Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6ZMZ3

- SYNE3_HUMAN

UniProt

Q6ZMZ3 - SYNE3_HUMAN

Protein

Nesprin-3

Gene

SYNE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells.3 Publications

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cytoskeletal anchoring at nuclear membrane Source: UniProtKB
    2. cytoskeleton organization Source: UniProtKB
    3. establishment of protein localization to membrane Source: UniProtKB
    4. regulation of cell shape Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nesprin-3
    Alternative name(s):
    Nuclear envelope spectrin repeat protein 3
    Gene namesi
    Name:SYNE3
    Synonyms:C14orf49
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:19861. SYNE3.

    Subcellular locationi

    Nucleus outer membrane 1 Publication; Single-pass type IV membrane protein 1 Publication. Nucleus envelope 1 Publication. Rough endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: UniProtKB
    3. nuclear envelope Source: UniProtKB
    4. nuclear outer membrane Source: UniProtKB-SubCell
    5. rough endoplasmic reticulum Source: UniProtKB-SubCell
    6. SUN-KASH complex Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134931380.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 975975Nesprin-3PRO_0000281120Add
    BLAST

    Proteomic databases

    MaxQBiQ6ZMZ3.
    PaxDbiQ6ZMZ3.
    PRIDEiQ6ZMZ3.

    PTM databases

    PhosphoSiteiQ6ZMZ3.

    Expressioni

    Tissue specificityi

    Expressed in aortic endothelial cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ6ZMZ3.
    BgeeiQ6ZMZ3.
    CleanExiHS_C14orf49.
    GenevestigatoriQ6ZMZ3.

    Organism-specific databases

    HPAiHPA055227.

    Interactioni

    Subunit structurei

    Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with PLEC (via actin-binding domain). Interacts with DST. Interacts with SYNE1 via spectrin repeats. Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is required for SYNE3 nuclear envelope localization.3 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000334308.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZMZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 925925CytoplasmicPROSITE-ProRule annotationAdd
    BLAST
    Topological domaini947 – 97529Perinuclear spacePROSITE-ProRule annotationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei926 – 94621Helical; Anchor for type IV membrane proteinPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati220 – 325106Spectrin 1Add
    BLAST
    Repeati647 – 74094Spectrin 2Add
    BLAST
    Domaini917 – 97559KASHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili617 – 64529Sequence AnalysisAdd
    BLAST

    Domaini

    The KASH domain is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains.1 Publication

    Sequence similaritiesi

    Belongs to the nesprin family.Curated
    Contains 1 KASH domain.PROSITE-ProRule annotation
    Contains 2 spectrin repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG145316.
    HOGENOMiHOG000154475.
    HOVERGENiHBG094014.
    InParanoidiQ6ZMZ3.
    OMAiIKAQWEE.
    OrthoDBiEOG7XM2X7.
    PhylomeDBiQ6ZMZ3.
    TreeFamiTF331132.

    Family and domain databases

    InterProiIPR012315. KASH.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF10541. KASH. 1 hit.
    PF00435. Spectrin. 1 hit.
    [Graphical view]
    SMARTiSM00150. SPEC. 3 hits.
    [Graphical view]
    PROSITEiPS51049. KASH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZMZ3-1) [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

    MTQQPQDDFD RSVEDAQAWM KAVQDQLQVN DNTQGPRAAL EARLWETEKI    50
    CQLEPEGRVR VDLVLRMAEA LLACCPGDQK PGILARLKDI KAQWEETVTY 100
    MTHCHSRIEW VWLHWSEYLL ARDEFYRWFQ KMMVTLEPHI ELQLGLKEKQ 150
    WQLSHAQVLL HNVDNQAVLL DRLLEEAASL FNRIGDPSVD EDAQKRMKAE 200
    YDAVKAKAQK RVDLLEQVAR EHEEYQAGVD EFQLWLKAVV EKVNGCLGRN 250
    CKLPITQRLS TLQDIAKDFP RGEESLETLE EQSAGVIRNT SPLGAEKITG 300
    ELEEMRKVLE KLRALWEEEE ERLRGLLRSR GAWEQQIKQL EAELSEFRMV 350
    LQRLAQEGLQ PAAKAGTEDE LVAHWRRYSA TRAALASEEP RVDRLQAQLK 400
    ELIVFPHNLK PLSDSVIATI QEYQSLKVKS ARLRNAAAVE LWQHFQRPLQ 450
    DLQLWKALAQ RLLEVTASLP DLPSLHTFLP QIEAALMESS RLKELLTMLQ 500
    LKKDLLIGIF GQERATALLE QVAGSMRDRD LLHNSLLQRK SKLQSLLAQH 550
    KDFGAAFEPL QRKLLDLQVR VQAEKGLQRD LPGKQAQLSR LQGLQEEGLD 600
    LGAQMEAARP LVQENPNHQH KMDQLSSDFQ ALQRSLEDLV DRCRQSVQEH 650
    CTFSHQLLEL RQWIVVTTQK LEAHRGEAGP GDAESQEAEF ERLVAEFPEK 700
    EAQLSLVEAQ GWLVMEKSSP EGAAVVQEEL RELAESWRAL RLLEESLLSL 750
    IRNWHLQRME VDSGKKMVFT NNIPKSGFLI NPMDPIPRHR RRANLLQEEE 800
    GSHEDFSQLL RNFGQWLQVE NSKLVRIIAM RTSTAEDLRT RKSKLQELEA 850
    RVPEGQHLFE NLLRLGPARG TSDELEDLRY QWMLYKSKLK DSGHLLTQSS 900
    PGEPTGFQKT RRWRGLGSLF RRACCVALPL QLLLLLFLLL LFLLPIREED 950
    RSCTLANNFA RSFTLMLRYN GPPPT 975
    Length:975
    Mass (Da):112,216
    Last modified:March 20, 2007 - v2
    Checksum:iA409AF86E1E781F4
    GO
    Isoform 2 (identifier: Q6ZMZ3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         793-797: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:970
    Mass (Da):111,677
    Checksum:i1A0FB44FD60A578D
    GO
    Isoform 3 (identifier: Q6ZMZ3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         593-596: GLQE → VRGL
         597-975: Missing.

    Show »
    Length:596
    Mass (Da):68,582
    Checksum:i093499D5CF2671F4
    GO

    Sequence cautioni

    The sequence BAC05312.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD18582.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAD62365.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti668 – 6681T → M.2 Publications
    Corresponds to variant rs9671369 [ dbSNP | Ensembl ].
    VAR_031231
    Natural varianti795 – 7951Missing.1 Publication
    Corresponds to variant rs76499929 [ dbSNP | Ensembl ].
    VAR_068433
    Natural varianti864 – 8641R → H.
    Corresponds to variant rs17092216 [ dbSNP | Ensembl ].
    VAR_031232
    Natural varianti923 – 9231A → V.1 Publication
    Corresponds to variant rs12434757 [ dbSNP | Ensembl ].
    VAR_031233
    Natural varianti946 – 9461I → V.
    Corresponds to variant rs10130647 [ dbSNP | Ensembl ].
    VAR_031234

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei593 – 5964GLQE → VRGL in isoform 3. 1 PublicationVSP_023976
    Alternative sequencei597 – 975379Missing in isoform 3. 1 PublicationVSP_023977Add
    BLAST
    Alternative sequencei793 – 7975Missing in isoform 2. 1 PublicationVSP_023978

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248076 mRNA. Translation: CAD62365.1. Different initiation.
    AL138539 Genomic DNA. No translation available.
    BC146604 mRNA. Translation: AAI46605.1.
    AK098471 mRNA. Translation: BAC05312.1. Different initiation.
    AK131436 mRNA. Translation: BAD18582.1. Different initiation.
    CCDSiCCDS9935.1. [Q6ZMZ3-1]
    RefSeqiNP_689805.3. NM_152592.3. [Q6ZMZ3-1]
    XP_005267433.1. XM_005267376.2. [Q6ZMZ3-1]
    XP_005267434.1. XM_005267377.1. [Q6ZMZ3-1]
    XP_006720126.1. XM_006720063.1. [Q6ZMZ3-1]
    XP_006720127.1. XM_006720064.1. [Q6ZMZ3-2]
    UniGeneiHs.354645.

    Genome annotation databases

    EnsembliENST00000334258; ENSP00000334308; ENSG00000176438. [Q6ZMZ3-1]
    ENST00000553340; ENSP00000450774; ENSG00000176438. [Q6ZMZ3-3]
    ENST00000557275; ENSP00000450562; ENSG00000176438. [Q6ZMZ3-2]
    GeneIDi161176.
    KEGGihsa:161176.
    UCSCiuc001yei.4. human. [Q6ZMZ3-1]
    uc001yej.1. human. [Q6ZMZ3-3]
    uc010avi.3. human. [Q6ZMZ3-2]

    Polymorphism databases

    DMDMi134035037.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248076 mRNA. Translation: CAD62365.1 . Different initiation.
    AL138539 Genomic DNA. No translation available.
    BC146604 mRNA. Translation: AAI46605.1 .
    AK098471 mRNA. Translation: BAC05312.1 . Different initiation.
    AK131436 mRNA. Translation: BAD18582.1 . Different initiation.
    CCDSi CCDS9935.1. [Q6ZMZ3-1 ]
    RefSeqi NP_689805.3. NM_152592.3. [Q6ZMZ3-1 ]
    XP_005267433.1. XM_005267376.2. [Q6ZMZ3-1 ]
    XP_005267434.1. XM_005267377.1. [Q6ZMZ3-1 ]
    XP_006720126.1. XM_006720063.1. [Q6ZMZ3-1 ]
    XP_006720127.1. XM_006720064.1. [Q6ZMZ3-2 ]
    UniGenei Hs.354645.

    3D structure databases

    ProteinModelPortali Q6ZMZ3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000334308.

    PTM databases

    PhosphoSitei Q6ZMZ3.

    Polymorphism databases

    DMDMi 134035037.

    Proteomic databases

    MaxQBi Q6ZMZ3.
    PaxDbi Q6ZMZ3.
    PRIDEi Q6ZMZ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334258 ; ENSP00000334308 ; ENSG00000176438 . [Q6ZMZ3-1 ]
    ENST00000553340 ; ENSP00000450774 ; ENSG00000176438 . [Q6ZMZ3-3 ]
    ENST00000557275 ; ENSP00000450562 ; ENSG00000176438 . [Q6ZMZ3-2 ]
    GeneIDi 161176.
    KEGGi hsa:161176.
    UCSCi uc001yei.4. human. [Q6ZMZ3-1 ]
    uc001yej.1. human. [Q6ZMZ3-3 ]
    uc010avi.3. human. [Q6ZMZ3-2 ]

    Organism-specific databases

    CTDi 161176.
    GeneCardsi GC14M095884.
    H-InvDB HIX0011939.
    HGNCi HGNC:19861. SYNE3.
    HPAi HPA055227.
    MIMi 610861. gene.
    neXtProti NX_Q6ZMZ3.
    PharmGKBi PA134931380.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145316.
    HOGENOMi HOG000154475.
    HOVERGENi HBG094014.
    InParanoidi Q6ZMZ3.
    OMAi IKAQWEE.
    OrthoDBi EOG7XM2X7.
    PhylomeDBi Q6ZMZ3.
    TreeFami TF331132.

    Miscellaneous databases

    GenomeRNAii 161176.
    NextBioi 88029.
    PROi Q6ZMZ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZMZ3.
    Bgeei Q6ZMZ3.
    CleanExi HS_C14orf49.
    Genevestigatori Q6ZMZ3.

    Family and domain databases

    InterProi IPR012315. KASH.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF10541. KASH. 1 hit.
    PF00435. Spectrin. 1 hit.
    [Graphical view ]
    SMARTi SM00150. SPEC. 3 hits.
    [Graphical view ]
    PROSITEi PS51049. KASH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: B-cell.
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1), VARIANTS MET-668 AND LEU-795 DEL.
    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 41-975 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-975 (ISOFORM 1), VARIANTS MET-668 AND VAL-923.
      Tissue: Synovial cell and Thyroid.
    5. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin."
      Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H., van den Bout I., Raymond K., Sonnenberg A.
      J. Cell Biol. 171:799-810(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness."
      Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.
      Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH SUN1 AND SUN2.
    7. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
      Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
      J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOR1A.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Nesprin-3 regulates endothelial cell morphology, perinuclear cytoskeletal architecture, and flow-induced polarization."
      Morgan J.T., Pfeiffer E.R., Thirkill T.L., Kumar P., Peng G., Fridolfsson H.N., Douglas G.C., Starr D.A., Barakat A.I.
      Mol. Biol. Cell 22:4324-4334(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. Cited for: INTERACTION WITH SYNE1.

    Entry informationi

    Entry nameiSYNE3_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZMZ3
    Secondary accession number(s): A6H8H3, Q86SX5, Q8N7G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 94 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 14
      Human chromosome 14: 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