Reviewed, UniProtKB/Swiss-Prot Q9QXM1 (JMY_MOUSE)

Names and origin

Protein names

Recommended name:
    Junction-mediating and -regulatory protein

Gene names

Name:

Jmy

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

Protein attributes

Sequence length	983 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. Ref.1 Ref.4
Subunit structure	Interacts with p300/EP300, the complex being recruited to activated p53/TP53. Interacts with TTC5. Ref.1 Ref.4
Subcellular location	NucleusProbable.
Tissue specificity	Widely expressed, except in testis where it is expressed at low level. Ref.1
Induction	Accumulates in DNA-damaged cells (at protein level). Ref.5
Post-translational modification	Ubiquitinated by MDM2, leading to its subsequent degradation by the proteasome. In case of DNA damage, the interaction with MDM2 is altered, preventing degradation and allowing interaction with p300/EP300 and its function in p53/TP53 stress response. Ref.5
Sequence similarities	Contains 1 WH2 domain.
Sequence caution	The sequence AAH69906.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	Actin-binding
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Ref.1 Inferred from direct assay. Source: MGI positive regulation of transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Ref.1 Inferred from direct assay. Source: MGI
Cellular component	nucleus Ref.1 Inferred by curator. Source: HGNC
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EP300	Q09472	6	EBI-866001,EBI-447295	From a different organism.
MDM2	Q00987	1	EBI-866001,EBI-389668	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9QXM1-1)

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 (identifier: Q9QXM1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     445-446: VY → FP
     447-983: Missing.

Isoform 3 (identifier: Q9QXM1-3)

Also known as: DeltaP;

The sequence of this isoform differs from the canonical sequence as follows:
     794-812: Missing.

Notes: Alters the p53/TP53 response.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 983	983	Junction-mediating and -regulatory protein		PRO_0000324612
Regions
	Domain	916 – 933	18	WH2
	Region	1 – 119	119	Interaction with p300/EP300
	Region	469 – 558	90	Interaction with p300/EP300
	Coiled coil	315 – 351	37	Potential
	Coiled coil	480 – 528	49	Potential
	Coiled coil	571 – 612	42	Potential
	Compositional bias	762 – 818	57	Pro-rich
Amino acid modifications
	Modified residue	64	1	Phosphothreonine Ref.6
	Modified residue	75	1	Phosphoserine Ref.6
	Modified residue	969	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	445 – 446	2	VY → FP in isoform 2.		VSP_032311
	Alternative sequence	447 – 983	537	Missing in isoform 2.		VSP_032312
	Alternative sequence	794 – 812	19	Missing in isoform 3.		VSP_032313
Experimental info
	Sequence conflict	54	1	Q → H in BAE24898. Ref.3
	Sequence conflict	63	1	G → V in AAH20052. Ref.2
	Sequence conflict	70	1	S → R in BAE24898. Ref.3
	Sequence conflict	153	1	I → T in AAH20052 and AAH90835. Ref.2
	Sequence conflict	153	1	I → T in BAE24898. Ref.3
	Sequence conflict	159	1	V → A in AAH20052 and AAH90835. Ref.2
	Sequence conflict	159	1	V → A in BAE24898. Ref.3
	Sequence conflict	189	1	M → I in AAH20052. Ref.2
	Sequence conflict	214	1	S → P in AAH20052 and AAH90835. Ref.2
	Sequence conflict	214	1	S → P in BAE24898. Ref.3
	Sequence conflict	331	1	R → K in AAH20052. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EC58500CC05B8BAA	FASTA	983	110,586
	10 20 30 40 50 60 MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE 70 80 90 100 110 120 QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS QAWAEGGSPR SARSLKGDPP 130 140 150 160 170 180 RGPAGRGPES PLRSPARAKA SPLRRSAESR DAIASATPVP PAPPVPPVSS VRVVSASGAV 190 200 210 220 230 240 SEEIEVLEMV REDEAPQPLP DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN 250 260 270 280 290 300 SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL 310 320 330 340 350 360 FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL DLYQMEDEAY 370 380 390 400 410 420 SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA 430 440 450 460 470 480 HMAVLSIQDL TVKYFEITAK AQKAVYDRMR ADQKKFGKAS WAAAAERMEK LQYAVSKETL 490 500 510 520 530 540 QMMRAKEICL EQKKHALKEE MQSLQGGTEA IARLDQLESD YYDLQLQLYE VQFEILKCEE 550 560 570 580 590 600 LLLTAQLESI KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL 610 620 630 640 650 660 EARRGRVSAK KAYLRNKKEI CIAKHHEKFQ QRFQSEDEYR AHHTIQIKRD KLHDEEERKS 670 680 690 700 710 720 AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRVAHSRRK STASPVPCEE QCHSLPTVLQ 730 740 750 760 770 780 GQEKTEVGGG GSQLGPSQTA EPQSLVQLED TSSEQLESTS LPPRAVVSSE LPPPQSAPLL 790 800 810 820 830 840 TSIDPKPCSV TIDPLPPPLP PTPPPPPPPP PPPPPPLPVA KDNGASTTAE TLEKDALRTE 850 860 870 880 890 900 GNERSIPKSA SAPAAHLFDS SQLVSARKKL RKTVEGLQRR RVSSPMDEVL ASLKRGSFHL 910 920 930 940 950 960 KKVEQRTLPP FPDEDDSNNI LAQIRKGVKL KKVQKEVLRE SFTLLPDTDP LTRSIHEALR 970 980 RIKEASPESE DEEEALPCTD WEN
	Isoform 2. Checksum: D5195484B4AE0A56		446	49,644
	10 20 30 40 50 60 MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE 70 80 90 100 110 120 QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS QAWAEGGSPR SARSLKGDPP 130 140 150 160 170 180 RGPAGRGPES PLRSPARAKA SPLRRSAESR DAIASATPVP PAPPVPPVSS VRVVSASGAV 190 200 210 220 230 240 SEEIEVLEMV REDEAPQPLP DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN 250 260 270 280 290 300 SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL 310 320 330 340 350 360 FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL DLYQMEDEAY 370 380 390 400 410 420 SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA 430 440 HMAVLSIQDL TVKYFEITAK AQKAFP
	Isoform 3 (DeltaP). Checksum: FFA558D7E734B4FB		964	108,705
	10 20 30 40 50 60 MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE 70 80 90 100 110 120 QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS QAWAEGGSPR SARSLKGDPP 130 140 150 160 170 180 RGPAGRGPES PLRSPARAKA SPLRRSAESR DAIASATPVP PAPPVPPVSS VRVVSASGAV 190 200 210 220 230 240 SEEIEVLEMV REDEAPQPLP DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN 250 260 270 280 290 300 SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL 310 320 330 340 350 360 FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL DLYQMEDEAY 370 380 390 400 410 420 SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA 430 440 450 460 470 480 HMAVLSIQDL TVKYFEITAK AQKAVYDRMR ADQKKFGKAS WAAAAERMEK LQYAVSKETL 490 500 510 520 530 540 QMMRAKEICL EQKKHALKEE MQSLQGGTEA IARLDQLESD YYDLQLQLYE VQFEILKCEE 550 560 570 580 590 600 LLLTAQLESI KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL 610 620 630 640 650 660 EARRGRVSAK KAYLRNKKEI CIAKHHEKFQ QRFQSEDEYR AHHTIQIKRD KLHDEEERKS 670 680 690 700 710 720 AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRVAHSRRK STASPVPCEE QCHSLPTVLQ 730 740 750 760 770 780 GQEKTEVGGG GSQLGPSQTA EPQSLVQLED TSSEQLESTS LPPRAVVSSE LPPPQSAPLL 790 800 810 820 830 840 TSIDPKPCSV TIDPPPPLPV AKDNGASTTA ETLEKDALRT EGNERSIPKS ASAPAAHLFD 850 860 870 880 890 900 SSQLVSARKK LRKTVEGLQR RRVSSPMDEV LASLKRGSFH LKKVEQRTLP PFPDEDDSNN 910 920 930 940 950 960 ILAQIRKGVK LKKVQKEVLR ESFTLLPDTD PLTRSIHEAL RRIKEASPES EDEEEALPCT DWEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel cofactor for p300 that regulates the p53 response." Shikama N., Lee C.-W., France S., Delavaine L., Lyon J., Krstic-Demonacos M., La Thangue N.B. Mol. Cell 4:365-376(1999) [PubMed: 10518217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300, TISSUE SPECIFICITY.
[2]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[3]	"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] OF 1-555 AND 940-983 (ISOFORM 1). Strain: C57BL/6J. Tissue: Spinal ganglion and Urinary bladder.
[4]	"A TPR motif cofactor contributes to p300 activity in the p53 response." Demonacos C., Krstic-Demonacos M., La Thangue N.B. Mol. Cell 8:71-84(2001) [PubMed: 11511361] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 3), INTERACTION WITH TTC5.
[5]	"Mdm2 targets the p53 transcription cofactor JMY for degradation." Coutts A.S., Boulahbel H., Graham A., La Thangue N.B. EMBO Rep. 8:84-90(2007) [PubMed: 17170761] [Abstract] Cited for: UBIQUITINATION, INDUCTION.
[6]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 AND SER-75, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF201390 mRNA. Translation: AAF17555.1. BC020052 mRNA. Translation: AAH20052.1. BC069906 mRNA. Translation: AAH69906.1. Sequence problems. BC090835 mRNA. Translation: AAH90835.1. AK035559 mRNA. Translation: BAC29105.1. AK141957 mRNA. Translation: BAE24898.1.
RefSeq	NP_067285.2.
UniGene	Mm.390630
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QXM1. 2 interactions.
PTM databases
PhosphoSite	Q9QXM1.
Proteomic databases
PRIDE	Q9QXM1.
Genome annotation databases
Ensembl	ENSMUSG00000021690. Mus musculus. [Contig view]
GeneID	57748.
KEGG	mmu:57748.
Organism-specific databases
MGI	MGI:1913096. Jmy.
Phylogenomic databases
HOGENOM	Q9QXM1.
HOVERGEN	Q9QXM1.
Gene expression databases
ArrayExpress	Q9QXM1.
CleanEx	MM_JMY.
Family and domain databases
InterPro	IPR006077. Vinculin/catenin. IPR003124. WH2_actin_bd. [Graphical view]
Pfam	PF02205. WH2. 1 hit. [Graphical view]
PRINTS	PR00806. VINCULIN.
SMART	SM00246. WH2. 1 hit. [Graphical view]
PROSITE	PS51082. WH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	313889.
SOURCE	Search...

Entry information

Entry name

JMY_MOUSE

Accession

Primary (citable) accession number: Q9QXM1
Secondary accession number(s): Q3UQZ0 , Q5BL16, Q6NST0, Q8CBP9, Q8VDZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 1, 2000
Last modified:	December 16, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)