Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P24821

- TENA_HUMAN

UniProt

P24821 - TENA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tenascin

Gene

TNC

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 matrix Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. focal adhesion Source: UniProtKB
  6. interstitial matrix Source: Ensembl
  7. 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.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 non-syndromic 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

BgeeiP24821.
CleanExiHS_TNC.
ExpressionAtlasiP24821. baseline and differential.
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 – 8137Combined sources
Beta strandi819 – 8246Combined sources
Helixi827 – 8293Combined sources
Beta strandi831 – 8399Combined sources
Beta strandi842 – 8443Combined sources
Beta strandi847 – 8526Combined sources
Beta strandi857 – 8604Combined sources
Beta strandi868 – 87710Combined sources
Beta strandi885 – 8906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120463.
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

        10         20         30         40         50
MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF
60 70 80 90 100
NHVYNIKLPV GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF
110 120 130 140 150
THRINIPRRA CGCAAAPDVK ELLSRLEELE NLVSSLREQC TAGAGCCLQP
160 170 180 190 200
ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW KGPNCSEPEC PGNCHLRGRC
210 220 230 240 250
IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE GYAGADCSRE
260 270 280 290 300
ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV
310 320 330 340 350
CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC
360 370 380 390 400
HTQGRCEEGQ CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG
410 420 430 440 450
ADCGELKCPN GCSGHGRCVN GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV
460 470 480 490 500
EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC VNGMCVCDDG YTGEDCRDRQ
510 520 530 540 550
CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG RCVNGQCVCH
560 570 580 590 600
EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN
610 620 630 640 650
LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT
660 670 680 690 700
EYLVVYTPTH EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK
710 720 730 740 750
SIPVSARVAT YLPAPEGLKF KSIKETSVEV EWDPLDIAFE TWEIIFRNMN
760 770 780 790 800
KEDEGEITKS LRRPETSYRQ TGLAPGQEYE ISLHIVKNNT RGPGLKRVTT
810 820 830 840 850
TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK DVPGDRTTID
860 870 880 890 900
LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR
910 920 930 940 950
RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT
960 970 980 990 1000
TLTGLRPGTE YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS
1010 1020 1030 1040 1050
LTLLWKTPLA KFDRYRLNYS LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN
1060 1070 1080 1090 1100
VLLTAEKGRH KSKPARVKAS TEQAPELENL TVTEVGWDGL RLNWTAADQA
1110 1120 1130 1140 1150
YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY TVSIYGVIQG
1160 1170 1180 1190 1200
YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ
1210 1220 1230 1240 1250
EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE
1260 1270 1280 1290 1300
VLTEEVPDMG NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH
1310 1320 1330 1340 1350
NLTVPGSLRS MEIPGLRAGT PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL
1360 1370 1380 1390 1400
GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ VQEVNKVEAA QNLTLPGSLR
1410 1420 1430 1440 1450
AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAKEPE IGNLNVSDIT
1460 1470 1480 1490 1500
PESFNLSWMA TDGIFETFTI EIIDSNRLLE TVEYNISGAE RTAHISGLPP
1510 1520 1530 1540 1550
STDFIVYLSG LAPSIRTKTI SATATTEALP LLENLTISDI NPYGFTVSWM
1560 1570 1580 1590 1600
ASENAFDSFL VTVVDSGKLL DPQEFTLSGT QRKLELRGLI TGIGYEVMVS
1610 1620 1630 1640 1650
GFTQGHQTKP LRAEIVTEAE PEVDNLLVSD ATPDGFRLSW TADEGVFDNF
1660 1670 1680 1690 1700
VLKIRDTKKQ SEPLEITLLA PERTRDITGL REATEYEIEL YGISKGRRSQ
1710 1720 1730 1740 1750
TVSAIATTAM GSPKEVIFSD ITENSATVSW RAPTAQVESF RITYVPITGG
1760 1770 1780 1790 1800
TPSMVTVDGT KTQTRLVKLI PGVEYLVSII AMKGFEESEP VSGSFTTALD
1810 1820 1830 1840 1850
GPSGLVTANI TDSEALARWQ PAIATVDSYV ISYTGEKVPE ITRTVSGNTV
1860 1870 1880 1890 1900
EYALTDLEPA TEYTLRIFAE KGPQKSSTIT AKFTTDLDSP RDLTATEVQS
1910 1920 1930 1940 1950
ETALLTWRPP RASVTGYLLV YESVDGTVKE VIVGPDTTSY SLADLSPSTH
1960 1970 1980 1990 2000
YTAKIQALNG PLRSNMIQTI FTTIGLLYPF PKDCSQAMLN GDTTSGLYTI
2010 2020 2030 2040 2050
YLNGDKAEAL EVFCDMTSDG GGWIVFLRRK NGRENFYQNW KAYAAGFGDR
2060 2070 2080 2090 2100
REEFWLGLDN LNKITAQGQY ELRVDLRDHG ETAFAVYDKF SVGDAKTRYK
2110 2120 2130 2140 2150
LKVEGYSGTA GDSMAYHNGR SFSTFDKDTD SAITNCALSY KGAFWYRNCH
2160 2170 2180 2190 2200
RVNLMGRYGD NNHSQGVNWF HWKGHEHSIQ FAEMKLRPSN FRNLEGRRKR

A
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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ]
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 non-syndromic sensorineural deafness type DFNA.
PharmGKBi PA35103.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120463.
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

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

Gene expression databases

Bgeei P24821.
CleanExi HS_TNC.
ExpressionAtlasi P24821. baseline and differential.
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: November 26, 2014
This is version 174 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