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Cellular tumor antigen p53 (Fragment)

 Q1MSX0_HUMAN            Unreviewed;       382 AA.
Q1MSX0;
30-MAY-2006, integrated into UniProtKB/TrEMBL.
30-MAY-2006, sequence version 1.
23-MAY-2018, entry version 86.
RecName: Full=Cellular tumor antigen p53 {ECO:0000256|RuleBase:RU003304};
Flags: Fragment;
Name=TP53 {ECO:0000313|EMBL:CAJ28922.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:CAJ28922.1};
[1] {ECO:0000313|EMBL:CAJ28922.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Classical Hodgkin Lymphoma {ECO:0000313|EMBL:CAJ28922.1};
PubMed=17065008; DOI=10.1080/10428190600667721;
Feuerborn A., Moritz C., von Bonin F., Dobbelstein M., Tromper M.,
Strzenhofecker B., Kube D.;
"Dysfunctional p53 deletion mutants in cell lines derived from
Hodgkin's lymphoma.";
Leuk. Lymphoma 47:1932-1940(2006).
[2] {ECO:0000313|EMBL:ABL09846.1}
NUCLEOTIDE SEQUENCE.
Janz M., Stuhmer T., Vassilev L.T., Bargou R.C.;
"Pharmacologic activation of p53-dependent and p53-independent
apoptotic pathways in Hodgkin/Reed-Sternberg cells.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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. {ECO:0000256|RuleBase:RU003304}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|RuleBase:RU003304};
Note=Binds 1 zinc ion per subunit.
{ECO:0000256|RuleBase:RU003304};
-!- SUBUNIT: Binds DNA as a homotetramer.
{ECO:0000256|RuleBase:RU003304}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}.
Nucleus {ECO:0000256|RuleBase:RU003304}.
-!- SIMILARITY: Belongs to the p53 family.
{ECO:0000256|RuleBase:RU003401}.
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EMBL; EF101867; ABL09846.1; -; mRNA.
EMBL; AM076970; CAJ28922.1; -; mRNA.
UniGene; Hs.437460; -.
UniGene; Hs.740601; -.
PeptideAtlas; Q1MSX0; -.
PRIDE; Q1MSX0; -.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
HOVERGEN; HBG005201; -.
ChiTaRS; TP53; human.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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_sf.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR036674; p53_tetramer_sf.
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;
Activator {ECO:0000256|RuleBase:RU003304};
Apoptosis {ECO:0000256|RuleBase:RU003304};
Cell cycle {ECO:0000256|RuleBase:RU003304};
Cytoplasm {ECO:0000256|RuleBase:RU003304};
DNA-binding {ECO:0000256|RuleBase:RU003304};
Metal-binding {ECO:0000256|RuleBase:RU003304};
Nucleus {ECO:0000256|RuleBase:RU003304};
Phosphoprotein {ECO:0000256|RuleBase:RU003304};
Transcription {ECO:0000256|RuleBase:RU003304};
Transcription regulation {ECO:0000256|RuleBase:RU003304};
Zinc {ECO:0000256|RuleBase:RU003304}.
DOMAIN 5 29 P53_TAD. {ECO:0000259|Pfam:PF08563}.
DOMAIN 95 277 P53. {ECO:0000259|Pfam:PF00870}.
DOMAIN 308 346 P53_tetramer. {ECO:0000259|Pfam:PF07710}.
NON_TER 1 1 {ECO:0000313|EMBL:CAJ28922.1}.
NON_TER 382 382 {ECO:0000313|EMBL:CAJ28922.1}.
SEQUENCE 382 AA; 42627 MW; E6FFB57C3C77C206 CRC64;
MEEPQSDPSV EPPLSQETFS DLWKLLPENN VLSPLPSQAM DDLMLSPDDI EQWFTEDPGP
DEAPRMPEAA PRVAPAPAAP TPAAPAPAPS WPLSSSVPSQ KTYQGSYGFR LTCTYSPALN
KMFCQLAKTC PVQLWVDSTP PPGTRVRAMA IYKQSQHMTE VVRRCPHHER CSDSDGLAPP
QHLIRVEGNL RVEYLDDRNT FRHSVVVPYE PPEVGSDCTT IHYNYMCNSS CMGGMNRRPI
LTIITLEDSS GNLLGRNSFE VRVCACPGRD RRTEEENLRK KGEPHHELPP GSTKRALPNN
TSSSPQPKKK PLDGEYFTLQ IRGRERFEMF RELNEALELK DAQAGKEPGG SRAHSSHLKS
KKGQSTSRHK KLMFKTEGPD SD


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