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O15061

- SYNEM_HUMAN

UniProt

O15061 - SYNEM_HUMAN

Protein

Synemin

Gene

SYNM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells.3 Publications

    GO - Molecular functioni

    1. intermediate filament binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: UniProtKB
    4. structural constituent of muscle Source: UniProtKB
    5. vinculin binding Source: UniProtKB

    GO - Biological processi

    1. intermediate filament cytoskeleton organization Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synemin
    Alternative name(s):
    Desmuslin
    Gene namesi
    Name:SYNM
    Synonyms:DMN, KIAA0353, SYN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:24466. SYNM.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionadherens junction
    Note: There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. costamere Source: UniProtKB
    3. intermediate filament Source: UniProtKB
    4. membrane Source: Ensembl
    5. neurofilament cytoskeleton Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Intermediate filament

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164726408.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15651565SyneminPRO_0000063778Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei429 – 4291Phosphoserine1 Publication
    Modified residuei598 – 5981Phosphothreonine1 Publication
    Modified residuei1044 – 10441Phosphoserine2 Publications
    Modified residuei1049 – 10491Phosphoserine2 Publications
    Modified residuei1181 – 11811Phosphoserine2 Publications
    Modified residuei1184 – 11841Phosphoserine1 Publication
    Modified residuei1435 – 14351Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO15061.
    PaxDbiO15061.
    PRIDEiO15061.

    PTM databases

    PhosphoSiteiO15061.

    Expressioni

    Tissue specificityi

    Isoform 2 is strongly detected in adult heart, fetal skeletal muscles and fetal heart. Isoform 1 is weakly detected in fetal heart and also in fetal skeletal muscle. Isoform 1 and isoform 2 are detected in adult bladder (at protein level). The mRNA is predominantly expressed in heart and muscle with some expression in brain which may be due to tissue-specific isoforms.2 Publications

    Developmental stagei

    In lens, first detected at 16 weeks when expression is weakly and uniformly distributed. Subsequently, expression becomes much stronger in the epithelium of the anterior part at 25 weeks and later. In retina, weakly expressed at 15 weeks in the nerve fiber and ganglion cell layers (NFL and GCL). From 25 weeks onwards, much stronger expression is observed in the endfeet of Mueller cells, the NFL, and GCL, and much lower expression is observed in a minor subpopulation of cells in the inner cell layer (INL). At 30 and 36 weeks, expression remains in the neural retina, and subsequently becomes stronger in the NFL, GCL, and INL and is decreased in Mueller cells. At 36 weeks, also expressed at the external border of the outer nuclear layer (ONL) (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO15061.
    BgeeiO15061.
    CleanExiHS_SYNM.
    GenevestigatoriO15061.

    Organism-specific databases

    HPAiCAB017192.

    Interactioni

    Subunit structurei

    Interacts with GFAP and VIM By similarity. Isoform 1 interacts with TLN1 and VCL. Isoform 2 interacts with DES and DTNA. Isoform 1 and isoform 2 interact with DMD and UTRN.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi116923. 12 interactions.
    IntActiO15061. 1 interaction.
    MINTiMINT-198289.
    STRINGi9606.ENSP00000336775.

    Structurei

    3D structure databases

    ProteinModelPortaliO15061.
    SMRiO15061. Positions 251-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1010Head
    Regioni11 – 320310Interaction with DMD and UTRNAdd
    BLAST
    Regioni11 – 300290RodAdd
    BLAST
    Regioni11 – 4939Coil 1AAdd
    BLAST
    Regioni50 – 589Linker 1
    Regioni59 – 163105Coil 1BAdd
    BLAST
    Regioni164 – 18623Linker 12Add
    BLAST
    Regioni187 – 300114Coil 2Add
    BLAST
    Regioni301 – 15651265TailAdd
    BLAST
    Regioni1152 – 1463312Interaction with TLN1 and VCLAdd
    BLAST
    Regioni1244 – 1563320Interaction with DMD and UTRNAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG139727.
    HOGENOMiHOG000154476.
    HOVERGENiHBG008974.
    InParanoidiO15061.
    KOiK10376.
    PhylomeDBiO15061.

    Family and domain databases

    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    [Graphical view]
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15061-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE     50
    GLWAEGQARC AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA 100
    EERAARGRLD AELGAQQREL QEALGARAAL EALLGRLQAE RRGLDAAHER 150
    DVRELRARAA SLTMHFRARA TGPAAPPPRL REVHDSYALL VAESWRETVQ 200
    LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE ALGLEQLRAR 250
    LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV 300
    KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ 350
    RENERNLFSR QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG 400
    SGYSSSATTQ QENSYGKAVS SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK 450
    AGDTREVPVY IGEDSTIARE SYRDRRDKVA AGASESTRSN ERTVILGKKT 500
    EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE ELTKLDKEAR 550
    QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV 600
    KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF 650
    TQSPETEASA DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD 700
    EAGLDYLLSK DIKEVGLKGK SAEQMIGDII NLGLKGREGR AKVVNVEIVE 750
    EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP WGLVKEEEGY GESDVTFSVN 800
    QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG GHDRDDGSVY 850
    GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG 900
    DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV 950
    EVIGQLEETL PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV 1000
    AEVNVSQTVD ADRLDLEELS KDEASEMEKA VESVVRESLS RQRSPAPGSP 1050
    DEEGGAEAPA AGIRFRRWAT RELYIPSGES EVAGGASHSS GQRTPQGPVS 1100
    ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM SYEGPTAEVV 1150
    EVSAGGDLSQ AASPTGASRS VRHVTLGPGQ SPLSREVIFL GPAPACPEAW 1200
    GSPEPGPAES SADMDGSGRH STFGCRQFHA EKEIIFQGPI SAAGKVGDYF 1250
    ATEESVGTQT SVRQLQLGPK EGFSGQIQFT APLSDKVELG VIGDSVHMEG 1300
    LPGSSTSIRH ISIGPQRHQT TQQIVYHGLV PQLGESGDSE STVHGEGSAD 1350
    VHQATHSHTS GRQTVMTEKS TFQSVVSESP QEDSAGDTSG AEMTSGVSRS 1400
    FRHIRLGPTE TETSEHIAIR GPVSRTFVLA GSADSPELGK LADSSRTLRH 1450
    IAPGPKETSF TFQMDVSNVE AIRSRTQEAG ALGVSDRGSW RDADSRNDQA 1500
    VGVSFKASAG EGDQAHREQG KEQAMFDKKV QLQRMVDQRS VISDEKKVAL 1550
    LYLDNEEEEN DGHWF 1565
    Length:1,565
    Mass (Da):172,768
    Last modified:January 23, 2002 - v2
    Checksum:i18D19000D3CEA537
    GO
    Isoform 2 (identifier: O15061-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1152-1463: Missing.

    Show »
    Length:1,253
    Mass (Da):140,135
    Checksum:i88162E538D848F2A
    GO
    Isoform 3 (identifier: O15061-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         336-339: EFRN → DGCE
         340-1565: Missing.

    Show »
    Length:339
    Mass (Da):39,042
    Checksum:i090EEA199A0041C4
    GO

    Sequence cautioni

    The sequence AAI10067.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA20810.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41W → L in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti4 – 41W → L in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti4 – 41W → L in CAG27071. 1 PublicationCurated
    Sequence conflicti24 – 241Missing in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti24 – 241Missing in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti52 – 521Missing in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti52 – 521Missing in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti197 – 1971E → G in CAG27071. 1 PublicationCurated
    Sequence conflicti241 – 2411A → T in CAG27071. 1 PublicationCurated
    Sequence conflicti274 – 2741D → G in CAG27071. 1 PublicationCurated
    Sequence conflicti318 – 3181E → G in CAG27071. 1 PublicationCurated
    Sequence conflicti322 – 3221E → Q in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti322 – 3221E → Q in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti322 – 3221E → Q in CAG27071. 1 PublicationCurated
    Sequence conflicti373 – 3731A → V in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti373 – 3731A → V in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti555 – 5551Q → H in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti555 – 5551Q → H in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti564 – 5641K → N in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti564 – 5641K → N in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti655 – 6551E → Q in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti655 – 6551E → Q in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti666 – 6661T → A in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti666 – 6661T → A in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti687 – 6871V → L in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti687 – 6871V → L in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti720 – 7201K → N in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti720 – 7201K → N in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti845 – 8451D → N in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti845 – 8451D → N in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti856 – 8561E → Q in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti856 – 8561E → Q in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti874 – 8741R → P in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti874 – 8741R → P in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti965 – 9651R → K in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti965 – 9651R → K in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1004 – 10041N → D in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti1004 – 10041N → D in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1019 – 10191L → V in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti1019 – 10191L → V in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1039 – 10391L → M in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti1039 – 10391L → M in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1076 – 10761P → L in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti1076 – 10761P → L in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1151 – 11511E → G in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1292 – 12921I → T in CAC83859. (PubMed:11737198)Curated
    Sequence conflicti1493 – 14931A → R in AAI10067. (PubMed:15489334)Curated
    Sequence conflicti1509 – 15091A → V in CAC83858. (PubMed:11737198)Curated
    Sequence conflicti1509 – 15091A → V in CAC83859. (PubMed:11737198)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721A → V.2 Publications
    VAR_012295
    Natural varianti330 – 3301V → I.1 Publication
    VAR_012296
    Natural varianti338 – 3381R → W.1 Publication
    VAR_012297
    Natural varianti355 – 3551R → W.3 Publications
    Corresponds to variant rs3743242 [ dbSNP | Ensembl ].
    VAR_059378
    Natural varianti462 – 4621G → S.2 Publications
    Corresponds to variant rs3134595 [ dbSNP | Ensembl ].
    VAR_059379
    Natural varianti567 – 5671P → L.2 Publications
    VAR_012298
    Natural varianti612 – 6121E → A.1 Publication
    VAR_012299
    Natural varianti761 – 7611P → L.1 Publication
    VAR_012300
    Natural varianti946 – 9461R → W.1 Publication
    VAR_012301
    Natural varianti976 – 9761Q → R.1 Publication
    VAR_012302
    Natural varianti1059 – 10591P → L.1 Publication
    VAR_012303
    Natural varianti1067 – 10671R → P.1 Publication
    VAR_012304
    Natural varianti1077 – 10771S → L.1 Publication
    VAR_012305
    Natural varianti1130 – 11301G → S.
    Corresponds to variant rs9920074 [ dbSNP | Ensembl ].
    VAR_059380
    Natural varianti1345 – 13451G → A.
    Corresponds to variant rs7167599 [ dbSNP | Ensembl ].
    VAR_059381
    Natural varianti1386 – 13861G → E.1 Publication
    Corresponds to variant rs2292288 [ dbSNP | Ensembl ].
    VAR_012306
    Natural varianti1462 – 14621F → C.
    Corresponds to variant rs2292287 [ dbSNP | Ensembl ].
    VAR_012307

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei336 – 3394EFRN → DGCE in isoform 3. 1 PublicationVSP_036478
    Alternative sequencei340 – 15651226Missing in isoform 3. 1 PublicationVSP_036479Add
    BLAST
    Alternative sequencei1152 – 1463312Missing in isoform 2. 2 PublicationsVSP_002465Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310521 mRNA. Translation: CAC83858.1.
    AJ310522 mRNA. Translation: CAC83859.1.
    AF359284 mRNA. Translation: AAK57487.1.
    AJ697971 mRNA. Translation: CAG27071.1.
    AB002351 mRNA. Translation: BAA20810.2. Different initiation.
    BC110066 mRNA. Translation: AAI10067.1. Different initiation.
    BC151243 mRNA. Translation: AAI51244.1.
    RefSeqiNP_056101.5. NM_015286.5.
    NP_663780.2. NM_145728.2.
    UniGeneiHs.207106.

    Genome annotation databases

    EnsembliENST00000336292; ENSP00000336775; ENSG00000182253.
    GeneIDi23336.
    KEGGihsa:23336.
    UCSCiuc002buo.3. human. [O15061-2]
    uc002bup.3. human. [O15061-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310521 mRNA. Translation: CAC83858.1 .
    AJ310522 mRNA. Translation: CAC83859.1 .
    AF359284 mRNA. Translation: AAK57487.1 .
    AJ697971 mRNA. Translation: CAG27071.1 .
    AB002351 mRNA. Translation: BAA20810.2 . Different initiation.
    BC110066 mRNA. Translation: AAI10067.1 . Different initiation.
    BC151243 mRNA. Translation: AAI51244.1 .
    RefSeqi NP_056101.5. NM_015286.5.
    NP_663780.2. NM_145728.2.
    UniGenei Hs.207106.

    3D structure databases

    ProteinModelPortali O15061.
    SMRi O15061. Positions 251-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116923. 12 interactions.
    IntActi O15061. 1 interaction.
    MINTi MINT-198289.
    STRINGi 9606.ENSP00000336775.

    PTM databases

    PhosphoSitei O15061.

    Proteomic databases

    MaxQBi O15061.
    PaxDbi O15061.
    PRIDEi O15061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336292 ; ENSP00000336775 ; ENSG00000182253 .
    GeneIDi 23336.
    KEGGi hsa:23336.
    UCSCi uc002buo.3. human. [O15061-2 ]
    uc002bup.3. human. [O15061-1 ]

    Organism-specific databases

    CTDi 23336.
    GeneCardsi GC15P099645.
    H-InvDB HIX0172820.
    HGNCi HGNC:24466. SYNM.
    HPAi CAB017192.
    MIMi 606087. gene.
    neXtProti NX_O15061.
    PharmGKBi PA164726408.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG139727.
    HOGENOMi HOG000154476.
    HOVERGENi HBG008974.
    InParanoidi O15061.
    KOi K10376.
    PhylomeDBi O15061.

    Miscellaneous databases

    ChiTaRSi SYNM. human.
    GenomeRNAii 23336.
    NextBioi 45283.
    PROi O15061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15061.
    Bgeei O15061.
    CleanExi HS_SYNM.
    Genevestigatori O15061.

    Family and domain databases

    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    [Graphical view ]
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human synemin gene generates splice variants encoding two distinct intermediate filament proteins."
      Titeux M., Brocheriou V., Xue Z., Gao J., Pellissier J.-F., Guicheney P., Paulin D., Li Z.
      Eur. J. Biochem. 268:6435-6449(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT, TISSUE SPECIFICITY, VARIANTS VAL-272; TRP-355; LEU-567 AND GLU-1386.
      Tissue: Placenta and Skeletal muscle.
    2. "Desmuslin, an intermediate filament protein that interacts with alpha-dystrobrevin and desmin."
      Mizuno Y., Thompson T.G., Guyon J.R., Lidov H.G.W., Brosius M., Imamura M., Ozawa E., Watkins S.C., Kunkel L.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:6156-6161(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH DES AND DTNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    3. "Synemin gene generates different spliced isoforms expressed selectively in either astrocytes or neurons."
      Xue Z., Izmiryan A., Paulin D., Li Z.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. Nagase T., Kikuno R., Yamakawa H., Ohara O.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS TRP-355 AND SER-462.
      Tissue: Brain.
    5. "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] (ISOFORM 1), VARIANTS TRP-355 AND SER-462.
    6. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-1565 (ISOFORM 1).
      Tissue: Brain.
    7. "Synemin expression in developing normal and pathological human retina and lens."
      Tawk M., Titeux M., Fallet C., Li Z., Daumas-Duport C., Cavalcante L.A., Paulin D., Moura-Neto V.
      Exp. Neurol. 183:499-507(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. "Interactions of intermediate filament protein synemin with dystrophin and utrophin."
      Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.
      Biochem. Biophys. Res. Commun. 346:768-777(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DMD AND UTRN.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Human alpha-synemin interacts directly with vinculin and metavinculin."
      Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
      Biochem. J. 409:657-667(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VCL.
    11. "Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin."
      Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
      Exp. Cell Res. 314:1839-1849(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLN1, SUBCELLULAR LOCATION.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044; SER-1049 AND SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-598 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044; SER-1049 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3."
      Mizuno Y., Puca A.A., O'Brien K.F., Beggs A.H., Kunkel L.M.
      BMC Genet. 2:8-8(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-272; ILE-330; TRP-338; LEU-567; ALA-612; LEU-761; TRP-946; ARG-976; LEU-1059; PRO-1067 AND LEU-1077.

    Entry informationi

    Entry nameiSYNEM_HUMAN
    AccessioniPrimary (citable) accession number: O15061
    Secondary accession number(s): A7E2Y2
    , Q2TBJ4, Q5NJJ9, Q8TE61, Q8TE62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 119 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 15
      Human chromosome 15: 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