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Q9JJP2 (P73_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor protein p73
Alternative name(s):
p53-like transcription factor
p53-related protein
Gene names
Name:Tp73
Synonyms:P73, Trp73
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Ref.6 Ref.7 UniProtKB O15350

Cofactor

Binds 1 zinc ion per subunit By similarity. UniProtKB O15350

Subunit structure

Found in a complex with p53/TP53 and CABLES1. The C-terminal oligomerization domain binds to the ABL1 tyrosine kinase SH3 domain. Interacts with HECW2, HIPK2, RANBP9 and WWOX By similarity. Interacts (via SAM domain) with FBXO45 (via B30.2/SPRY domain) By similarity. Interacts with YAP1 (phosphorylated form) By similarity. Interacts with HCK (via SH3 domain); this inhibits TP73 activity and degradation By similarity. UniProtKB O15350

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Accumulates in the nucleus in response to DNA damage. Ref.8

Tissue specificity

Found in striatal neurons of mutant huntingtin (htt) transgenic mice (at protein level). Isoform 1 is expressed in the nasal epithelium, the vomeronasal organ, the hippocampus and the hypothalamus. Ref.1 Ref.9

Domain

Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL1 tyrosine kinase SH3 domain By similarity. UniProtKB O15350

The WW-binding motif mediates interaction with WWOX By similarity. UniProtKB O15350

Post-translational modification

Sumoylated on Lys-622, which potentiates proteasomal degradation but does not affect transcriptional activity By similarity.

Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function By similarity. Higher levels of phosphorylation seen in striatal neurons of. mutant huntingtin (htt) transgenic mice.

Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome By similarity.

Disruption phenotype

Mice lacking Tp73 display a runting phenotype and high rates of mortality due to massive gastrointestinal hemorrhages or intracranial bleeding. The gastrointestinal tract suffers loss of enterocytes and excessive mucosecretions in the duodenum, ileum and cecum. Survivors exhibit hippocampal dysgenesis, hydrocephalus, chronic infections and inflammation, as well as abnormalities in pheromone sensory pathways. Ref.1

Miscellaneous

Activated and stabilized by interaction with RANBP9 By similarity. UniProtKB O15350

Sequence similarities

Belongs to the p53 family. UniProtKB O15350

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

The sequence CAM18775.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DiseaseTumor suppressor
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell cycle arrest

Inferred from direct assay PubMed 16044147. Source: MGI

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 16044147. Source: MGI

cellular response to UV

Inferred from Biological aspect of Ancestor. Source: RefGenome

cerebrospinal fluid secretion

Inferred from mutant phenotype Ref.1. Source: MGI

digestive tract morphogenesis

Inferred from mutant phenotype Ref.1. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 15525772. Source: MGI

hippocampus development

Inferred from mutant phenotype Ref.1. Source: MGI

inflammatory response

Inferred from mutant phenotype Ref.1. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic G1 DNA damage checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of JUN kinase activity

Inferred from direct assay PubMed 15483136. Source: MGI

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 10894779PubMed 12427836. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron development

Inferred from mutant phenotype PubMed 12427836. Source: MGI

positive regulation of apoptotic signaling pathway

Inferred from genetic interaction PubMed 16044147. Source: MGI

positive regulation of cell size

Inferred from mutant phenotype PubMed 12427836PubMed 15483136. Source: MGI

positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from genetic interaction PubMed 15983387. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16044147. Source: MGI

post-embryonic development

Inferred from mutant phenotype Ref.1PubMed 15483136. Source: MGI

protein tetramerization

Inferred from electronic annotation. Source: InterPro

regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 15483136. Source: MGI

release of cytochrome c from mitochondria

Inferred from direct assay PubMed 15483136. Source: MGI

response to X-ray

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to gamma radiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 14555234PubMed 15483136PubMed 15525772. Source: MGI

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Inferred from direct assay PubMed 16363065. Source: MGI

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

damaged DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

double-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from physical interaction PubMed 10894779. Source: MGI

protein binding

Inferred from physical interaction PubMed 11278685. Source: IntAct

sequence-specific DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 16044147. Source: MGI

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Yap1P469382EBI-1770138,EBI-1211949

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.3 (identifier: Q9JJP2-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.1 Ref.3 Ref.5 (identifier: Q9JJP2-2)

Also known as: dN-Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT
Note: Produced by alternative promoter usage.
Isoform 3 Ref.3 (identifier: Q9JJP2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT
     489-493: SFLTG → RTLGL
     494-631: Missing.
Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.
Isoform 4 Ref.2 (identifier: Q9JJP2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT
     394-489: Missing.
Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Tumor protein p73
PRO_0000370211

Regions

Domain479 – 54567SAM
Region1 – 4343Transactivation By similarity UniProtKB O15350
Region123 – 302180DNA-binding By similarity UniProtKB O15350
Region337 – 37842Oligomerization Potential
Region337 – 37236Interaction with HIPK2 By similarity UniProtKB O15350
Motif477 – 4815WW-binding UniProtKB O15350
Compositional bias5 – 106Poly-Ser
Compositional bias383 – 3886Poly-Gln

Sites

Metal binding1861Zinc By similarity UniProtKB O15350
Metal binding1891Zinc By similarity UniProtKB O15350
Metal binding2501Zinc By similarity UniProtKB O15350
Metal binding2541Zinc By similarity UniProtKB O15350

Amino acid modifications

Modified residue241Phosphothreonine; by PLK1 By similarity
Modified residue251Phosphotyrosine; by SRC and HCK By similarity
Modified residue911Phosphotyrosine; by ABL1 By similarity
Cross-link622Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity UniProtKB O15350

Natural variations

Alternative sequence1 – 5454MAQTS…HLQGM → MLYVGDPMRHLAT in isoform 2, isoform 3 and isoform 4. Ref.1 Ref.2 Ref.3 Ref.5
VSP_053081
Alternative sequence394 – 48996Missing in isoform 4. Ref.2
VSP_053082
Alternative sequence489 – 4935SFLTG → RTLGL in isoform 3. Ref.3
VSP_053083
Alternative sequence494 – 631138Missing in isoform 3. Ref.3
VSP_053084

Experimental info

Sequence conflict1181H → D in BAB30732. Ref.2
Sequence conflict1271S → G in BAE24089. Ref.2
Sequence conflict2541C → S in AAD32213. Ref.5
Sequence conflict352 – 3532RG → SAS in AAD32213. Ref.5
Sequence conflict3761P → H in AAD32213. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E364D566A90CBF1D

FASTA63169,096
        10         20         30         40         50         60 
MAQTSSSSSS TFEHLWSSLE PDSTYFDLPQ PSQGTSEASG SEESNMDVFH LQGMAQFNLL 

        70         80         90        100        110        120 
SSAMDQMGSR AAPASPYTPE HAASAPTHSP YAQPSSTFDT MSPAPVIPSN TDYPGPHHFE 

       130        140        150        160        170        180 
VTFQQSSTAK SATWTYSPLL KKLYCQIAKT CPIQIKVSTP PPPGTAIRAM PVYKKAEHVT 

       190        200        210        220        230        240 
DIVKRCPNHE LGRDFNEGQS APASHLIRVE GNNLAQYVDD PVTGRQSVVV PYEPPQVGTE 

       250        260        270        280        290        300 
FTTILYNFMC NSSCVGGMNR RPILVIITLE TRDGQVLGRR SFEGRICACP GRDRKADEDH 

       310        320        330        340        350        360 
YREQQALNES TTKNGAASKR AFKQSPPAIP ALGTNVKKRR HGDEDMFYMH VRGRENFEIL 

       370        380        390        400        410        420 
MKVKESLELM ELVPQPLVDS YRQQQQQQLL QRPSHLQPPS YGPVLSPMNK VHGGVNKLPS 

       430        440        450        460        470        480 
VNQLVGQPPP HSSAAGPNLG PMGSGMLNSH GHSMPANGEM NGGHSSQTMV SGSHCTPPPP 

       490        500        510        520        530        540 
YHADPSLVSF LTGLGCPNCI ECFTSQGLQS IYHLQNLTIE DLGALKVPDQ YRMTIWRGLQ 

       550        560        570        580        590        600 
DLKQSHDCGQ QLLRSSSNAA TISIGGSGEL QRQRVMEAVH FRVRHTITIP NRGGAGAVTG 

       610        620        630 
PDEWADFGFD LPDCKSRKQP IKEEFTETES H 

« Hide

Isoform 2 (dN-Alpha) [UniParc].

Checksum: 8580C7EFA21B5797
Show »

FASTA59064,725
Isoform 3 [UniParc].

Checksum: 13C8757F5A4A5FFC
Show »

FASTA45249,392
Isoform 4 [UniParc].

Checksum: FA7D89986822E491
Show »

FASTA49455,025

References

« Hide 'large scale' references
[1]"p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours."
Yang A., Walker N., Bronson R., Kaghad M., Oosterwegel M., Bonnin J., Vagner C., Bonnet H., Dikkes P., Sharpe A., McKeon F., Caput D.
Nature 404:99-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-631 (ISOFORM 1/2).
Strain: C57BL/6J.
Tissue: Egg and Head.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Fetal brain.
[6]"Mouse p73 gene maps to the distal part of chromosome 4 and might be involved in the progression of gamma-radiation-induced T-cell lymphomas."
Herranz M., Santos J., Salido E., Fernandez-Piqueras J., Serrano M.
Cancer Res. 59:2068-2071(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-631 (ISOFORMS 1/2), FUNCTION.
Strain: 129/Sv.
[7]"p63 and p73 are required for p53-dependent apoptosis in response to DNA damage."
Flores E.R., Tsai K.Y., Crowley D., Sengupta S., Yang A., McKeon F., Jacks T.
Nature 416:560-564(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"p73alpha is a candidate effector in the p53 independent apoptosis pathway of cisplatin damaged primary murine colonocytes."
Oniscu A., Sphyris N., Morris R.G., Bader S., Harrison D.J.
J. Clin. Pathol. 57:492-498(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Transcriptional repression induces a slowly progressive atypical neuronal death associated with changes of YAP isoforms and p73."
Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y., Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M., Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.
J. Cell Biol. 172:589-604(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y19234 mRNA. Translation: CAB81953.1.
Y19235 mRNA. Translation: CAB81954.1.
AK017412 mRNA. Translation: BAB30732.1.
AK139633 mRNA. Translation: BAE24089.1.
AL806525 Genomic DNA. Translation: CAM18773.1.
AL806525 Genomic DNA. Translation: CAM18774.1.
AL806525 Genomic DNA. Translation: CAM18775.1. Different initiation.
CH466594 Genomic DNA. Translation: EDL14957.1.
BC066045 mRNA. Translation: AAH66045.1.
AF138873 Genomic DNA. Translation: AAD32213.1.
CCDSCCDS51396.1. [Q9JJP2-4]
CCDS51397.1. [Q9JJP2-2]
RefSeqNP_001119802.1. NM_001126330.1. [Q9JJP2-2]
NP_001119803.1. NM_001126331.1. [Q9JJP2-4]
NP_035772.2. NM_011642.3.
UniGeneMm.78015.

3D structure databases

ProteinModelPortalQ9JJP2.
SMRQ9JJP2. Positions 107-381, 486-542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204326. 5 interactions.
DIPDIP-41942N.
IntActQ9JJP2. 2 interactions.
MINTMINT-3388880.

PTM databases

PhosphoSiteQ9JJP2.

Proteomic databases

PRIDEQ9JJP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097762; ENSMUSP00000095368; ENSMUSG00000029026. [Q9JJP2-4]
ENSMUST00000105643; ENSMUSP00000101268; ENSMUSG00000029026. [Q9JJP2-3]
ENSMUST00000133533; ENSMUSP00000114418; ENSMUSG00000029026. [Q9JJP2-2]
GeneID22062.
KEGGmmu:22062.
UCSCuc008wbg.2. mouse. [Q9JJP2-2]
uc008wbh.2. mouse. [Q9JJP2-1]
uc012dqi.1. mouse. [Q9JJP2-4]

Organism-specific databases

CTD22062.
MGIMGI:1336991. Trp73.

Phylogenomic databases

eggNOGNOG80479.
GeneTreeENSGT00390000015092.
InParanoidB1AX90.
KOK10148.
OrthoDBEOG7JQBNW.
PhylomeDBQ9JJP2.
TreeFamTF106101.

Gene expression databases

ArrayExpressQ9JJP2.
BgeeQ9JJP2.
GenevestigatorQ9JJP2.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR002117. p53_tumour_suppressor.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
PANTHERPTHR11447. PTHR11447. 1 hit.
PfamPF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR00386. P53SUPPRESSR.
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301868.
PROQ9JJP2.
SOURCESearch...

Entry information

Entry nameP73_MOUSE
AccessionPrimary (citable) accession number: Q9JJP2
Secondary accession number(s): B1AX89 expand/collapse secondary AC list , B1AX90, Q3UT91, Q9CU77, Q9JJP1, Q9WUJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot