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Reviewed, UniProtKB/Swiss-Prot P24821 (TENA_HUMAN)

Last modified June 16, 2009. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tenascin
      Short name=TN
Alternative name(s):
    Tenascin-C
      Short name=TN-C
    Hexabrachion
    Cytotactin
    Neuronectin
    GMEM
    JI
    Myotendinous antigen
    Glioma-associated-extracellular matrix antigen
    GP 150-225
Gene names
Name: TNC
Synonyms: HXB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.7

Subcellular location

Secreted › extracellular space › extracellular matrix.

Induction

By TGF-beta.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the tenascin family.

Contains 15 EGF-like domains.

Contains 1 fibrinogen C-terminal domain.

Contains 15 fibronectin type-III domains.

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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.

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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
Domain622 – 71089Fibronectin type-III 1
Domain713 – 80189Fibronectin type-III 2
Domain802 – 89190Fibronectin type-III 3
Domain892 – 98392Fibronectin type-III 4
Domain984 – 107188Fibronectin type-III 5
Domain1075 – 116288Fibronectin type-III 6
Domain1164 – 125390Fibronectin type-III 7
Domain1255 – 134490Fibronectin type-III 8
Domain1348 – 143588Fibronectin type-III 9
Domain1439 – 152688Fibronectin type-III 10
Domain1528 – 161790Fibronectin type-III 11
Domain1619 – 170890Fibronectin type-III 12
Domain1709 – 179789Fibronectin type-III 13
Domain1798 – 188588Fibronectin type-III 14
Domain1886 – 197388Fibronectin type-III 15
Domain1975 – 2190216Fibrinogen C-terminal
Coiled coil118 – 14528 Potential

Amino acid modifications

Modified residue721Phosphoserine By similarity
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Ref.9
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation7881N-linked (GlcNAc...) Potential
Glycosylation10181N-linked (GlcNAc...)
Glycosylation10341N-linked (GlcNAc...)
Glycosylation10791N-linked (GlcNAc...) Ref.9
Glycosylation10931N-linked (GlcNAc...) Ref.9
Glycosylation11191N-linked (GlcNAc...) Potential
Glycosylation11841N-linked (GlcNAc...)
Glycosylation12101N-linked (GlcNAc...) Potential
Glycosylation12611N-linked (GlcNAc...) Ref.9
Glycosylation12751N-linked (GlcNAc...)
Glycosylation13011N-linked (GlcNAc...) Ref.9
Glycosylation13661N-linked (GlcNAc...)
Glycosylation13921N-linked (GlcNAc...) Potential
Glycosylation14451N-linked (GlcNAc...) Potential
Glycosylation14551N-linked (GlcNAc...) Potential
Glycosylation14851N-linked (GlcNAc...) Ref.9
Glycosylation15341N-linked (GlcNAc...) Potential
Glycosylation18091N-linked (GlcNAc...) Ref.8
Glycosylation21621N-linked (GlcNAc...) Ref.9
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: dbSNP rs7020958.
VAR_055778
Natural variant5391Q → R: dbSNP rs1757095. Ref.1 Ref.3 Ref.6
VAR_024266
Natural variant6051V → I: dbSNP rs3827816.
VAR_024267
Natural variant6801Q → R: dbSNP rs1061494. Ref.2
VAR_024268
Natural variant8501D → H: dbSNP rs3748169.
VAR_055779
Natural variant17811A → T: dbSNP rs2274750.
VAR_020169
Natural variant20081Q → E: dbSNP rs13321.
VAR_014665

Experimental info

Sequence conflict2441Missing in CAA39628. Ref.2
Sequence conflict3701L → V in CAA39628. Ref.2
Sequence conflict10661R → H Ref.1
Sequence conflict10661R → H Ref.3
Sequence conflict10661R → H Ref.6
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN Ref.1
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN Ref.3
Sequence conflict1600 – 16089SGFTQGHQT → LWLHPRASN Ref.6
Sequence conflict16771L → I in CAA39628. Ref.2
Sequence conflict20541F → FLH Ref.1
Sequence conflict20541F → FLH Ref.3
Sequence conflict20551W → L in AAA52703. Ref.6
Sequence conflict2140 – 21434YKGA → TRG in CAA39628. Ref.2

Secondary structure

1 ............... 2201
Helix Strand Turn

Details...

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Sequences

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

Last modified December 15, 1998. Version 2.
Checksum: BE96820DB742E981

FASTA2,201240,866
        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 
CVCDEGFAGL 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 PERTRDLTGL 

      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 YLNGDKAQAL 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).

Checksum: F53B0F5F5DB10031
Show »

FASTA1,746191,386
Isoform 3.

Checksum: 747656B1B47BAA7E
Show »

FASTA1,837201,372
Isoform 4 (HT-33).

Checksum: 6FDBF5CB168CD8FA
Show »

FASTA2,110230,880
Isoform 5.

Checksum: 62D5196B812D03D1
Show »

FASTA1,655181,541
Isoform 6 (P31).

Checksum: 4A10BEE880AD4F00
Show »

FASTA1,564171,373

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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: 1704365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-539.
[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: 1707164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), PROTEIN SEQUENCE OF 23-32, VARIANT ARG-680.
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: 1719530] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-539.
[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: 7531707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"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: 7524681] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-125 (ISOFORMS 1/2/3/4/5/6).
Tissue: Fetal cartilage.
[6]"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: 2466295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 431-2055 (ISOFORMS 1 AND 6), VARIANT ARG-539.
Tissue: Glioblastoma.
[7]"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: 8824254] [Abstract]
Cited for: INTERACTION WITH CSPG4.
[8]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1809, MASS SPECTROMETRY.
Tissue: Plasma.
[9]"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: 18780401] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-1079; ASN-1093; ASN-1261; ASN-1301; ASN-1485 AND ASN-2162, MASS SPECTROMETRY.
Tissue: Milk.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1018; ASN-1034; ASN-1184; ASN-1275; ASN-1301; ASN-1366 AND ASN-1485, MASS SPECTROMETRY.
Tissue: Liver.
[12]"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: 1279805] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF FIBRONECTIN TYPE-III 3.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X56160 mRNA. Translation: CAA39628.1.
X78565 mRNA. Translation: CAA55309.1.
M55618 mRNA. Translation: AAA88083.1.
M24630 mRNA. Translation: AAA52703.1.
X80280 mRNA. No translation available.
IPIIPI00031008.
IPI00220211.
IPI00220212.
IPI00220213.
IPI00220214.
IPI00220216.
PIRA32160. I38337.
UniGeneHs.143250

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TENX-ray1.80A802-891[»]
2RB8X-ray1.45A802-893[»]
2RBLX-ray2.10A/B/M802-893[»]
ModBaseSearch...

PTM databases

PhosphoSiteP24821.

Proteomic databases

PRIDEP24821.

Genome annotation databases

EnsemblENSG00000041982. Homo sapiens. [Contig view]

Organism-specific databases

GeneCardsGC09M116822.
H-InvDBHIX0008324.
HGNCHGNC:5318. TNC.
HPACAB004592.
HPA004823.
MIM187380. gene.
PharmGKBPA35103.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP24821.

Enzyme and pathway databases

Pathway_Interaction_DBsyndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_13552. Integrin cell surface interactions.

Gene expression databases

ArrayExpressP24821.
BgeeP24821.
CleanExHS_TNC.
GermOnlineENSG00000041982. Homo sapiens.

Family and domain databases

InterProIPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR013111. EGF_extracell.
IPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
[Graphical view]
Gene3DG3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:2.60.40.30. FN_III-like. 15 hits.
PfamPF00008. EGF. 2 hits.
PF07974. EGF_2. 12 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 15 hits.
[Graphical view]
SMARTSM00181. EGF. 12 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 15 hits.
[Graphical view]
PROSITEPS00022. EGF_1. 15 hits.
PS01186. EGF_2. 15 hits.
PS50026. EGF_3. 5 hits.
PS00514. FIBRINOGEN_C_1. False negative.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 15 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameTENA_HUMAN
AccessionPrimary (citable) accession number: P24821
Secondary accession number(s): Q14583, Q15567
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents