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Q8N9B5

- JMY_HUMAN

UniProt

Q8N9B5 - JMY_HUMAN

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Protein

Junction-mediating and -regulatory protein

Gene

JMY

Organism
Homo sapiens (Human)
Status
Reviewed - 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 (By similarity).By similarity

GO - Molecular functioni

  1. transcription coactivator activity Source: HGNC

GO - Biological processi

  1. 'de novo' actin filament nucleation Source: UniProtKB
  2. actin polymerization-dependent cell motility Source: UniProtKB
  3. Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  4. cell cycle arrest Source: UniProtKB
  5. DNA repair Source: UniProtKB-KW
  6. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  7. positive regulation of apoptotic process Source: UniProtKB
  8. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  9. regulation of transcription from RNA polymerase II promoter Source: HGNC
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:28916. JMY.

Subcellular locationi

Nucleus By similarity. Cytoplasmcytoskeleton 1 Publication
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.By similarity

GO - Cellular componenti

  1. cell leading edge Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164721124.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 988988Junction-mediating and -regulatory proteinPRO_0000324611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei974 – 9741Phosphoserine1 Publication

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8N9B5.
PaxDbiQ8N9B5.
PRIDEiQ8N9B5.

PTM databases

PhosphoSiteiQ8N9B5.

Miscellaneous databases

PMAP-CutDBQ8N9B5.

Expressioni

Inductioni

By E2F.1 Publication

Gene expression databases

BgeeiQ8N9B5.
GenevestigatoriQ8N9B5.

Organism-specific databases

HPAiHPA043308.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009872EBI-866435,EBI-389668

Protein-protein interaction databases

BioGridi126372. 5 interactions.
IntActiQ8N9B5. 2 interactions.
MINTiMINT-4052528.
STRINGi9606.ENSP00000379441.

Structurei

3D structure databases

ProteinModelPortaliQ8N9B5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini921 – 93818WH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 126126Interaction with p300/EP300By similarityAdd
BLAST
Regioni478 – 56790Interaction with p300/EP300By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili324 – 36037Sequence AnalysisAdd
BLAST
Coiled coili489 – 54153Sequence AnalysisAdd
BLAST
Coiled coili590 – 62132Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi781 – 82747Pro-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG39317.
GeneTreeiENSGT00510000046704.
HOGENOMiHOG000074181.
HOVERGENiHBG067146.
InParanoidiQ8N9B5.
OMAiKFQQRLR.
OrthoDBiEOG7QVM1Z.
PhylomeDBiQ8N9B5.
TreeFamiTF331023.

Family and domain databases

InterProiIPR003124. WH2_dom.
[Graphical view]
SMARTiSM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N9B5-1) [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 QAGARGGAEA GGAASDGSRG PGSPAGRGRP EATASATLVR
110 120 130 140 150
SPGPRRSSAW AEGGSPRSTR SLLGDPRLRS PGSKGAESRL RSPVRAKPIP
160 170 180 190 200
GQKTSEADDA AGAAAAAARP APREAQVSSV RIVSASGTVS EEIEVLEMVK
210 220 230 240 250
EDEAPLALSD AEQPPPATEL ESPAEECSWA GLFSFQDLRA VHQQLCSVNS
260 270 280 290 300
QLEPCLPVFP EEPSGMWTVL FGGAPEMTEQ EIDTLCYQLQ VYLGHGLDTC
310 320 330 340 350
GWKILSQVLF TETDDPEEYY ESLSELRQKG YEEVLQRARK RIQELLDKHK
360 370 380 390 400
NTESMVELLD LYQMEDEAYS SLAEATTELY QYLLQPFRDM RELAMLRRQQ
410 420 430 440 450
IKISMENDYL GPRRIESLQK EDADWQRKAH MAVLSIQDLT VKYFEITAKA
460 470 480 490 500
QKAVYDRMRA DQKKFGKASW AAAAERMEKL QYAVSKETLQ MMRAKEICLE
510 520 530 540 550
QRKHALKEEM QSLRGGTEAI ARLDQLEADY YDLQLQLYEV QFEILKCEEL
560 570 580 590 600
LLTAQLESIK RLISEKRDEV VYYDTYESME AMLEKEEMAA SAYLQREELQ
610 620 630 640 650
KLQQKARQLE ARRGRVSAKK SYLRNKKEIC IAKHNEKIQQ RTRIEDEYRT
660 670 680 690 700
HHTVQLKREK LHDEEERKSA WVSQERQRTL DRLRTFKQRY PGQVILKSTR
710 720 730 740 750
LRLAHARRKG AASPVLQEDH CDSLPSVLQV EEKTEEVGEG RVKRGPSQTT
760 770 780 790 800
EPQSLVQLED TSLTQLEATS LPLSGVTSEL PPTISLPLLN NNLEPCSVTI
810 820 830 840 850
NPLPSPLPPT PPPPPPPPPP PPPPPLPVAK DSGPETLEKD LPRKEGNEKR
860 870 880 890 900
IPKSASAPSA HLFDSSQLVS ARKKLRKTAE GLQRRRVSSP MDEVLASLKR
910 920 930 940 950
GSFHLKKVEQ RTLPPFPDED DSNNILAQIR KGVKLKKVQK DVLRESFTLL
960 970 980
PDTDPLTRSI HEALRRIKEA SPESEDEEEA LPCTDWEN
Length:988
Mass (Da):111,445
Last modified:March 18, 2008 - v2
Checksum:i7166FF8AE325F37A
GO
Isoform 2 (identifier: Q8N9B5-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:976
Mass (Da):110,280
Checksum:i27175E3EFA32295E
GO

Sequence cautioni

The sequence AAI30625.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC04495.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAW95834.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti364 – 3641M → L.2 Publications
Corresponds to variant rs13182512 [ dbSNP | Ensembl ].
VAR_039846
Natural varianti592 – 5921A → V.
Corresponds to variant rs12109475 [ dbSNP | Ensembl ].
VAR_039847
Natural varianti720 – 7201H → R.
Corresponds to variant rs16876657 [ dbSNP | Ensembl ].
VAR_039848

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei814 – 82512Missing in isoform 2. 1 PublicationVSP_032310Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4047.3. [Q8N9B5-1]
RefSeqiNP_689618.4. NM_152405.4. [Q8N9B5-1]
UniGeneiHs.482605.

Genome annotation databases

EnsembliENST00000396137; ENSP00000379441; ENSG00000152409. [Q8N9B5-1]
GeneIDi133746.
KEGGihsa:133746.
UCSCiuc003kfw.1. human. [Q8N9B5-1]

Polymorphism databases

DMDMi172045777.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS4047.3. [Q8N9B5-1 ]
RefSeqi NP_689618.4. NM_152405.4. [Q8N9B5-1 ]
UniGenei Hs.482605.

3D structure databases

ProteinModelPortali Q8N9B5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126372. 5 interactions.
IntActi Q8N9B5. 2 interactions.
MINTi MINT-4052528.
STRINGi 9606.ENSP00000379441.

PTM databases

PhosphoSitei Q8N9B5.

Polymorphism databases

DMDMi 172045777.

Proteomic databases

MaxQBi Q8N9B5.
PaxDbi Q8N9B5.
PRIDEi Q8N9B5.

Protocols and materials databases

DNASUi 133746.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396137 ; ENSP00000379441 ; ENSG00000152409 . [Q8N9B5-1 ]
GeneIDi 133746.
KEGGi hsa:133746.
UCSCi uc003kfw.1. human. [Q8N9B5-1 ]

Organism-specific databases

CTDi 133746.
GeneCardsi GC05P078531.
H-InvDB HIX0004982.
HGNCi HGNC:28916. JMY.
HPAi HPA043308.
MIMi 604279. gene.
neXtProti NX_Q8N9B5.
PharmGKBi PA164721124.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39317.
GeneTreei ENSGT00510000046704.
HOGENOMi HOG000074181.
HOVERGENi HBG067146.
InParanoidi Q8N9B5.
OMAi KFQQRLR.
OrthoDBi EOG7QVM1Z.
PhylomeDBi Q8N9B5.
TreeFami TF331023.

Miscellaneous databases

GenomeRNAii 133746.
NextBioi 83276.
PMAP-CutDB Q8N9B5.
PROi Q8N9B5.
SOURCEi Search...

Gene expression databases

Bgeei Q8N9B5.
Genevestigatori Q8N9B5.

Family and domain databases

InterProi IPR003124. WH2_dom.
[Graphical view ]
SMARTi SM00246. WH2. 1 hit.
[Graphical view ]
PROSITEi PS51082. WH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJMY_HUMAN
AccessioniPrimary (citable) accession number: Q8N9B5
Secondary accession number(s): A1L4P5, B5MDS2, B5MDT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3