Q9JJP2 (P73_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor protein p73

Alternative name(s):
p53-like transcription factor
p53-related protein

Gene names

Name:	Tp73
Synonyms:	P73, Trp73

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ubiquitinated; 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 process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing
Disease	Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB DNA 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. 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 hippocampus development Inferred from mutant phenotype Ref.1. Source: MGI inflammatory response Inferred from mutant phenotype Ref.1. Source: MGI mitotic cell cycle G1/S transition DNA damage checkpoint Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of JUN kinase activity Inferred from direct assay. Source: MGI negative regulation of neuron apoptosis Inferred from direct assay. 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. Source: MGI positive regulation of cell size Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB post-embryonic development Inferred from mutant phenotype Ref.1. Source: MGI protein tetramerization Inferred from electronic annotation. Source: InterPro release of cytochrome c from mitochondria Inferred from direct assay. 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	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. Source: MGI sequence-specific DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: MGI
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 631	631	Tumor protein p73		PRO_0000370211
Regions
	Domain	479 – 545	67	SAM
	Region	1 – 43	43	Transactivation By similarity UniProtKB O15350
	Region	123 – 302	180	DNA-binding By similarity UniProtKB O15350
	Region	337 – 378	42	Oligomerization Potential
	Region	337 – 372	36	Interaction with HIPK2 By similarity UniProtKB O15350
	Motif	477 – 481	5	WW-binding UniProtKB O15350
	Compositional bias	5 – 10	6	Poly-Ser
	Compositional bias	383 – 388	6	Poly-Gln
Sites
	Metal binding	186	1	Zinc By similarity UniProtKB O15350
	Metal binding	189	1	Zinc By similarity UniProtKB O15350
	Metal binding	250	1	Zinc By similarity UniProtKB O15350
	Metal binding	254	1	Zinc By similarity UniProtKB O15350
Amino acid modifications
	Modified residue	24	1	Phosphothreonine; by PLK1 By similarity
	Modified residue	25	1	Phosphotyrosine; by SRC and HCK By similarity
	Modified residue	91	1	Phosphotyrosine; by ABL1 By similarity
	Cross-link	622		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity UniProtKB O15350
Natural variations
	Alternative sequence	1 – 54	54	MAQTS…HLQGM → MLYVGDPMRHLAT in isoform 2, isoform 3 and isoform 4. Ref.1 Ref.2 Ref.3 Ref.5		VSP_053081
	Alternative sequence	394 – 489	96	Missing in isoform 4. Ref.2		VSP_053082
	Alternative sequence	489 – 493	5	SFLTG → RTLGL in isoform 3. Ref.3		VSP_053083
	Alternative sequence	494 – 631	138	Missing in isoform 3. Ref.3		VSP_053084
Experimental info
	Sequence conflict	118	1	H → D in BAB30732. Ref.2
	Sequence conflict	127	1	S → G in BAE24089. Ref.2
	Sequence conflict	254	1	C → S in AAD32213. Ref.5
	Sequence conflict	352 – 353	2	RG → SAS in AAD32213. Ref.5
	Sequence conflict	376	1	P → H in AAD32213. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E364D566A90CBF1D	FASTA	631	69,096
	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
	Isoform 2 (dN-Alpha) [UniParc]. Checksum: 8580C7EFA21B5797	FASTA	590	64,725
	10 20 30 40 50 60 MLYVGDPMRH LATAQFNLLS SAMDQMGSRA APASPYTPEH AASAPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD IVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLAQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILVIITLET RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNEST TKNGAASKRA FKQSPPAIPA LGTNVKKRRH 310 320 330 340 350 360 GDEDMFYMHV RGRENFEILM KVKESLELME LVPQPLVDSY RQQQQQQLLQ RPSHLQPPSY 370 380 390 400 410 420 GPVLSPMNKV HGGVNKLPSV NQLVGQPPPH SSAAGPNLGP MGSGMLNSHG HSMPANGEMN 430 440 450 460 470 480 GGHSSQTMVS GSHCTPPPPY HADPSLVSFL TGLGCPNCIE CFTSQGLQSI YHLQNLTIED 490 500 510 520 530 540 LGALKVPDQY RMTIWRGLQD LKQSHDCGQQ LLRSSSNAAT ISIGGSGELQ RQRVMEAVHF 550 560 570 580 590 RVRHTITIPN RGGAGAVTGP DEWADFGFDL PDCKSRKQPI KEEFTETESH
	Isoform 3 [UniParc]. Checksum: 13C8757F5A4A5FFC	FASTA	452	49,392
	10 20 30 40 50 60 MLYVGDPMRH LATAQFNLLS SAMDQMGSRA APASPYTPEH AASAPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD IVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLAQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILVIITLET RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNEST TKNGAASKRA FKQSPPAIPA LGTNVKKRRH 310 320 330 340 350 360 GDEDMFYMHV RGRENFEILM KVKESLELME LVPQPLVDSY RQQQQQQLLQ RPSHLQPPSY 370 380 390 400 410 420 GPVLSPMNKV HGGVNKLPSV NQLVGQPPPH SSAAGPNLGP MGSGMLNSHG HSMPANGEMN 430 440 450 GGHSSQTMVS GSHCTPPPPY HADPSLVRTL GL
	Isoform 4 [UniParc]. Checksum: FA7D89986822E491	FASTA	494	55,025
	10 20 30 40 50 60 MLYVGDPMRH LATAQFNLLS SAMDQMGSRA APASPYTPEH AASAPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD IVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLAQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILVIITLET RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNEST TKNGAASKRA FKQSPPAIPA LGTNVKKRRH 310 320 330 340 350 360 GDEDMFYMHV RGRENFEILM KVKESLELME LVPQPLVDSY RQQQQQQLLQ RPFLTGLGCP 370 380 390 400 410 420 NCIECFTSQG LQSIYHLQNL TIEDLGALKV PDQYRMTIWR GLQDLKQSHD CGQQLLRSSS 430 440 450 460 470 480 NAATISIGGS GELQRQRVME AVHFRVRHTI TIPNRGGAGA VTGPDEWADF GFDLPDCKSR 490 KQPIKEEFTE TESH

References

	« Hide 'large scale' referencesShow '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: 10716451] [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. , 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: 16141072] [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. , 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: 19468303] [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: 15489334] [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: 10232589] [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: 11932750] [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: 15113856] [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: 16461361] [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.
IPI	IPI00648269. IPI00648744. IPI00652590. IPI00896107.
RefSeq	NP_001119802.1. NM_001126330.1. NP_001119803.1. NM_001126331.1. NP_035772.2. NM_011642.3.
UniGene	Mm.78015.
3D structure databases
HSSP	HSSP built from PDB template 1DXS based on UniProtKB O15350.
ProteinModelPortal	Q9JJP2.
SMR	Q9JJP2. Positions 104-307, 348-381, 486-542.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9JJP2. 2 interactions.
MINT	MINT-3388880.
STRING	Q9JJP2.
PTM databases
PhosphoSite	Q9JJP2.
Proteomic databases
PRIDE	Q9JJP2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030892; ENSMUSP00000030892; ENSMUSG00000029026. ENSMUST00000097762; ENSMUSP00000095368; ENSMUSG00000029026. ENSMUST00000105643; ENSMUSP00000101268; ENSMUSG00000029026. ENSMUST00000105644; ENSMUSP00000101269; ENSMUSG00000029026. ENSMUST00000133533; ENSMUSP00000114418; ENSMUSG00000029026.
GeneID	22062.
KEGG	mmu:22062.
UCSC	uc008wbg.2. mouse. uc008wbh.2. mouse. uc012dqi.1. mouse.
Organism-specific databases
CTD	22062.
MGI	MGI:1336991. Trp73.
Phylogenomic databases
eggNOG	roNOG10897.
GeneTree	ENSGT00390000015092.
InParanoid	Q9JJP2.
OrthoDB	EOG4P5K8S.
PhylomeDB	Q9JJP2.
Gene expression databases
ArrayExpress	Q9JJP2.
Bgee	Q9JJP2.
Genevestigator	Q9JJP2.
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. IPR002117. p53_tumour_suppressor. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. [Graphical view]
Gene3D	G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit. G3DSA:4.10.170.10. p53_tetrameristn. 1 hit. G3DSA:1.10.150.50. SAM_type. 1 hit.
KO	K10148.
PANTHER	PTHR11447. Trp53. 1 hit.
Pfam	PF00870. P53. 1 hit. PF07710. P53_tetramer. 1 hit. PF07647. SAM_2. 1 hit. [Graphical view]
PRINTS	PR00386. P53SUPPRESSR.
SMART	SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit. SSF47719. p53_tetrameristn. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS00348. P53. 1 hit. PS50105. SAM_DOMAIN. False negative. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

P73_MOUSE

Accession

Primary (citable) accession number: Q9JJP2
Secondary accession number(s): B1AX89 , B1AX90, Q3UT91, Q9CU77, Q9JJP1, Q9WUJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program