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P24821

- TENA_HUMAN

UniProt

P24821 - TENA_HUMAN

Protein

Tenascin

Gene

TNC

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 172 (01 Oct 2014)
      Sequence version 3 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.

    GO - Molecular functioni

    1. syndecan binding Source: MGI

    GO - Biological processi

    1. bud outgrowth involved in lung branching Source: Ensembl
    2. cell adhesion Source: ProtInc
    3. cellular response to prostaglandin D stimulus Source: Ensembl
    4. cellular response to retinoic acid Source: Ensembl
    5. cellular response to vitamin D Source: Ensembl
    6. extracellular matrix organization Source: Reactome
    7. mesenchymal-epithelial cell signaling involved in prostate gland development Source: Ensembl
    8. negative regulation of cell adhesion Source: Ensembl
    9. neuromuscular junction development Source: Ensembl
    10. odontogenesis of dentin-containing tooth Source: Ensembl
    11. osteoblast differentiation Source: UniProt
    12. peripheral nervous system axon regeneration Source: Ensembl
    13. positive regulation of cell proliferation Source: Ensembl
    14. positive regulation of gene expression Source: Ensembl
    15. prostate gland epithelium morphogenesis Source: Ensembl
    16. response to ethanol Source: Ensembl
    17. response to fibroblast growth factor Source: Ensembl
    18. response to mechanical stimulus Source: Ensembl
    19. response to wounding Source: BHF-UCL
    20. wound healing Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tenascin
    Short name:
    TN
    Alternative name(s):
    Cytotactin
    GMEM
    GP 150-225
    Glioma-associated-extracellular matrix antigen
    Hexabrachion
    JI
    Myotendinous antigen
    Neuronectin
    Tenascin-C
    Short name:
    TN-C
    Gene namesi
    Name:TNC
    Synonyms:HXB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:5318. TNC.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. interstitial matrix Source: Ensembl
    5. membrane Source: UniProt

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Deafness, autosomal dominant, 56 (DFNA56) [MIM:615629]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA56 is characterized by progressive hearing impairment with post-lingual onset.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1773 – 17731V → M in DFNA56. 1 Publication
    VAR_070984
    Natural varianti1796 – 17961T → S in DFNA56. 1 Publication
    VAR_070985

    Keywords - Diseasei

    Deafness, Disease mutation, Non-syndromic deafness

    Organism-specific databases

    MIMi615629. phenotype.
    Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    PharmGKBiPA35103.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 22012179TenascinPRO_0000007741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
    Disulfide bondi190 ↔ 200By similarity
    Disulfide bondi194 ↔ 205By similarity
    Disulfide bondi207 ↔ 216By similarity
    Disulfide bondi221 ↔ 231By similarity
    Disulfide bondi225 ↔ 236By similarity
    Disulfide bondi238 ↔ 247By similarity
    Disulfide bondi252 ↔ 263By similarity
    Disulfide bondi256 ↔ 268By similarity
    Disulfide bondi270 ↔ 279By similarity
    Disulfide bondi284 ↔ 294By similarity
    Disulfide bondi288 ↔ 299By similarity
    Disulfide bondi301 ↔ 310By similarity
    Disulfide bondi315 ↔ 325By similarity
    Disulfide bondi319 ↔ 330By similarity
    Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi332 ↔ 341By similarity
    Disulfide bondi346 ↔ 356By similarity
    Disulfide bondi350 ↔ 361By similarity
    Disulfide bondi363 ↔ 372By similarity
    Disulfide bondi377 ↔ 387By similarity
    Disulfide bondi381 ↔ 392By similarity
    Disulfide bondi394 ↔ 403By similarity
    Disulfide bondi408 ↔ 418By similarity
    Disulfide bondi412 ↔ 423By similarity
    Disulfide bondi425 ↔ 434By similarity
    Disulfide bondi439 ↔ 449By similarity
    Disulfide bondi443 ↔ 454By similarity
    Disulfide bondi456 ↔ 465By similarity
    Disulfide bondi470 ↔ 480By similarity
    Disulfide bondi474 ↔ 485By similarity
    Disulfide bondi487 ↔ 496By similarity
    Disulfide bondi501 ↔ 511By similarity
    Disulfide bondi505 ↔ 516By similarity
    Disulfide bondi518 ↔ 527By similarity
    Disulfide bondi532 ↔ 542By similarity
    Disulfide bondi536 ↔ 547By similarity
    Disulfide bondi549 ↔ 558By similarity
    Disulfide bondi563 ↔ 573By similarity
    Disulfide bondi567 ↔ 578By similarity
    Disulfide bondi580 ↔ 589By similarity
    Disulfide bondi594 ↔ 604By similarity
    Disulfide bondi598 ↔ 609By similarity
    Disulfide bondi611 ↔ 620By similarity
    Glycosylationi788 – 7881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1018 – 10181N-linked (GlcNAc...)1 Publication
    Glycosylationi1034 – 10341N-linked (GlcNAc...)1 Publication
    Glycosylationi1079 – 10791N-linked (GlcNAc...)1 Publication
    Glycosylationi1093 – 10931N-linked (GlcNAc...)1 Publication
    Glycosylationi1119 – 11191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1184 – 11841N-linked (GlcNAc...)1 Publication
    Glycosylationi1210 – 12101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1261 – 12611N-linked (GlcNAc...)1 Publication
    Glycosylationi1275 – 12751N-linked (GlcNAc...)1 Publication
    Glycosylationi1301 – 13011N-linked (GlcNAc...)2 Publications
    Glycosylationi1366 – 13661N-linked (GlcNAc...)1 Publication
    Glycosylationi1392 – 13921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1445 – 14451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1455 – 14551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1485 – 14851N-linked (GlcNAc...)2 Publications
    Glycosylationi1534 – 15341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1809 – 18091N-linked (GlcNAc...)1 Publication
    Glycosylationi2162 – 21621N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP24821.
    PaxDbiP24821.
    PRIDEiP24821.

    PTM databases

    PhosphoSiteiP24821.

    Expressioni

    Inductioni

    By TGFB1.

    Gene expression databases

    ArrayExpressiP24821.
    BgeeiP24821.
    CleanExiHS_TNC.
    GenevestigatoriP24821.

    Organism-specific databases

    HPAiCAB004592.
    HPA004823.

    Interactioni

    Subunit structurei

    Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule. Interacts with CSPG4.1 Publication

    Protein-protein interaction databases

    BioGridi109602. 3 interactions.
    STRINGi9606.ENSP00000265131.

    Structurei

    Secondary structure

    1
    2201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi807 – 8137
    Beta strandi819 – 8246
    Helixi827 – 8293
    Beta strandi831 – 8399
    Beta strandi842 – 8443
    Beta strandi847 – 8526
    Beta strandi857 – 8604
    Beta strandi868 – 87710
    Beta strandi885 – 8906

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TENX-ray1.80A802-891[»]
    2RB8X-ray1.45A802-893[»]
    2RBLX-ray2.10A/B/M802-893[»]
    ProteinModelPortaliP24821.
    SMRiP24821. Positions 135-1976, 1980-2189.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24821.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini174 – 18613EGF-like 1; incompletePROSITE-ProRule annotationAdd
    BLAST
    Domaini186 – 21732EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 24832EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini248 – 28033EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 31132EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini311 – 34232EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 37332EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini373 – 40432EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 43532EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini435 – 46632EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini466 – 49732EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini497 – 52832EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 55932EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini559 – 59032EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 62132EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 71591Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini716 – 80489Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini805 – 89490Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini895 – 99096Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini991 – 107585Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1076 – 116590Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1167 – 125690Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1258 – 135093Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1351 – 143989Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1440 – 153192Fibronectin type-III 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1533 – 162189Fibronectin type-III 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1622 – 171190Fibronectin type-III 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1712 – 180190Fibronectin type-III 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1802 – 188887Fibronectin type-III 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1889 – 197789Fibronectin type-III 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1975 – 2190216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili118 – 14528Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tenascin family.Curated
    Contains 15 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
    Contains 15 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG008949.
    InParanoidiP24821.
    KOiK06252.
    OMAiGCCLQPA.
    OrthoDBiEOG7X9G60.
    PhylomeDBiP24821.
    TreeFamiTF329915.

    Family and domain databases

    Gene3Di2.60.40.10. 15 hits.
    3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR013111. EGF_extracell.
    IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF07974. EGF_2. 7 hits.
    PF00147. Fibrinogen_C. 1 hit.
    PF00041. fn3. 15 hits.
    PF12661. hEGF. 3 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 12 hits.
    SM00186. FBG. 1 hit.
    SM00060. FN3. 15 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 12 hits.
    SSF56496. SSF56496. 1 hit.
    PROSITEiPS00022. EGF_1. 15 hits.
    PS01186. EGF_2. 15 hits.
    PS50026. EGF_3. 5 hits.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    PS50853. FN3. 15 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Isoforms are produced in a tissue- and time-specific manner during development.

    Isoform 1 (identifier: P24821-1) [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

    MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF     50
    NHVYNIKLPV GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF 100
    THRINIPRRA CGCAAAPDVK ELLSRLEELE NLVSSLREQC TAGAGCCLQP 150
    ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW KGPNCSEPEC PGNCHLRGRC 200
    IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE GYAGADCSRE 250
    ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV 300
    CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC 350
    HTQGRCEEGQ CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG 400
    ADCGELKCPN GCSGHGRCVN GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV 450
    EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC VNGMCVCDDG YTGEDCRDRQ 500
    CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG RCVNGQCVCH 550
    EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN 600
    LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT 650
    EYLVVYTPTH EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK 700
    SIPVSARVAT YLPAPEGLKF KSIKETSVEV EWDPLDIAFE TWEIIFRNMN 750
    KEDEGEITKS LRRPETSYRQ TGLAPGQEYE ISLHIVKNNT RGPGLKRVTT 800
    TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK DVPGDRTTID 850
    LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR 900
    RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT 950
    TLTGLRPGTE YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS 1000
    LTLLWKTPLA KFDRYRLNYS LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN 1050
    VLLTAEKGRH KSKPARVKAS TEQAPELENL TVTEVGWDGL RLNWTAADQA 1100
    YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY TVSIYGVIQG 1150
    YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ 1200
    EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE 1250
    VLTEEVPDMG NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH 1300
    NLTVPGSLRS MEIPGLRAGT PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL 1350
    GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ VQEVNKVEAA QNLTLPGSLR 1400
    AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAKEPE IGNLNVSDIT 1450
    PESFNLSWMA TDGIFETFTI EIIDSNRLLE TVEYNISGAE RTAHISGLPP 1500
    STDFIVYLSG LAPSIRTKTI SATATTEALP LLENLTISDI NPYGFTVSWM 1550
    ASENAFDSFL VTVVDSGKLL DPQEFTLSGT QRKLELRGLI TGIGYEVMVS 1600
    GFTQGHQTKP LRAEIVTEAE PEVDNLLVSD ATPDGFRLSW TADEGVFDNF 1650
    VLKIRDTKKQ SEPLEITLLA PERTRDITGL REATEYEIEL YGISKGRRSQ 1700
    TVSAIATTAM GSPKEVIFSD ITENSATVSW RAPTAQVESF RITYVPITGG 1750
    TPSMVTVDGT KTQTRLVKLI PGVEYLVSII AMKGFEESEP VSGSFTTALD 1800
    GPSGLVTANI TDSEALARWQ PAIATVDSYV ISYTGEKVPE ITRTVSGNTV 1850
    EYALTDLEPA TEYTLRIFAE KGPQKSSTIT AKFTTDLDSP RDLTATEVQS 1900
    ETALLTWRPP RASVTGYLLV YESVDGTVKE VIVGPDTTSY SLADLSPSTH 1950
    YTAKIQALNG PLRSNMIQTI FTTIGLLYPF PKDCSQAMLN GDTTSGLYTI 2000
    YLNGDKAEAL EVFCDMTSDG GGWIVFLRRK NGRENFYQNW KAYAAGFGDR 2050
    REEFWLGLDN LNKITAQGQY ELRVDLRDHG ETAFAVYDKF SVGDAKTRYK 2100
    LKVEGYSGTA GDSMAYHNGR SFSTFDKDTD SAITNCALSY KGAFWYRNCH 2150
    RVNLMGRYGD NNHSQGVNWF HWKGHEHSIQ FAEMKLRPSN FRNLEGRRKR 2200
    A 2201
    Length:2,201
    Mass (Da):240,853
    Last modified:December 15, 2009 - v3
    Checksum:iB2BEF378AA6F1D85
    GO
    Isoform 2 (identifier: P24821-2) [UniParc]FASTAAdd to Basket

    Also known as: HT-5

    The sequence of this isoform differs from the canonical sequence as follows:
         1072-1435: Missing.
         1527-1617: Missing.

    Show »
    Length:1,746
    Mass (Da):191,373
    Checksum:i588B877CF66A227D
    GO
    Isoform 3 (identifier: P24821-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1072-1435: Missing.

    Show »
    Length:1,837
    Mass (Da):201,359
    Checksum:i54B916A3A6664FDE
    GO
    Isoform 4 (identifier: P24821-4) [UniParc]FASTAAdd to Basket

    Also known as: HT-33

    The sequence of this isoform differs from the canonical sequence as follows:
         1527-1617: Missing.

    Show »
    Length:2,110
    Mass (Da):230,867
    Checksum:i379795176A2B7252
    GO
    Isoform 5 (identifier: P24821-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1072-1617: Missing.

    Show »
    Length:1,655
    Mass (Da):181,528
    Checksum:iFA3D6624965AE06A
    GO
    Isoform 6 (identifier: P24821-6) [UniParc]FASTAAdd to Basket

    Also known as: P31

    The sequence of this isoform differs from the canonical sequence as follows:
         1072-1708: Missing.

    Show »
    Length:1,564
    Mass (Da):171,360
    Checksum:iB240934A9414ABC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441Missing in CAA39628. (PubMed:1707164)Curated
    Sequence conflicti370 – 3701V → L no nucleotide entry (PubMed:1704365)Curated
    Sequence conflicti370 – 3701V → L in AAA88083. (PubMed:1719530)Curated
    Sequence conflicti370 – 3701V → L in CAA55309. (PubMed:7531707)Curated
    Sequence conflicti1066 – 10661R → H no nucleotide entry (PubMed:1704365)Curated
    Sequence conflicti1066 – 10661R → H in AAA88083. (PubMed:1719530)Curated
    Sequence conflicti1066 – 10661R → H in AAA52703. (PubMed:2466295)Curated
    Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN no nucleotide entry (PubMed:1704365)Curated
    Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN in AAA88083. (PubMed:1719530)Curated
    Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN in AAA52703. (PubMed:2466295)Curated
    Sequence conflicti2054 – 20541F → FLH no nucleotide entry (PubMed:1704365)Curated
    Sequence conflicti2054 – 20541F → FLH in AAA88083. (PubMed:1719530)Curated
    Sequence conflicti2055 – 20551W → L in AAA52703. (PubMed:2466295)Curated
    Sequence conflicti2140 – 21434YKGA → TRG in CAA39628. (PubMed:1707164)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131G → S.
    Corresponds to variant rs7020958 [ dbSNP | Ensembl ].
    VAR_055778
    Natural varianti539 – 5391Q → R.3 Publications
    Corresponds to variant rs1757095 [ dbSNP | Ensembl ].
    VAR_024266
    Natural varianti605 – 6051V → I.
    Corresponds to variant rs3827816 [ dbSNP | Ensembl ].
    VAR_024267
    Natural varianti680 – 6801Q → R.1 Publication
    Corresponds to variant rs1061494 [ dbSNP | Ensembl ].
    VAR_024268
    Natural varianti850 – 8501D → H.
    Corresponds to variant rs3748169 [ dbSNP | Ensembl ].
    VAR_055779
    Natural varianti1677 – 16771I → L.4 Publications
    Corresponds to variant rs2104772 [ dbSNP | Ensembl ].
    VAR_060738
    Natural varianti1773 – 17731V → M in DFNA56. 1 Publication
    VAR_070984
    Natural varianti1781 – 17811A → T.
    Corresponds to variant rs2274750 [ dbSNP | Ensembl ].
    VAR_020169
    Natural varianti1796 – 17961T → S in DFNA56. 1 Publication
    VAR_070985
    Natural varianti2008 – 20081E → Q.5 Publications
    Corresponds to variant rs13321 [ dbSNP | Ensembl ].
    VAR_014665

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1072 – 1708637Missing in isoform 6. 1 PublicationVSP_001415Add
    BLAST
    Alternative sequencei1072 – 1617546Missing in isoform 5. 1 PublicationVSP_001414Add
    BLAST
    Alternative sequencei1072 – 1435364Missing in isoform 2 and isoform 3. 1 PublicationVSP_001412Add
    BLAST
    Alternative sequencei1527 – 161791Missing in isoform 2 and isoform 4. 1 PublicationVSP_001413Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55618 mRNA. Translation: AAA88083.1.
    X56160 mRNA. Translation: CAA39628.1.
    X78565 mRNA. Translation: CAA55309.1.
    AL162425 Genomic DNA. Translation: CAI15110.1.
    X80280 mRNA. No translation available.
    M24630 mRNA. Translation: AAA52703.1.
    CCDSiCCDS6811.1. [P24821-1]
    PIRiI38337. A32160.
    RefSeqiNP_002151.2. NM_002160.3. [P24821-1]
    XP_005252029.1. XM_005251972.1. [P24821-4]
    XP_005252031.1. XM_005251974.1. [P24821-5]
    XP_005252032.1. XM_005251975.1. [P24821-6]
    UniGeneiHs.143250.
    Hs.734766.

    Genome annotation databases

    EnsembliENST00000350763; ENSP00000265131; ENSG00000041982. [P24821-1]
    ENST00000535648; ENSP00000438152; ENSG00000041982. [P24821-2]
    ENST00000537320; ENSP00000443478; ENSG00000041982. [P24821-6]
    GeneIDi3371.
    KEGGihsa:3371.
    UCSCiuc004bjj.4. human. [P24821-1]

    Polymorphism databases

    DMDMi281185495.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55618 mRNA. Translation: AAA88083.1 .
    X56160 mRNA. Translation: CAA39628.1 .
    X78565 mRNA. Translation: CAA55309.1 .
    AL162425 Genomic DNA. Translation: CAI15110.1 .
    X80280 mRNA. No translation available.
    M24630 mRNA. Translation: AAA52703.1 .
    CCDSi CCDS6811.1. [P24821-1 ]
    PIRi I38337. A32160.
    RefSeqi NP_002151.2. NM_002160.3. [P24821-1 ]
    XP_005252029.1. XM_005251972.1. [P24821-4 ]
    XP_005252031.1. XM_005251974.1. [P24821-5 ]
    XP_005252032.1. XM_005251975.1. [P24821-6 ]
    UniGenei Hs.143250.
    Hs.734766.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TEN X-ray 1.80 A 802-891 [» ]
    2RB8 X-ray 1.45 A 802-893 [» ]
    2RBL X-ray 2.10 A/B/M 802-893 [» ]
    ProteinModelPortali P24821.
    SMRi P24821. Positions 135-1976, 1980-2189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109602. 3 interactions.
    STRINGi 9606.ENSP00000265131.

    PTM databases

    PhosphoSitei P24821.

    Polymorphism databases

    DMDMi 281185495.

    Proteomic databases

    MaxQBi P24821.
    PaxDbi P24821.
    PRIDEi P24821.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000350763 ; ENSP00000265131 ; ENSG00000041982 . [P24821-1 ]
    ENST00000535648 ; ENSP00000438152 ; ENSG00000041982 . [P24821-2 ]
    ENST00000537320 ; ENSP00000443478 ; ENSG00000041982 . [P24821-6 ]
    GeneIDi 3371.
    KEGGi hsa:3371.
    UCSCi uc004bjj.4. human. [P24821-1 ]

    Organism-specific databases

    CTDi 3371.
    GeneCardsi GC09M117782.
    HGNCi HGNC:5318. TNC.
    HPAi CAB004592.
    HPA004823.
    MIMi 187380. gene.
    615629. phenotype.
    neXtProti NX_P24821.
    Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    PharmGKBi PA35103.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG008949.
    InParanoidi P24821.
    KOi K06252.
    OMAi GCCLQPA.
    OrthoDBi EOG7X9G60.
    PhylomeDBi P24821.
    TreeFami TF329915.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.

    Miscellaneous databases

    EvolutionaryTracei P24821.
    GeneWikii Tenascin_C.
    GenomeRNAii 3371.
    NextBioi 13334.
    PROi P24821.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24821.
    Bgeei P24821.
    CleanExi HS_TNC.
    Genevestigatori P24821.

    Family and domain databases

    Gene3Di 2.60.40.10. 15 hits.
    3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR013111. EGF_extracell.
    IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF07974. EGF_2. 7 hits.
    PF00147. Fibrinogen_C. 1 hit.
    PF00041. fn3. 15 hits.
    PF12661. hEGF. 3 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 12 hits.
    SM00186. FBG. 1 hit.
    SM00060. FN3. 15 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 12 hits.
    SSF56496. SSF56496. 1 hit.
    PROSITEi PS00022. EGF_1. 15 hits.
    PS01186. EGF_2. 15 hits.
    PS50026. EGF_3. 5 hits.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    PS50853. FN3. 15 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain protein containing unique epidermal growth factor repeats."
      Nies D.E., Hemesath T.J., Kim J.H., Gulcher J.R., Stefansson K.
      J. Biol. Chem. 266:2818-2823(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-539; LEU-1677 AND GLN-2008.
    2. "Human tenascin: primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies."
      Siri A., Carnemolla B., Saginati M., Leprini A., Casari G., Baralle F., Zardi L.
      Nucleic Acids Res. 19:525-531(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), PROTEIN SEQUENCE OF 23-32, VARIANTS ARG-680 AND GLN-2008.
      Tissue: Fetal brain and Melanoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-539; LEU-1677 AND GLN-2008.
    4. "Human tenascin gene. Structure of the 5'-region, identification, and characterization of the transcription regulatory sequences."
      Gherzi R., Carnemolla B., Siri A., Ponassi M., Balza E., Zardi L.
      J. Biol. Chem. 270:3429-3434(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LEU-1677 AND GLN-2008.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Analysis of aggrecan and tenascin gene expression in mouse skeletal tissues by northern and in situ hybridization using species specific cDNA probes."
      Glumoff V., Savontaus M., Vehanen J., Vuorio E.
      Biochim. Biophys. Acta 1219:613-622(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-125 (ISOFORMS 1/2/3/4/5/6).
      Tissue: Fetal cartilage.
    7. "An alternatively spliced region of the human hexabrachion contains a repeat of potential N-glycosylation sites."
      Gulcher J.R., Nies D.E., Marton L.S., Stefansson K.
      Proc. Natl. Acad. Sci. U.S.A. 86:1588-1592(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 431-2055 (ISOFORMS 1 AND 6), VARIANTS ARG-539; LEU-1677 AND GLN-2008.
      Tissue: Glioblastoma.
    8. "Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules."
      Burg M.A., Tillet E., Timpl R., Stallcup W.B.
      J. Biol. Chem. 271:26110-26116(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4.
    9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1809.
      Tissue: Plasma.
    10. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-1079; ASN-1093; ASN-1261; ASN-1301; ASN-1485 AND ASN-2162.
      Tissue: Milk.
    11. "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-1018; ASN-1034; ASN-1184; ASN-1275; ASN-1301; ASN-1366 AND ASN-1485.
      Tissue: Liver.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein."
      Leahy D.J., Hendrickson W.A., Aukhil I., Erickson H.P.
      Science 258:987-991(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF FIBRONECTIN TYPE-III 3.
    14. "Exome sequencing and linkage analysis identified tenascin-C (TNC) as a novel causative gene in nonsyndromic hearing loss."
      Zhao Y., Zhao F., Zong L., Zhang P., Guan L., Zhang J., Wang D., Wang J., Chai W., Lan L., Li Q., Han B., Yang L., Jin X., Yang W., Hu X., Wang X., Li N.
      , Li Y., Petit C., Wang J., Wang H.Y., Wang Q.
      PLoS ONE 8:E69549-E69549(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DFNA56 MET-1773 AND SER-1796.

    Entry informationi

    Entry nameiTENA_HUMAN
    AccessioniPrimary (citable) accession number: P24821
    Secondary accession number(s): C9IYT7
    , C9J575, C9J6D9, C9J848, Q14583, Q15567, Q5T7S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 172 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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