Cellular tumor antigen p53 - Xenopus laevis (African clawed frog)

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P07193 (P53_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cellular tumor antigen p53

Alternative name(s):
Tumor suppressor p53

Gene names

Name:

tp53

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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 By similarity.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Binds DNA as a homotetramer By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the p53 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Disease	Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein tetramerization Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 363

363

Cellular tumor antigen p53

PRO_0000185726

Regions

DNA binding

76 – 267

192

By similarity

Region

1 – 29

Transcription activation (acidic)

Region

248 – 255

Interaction with DNA By similarity

Region

300 – 331

Oligomerization

Region

344 – 356

Basic (repression of DNA-binding)

Motif

275 – 292

Bipartite nuclear localization signal By similarity

Motif

314 – 325

Nuclear export signal By similarity

Sites

Metal binding

150

Zinc By similarity

Metal binding

153

Zinc By similarity

Metal binding

213

Zinc By similarity

Metal binding

217

Zinc By similarity

Site

Interaction with DNA By similarity

Experimental info

Sequence conflict

T → S in CAA54672. Ref.2

Sequence conflict

Missing in CAA54672. Ref.2

Sequence conflict

296

Missing in CAA54672. Ref.2

Sequence conflict

296

Missing in AAC60746. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P07193 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: CE1F3E58F020D74D
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FASTA

363

40,693

        10         20         30         40         50         60 
MEPSSETGMD PPLSQETFED LWSLLPDPLQ TVTCRLDNLS EFPDYPLAAD MTVLQEGLMG 

        70         80         90        100        110        120 
NAVPTVTSCA VPSTDDYAGK YGLQLDFQQN GTAKSVTCTY SPELNKLFCQ LAKTCPLLVR 

       130        140        150        160        170        180 
VESPPPRGSI LRATAVYKKS EHVAEVVKRC PHHERSVEPG EDAAPPSHLM RVEGNLQAYY 

       190        200        210        220        230        240 
MEDVNSGRHS VCVPYEGPQV GTECTTVLYN YMCNSSCMGG MNRRPILTII TLETPQGLLL 

       250        260        270        280        290        300 
GRRCFEVRVC ACPGRDRRTE EDNYTKKRGL KPSGKRELAH PPSSEPPLPK KRLVVVDDDE 

       310        320        330        340        350        360 
EIFTLRIKGR SRYEMIKKLN DALELQESLD QQKVTIKCRK CRDEIKPKKG KKLLVKDEQP 


DSE

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References

[1]	"Cloning and characterization of a cDNA from Xenopus laevis coding for a protein homologous to human and murine p53." Soussi T., de Fromentel C.C., Mechali M., May P., Kress M. Oncogene 1:71-78(1987) [PubMed: 2830576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Overexpression of wild-type p53 interferes with normal development in Xenopus laevis embryos." Hoever M., Clement J.H., Wedlich D., Montenarh M., Knoechel W. Oncogene 9:109-120(1994) [PubMed: 8302570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M36962 mRNA. Translation: AAA49923.1. X05191 mRNA. Translation: CAA28821.1. X77546 mRNA. Translation: CAA54672.1. S68353 mRNA. Translation: AAC60746.1.
PIR	A29376.
RefSeq	NP_001081567.1. NM_001088098.1.
UniGene	Xl.394.
3D structure databases
ProteinModelPortal	P07193.
SMR	P07193. Positions 68-267, 301-328.
ModBase	Search...
Protein-protein interaction databases
IntAct	P07193. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397926.
KEGG	xla:397926.
Organism-specific databases
CTD	7157.
Xenbase	XB-GENE-6252168. tp53.
Phylogenomic databases
HOVERGEN	HBG005201.
Family and domain databases
InterPro	IPR008967. p53-like_TF_DNA-bd. IPR012346. p53/RUNT-type_TF_DNA-bd. IPR011615. p53_DNA-bd. IPR010991. p53_tetrameristn. IPR013872. p53_transactivation_domain. IPR002117. p53_tumour_suppressor. [Graphical view]
Gene3D	G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit. G3DSA:4.10.170.10. p53_tetrameristn. 1 hit.
KO	K04451.
PANTHER	PTHR11447. Trp53. 1 hit.
Pfam	PF00870. P53. 1 hit. PF08563. P53_TAD. 1 hit. PF07710. P53_tetramer. 1 hit. [Graphical view]
PRINTS	PR00386. P53SUPPRESSR.
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit. SSF47719. p53_tetrameristn. 1 hit.
PROSITE	PS00348. P53. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P53_XENLA

Accession

Primary (citable) accession number: P07193

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents