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)

Q9UH99

- SUN2_HUMAN

UniProt

Q9UH99 - SUN2_HUMAN

Protein

SUN domain-containing protein 2

Gene

SUN2

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 131 (01 Oct 2014)
      Sequence version 3 (25 Mar 2003)
      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. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5.1 Publication

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. lamin binding Source: UniProtKB
    3. microtubule binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. centrosome localization Source: UniProtKB
    2. cytoskeletal anchoring at nuclear membrane Source: UniProtKB
    3. mitotic spindle organization Source: UniProtKB
    4. nuclear envelope organization Source: MGI
    5. nuclear matrix anchoring at nuclear membrane Source: UniProtKB
    6. nuclear migration Source: UniProtKB
    7. nuclear migration along microfilament Source: UniProtKB
    8. positive regulation of cell migration Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SUN domain-containing protein 2
    Alternative name(s):
    Protein unc-84 homolog B
    Rab5-interacting protein
    Short name:
    Rab5IP
    Sad1/unc-84 protein-like 2
    Gene namesi
    Name:SUN2
    Synonyms:FRIGG, KIAA0668, RAB5IP, UNC84B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:14210. SUN2.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: Ensembl
    2. endosome membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. nuclear chromosome, telomeric region Source: Ensembl
    5. nuclear envelope Source: UniProtKB
    6. nuclear inner membrane Source: UniProtKB-SubCell
    7. nuclear membrane Source: HPA
    8. SUN-KASH complex Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165378369.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 717717SUN domain-containing protein 2PRO_0000218913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine1 Publication
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei54 – 541Phosphoserine2 Publications
    Modified residuei116 – 1161Phosphoserine1 Publication
    Glycosylationi636 – 6361N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UH99.
    PaxDbiQ9UH99.
    PRIDEiQ9UH99.

    PTM databases

    PhosphoSiteiQ9UH99.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in heart, lung and muscle. Weakly expressed in fetal heart. Slightly overexpressed in some heart tissues form patients with congenital heart defects.2 Publications

    Gene expression databases

    ArrayExpressiQ9UH99.
    BgeeiQ9UH99.
    CleanExiHS_UNC84B.
    GenevestigatoriQ9UH99.

    Organism-specific databases

    HPAiHPA001209.

    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 SYNE1, SYNE2 and SYNE3. Interacts with A-type lamin. Interaction with lamins B1 and C is hardly detectable By similarity. Interacts with EMD and RAB5A. Interacts with TMEM43.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1044964,EBI-1044964
    COPB1P536182EBI-1044964,EBI-359063
    EMDP504023EBI-1044964,EBI-489887
    KPNA2P522923EBI-1044964,EBI-349938
    SYNE1Q8NF913EBI-1044964,EBI-928867
    SYNE1Q8NF91-12EBI-1044964,EBI-6170938
    SYNE2Q8WXH05EBI-1044964,EBI-2372294
    SYNE2Q8WXH0-12EBI-1044964,EBI-6170976

    Protein-protein interaction databases

    BioGridi117312. 15 interactions.
    IntActiQ9UH99. 18 interactions.
    MINTiMINT-3080157.

    Structurei

    Secondary structure

    1
    717
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi525 – 54016
    Turni541 – 5444
    Helixi552 – 5543
    Beta strandi557 – 5637
    Helixi571 – 5744
    Turni575 – 5773
    Beta strandi579 – 5846
    Helixi588 – 5925
    Beta strandi601 – 6055
    Beta strandi609 – 62719
    Helixi631 – 6333
    Helixi635 – 6373
    Beta strandi645 – 65511
    Beta strandi660 – 6667
    Beta strandi669 – 6713
    Beta strandi673 – 6786
    Beta strandi687 – 6948
    Beta strandi697 – 6993
    Beta strandi701 – 7066
    Beta strandi708 – 7147

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNPX-ray2.39A520-717[»]
    4DXRX-ray2.32A522-717[»]
    4DXSX-ray2.71A522-717[»]
    4DXTX-ray2.22A522-717[»]
    4FI9X-ray3.05A523-717[»]
    ProteinModelPortaliQ9UH99.
    SMRiQ9UH99. Positions 522-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 212212Nuclear1 PublicationAdd
    BLAST
    Topological domaini234 – 717484Perinuclear space1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei213 – 23321HelicalAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini555 – 716162SUNPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 139139LMNA-bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili273 – 29624Sequence AnalysisAdd
    BLAST
    Coiled coili348 – 44093Sequence AnalysisAdd
    BLAST
    Coiled coili475 – 50632Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 164163Ser-richAdd
    BLAST
    Compositional biasi100 – 1056Poly-Arg
    Compositional biasi316 – 3227Poly-Gly
    Compositional biasi468 – 4714Poly-Gly

    Domaini

    The SUN domain may play a role in the nuclear anchoring and/or migration.

    Sequence similaritiesi

    Contains 1 SUN domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG285464.
    HOGENOMiHOG000253025.
    HOVERGENiHBG056957.
    OMAiVGTTWYR.
    OrthoDBiEOG7J446H.
    PhylomeDBiQ9UH99.
    TreeFamiTF323915.

    Family and domain databases

    InterProiIPR012919. Sad1_UNC_C.
    [Graphical view]
    PfamiPF07738. Sad1_UNC. 1 hit.
    [Graphical view]
    PROSITEiPS51469. SUN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UH99-1) [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

    MSRRSQRLTR YSQGDDDGSS SSGGSSVAGS QSTLFKDSPL RTLKRKSSNM    50
    KRLSPAPQLG PSSDAHTSYY SESLVHESWF PPRSSLEELH GDANWGEDLR 100
    VRRRRGTGGS ESSRASGLVG RKATEDFLGS SSGYSSEDDY VGYSDVDQQS 150
    SSSRLRSAVS RAGSLLWMVA TSPGRLFRLL YWWAGTTWYR LTTAASLLDV 200
    FVLTRRFSSL KTFLWFLLPL LLLTCLTYGA WYFYPYGLQT FHPALVSWWA 250
    AKDSRRPDEG WEARDSSPHF QAEQRVMSRV HSLERRLEAL AAEFSSNWQK 300
    EAMRLERLEL RQGAPGQGGG GGLSHEDTLA LLEGLVSRRE AALKEDFRRE 350
    TAARIQEELS ALRAEHQQDS EDLFKKIVRA SQESEARIQQ LKSEWQSMTQ 400
    ESFQESSVKE LRRLEDQLAG LQQELAALAL KQSSVAEEVG LLPQQIQAVR 450
    DDVESQFPAW ISQFLARGGG GRVGLLQREE MQAQLRELES KILTHVAEMQ 500
    GKSAREAAAS LSLTLQKEGV IGVTEEQVHH IVKQALQRYS EDRIGLADYA 550
    LESGGASVIS TRCSETYETK TALLSLFGIP LWYHSQSPRV ILQPDVHPGN 600
    CWAFQGPQGF AVVRLSARIR PTAVTLEHVP KALSPNSTIS SAPKDFAIFG 650
    FDEDLQQEGT LLGKFTYDQD GEPIQTFHFQ APTMATYQVV ELRILTNWGH 700
    PEYTCIYRFR VHGEPAH 717
    Length:717
    Mass (Da):80,311
    Last modified:March 25, 2003 - v3
    Checksum:iCCF43C118E935E84
    GO
    Isoform 2 (identifier: Q9UH99-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         141-141: V → VEDSEGRGSKVTETEPVSSFPA

    Note: No experimental confirmation available.

    Show »
    Length:738
    Mass (Da):82,502
    Checksum:iBD17ECBB9F58069B
    GO
    Isoform 3 (identifier: Q9UH99-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         683-717: TMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH → SSFPLCPWRLLPILGVCIYVAYHGGLGSWER

    Note: No experimental confirmation available.

    Show »
    Length:713
    Mass (Da):79,612
    Checksum:i1D110119E43E562C
    GO

    Sequence cautioni

    The sequence BAA31643.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti644 – 6441K → R in CAD97926. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331T → A.
    Corresponds to variant rs2072799 [ dbSNP | Ensembl ].
    VAR_052282
    Natural varianti89 – 891L → R.1 Publication
    Corresponds to variant rs35496634 [ dbSNP | Ensembl ].
    VAR_052283
    Natural varianti348 – 3481R → C.
    Corresponds to variant rs138708 [ dbSNP | Ensembl ].
    VAR_052284
    Natural varianti671 – 6711G → S.1 Publication
    Corresponds to variant rs2072797 [ dbSNP | Ensembl ].
    VAR_024624

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei141 – 1411V → VEDSEGRGSKVTETEPVSSF PA in isoform 2. 1 PublicationVSP_045882
    Alternative sequencei683 – 71735TMATY…GEPAH → SSFPLCPWRLLPILGVCIYV AYHGGLGSWER in isoform 3. 1 PublicationVSP_053702Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014568 mRNA. Translation: BAA31643.1. Different initiation.
    AY682988 mRNA. Translation: AAT90500.1.
    CR456474 mRNA. Translation: CAG30360.1.
    BX537962 mRNA. Translation: CAD97926.1.
    AL008583 Genomic DNA. No translation available.
    AL021806 Genomic DNA. No translation available.
    AL021707 Genomic DNA. Translation: CAI21604.1.
    AL021707 Genomic DNA. Translation: CAQ07913.1.
    BC030684 mRNA. Translation: AAH30684.2.
    BC094797 mRNA. Translation: AAH94797.1.
    BC111549 mRNA. Translation: AAI11550.1.
    BC111717 mRNA. Translation: AAI11718.1.
    AF202723 mRNA. Translation: AAF15887.1.
    CCDSiCCDS13978.1. [Q9UH99-1]
    CCDS56231.1. [Q9UH99-2]
    PIRiT00371.
    RefSeqiNP_001186508.1. NM_001199579.1. [Q9UH99-2]
    NP_001186509.1. NM_001199580.1. [Q9UH99-1]
    NP_056189.1. NM_015374.2. [Q9UH99-1]
    XP_005261558.1. XM_005261501.2. [Q9UH99-1]
    UniGeneiHs.517622.
    Hs.744734.

    Genome annotation databases

    EnsembliENST00000405018; ENSP00000385616; ENSG00000100242. [Q9UH99-2]
    ENST00000405510; ENSP00000385740; ENSG00000100242. [Q9UH99-1]
    ENST00000406622; ENSP00000383992; ENSG00000100242. [Q9UH99-1]
    GeneIDi25777.
    KEGGihsa:25777.
    UCSCiuc003awh.2. human. [Q9UH99-1]
    uc010gxq.2. human.

    Polymorphism databases

    DMDMi29337242.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014568 mRNA. Translation: BAA31643.1 . Different initiation.
    AY682988 mRNA. Translation: AAT90500.1 .
    CR456474 mRNA. Translation: CAG30360.1 .
    BX537962 mRNA. Translation: CAD97926.1 .
    AL008583 Genomic DNA. No translation available.
    AL021806 Genomic DNA. No translation available.
    AL021707 Genomic DNA. Translation: CAI21604.1 .
    AL021707 Genomic DNA. Translation: CAQ07913.1 .
    BC030684 mRNA. Translation: AAH30684.2 .
    BC094797 mRNA. Translation: AAH94797.1 .
    BC111549 mRNA. Translation: AAI11550.1 .
    BC111717 mRNA. Translation: AAI11718.1 .
    AF202723 mRNA. Translation: AAF15887.1 .
    CCDSi CCDS13978.1. [Q9UH99-1 ]
    CCDS56231.1. [Q9UH99-2 ]
    PIRi T00371.
    RefSeqi NP_001186508.1. NM_001199579.1. [Q9UH99-2 ]
    NP_001186509.1. NM_001199580.1. [Q9UH99-1 ]
    NP_056189.1. NM_015374.2. [Q9UH99-1 ]
    XP_005261558.1. XM_005261501.2. [Q9UH99-1 ]
    UniGenei Hs.517622.
    Hs.744734.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UNP X-ray 2.39 A 520-717 [» ]
    4DXR X-ray 2.32 A 522-717 [» ]
    4DXS X-ray 2.71 A 522-717 [» ]
    4DXT X-ray 2.22 A 522-717 [» ]
    4FI9 X-ray 3.05 A 523-717 [» ]
    ProteinModelPortali Q9UH99.
    SMRi Q9UH99. Positions 522-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117312. 15 interactions.
    IntActi Q9UH99. 18 interactions.
    MINTi MINT-3080157.

    PTM databases

    PhosphoSitei Q9UH99.

    Polymorphism databases

    DMDMi 29337242.

    Proteomic databases

    MaxQBi Q9UH99.
    PaxDbi Q9UH99.
    PRIDEi Q9UH99.

    Protocols and materials databases

    DNASUi 25777.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000405018 ; ENSP00000385616 ; ENSG00000100242 . [Q9UH99-2 ]
    ENST00000405510 ; ENSP00000385740 ; ENSG00000100242 . [Q9UH99-1 ]
    ENST00000406622 ; ENSP00000383992 ; ENSG00000100242 . [Q9UH99-1 ]
    GeneIDi 25777.
    KEGGi hsa:25777.
    UCSCi uc003awh.2. human. [Q9UH99-1 ]
    uc010gxq.2. human.

    Organism-specific databases

    CTDi 25777.
    GeneCardsi GC22M039418.
    H-InvDB HIX0159176.
    HGNCi HGNC:14210. SUN2.
    HPAi HPA001209.
    MIMi 613569. gene.
    neXtProti NX_Q9UH99.
    PharmGKBi PA165378369.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285464.
    HOGENOMi HOG000253025.
    HOVERGENi HBG056957.
    OMAi VGTTWYR.
    OrthoDBi EOG7J446H.
    PhylomeDBi Q9UH99.
    TreeFami TF323915.

    Enzyme and pathway databases

    Reactomei REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    ChiTaRSi SUN2. human.
    GeneWikii UNC84B.
    GenomeRNAii 25777.
    NextBioi 46920.
    PROi Q9UH99.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UH99.
    Bgeei Q9UH99.
    CleanExi HS_UNC84B.
    Genevestigatori Q9UH99.

    Family and domain databases

    InterProi IPR012919. Sad1_UNC_C.
    [Graphical view ]
    Pfami PF07738. Sad1_UNC. 1 hit.
    [Graphical view ]
    PROSITEi PS51469. SUN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion."
      Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E., Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.
      J. Biol. Chem. 275:24661-24669(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAB5A.
      Tissue: B-cell.
    2. "Characterization of the structures involved in localization of the SUN proteins to the nuclear envelope and the centrosome."
      Wang Q., Du X., Cai Z., Greene M.I.
      DNA Cell Biol. 25:554-562(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, SUBUNIT, ASSOCIATION WITH THE CENTROSOME.
    3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal kidney.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1; 2 AND 3), VARIANTS ARG-89 AND SER-671.
      Tissue: Brain and Pancreas.
    8. "UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development."
      Malone C.J., Fixsen W.D., Horvitz H.R., Han M.
      Development 126:3171-3181(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 278-717 (ISOFORM 1).
    9. "Isolation of differentially expressed genes in human heart tissues."
      Sun G., Yuen Chan S., Yuan Y., Wang Chan K., Qiu G., Sun K., Ping Leung M.
      Biochim. Biophys. Acta 1588:241-246(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate."
      Gronborg M., Kristiansen T.Z., Stensballe A., Andersen J.S., Ohara O., Mann M., Jensen O.N., Pandey A.
      Mol. Cell. Proteomics 1:517-527(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-12; SER-54 AND SER-116.
    11. "Nuclear membrane proteins with potential disease links found by subtractive proteomics."
      Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.
      Science 301:1380-1382(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    12. "Sun2 is a novel mammalian inner nuclear membrane protein."
      Hodzic D.M., Yeater D.B., Bengtsson L., Otto H., Stahl P.D.
      J. Biol. Chem. 279:25805-25812(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
    13. "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-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Functional association of Sun1 with nuclear pore complexes."
      Liu Q., Pante N., Misteli T., Elsagga M., Crisp M., Hodzic D., Burke B., Roux K.J.
      J. Cell Biol. 178:785-798(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. Cited for: INTERACTION WITH SUN1.
    16. "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: INTERACTION WITH SYNE1; SYNE2 AND SYNE3, FUNCTION OF THE LINC COMPLEXES.
    17. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-636.
      Tissue: Liver.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "TMEM43 mutations in Emery-Dreifuss muscular dystrophy-related myopathy."
      Liang W.C., Mitsuhashi H., Keduka E., Nonaka I., Noguchi S., Nishino I., Hayashi Y.K.
      Ann. Neurol. 69:1005-1013(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM43.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSUN2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UH99
    Secondary accession number(s): B0QY62
    , O75156, Q2NKN8, Q2T9F7, Q504T5, Q6B4H1, Q7Z3E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2002
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3