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Q8N9B5 (JMY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Junction-mediating and -regulatory protein
Gene names
Name:JMY
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length988 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeleton. Note: Localizes to the nucleus in most cell types. Accumulates in nucleus under DNA damage conditions, increasing p53/TP53 transcription response and reducing its influence on cell motility By similarity. 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. Ref.8

Induction

By E2F. 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 By similarity.

Sequence similarities

Belongs to the JMY family.

Contains 1 WH2 domain.

Sequence caution

The sequence AAI30625.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC04495.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAW95834.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandActin-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' actin filament nucleation

Inferred from sequence or structural similarity. Source: UniProtKB

Arp2/3 complex-mediated actin nucleation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

actin polymerization-dependent cell motility

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentcell leading edge

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functiontranscription coactivator activity

Inferred from sequence or structural similarity. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q009872EBI-866435,EBI-389668

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N9B5-1)

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: Q8N9B5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     814-825: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 988988Junction-mediating and -regulatory protein
PRO_0000324611

Regions

Domain921 – 93818WH2
Region1 – 126126Interaction with p300/EP300 By similarity
Region478 – 56790Interaction with p300/EP300 By similarity
Coiled coil324 – 36037 Potential
Coiled coil489 – 54153 Potential
Coiled coil590 – 62132 Potential
Compositional bias781 – 82747Pro-rich

Amino acid modifications

Modified residue9741Phosphoserine Ref.6

Natural variations

Alternative sequence814 – 82512Missing in isoform 2.
VSP_032310
Natural variant3641M → L. Ref.2 Ref.4
Corresponds to variant rs13182512 [ dbSNP | Ensembl ].
VAR_039846
Natural variant5921A → V.
Corresponds to variant rs12109475 [ dbSNP | Ensembl ].
VAR_039847
Natural variant7201H → R.
Corresponds to variant rs16876657 [ dbSNP | Ensembl ].
VAR_039848

Sequences

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

Last modified March 18, 2008. Version 2.
Checksum: 7166FF8AE325F37A

FASTA988111,445
        10         20         30         40         50         60 
MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE 

        70         80         90        100        110        120 
QAGARGGAEA GGAASDGSRG PGSPAGRGRP EATASATLVR SPGPRRSSAW AEGGSPRSTR 

       130        140        150        160        170        180 
SLLGDPRLRS PGSKGAESRL RSPVRAKPIP GQKTSEADDA AGAAAAAARP APREAQVSSV 

       190        200        210        220        230        240 
RIVSASGTVS EEIEVLEMVK EDEAPLALSD AEQPPPATEL ESPAEECSWA GLFSFQDLRA 

       250        260        270        280        290        300 
VHQQLCSVNS QLEPCLPVFP EEPSGMWTVL FGGAPEMTEQ EIDTLCYQLQ VYLGHGLDTC 

       310        320        330        340        350        360 
GWKILSQVLF TETDDPEEYY ESLSELRQKG YEEVLQRARK RIQELLDKHK NTESMVELLD 

       370        380        390        400        410        420 
LYQMEDEAYS SLAEATTELY QYLLQPFRDM RELAMLRRQQ IKISMENDYL GPRRIESLQK 

       430        440        450        460        470        480 
EDADWQRKAH MAVLSIQDLT VKYFEITAKA QKAVYDRMRA DQKKFGKASW AAAAERMEKL 

       490        500        510        520        530        540 
QYAVSKETLQ MMRAKEICLE QRKHALKEEM QSLRGGTEAI ARLDQLEADY YDLQLQLYEV 

       550        560        570        580        590        600 
QFEILKCEEL LLTAQLESIK RLISEKRDEV VYYDTYESME AMLEKEEMAA SAYLQREELQ 

       610        620        630        640        650        660 
KLQQKARQLE ARRGRVSAKK SYLRNKKEIC IAKHNEKIQQ RTRIEDEYRT HHTVQLKREK 

       670        680        690        700        710        720 
LHDEEERKSA WVSQERQRTL DRLRTFKQRY PGQVILKSTR LRLAHARRKG AASPVLQEDH 

       730        740        750        760        770        780 
CDSLPSVLQV EEKTEEVGEG RVKRGPSQTT EPQSLVQLED TSLTQLEATS LPLSGVTSEL 

       790        800        810        820        830        840 
PPTISLPLLN NNLEPCSVTI NPLPSPLPPT PPPPPPPPPP PPPPPLPVAK DSGPETLEKD 

       850        860        870        880        890        900 
LPRKEGNEKR IPKSASAPSA HLFDSSQLVS ARKKLRKTAE GLQRRRVSSP MDEVLASLKR 

       910        920        930        940        950        960 
GSFHLKKVEQ RTLPPFPDED DSNNILAQIR KGVKLKKVQK DVLRESFTLL PDTDPLTRSI 

       970        980 
HEALRRIKEA SPESEDEEEA LPCTDWEN 

« Hide

Isoform 2 [UniParc].

Checksum: 27175E3EFA32295E
Show »

FASTA976110,280

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-364.
[3]"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] OF 345-988 (ISOFORM 2).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-988 (ISOFORM 1), VARIANT LEU-364.
Tissue: Substantia nigra.
[5]"Novel link between E2F and p53: proapoptotic cofactors of p53 are transcriptionally upregulated by E2F."
Hershko T., Chaussepied M., Oren M., Ginsberg D.
Cell Death Differ. 12:377-383(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"p53-cofactor JMY is a multifunctional actin nucleation factor."
Zuchero J.B., Coutts A.S., Quinlan M.E., Thangue N.B., Mullins R.D.
Nat. Cell Biol. 11:451-459(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC016559 Genomic DNA. No translation available.
AC020898 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95834.1. Sequence problems.
BC130624 mRNA. Translation: AAI30625.1. Different initiation.
AK095189 mRNA. Translation: BAC04495.1. Different initiation.
RefSeqNP_689618.4. NM_152405.4.
UniGeneHs.482605.

3D structure databases

ProteinModelPortalQ8N9B5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126372. 2 interactions.
IntActQ8N9B5. 2 interactions.
MINTMINT-4052528.
STRING9606.ENSP00000379441.

PTM databases

PhosphoSiteQ8N9B5.

Polymorphism databases

DMDM172045777.

Proteomic databases

PaxDbQ8N9B5.
PRIDEQ8N9B5.

Protocols and materials databases

DNASU133746.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396137; ENSP00000379441; ENSG00000152409. [Q8N9B5-1]
GeneID133746.
KEGGhsa:133746.
UCSCuc003kfw.1. human. [Q8N9B5-1]

Organism-specific databases

CTD133746.
GeneCardsGC05P078609.
H-InvDBHIX0004982.
HGNCHGNC:28916. JMY.
HPAHPA043308.
MIM604279. gene.
neXtProtNX_Q8N9B5.
PharmGKBPA164721124.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39317.
HOGENOMHOG000074181.
HOVERGENHBG067146.
InParanoidQ8N9B5.
OMAKFQQRLR.
OrthoDBEOG7QVM1Z.
PhylomeDBQ8N9B5.
TreeFamTF331023.

Gene expression databases

BgeeQ8N9B5.
GenevestigatorQ8N9B5.

Family and domain databases

InterProIPR003124. WH2_dom.
[Graphical view]
SMARTSM00246. WH2. 1 hit.
[Graphical view]
PROSITEPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi133746.
NextBio83276.
PMAP-CutDBQ8N9B5.
PROQ8N9B5.
SOURCESearch...

Entry information

Entry nameJMY_HUMAN
AccessionPrimary (citable) accession number: Q8N9B5
Secondary accession number(s): A1L4P5, B5MDS2, B5MDT0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM