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P24821

- TENA_HUMAN

UniProt

P24821 - TENA_HUMAN

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Protein
Tenascin
Gene
TNC, HXB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 Publication
Add
BLAST
Chaini23 – 22012179Tenascin
PRO_0000007741Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP24821.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili118 – 14528 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the tenascin family.
Contains 15 EGF-like domains.

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

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.
VSP_001415Add
BLAST
Alternative sequencei1072 – 1617546Missing in isoform 5.
VSP_001414Add
BLAST
Alternative sequencei1072 – 1435364Missing in isoform 2 and isoform 3.
VSP_001412Add
BLAST
Alternative sequencei1527 – 161791Missing in isoform 2 and isoform 4.
VSP_001413Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441Missing in CAA39628. 1 Publication
Sequence conflicti370 – 3701V → L no nucleotide entry 1 Publication
Sequence conflicti370 – 3701V → L in AAA88083. 1 Publication
Sequence conflicti370 – 3701V → L in CAA55309. 1 Publication
Sequence conflicti1066 – 10661R → H no nucleotide entry 1 Publication
Sequence conflicti1066 – 10661R → H in AAA88083. 1 Publication
Sequence conflicti1066 – 10661R → H in AAA52703. 1 Publication
Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN no nucleotide entry 1 Publication
Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN in AAA88083. 1 Publication
Sequence conflicti1600 – 16089SGFTQGHQT → LWLHPRASN in AAA52703. 1 Publication
Sequence conflicti2054 – 20541F → FLH no nucleotide entry 1 Publication
Sequence conflicti2054 – 20541F → FLH in AAA88083. 1 Publication
Sequence conflicti2055 – 20551W → L in AAA52703. 1 Publication
Sequence conflicti2140 – 21434YKGA → TRG in CAA39628. 1 Publication

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

EnsembliENST00000340094; 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]
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 ENST00000340094 ; 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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 171 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

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