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O95859

- TSN12_HUMAN

UniProt

O95859 - TSN12_HUMAN

Protein

Tetraspanin-12

Gene

TSPAN12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) By similarity. Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity.By similarity2 Publications

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell surface receptor signaling pathway Source: UniProtKB
    3. regulation of angiogenesis Source: UniProtKB
    4. retina layer formation Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tetraspanin-12
    Short name:
    Tspan-12
    Alternative name(s):
    Tetraspan NET-2
    Transmembrane 4 superfamily member 12
    Gene namesi
    Name:TSPAN12
    Synonyms:NET2, TM4SF12
    ORF Names:UNQ774/PRO1568
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21641. TSPAN12.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: ProtInc
    2. integral component of plasma membrane Source: UniProtKB
    3. membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Vitreoretinopathy, exudative 5 (EVR5) [MIM:613310]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. TSPAN12 dominant and recessive mutations have been identified in patients with exudative vitreoretinopathy. Patients with mutations in both alleles of TSPAN12 have severe exudative vitreoretinopathy or retinal dysplasia. These mutations appear to result in a milder phenotype in heterozygous mutation carriers (PubMed:22427576).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491T → M in EVR5. 1 Publication
    VAR_068899
    Natural varianti101 – 1011L → H in EVR5. 1 Publication
    VAR_063576
    Natural varianti138 – 1381Y → C in EVR5. 1 Publication
    VAR_068900
    Natural varianti188 – 1881G → R in EVR5. 1 Publication
    VAR_063577
    Natural varianti210 – 2101M → R in EVR5. 1 Publication
    VAR_063578
    Natural varianti223 – 2231L → P in EVR5. 1 Publication
    VAR_068901
    Natural varianti237 – 2371A → P in EVR5. 1 Publication
    VAR_063579

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91C → S: Impairs interaction with ADAM10; when associated with S-12 and S-83. 1 Publication
    Mutagenesisi12 – 121C → S: Impairs interaction with ADAM10; when associated with S-9 and S-83. 1 Publication
    Mutagenesisi83 – 831C → S: Impairs interaction with ADAM10; when associated with S-9 and S-12. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613310. phenotype.
    Orphaneti891. Familial exudative vitreoretinopathy.
    PharmGKBiPA134954047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Tetraspanin-12PRO_0000219257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi9 – 91S-palmitoyl cysteineBy similarity
    Lipidationi12 – 121S-palmitoyl cysteineBy similarity
    Lipidationi83 – 831S-palmitoyl cysteineBy similarity

    Post-translational modificationi

    Palmitoylated; required for interaction with ADAM10. The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiO95859.
    PRIDEiO95859.

    PTM databases

    PhosphoSiteiO95859.

    Expressioni

    Gene expression databases

    ArrayExpressiO95859.
    BgeeiO95859.
    CleanExiHS_TSPAN12.
    GenevestigatoriO95859.

    Organism-specific databases

    HPAiHPA051570.

    Interactioni

    Subunit structurei

    Component of a complex, at least composed of TSPAN12, FZD4 and norrin (NDP) By similarity. Interacts (when palmitoylated) with ADAM10. Interacts with MMP14/MT1-MMP.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi117098. 1 interaction.
    IntActiO95859. 3 interactions.
    STRINGi9606.ENSP00000222747.

    Structurei

    3D structure databases

    ProteinModelPortaliO95859.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 5926ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini81 – 899CytoplasmicSequence Analysis
    Topological domaini111 – 224114ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini246 – 30560CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei60 – 8021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei90 – 11021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei225 – 24521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tetraspanin (TM4SF) family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG257008.
    HOGENOMiHOG000252919.
    HOVERGENiHBG054253.
    InParanoidiO95859.
    KOiK17355.
    OMAiTYEQEIM.
    OrthoDBiEOG7SFHX2.
    PhylomeDBiO95859.
    TreeFamiTF316345.

    Family and domain databases

    InterProiIPR000301. Tetraspanin.
    IPR018499. Tetraspanin/Peripherin.
    IPR018503. Tetraspanin_CS.
    IPR008952. Tetraspanin_EC2.
    [Graphical view]
    PfamiPF00335. Tetraspannin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002419. Tetraspanin. 1 hit.
    PRINTSiPR00259. TMFOUR.
    SUPFAMiSSF48652. SSF48652. 1 hit.
    PROSITEiPS00421. TM4_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95859-1) [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

    MAREDSVKCL RCLLYALNLL FWLMSISVLA VSAWMRDYLN NVLTLTAETR    50
    VEEAVILTYF PVVHPVMIAV CCFLIIVGML GYCGTVKRNL LLLAWYFGSL 100
    LVIFCVELAC GVWTYEQELM VPVQWSDMVT LKARMTNYGL PRYRWLTHAW 150
    NFFQREFKCC GVVYFTDWLE MTEMDWPPDS CCVREFPGCS KQAHQEDLSD 200
    LYQEGCGKKM YSFLRGTKQL QVLRFLGISI GVTQILAMIL TITLLWALYY 250
    DRREPGTDQM MSLKNDNSQH LSCPSVELLK PSLSRIFEHT SMANSFNTHF 300
    EMEEL 305
    Length:305
    Mass (Da):35,383
    Last modified:May 1, 1999 - v1
    Checksum:iEBF4D5E1371E92DC
    GO
    Isoform 2 (identifier: O95859-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-120: MAREDSVKCL...GVWTYEQELM → MAHKLLL

    Note: No experimental confirmation available.

    Show »
    Length:192
    Mass (Da):22,511
    Checksum:iE789CE4F377F3F17
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491T → M in EVR5. 1 Publication
    VAR_068899
    Natural varianti57 – 571L → S.1 Publication
    Corresponds to variant rs17852934 [ dbSNP | Ensembl ].
    VAR_062253
    Natural varianti101 – 1011L → H in EVR5. 1 Publication
    VAR_063576
    Natural varianti138 – 1381Y → C in EVR5. 1 Publication
    VAR_068900
    Natural varianti188 – 1881G → R in EVR5. 1 Publication
    VAR_063577
    Natural varianti210 – 2101M → R in EVR5. 1 Publication
    VAR_063578
    Natural varianti223 – 2231L → P in EVR5. 1 Publication
    VAR_068901
    Natural varianti237 – 2371A → P in EVR5. 1 Publication
    VAR_063579

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 120120MARED…EQELM → MAHKLLL in isoform 2. 1 PublicationVSP_038525Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124522 mRNA. Translation: AAD17317.1.
    AY358703 mRNA. Translation: AAQ89066.1.
    AK299247 mRNA. Translation: BAG61278.1.
    AK312239 mRNA. Translation: BAG35172.1.
    AC004456 Genomic DNA. Translation: AAQ96879.1.
    CH236947 Genomic DNA. Translation: EAL24349.1.
    BC031265 mRNA. Translation: AAH31265.1.
    CCDSiCCDS5777.1. [O95859-1]
    RefSeqiNP_036470.1. NM_012338.3. [O95859-1]
    XP_005250296.1. XM_005250239.1. [O95859-1]
    UniGeneiHs.16529.

    Genome annotation databases

    EnsembliENST00000222747; ENSP00000222747; ENSG00000106025. [O95859-1]
    ENST00000415871; ENSP00000397699; ENSG00000106025. [O95859-1]
    GeneIDi23554.
    KEGGihsa:23554.
    UCSCiuc003vjk.3. human. [O95859-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124522 mRNA. Translation: AAD17317.1 .
    AY358703 mRNA. Translation: AAQ89066.1 .
    AK299247 mRNA. Translation: BAG61278.1 .
    AK312239 mRNA. Translation: BAG35172.1 .
    AC004456 Genomic DNA. Translation: AAQ96879.1 .
    CH236947 Genomic DNA. Translation: EAL24349.1 .
    BC031265 mRNA. Translation: AAH31265.1 .
    CCDSi CCDS5777.1. [O95859-1 ]
    RefSeqi NP_036470.1. NM_012338.3. [O95859-1 ]
    XP_005250296.1. XM_005250239.1. [O95859-1 ]
    UniGenei Hs.16529.

    3D structure databases

    ProteinModelPortali O95859.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117098. 1 interaction.
    IntActi O95859. 3 interactions.
    STRINGi 9606.ENSP00000222747.

    PTM databases

    PhosphoSitei O95859.

    Proteomic databases

    PaxDbi O95859.
    PRIDEi O95859.

    Protocols and materials databases

    DNASUi 23554.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222747 ; ENSP00000222747 ; ENSG00000106025 . [O95859-1 ]
    ENST00000415871 ; ENSP00000397699 ; ENSG00000106025 . [O95859-1 ]
    GeneIDi 23554.
    KEGGi hsa:23554.
    UCSCi uc003vjk.3. human. [O95859-1 ]

    Organism-specific databases

    CTDi 23554.
    GeneCardsi GC07M120427.
    GeneReviewsi TSPAN12.
    HGNCi HGNC:21641. TSPAN12.
    HPAi HPA051570.
    MIMi 613138. gene.
    613310. phenotype.
    neXtProti NX_O95859.
    Orphaneti 891. Familial exudative vitreoretinopathy.
    PharmGKBi PA134954047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257008.
    HOGENOMi HOG000252919.
    HOVERGENi HBG054253.
    InParanoidi O95859.
    KOi K17355.
    OMAi TYEQEIM.
    OrthoDBi EOG7SFHX2.
    PhylomeDBi O95859.
    TreeFami TF316345.

    Miscellaneous databases

    GeneWikii TSPAN12.
    GenomeRNAii 23554.
    NextBioi 46116.
    PROi O95859.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95859.
    Bgeei O95859.
    CleanExi HS_TSPAN12.
    Genevestigatori O95859.

    Family and domain databases

    InterProi IPR000301. Tetraspanin.
    IPR018499. Tetraspanin/Peripherin.
    IPR018503. Tetraspanin_CS.
    IPR008952. Tetraspanin_EC2.
    [Graphical view ]
    Pfami PF00335. Tetraspannin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002419. Tetraspanin. 1 hit.
    PRINTSi PR00259. TMFOUR.
    SUPFAMi SSF48652. SSF48652. 1 hit.
    PROSITEi PS00421. TM4_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Adrenal gland and Teratocarcinoma.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANT SER-57.
      Tissue: Brain.
    7. "Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein."
      Xu D., Sharma C., Hemler M.E.
      FASEB J. 23:3674-3681(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAM10, PALMITOYLATION, MUTAGENESIS OF CYS-9; CYS-12 AND CYS-83.
    8. "Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase-dependent pericellular proteolysis."
      Lafleur M.A., Xu D., Hemler M.E.
      Mol. Biol. Cell 20:2030-2040(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Next-generation sequencing of a 40 Mb linkage interval reveals TSPAN12 mutations in patients with familial exudative vitreoretinopathy."
      Nikopoulos K., Gilissen C., Hoischen A., van Nouhuys C.E., Boonstra F.N., Blokland E.A., Arts P., Wieskamp N., Strom T.M., Ayuso C., Tilanus M.A., Bouwhuis S., Mukhopadhyay A., Scheffer H., Hoefsloot L.H., Veltman J.A., Cremers F.P., Collin R.W.
      Am. J. Hum. Genet. 86:240-247(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EVR5 ARG-188 AND PRO-237.
    10. Cited for: VARIANTS EVR5 HIS-101 AND ARG-210.
    11. Cited for: VARIANTS EVR5 MET-49; CYS-138 AND PRO-223.

    Entry informationi

    Entry nameiTSN12_HUMAN
    AccessioniPrimary (citable) accession number: O95859
    Secondary accession number(s): A4D0V8
    , B4DRG6, Q549U9, Q8N5Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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 7
      Human chromosome 7: 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