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P24821 (TENA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TNC
Synonyms:HXB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8

Subcellular location

Secretedextracellular spaceextracellular matrix.

Induction

By TGFB1.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the tenascin family.

Contains 15 EGF-like domains.

Contains 1 fibrinogen C-terminal domain.

Contains 15 fibronectin type-III domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Non-syndromic deafness
   DomainCoiled coil
EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbud outgrowth involved in lung branching

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

cellular response to prostaglandin D stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin D

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

mesenchymal-epithelial cell signaling involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

peripheral nervous system axon regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

prostate gland epithelium morphogenesis

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to fibroblast growth factor

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from expression pattern PubMed 16891397. Source: BHF-UCL

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

interstitial matrix

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

   Molecular_functionsyndecan binding

Inferred from physical interaction PubMed 8769660. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms are produced in a tissue- and time-specific manner during development.
Isoform 1 (identifier: P24821-1)

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.
Isoform 2 (identifier: P24821-2)

Also known as: HT-5;

The sequence of this isoform differs from the canonical sequence as follows:
     1072-1435: Missing.
     1527-1617: Missing.
Isoform 3 (identifier: P24821-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1072-1435: Missing.
Isoform 4 (identifier: P24821-4)

Also known as: HT-33;

The sequence of this isoform differs from the canonical sequence as follows:
     1527-1617: Missing.
Isoform 5 (identifier: P24821-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1072-1617: Missing.
Isoform 6 (identifier: P24821-6)

Also known as: P31;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 22012179Tenascin
PRO_0000007741

Regions

Domain174 – 18613EGF-like 1; incomplete
Domain186 – 21732EGF-like 2
Domain217 – 24832EGF-like 3
Domain248 – 28033EGF-like 4
Domain280 – 31132EGF-like 5
Domain311 – 34232EGF-like 6
Domain342 – 37332EGF-like 7
Domain373 – 40432EGF-like 8
Domain404 – 43532EGF-like 9
Domain435 – 46632EGF-like 10
Domain466 – 49732EGF-like 11
Domain497 – 52832EGF-like 12
Domain528 – 55932EGF-like 13
Domain559 – 59032EGF-like 14
Domain590 – 62132EGF-like 15
Domain625 – 71591Fibronectin type-III 1
Domain716 – 80489Fibronectin type-III 2
Domain805 – 89490Fibronectin type-III 3
Domain895 – 99096Fibronectin type-III 4
Domain991 – 107585Fibronectin type-III 5
Domain1076 – 116590Fibronectin type-III 6
Domain1167 – 125690Fibronectin type-III 7
Domain1258 – 135093Fibronectin type-III 8
Domain1351 – 143989Fibronectin type-III 9
Domain1440 – 153192Fibronectin type-III 10
Domain1533 – 162189Fibronectin type-III 11
Domain1622 – 171190Fibronectin type-III 12
Domain1712 – 180190Fibronectin type-III 13
Domain1802 – 188887Fibronectin type-III 14
Domain1889 – 197789Fibronectin type-III 15
Domain1975 – 2190216Fibrinogen C-terminal
Coiled coil118 – 14528 Potential

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Ref.10
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation7881N-linked (GlcNAc...) Potential
Glycosylation10181N-linked (GlcNAc...) Ref.11
Glycosylation10341N-linked (GlcNAc...) Ref.11
Glycosylation10791N-linked (GlcNAc...) Ref.10
Glycosylation10931N-linked (GlcNAc...) Ref.10
Glycosylation11191N-linked (GlcNAc...) Potential
Glycosylation11841N-linked (GlcNAc...) Ref.11
Glycosylation12101N-linked (GlcNAc...) Potential
Glycosylation12611N-linked (GlcNAc...) Ref.10
Glycosylation12751N-linked (GlcNAc...) Ref.11
Glycosylation13011N-linked (GlcNAc...) Ref.10 Ref.11
Glycosylation13661N-linked (GlcNAc...) Ref.11
Glycosylation13921N-linked (GlcNAc...) Potential
Glycosylation14451N-linked (GlcNAc...) Potential
Glycosylation14551N-linked (GlcNAc...) Potential
Glycosylation14851N-linked (GlcNAc...) Ref.10 Ref.11
Glycosylation15341N-linked (GlcNAc...) Potential
Glycosylation18091N-linked (GlcNAc...) Ref.9
Glycosylation21621N-linked (GlcNAc...) Ref.10
Disulfide bond190 ↔ 200 By similarity
Disulfide bond194 ↔ 205 By similarity
Disulfide bond207 ↔ 216 By similarity
Disulfide bond221 ↔ 231 By similarity
Disulfide bond225 ↔ 236 By similarity
Disulfide bond238 ↔ 247 By similarity
Disulfide bond252 ↔ 263 By similarity
Disulfide bond256 ↔ 268 By similarity
Disulfide bond270 ↔ 279 By similarity
Disulfide bond284 ↔ 294 By similarity
Disulfide bond288 ↔ 299 By similarity
Disulfide bond301 ↔ 310 By similarity
Disulfide bond315 ↔ 325 By similarity
Disulfide bond319 ↔ 330 By similarity
Disulfide bond332 ↔ 341 By similarity
Disulfide bond346 ↔ 356 By similarity
Disulfide bond350 ↔ 361 By similarity
Disulfide bond363 ↔ 372 By similarity
Disulfide bond377 ↔ 387 By similarity
Disulfide bond381 ↔ 392 By similarity
Disulfide bond394 ↔ 403 By similarity
Disulfide bond408 ↔ 418 By similarity
Disulfide bond412 ↔ 423 By similarity
Disulfide bond425 ↔ 434 By similarity
Disulfide bond439 ↔ 449 By similarity
Disulfide bond443 ↔ 454 By similarity
Disulfide bond456 ↔ 465 By similarity
Disulfide bond470 ↔ 480 By similarity
Disulfide bond474 ↔ 485 By similarity
Disulfide bond487 ↔ 496 By similarity
Disulfide bond501 ↔ 511 By similarity
Disulfide bond505 ↔ 516 By similarity
Disulfide bond518 ↔ 527 By similarity
Disulfide bond532 ↔ 542 By similarity
Disulfide bond536 ↔ 547 By similarity
Disulfide bond549 ↔ 558 By similarity
Disulfide bond563 ↔ 573 By similarity
Disulfide bond567 ↔ 578 By similarity
Disulfide bond580 ↔ 589 By similarity
Disulfide bond594 ↔ 604 By similarity
Disulfide bond598 ↔ 609 By similarity
Disulfide bond611 ↔ 620 By similarity

Natural variations

Alternative sequence1072 – 1708637Missing in isoform 6.
VSP_001415
Alternative sequence1072 – 1617546Missing in isoform 5.
VSP_001414
Alternative sequence1072 – 1435364Missing in isoform 2 and isoform 3.
VSP_001412
Alternative sequence1527 – 161791Missing in isoform 2 and isoform 4.
VSP_001413
Natural variant2131G → S.
Corresponds to variant rs7020958 [ dbSNP | Ensembl ].
VAR_055778
Natural variant5391Q → R. Ref.1 Ref.3 Ref.7
Corresponds to variant rs1757095 [ dbSNP | Ensembl ].
VAR_024266
Natural variant6051V → I.
Corresponds to variant rs3827816 [ dbSNP | Ensembl ].
VAR_024267
Natural variant6801Q → R. Ref.2
Corresponds to variant rs1061494 [ dbSNP | Ensembl ].
VAR_024268
Natural variant8501D → H.
Corresponds to variant rs3748169 [ dbSNP | Ensembl ].
VAR_055779
Natural variant16771I → L. Ref.1 Ref.3 Ref.4 Ref.7
Corresponds to variant rs2104772 [ dbSNP | Ensembl ].
VAR_060738
Natural variant17731V → M in DFNA56. Ref.14
VAR_070984
Natural variant17811A → T.
Corresponds to variant rs2274750 [ dbSNP | Ensembl ].
VAR_020169
Natural variant17961T → S in DFNA56. Ref.14
VAR_070985
Natural variant20081E → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs13321 [ dbSNP | Ensembl ].
VAR_014665

Experimental info

Sequence conflict2441Missing in CAA39628. Ref.2
Sequence conflict3701V → L no nucleotide entry Ref.1
Sequence conflict3701V → L in AAA88083. Ref.3
Sequence conflict3701V → L in CAA55309. Ref.4
Sequence conflict10661R → H no nucleotide entry Ref.1
Sequence conflict10661R → H in AAA88083. Ref.3
Sequence conflict10661R → H in AAA52703. Ref.7
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN no nucleotide entry Ref.1
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN in AAA88083. Ref.3
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN in AAA52703. Ref.7
Sequence conflict20541F → FLH no nucleotide entry Ref.1
Sequence conflict20541F → FLH in AAA88083. Ref.3
Sequence conflict20551W → L in AAA52703. Ref.7
Sequence conflict2140 – 21434YKGA → TRG in CAA39628. Ref.2

Secondary structure

................... 2201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 2009. Version 3.
Checksum: B2BEF378AA6F1D85

FASTA2,201240,853
        10         20         30         40         50         60 
MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF NHVYNIKLPV 

        70         80         90        100        110        120 
GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK 

       130        140        150        160        170        180 
ELLSRLEELE NLVSSLREQC TAGAGCCLQP ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW 

       190        200        210        220        230        240 
KGPNCSEPEC PGNCHLRGRC IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE 

       250        260        270        280        290        300 
GYAGADCSRE ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV 

       310        320        330        340        350        360 
CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC HTQGRCEEGQ 

       370        380        390        400        410        420 
CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG ADCGELKCPN GCSGHGRCVN 

       430        440        450        460        470        480 
GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC 

       490        500        510        520        530        540 
VNGMCVCDDG YTGEDCRDRQ CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG 

       550        560        570        580        590        600 
RCVNGQCVCH EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN 

       610        620        630        640        650        660 
LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT EYLVVYTPTH 

       670        680        690        700        710        720 
EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF 

       730        740        750        760        770        780 
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE 

       790        800        810        820        830        840 
ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK 

       850        860        870        880        890        900 
DVPGDRTTID LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR 

       910        920        930        940        950        960 
RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT TLTGLRPGTE 

       970        980        990       1000       1010       1020 
YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS LTLLWKTPLA KFDRYRLNYS 

      1030       1040       1050       1060       1070       1080 
LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN VLLTAEKGRH KSKPARVKAS TEQAPELENL 

      1090       1100       1110       1120       1130       1140 
TVTEVGWDGL RLNWTAADQA YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY 

      1150       1160       1170       1180       1190       1200 
TVSIYGVIQG YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ 

      1210       1220       1230       1240       1250       1260 
EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE VLTEEVPDMG 

      1270       1280       1290       1300       1310       1320 
NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH NLTVPGSLRS MEIPGLRAGT 

      1330       1340       1350       1360       1370       1380 
PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ 

      1390       1400       1410       1420       1430       1440 
VQEVNKVEAA QNLTLPGSLR AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAKEPE 

      1450       1460       1470       1480       1490       1500 
IGNLNVSDIT PESFNLSWMA TDGIFETFTI EIIDSNRLLE TVEYNISGAE RTAHISGLPP 

      1510       1520       1530       1540       1550       1560 
STDFIVYLSG LAPSIRTKTI SATATTEALP LLENLTISDI NPYGFTVSWM ASENAFDSFL 

      1570       1580       1590       1600       1610       1620 
VTVVDSGKLL DPQEFTLSGT QRKLELRGLI TGIGYEVMVS GFTQGHQTKP LRAEIVTEAE 

      1630       1640       1650       1660       1670       1680 
PEVDNLLVSD ATPDGFRLSW TADEGVFDNF VLKIRDTKKQ SEPLEITLLA PERTRDITGL 

      1690       1700       1710       1720       1730       1740 
REATEYEIEL YGISKGRRSQ TVSAIATTAM GSPKEVIFSD ITENSATVSW RAPTAQVESF 

      1750       1760       1770       1780       1790       1800 
RITYVPITGG TPSMVTVDGT KTQTRLVKLI PGVEYLVSII AMKGFEESEP VSGSFTTALD 

      1810       1820       1830       1840       1850       1860 
GPSGLVTANI TDSEALARWQ PAIATVDSYV ISYTGEKVPE ITRTVSGNTV EYALTDLEPA 

      1870       1880       1890       1900       1910       1920 
TEYTLRIFAE KGPQKSSTIT AKFTTDLDSP RDLTATEVQS ETALLTWRPP RASVTGYLLV 

      1930       1940       1950       1960       1970       1980 
YESVDGTVKE VIVGPDTTSY SLADLSPSTH YTAKIQALNG PLRSNMIQTI FTTIGLLYPF 

      1990       2000       2010       2020       2030       2040 
PKDCSQAMLN GDTTSGLYTI YLNGDKAEAL EVFCDMTSDG GGWIVFLRRK NGRENFYQNW 

      2050       2060       2070       2080       2090       2100 
KAYAAGFGDR REEFWLGLDN LNKITAQGQY ELRVDLRDHG ETAFAVYDKF SVGDAKTRYK 

      2110       2120       2130       2140       2150       2160 
LKVEGYSGTA GDSMAYHNGR SFSTFDKDTD SAITNCALSY KGAFWYRNCH RVNLMGRYGD 

      2170       2180       2190       2200 
NNHSQGVNWF HWKGHEHSIQ FAEMKLRPSN FRNLEGRRKR A 

« Hide

Isoform 2 (HT-5) [UniParc].

Checksum: 588B877CF66A227D
Show »

FASTA1,746191,373
Isoform 3 [UniParc].

Checksum: 54B916A3A6664FDE
Show »

FASTA1,837201,359
Isoform 4 (HT-33) [UniParc].

Checksum: 379795176A2B7252
Show »

FASTA2,110230,867
Isoform 5 [UniParc].

Checksum: FA3D6624965AE06A
Show »

FASTA1,655181,528
Isoform 6 (P31) [UniParc].

Checksum: B240934A9414ABC4
Show »

FASTA1,564171,360

References

« Hide 'large scale' references
[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]"Structure of the human hexabrachion (tenascin) gene."
Gulcher J.R., Nies D.E., Alexakos M.J., Ravikant N.A., Sturgill M.E., Marton L.S., Stefansson K.
Proc. Natl. Acad. Sci. U.S.A. 88:9438-9442(1991) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6811.1. [P24821-1]
PIRA32160. I38337.
RefSeqNP_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]
UniGeneHs.143250.
Hs.734766.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TENX-ray1.80A802-891[»]
2RB8X-ray1.45A802-893[»]
2RBLX-ray2.10A/B/M802-893[»]
ProteinModelPortalP24821.
SMRP24821. Positions 135-1976, 1980-2189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109602. 3 interactions.
STRING9606.ENSP00000265131.

PTM databases

PhosphoSiteP24821.

Polymorphism databases

DMDM281185495.

Proteomic databases

MaxQBP24821.
PaxDbP24821.
PRIDEP24821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340094; ENSP00000344400; ENSG00000041982. [P24821-3]
ENST00000345230; ENSP00000345861; ENSG00000041982. [P24821-6]
ENST00000346706; ENSP00000344555; ENSG00000041982. [P24821-5]
ENST00000350763; ENSP00000265131; ENSG00000041982. [P24821-1]
ENST00000535648; ENSP00000438152; ENSG00000041982. [P24821-2]
ENST00000537320; ENSP00000443478; ENSG00000041982. [P24821-6]
GeneID3371.
KEGGhsa:3371.
UCSCuc004bjj.4. human. [P24821-1]

Organism-specific databases

CTD3371.
GeneCardsGC09M117782.
HGNCHGNC:5318. TNC.
HPACAB004592.
HPA004823.
MIM187380. gene.
615629. phenotype.
neXtProtNX_P24821.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBPA35103.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG008949.
InParanoidP24821.
KOK06252.
OMAGCCLQPA.
OrthoDBEOG7X9G60.
PhylomeDBP24821.
TreeFamTF329915.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP24821.
BgeeP24821.
CleanExHS_TNC.
GenevestigatorP24821.

Family and domain databases

Gene3D2.60.40.10. 15 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR000742. 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]
PfamPF07974. EGF_2. 7 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 15 hits.
PF12661. hEGF. 3 hits.
[Graphical view]
SMARTSM00181. EGF. 12 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 15 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 12 hits.
SSF56496. SSF56496. 1 hit.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP24821.
GeneWikiTenascin_C.
GenomeRNAi3371.
NextBio13334.
PROP24821.
SOURCESearch...

Entry information

Entry nameTENA_HUMAN
AccessionPrimary (citable) accession number: P24821
Secondary accession number(s): C9IYT7 expand/collapse secondary AC list , C9J575, C9J6D9, C9J848, Q14583, Q15567, Q5T7S3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 2009
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM