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UniProtKB/Swiss-Prot entry Q8N9B5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name JMY_HUMAN
Primary accession number Q8N9B5
Secondary accession number A1L4P5
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 18, 2008 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Junction-mediating and -regulatory protein
Synonyms None
Gene name
Name: JMY
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02919; PubMed=15372022 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-364.
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., 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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-988 (ISOFORM 2).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-988 (ISOFORM 1), AND VARIANT LEU-364.
TISSUE=Substantia nigra;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
INDUCTION.
DOI=10.1038/sj.cdd.4401575; PubMed=15706352 [NCBI, ExPASy, EBI, Israel, Japan]
Hershko T., Chaussepied M., Oren M., Ginsberg D.;
"Novel link between E2F and p53: proapoptotic cofactors of p53 are transcriptionally upregulated by E2F.";
Cell Death Differ. 12:377-383(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC016559; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC020898; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471084; EAW95834.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130624; AAI30625.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK095189; BAC04495.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_689618.3; -.
UniGene Hs.482605
3D structure databases
ModBase Q8N9B5.
Protein-protein interaction databases
IntAct Q8N9B5; -.
PTM databases
PhosphoSite Q8N9B5; -.
Organism-specific databases
MIM 604279; gene. [NCBI / EBI]
GeneCards Q8N9B5.
Gene expression databases
ArrayExpress Q8N9B5; -.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003779; Molecular function: actin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003713; Molecular function: transcription coactivator activity (inferred from sequence or structural similarity from HGNC).
GO:0007050; Biological process: cell cycle arrest (inferred from sequence or structural similarity from UniProtKB).
GO:0006281; Biological process: DNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0006917; Biological process: induction of apoptosis (inferred from sequence or structural similarity from HGNC).
GO:0051091; Biological process: positive regulation of transcription factor activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006357; Biological process: regulation of transcription from RNA polymerase II promoter (inferred from sequence or structural similarity from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR003124; WH2_actin_bd.
Graphical view of domain structure.
Pfam PF02205; WH2; 1.
Pfam graphical view of domain structure.
SMART SM00246; WH2; 1.
SMART graphical view of domain structure.
PROSITE PS51082; WH2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8N9B5.
Genome annotation databases
Ensembl ENSG00000152409; Homo sapiens. [Contig view]
GeneID 133746; -.
KEGG hsa:133746; -.
Phylogenomic databases
HOGENOM Q8N9B5; -.
HOVERGEN Q8N9B5; -.
Other
NextBio 83276; -.
SOURCE JMY; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Actin-binding; Alternative splicing; Coiled coil; DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   988  988     Junction-mediating and -regulatory protein. PRO_0000324611
DOMAIN   921   938  18     WH2. 
REGION   1   126  126     Interaction with p300/EP300 (By similarity). 
REGION   478   567  90     Interaction with p300/EP300 (By similarity). 
COILED   324   360  37     Potential. 
COILED   489   541  53     Potential. 
COILED   590   621  32     Potential. 
COMPBIAS   781   827  47     Pro-rich. 
MOD_RES   83    83        Phosphoserine (By similarity). 
MOD_RES   974   974        Phosphoserine. 
VAR_SEQ   814   825        Missing (in isoform 2). VSP_032310
VARIANT   364   364  1     M -> L (in dbSNP:rs13182512 [NCBI]). VAR_039846 
VARIANT   592   592  1     A -> V (in dbSNP:rs12109475 [NCBI]). VAR_039847 
VARIANT   720   720  1     H -> R (in dbSNP:rs16876657 [NCBI]). VAR_039848 
Sequence information
Length: 988 AA [This is the length of the unprocessed precursor] Molecular weight: 111445 Da [This is the MW of the unprocessed precursor] CRC64: 7166FF8AE325F37A [This is a checksum on the sequence]
        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 

Q8N9B5 in FASTA format

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