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Protein

Junction-mediating and -regulatory protein

Gene

Jmy

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a 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. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location.4 Publications

GO - Molecular functioni

  • transcription coactivator activity Source: MGI

GO - Biological processi

  • 'de novo' actin filament nucleation Source: UniProtKB
  • actin polymerization-dependent cell motility Source: UniProtKB
  • Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • regulation of DNA-templated transcription in response to stress Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Junction-mediating and -regulatory protein
Gene namesi
Name:Jmy
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1913096. Jmy.

Subcellular locationi

  • Nucleus 2 Publications
  • Cytoplasmcytoskeleton By similarity

  • Note: Localizes to the nucleus in most cell types. In primary neutrophils, it colocalizes with actin filaments at the leading edge and is excluded from the nucleus. Localization correlates with motility, because it moves from the nucleus to the cytoplasmic compartment when cells are differentiated from nonmotile cells into highly motile neutrophil-like cells (By similarity). Accumulates in nucleus under DNA damage conditions, increasing p53/TP53 transcription response and reducing its influence on cell motility.By similarity

GO - Cellular componenti

  • cell leading edge Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi981W → A: Decreases the activation of Arp2/3 wizhout affecting the intinsic nucleation activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003246121 – 983Junction-mediating and -regulatory proteinAdd BLAST983

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei108PhosphoserineCombined sources1
Modified residuei114PhosphoserineBy similarity1
Modified residuei704PhosphoserineBy similarity1
Modified residuei883PhosphoserineCombined sources1
Modified residuei969PhosphoserineCombined sources1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QXM1.
PeptideAtlasiQ9QXM1.
PRIDEiQ9QXM1.

PTM databases

iPTMnetiQ9QXM1.
PhosphoSitePlusiQ9QXM1.

Expressioni

Tissue specificityi

Widely expressed, except in testis where it is expressed at low level.1 Publication

Inductioni

Accumulates in DNA-damaged cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000021690.
CleanExiMM_JMY.

Interactioni

Subunit structurei

Interacts with p300/EP300, the complex being recruited to activated p53/TP53. Interacts with TTC5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q0947216EBI-866001,EBI-447295From a different organism.

Protein-protein interaction databases

BioGridi208310. 1 interactor.
IntActiQ9QXM1. 23 interactors.
STRINGi10090.ENSMUSP00000070339.

Structurei

3D structure databases

ProteinModelPortaliQ9QXM1.
SMRiQ9QXM1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini916 – 933WH2PROSITE-ProRule annotationAdd BLAST18

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 119Interaction with p300/EP3001 PublicationAdd BLAST119
Regioni469 – 558Interaction with p300/EP3001 PublicationAdd BLAST90

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili315 – 351Sequence analysisAdd BLAST37
Coiled coili480 – 528Sequence analysisAdd BLAST49
Coiled coili571 – 612Sequence analysisAdd BLAST42

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi762 – 818Pro-richAdd BLAST57

Sequence similaritiesi

Belongs to the JMY family.Curated
Contains 1 WH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IF4S. Eukaryota.
ENOG4111J4B. LUCA.
HOGENOMiHOG000074181.
HOVERGENiHBG067146.
InParanoidiQ9QXM1.
PhylomeDBiQ9QXM1.
TreeFamiTF331023.

Family and domain databases

InterProiIPR033324. Jmy.
IPR031738. JMY/WHAMM.
IPR031808. JMY/WHAMM_N.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23330:SF8. PTHR23330:SF8. 2 hits.
PfamiPF15871. JMY. 1 hit.
PF15920. WHAMM-JMY_N. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QXM1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT
60 70 80 90 100
AQRQRSGSRE QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS
110 120 130 140 150
QAWAEGGSPR SARSLKGDPP RGPAGRGPES PLRSPARAKA SPLRRSAESR
160 170 180 190 200
DAIASATPVP PAPPVPPVSS VRVVSASGAV SEEIEVLEMV REDEAPQPLP
210 220 230 240 250
DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN SQLEPCLPVF
260 270 280 290 300
PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL
310 320 330 340 350
FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL
360 370 380 390 400
DLYQMEDEAY SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY
410 420 430 440 450
LGPRRIESLQ KEDADWQRKA HMAVLSIQDL TVKYFEITAK AQKAVYDRMR
460 470 480 490 500
ADQKKFGKAS WAAAAERMEK LQYAVSKETL QMMRAKEICL EQKKHALKEE
510 520 530 540 550
MQSLQGGTEA IARLDQLESD YYDLQLQLYE VQFEILKCEE LLLTAQLESI
560 570 580 590 600
KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL
610 620 630 640 650
EARRGRVSAK KAYLRNKKEI CIAKHHEKFQ QRFQSEDEYR AHHTIQIKRD
660 670 680 690 700
KLHDEEERKS AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRVAHSRRK
710 720 730 740 750
STASPVPCEE QCHSLPTVLQ GQEKTEVGGG GSQLGPSQTA EPQSLVQLED
760 770 780 790 800
TSSEQLESTS LPPRAVVSSE LPPPQSAPLL TSIDPKPCSV TIDPLPPPLP
810 820 830 840 850
PTPPPPPPPP PPPPPPLPVA KDNGASTTAE TLEKDALRTE GNERSIPKSA
860 870 880 890 900
SAPAAHLFDS SQLVSARKKL RKTVEGLQRR RVSSPMDEVL ASLKRGSFHL
910 920 930 940 950
KKVEQRTLPP FPDEDDSNNI LAQIRKGVKL KKVQKEVLRE SFTLLPDTDP
960 970 980
LTRSIHEALR RIKEASPESE DEEEALPCTD WEN
Length:983
Mass (Da):110,586
Last modified:May 1, 2000 - v1
Checksum:iEC58500CC05B8BAA
GO
Isoform 2 (identifier: Q9QXM1-2) [UniParc]FASTAAdd to basket

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

Show »
Length:446
Mass (Da):49,644
Checksum:iD5195484B4AE0A56
GO
Isoform 3 (identifier: Q9QXM1-3) [UniParc]FASTAAdd to basket
Also known as: DeltaP

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

Note: Alters the p53/TP53 response.
Show »
Length:964
Mass (Da):108,705
Checksum:iFFA558D7E734B4FB
GO

Sequence cautioni

The sequence AAH69906 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54Q → H in BAE24898 (PubMed:16141072).Curated1
Sequence conflicti63G → V in AAH20052 (PubMed:15489334).Curated1
Sequence conflicti70S → R in BAE24898 (PubMed:16141072).Curated1
Sequence conflicti153I → T in AAH20052 (PubMed:15489334).Curated1
Sequence conflicti153I → T in AAH90835 (PubMed:15489334).Curated1
Sequence conflicti153I → T in BAE24898 (PubMed:16141072).Curated1
Sequence conflicti159V → A in AAH20052 (PubMed:15489334).Curated1
Sequence conflicti159V → A in AAH90835 (PubMed:15489334).Curated1
Sequence conflicti159V → A in BAE24898 (PubMed:16141072).Curated1
Sequence conflicti189M → I in AAH20052 (PubMed:15489334).Curated1
Sequence conflicti214S → P in AAH20052 (PubMed:15489334).Curated1
Sequence conflicti214S → P in AAH90835 (PubMed:15489334).Curated1
Sequence conflicti214S → P in BAE24898 (PubMed:16141072).Curated1
Sequence conflicti331R → K in AAH20052 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_032311445 – 446VY → FP in isoform 2. 1 Publication2
Alternative sequenceiVSP_032312447 – 983Missing in isoform 2. 1 PublicationAdd BLAST537
Alternative sequenceiVSP_032313794 – 812Missing in isoform 3. CuratedAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26688.1. [Q9QXM1-1]
RefSeqiNP_067285.2. NM_021310.3.
UniGeneiMm.100273.

Genome annotation databases

GeneIDi57748.
KEGGimmu:57748.
UCSCiuc007rlf.2. mouse. [Q9QXM1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26688.1. [Q9QXM1-1]
RefSeqiNP_067285.2. NM_021310.3.
UniGeneiMm.100273.

3D structure databases

ProteinModelPortaliQ9QXM1.
SMRiQ9QXM1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208310. 1 interactor.
IntActiQ9QXM1. 23 interactors.
STRINGi10090.ENSMUSP00000070339.

PTM databases

iPTMnetiQ9QXM1.
PhosphoSitePlusiQ9QXM1.

Proteomic databases

PaxDbiQ9QXM1.
PeptideAtlasiQ9QXM1.
PRIDEiQ9QXM1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi57748.
KEGGimmu:57748.
UCSCiuc007rlf.2. mouse. [Q9QXM1-1]

Organism-specific databases

CTDi133746.
MGIiMGI:1913096. Jmy.

Phylogenomic databases

eggNOGiENOG410IF4S. Eukaryota.
ENOG4111J4B. LUCA.
HOGENOMiHOG000074181.
HOVERGENiHBG067146.
InParanoidiQ9QXM1.
PhylomeDBiQ9QXM1.
TreeFamiTF331023.

Miscellaneous databases

PROiQ9QXM1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021690.
CleanExiMM_JMY.

Family and domain databases

InterProiIPR033324. Jmy.
IPR031738. JMY/WHAMM.
IPR031808. JMY/WHAMM_N.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23330:SF8. PTHR23330:SF8. 2 hits.
PfamiPF15871. JMY. 1 hit.
PF15920. WHAMM-JMY_N. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiJMY_MOUSE
AccessioniPrimary (citable) accession number: Q9QXM1
Secondary accession number(s): Q3UQZ0
, Q5BL16, Q6NST0, Q8CBP9, Q8VDZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.