA; PATSWPL; -.
OrthoDB; EOG091G0XY5; -.
TreeFam; TF106101; -.
Proteomes; UP000011712; Chromosome E1.
Bgee; ENSFCAG00000009623; -.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005657; C:replication fork; IBA:GO_Central.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
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:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
GO; GO:0002039; F:p53 binding; IBA:GO_Central.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000990; F:transcription factor activity, core RNA polymerase binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IEA:Ensembl.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IBA:GO_Central.
GO; GO:0031497; P:chromatin assembly; IEA:Ensembl.
GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
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:0006983; P:ER overload response; IEA:Ensembl.
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:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0051974; P:negative regulation of telomerase activity; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
GO; GO:0090403; P:oxidative stress-induced premature senescence; IEA:Ensembl.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:0031065; P:positive regulation of histone deacetylation; IBA:GO_Central.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032461; P:positive regulation of protein oligomerization; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0008104; P:protein localization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IBA:GO_Central.
GO; GO:0010165; P:response to X-ray; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:Ensembl.
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.
2: Evidence at transcript 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 1 386 Cellular tumor antigen p53.
/FTId=PRO_0000185701.
DNA_BIND 94 285 {ECO:0000250}.
REGION 1 313 Interaction with CCAR2.
{ECO:0000250|UniProtKB:P04637}.
REGION 1 44 Transcription activation (acidic).
REGION 63 102 Interaction with WWOX. {ECO:0000250}.
REGION 92 363 Interaction with HIPK1. {ECO:0000250}.
REGION 92 293 Required for interaction with ZNF385A.
{ECO:0000250}.
REGION 105 229 Required for interaction with FBXO42.
{ECO:0000250}.
REGION 108 285 Interaction with AXIN1. {ECO:0000250}.
REGION 249 287 Interaction with E4F1. {ECO:0000250}.
REGION 266 273 Interaction with DNA. {ECO:0000250}.
REGION 312 353 Interaction with HIPK2. {ECO:0000250}.
REGION 318 349 Oligomerization.
REGION 352 356 Interaction with USP7. {ECO:0000250}.
REGION 361 380 Basic (repression of DNA-binding).
MOTIF 298 314 Bipartite nuclear localization signal.
{ECO:0000250}.
MOTIF 332 343 Nuclear export signal. {ECO:0000250}.
MOTIF 363 365 [KR]-[STA]-K motif.
METAL 168 168 Zinc. {ECO:0000250}.
METAL 171 171 Zinc. {ECO:0000250}.
METAL 231 231 Zinc. {ECO:0000250}.
METAL 235 235 Zinc. {ECO:0000250}.
SITE 112 112 Interaction with DNA. {ECO:0000250}.
MOD_RES 15 15 Phosphoserine; by CDK5, PRPK, AMPK, NUAK1
and ATM. {ECO:0000250|UniProtKB:P04637}.
MOD_RES 18 18 Phosphothreonine; by CK1, VRK1 and VRK2.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 20 20 Phosphoserine; by CHEK2, CK1 and PLK3.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 33 33 Phosphoserine; by CDK5 and CDK7.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 37 37 Phosphoserine; by MAPKAPK5.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 46 46 Phosphoserine; by CDK5, DYRK2, HIPK2 and
PKC/PRKCG.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 112 112 N6-acetyllysine; by KAT6A.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 262 262 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 277 277 Phosphothreonine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 298 298 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 314 314 N6-acetyllysine.
{ECO:0000250|UniProtKB:P02340}.
MOD_RES 363 363 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 363 363 N6-methyllysine; by SMYD2; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 365 365 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 366 366 N6,N6-dimethyllysine; by EHMT1 and EHMT2;
alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 366 366 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 374 374 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 375 375 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 375 375 N6-acetyllysine; by KAT6A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 375 375 N6-methyllysine; by KMT5A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 385 385 Phosphoserine; by CK2, CDK2 and NUAK1.
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 284 284 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 379 379 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CONFLICT 285 285 K -> R (in Ref. 2; BAA03927).
{ECO:0000305}.
SEQUENCE 386 AA; 42692 MW; D08B43BA1BC8EB78 CRC64;
MQEPPLELTI EPPLSQETFS ELWNLLPENN VLSSELSSAM NELPLSEDVA NWLDEAPDDA
SGMSAVPAPA APAPATPAPA ISWPLSSFVP SQKTYPGAYG FHLGFLQSGT AKSVTCTYSP
PLNKLFCQLA KTCPVQLWVR SPPPPGTCVR AMAIYKKSEF MTEVVRRCPH HERCPDSSDG
LAPPQHLIRV EGNLHAKYLD DRNTFRHSVV VPYEPPEVGS DCTTIHYNFM CNSSCMGGMN
RRPIITIITL EDSNGKLLGR NSFEVRVCAC PGRDRRTEEE NFRKKGEPCP EPPPGSTKRA
LPPSTSSTPP QKKKPLDGEY FTLQIRGRER FEMFRELNEA LELKDAQSGK EPGGSRAHSS
HLKAKKGQST SRHKKPMLKR EGLDSD


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E0928Rb ELISA Cellular tumor antigen p53,Oryctolagus cuniculus,Rabbit,TP53,Tumor suppressor p53 96T
E0928m ELISA kit Cellular tumor antigen p53,Mouse,Mus musculus,P53,Tp53,Trp53,Tumor suppressor p53 96T
U0928Rb CLIA Cellular tumor antigen p53,Oryctolagus cuniculus,Rabbit,TP53,Tumor suppressor p53 96T
E0928Rb ELISA kit Cellular tumor antigen p53,Oryctolagus cuniculus,Rabbit,TP53,Tumor suppressor p53 96T
E0928m ELISA Cellular tumor antigen p53,Mouse,Mus musculus,P53,Tp53,Trp53,Tumor suppressor p53 96T
18-661-15115 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 mg
18-662-20095 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 ml
18-003-42884 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 mg Protein A
E0928c ELISA kit Cellular tumor antigen p53,Chicken,Gallus gallus,TP53,Tumor suppressor p53 96T
U0928c CLIA Cellular tumor antigen p53,Chicken,Gallus gallus,TP53,Tumor suppressor p53 96T
E0928c ELISA Cellular tumor antigen p53,Chicken,Gallus gallus,TP53,Tumor suppressor p53 96T
E0928c ELISA Canis familiaris,Canis lupus familiaris,Cellular tumor antigen p53,Dog,P53,TP53,Tumor suppressor p53 96T


 

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