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P22105

- TENX_HUMAN

UniProt

P22105 - TENX_HUMAN

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Protein

Tenascin-X

Gene

TNXB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors.1 Publication

GO - Molecular functioni

  1. heparin binding Source: UniProtKB
  2. integrin binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. cell adhesion Source: UniProtKB
  3. cell-matrix adhesion Source: Ensembl
  4. collagen fibril organization Source: Ensembl
  5. collagen metabolic process Source: UniProtKB
  6. elastic fiber assembly Source: UniProtKB
  7. extracellular fibril organization Source: Ensembl
  8. fatty acid metabolic process Source: Ensembl
  9. regulation of JUN kinase activity Source: Ensembl
  10. single organismal cell-cell adhesion Source: Ensembl
  11. triglyceride metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Tenascin-X
Short name:
TN-X
Alternative name(s):
Hexabrachion-like protein
Gene namesi
Name:TNXB
Synonyms:HXBL, TNX, TNXB1, TNXB2, XB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:11976. TNXB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
  3. intracellular Source: UniProtKB
  4. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Tenascin-X deficiency (TNXD) [MIM:606408]: TNXD leads to an Ehlers-Danlos-like syndrome characterized by hyperextensible skin, hypermobile joints, and tissue fragility. Tenascin-X-deficient patients, however, lack atrophic scars, a major diagnostic criteria for classic Ehlers-Danlos. Delayed wound healing, which is also common in classic EDS, is only present in a subset of patients.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Ehlers-Danlos syndrome

Organism-specific databases

MIMi130020. phenotype.
606408. phenotype.
Orphaneti230839. Ehlers-Danlos syndrome due to tenascin-X deficiency.
285. Ehlers-Danlos syndrome, hypermobility type.
PharmGKBiPA36662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 42894266Tenascin-XPRO_0000007751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi187 ↔ 197By similarity
Disulfide bondi191 ↔ 202By similarity
Disulfide bondi204 ↔ 213By similarity
Disulfide bondi218 ↔ 228By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi235 ↔ 244By similarity
Disulfide bondi249 ↔ 259By similarity
Disulfide bondi253 ↔ 264By similarity
Disulfide bondi266 ↔ 275By similarity
Disulfide bondi280 ↔ 290By similarity
Disulfide bondi284 ↔ 295By similarity
Disulfide bondi297 ↔ 306By similarity
Disulfide bondi311 ↔ 321By similarity
Disulfide bondi315 ↔ 326By similarity
Disulfide bondi328 ↔ 337By similarity
Disulfide bondi342 ↔ 352By similarity
Disulfide bondi346 ↔ 357By similarity
Disulfide bondi359 ↔ 368By similarity
Disulfide bondi373 ↔ 383By similarity
Disulfide bondi377 ↔ 388By similarity
Disulfide bondi390 ↔ 399By similarity
Disulfide bondi404 ↔ 414By similarity
Disulfide bondi408 ↔ 419By similarity
Disulfide bondi421 ↔ 430By similarity
Disulfide bondi435 ↔ 445By similarity
Disulfide bondi439 ↔ 450By similarity
Disulfide bondi452 ↔ 461By similarity
Disulfide bondi466 ↔ 476By similarity
Disulfide bondi470 ↔ 481By similarity
Disulfide bondi483 ↔ 492By similarity
Disulfide bondi497 ↔ 507By similarity
Disulfide bondi501 ↔ 512By similarity
Disulfide bondi514 ↔ 523By similarity
Disulfide bondi528 ↔ 538By similarity
Disulfide bondi532 ↔ 543By similarity
Disulfide bondi545 ↔ 554By similarity
Disulfide bondi559 ↔ 569By similarity
Disulfide bondi563 ↔ 574By similarity
Disulfide bondi576 ↔ 585By similarity
Disulfide bondi590 ↔ 600By similarity
Disulfide bondi594 ↔ 605By similarity
Disulfide bondi607 ↔ 616By similarity
Disulfide bondi621 ↔ 631By similarity
Disulfide bondi625 ↔ 636By similarity
Disulfide bondi638 ↔ 647By similarity
Disulfide bondi652 ↔ 662By similarity
Disulfide bondi656 ↔ 667By similarity
Disulfide bondi669 ↔ 678By similarity
Disulfide bondi688 ↔ 698By similarity
Disulfide bondi692 ↔ 703By similarity
Disulfide bondi705 ↔ 714By similarity
Disulfide bondi719 ↔ 729By similarity
Disulfide bondi723 ↔ 734By similarity
Disulfide bondi736 ↔ 745By similarity
Glycosylationi901 – 9011N-linked (GlcNAc...)1 Publication
Glycosylationi930 – 9301N-linked (GlcNAc...)1 Publication
Glycosylationi3900 – 39001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3953 – 39531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3965 – 39651N-linked (GlcNAc...)1 Publication
Disulfide bondi4075 ↔ 4105By similarity
Glycosylationi4140 – 41401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4227 ↔ 4240By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP22105.
PRIDEiP22105.

PTM databases

PhosphoSiteiP22105.

Expressioni

Tissue specificityi

Highly expressed in fetal adrenal, in fetal testis, fetal smooth, striated and cardiac muscle. Isoform XB-short is only expressed in the adrenal gland.

Developmental stagei

Expression levels are lower in adults than in children.1 Publication

Gene expression databases

BgeeiP22105.
ExpressionAtlasiP22105. baseline.
GenevestigatoriP22105.

Organism-specific databases

HPAiCAB005373.

Interactioni

Subunit structurei

Homotrimer. Interacts with type I, III and V collagens and tropoelastin via its 29th fibronectin type-III domain.2 Publications

Protein-protein interaction databases

IntActiP22105. 7 interactions.

Structurei

Secondary structure

1
4289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3707 – 37104Combined sources
Beta strandi3716 – 37194Combined sources
Beta strandi3728 – 37358Combined sources
Beta strandi3740 – 37423Combined sources
Beta strandi3752 – 37576Combined sources
Beta strandi3762 – 37654Combined sources
Beta strandi3773 – 37819Combined sources
Beta strandi3783 – 379513Combined sources
Beta strandi3894 – 38974Combined sources
Beta strandi3902 – 39043Combined sources
Beta strandi3906 – 39116Combined sources
Beta strandi3918 – 39258Combined sources
Beta strandi3927 – 39293Combined sources
Beta strandi3932 – 39376Combined sources
Beta strandi3941 – 39455Combined sources
Beta strandi3950 – 396213Combined sources
Beta strandi3970 – 39767Combined sources
Turni3981 – 39833Combined sources
Beta strandi3984 – 39863Combined sources
Beta strandi3994 – 39996Combined sources
Beta strandi4006 – 40138Combined sources
Beta strandi4019 – 40246Combined sources
Beta strandi4029 – 40335Combined sources
Beta strandi4041 – 405010Combined sources
Beta strandi4058 – 40636Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUHNMR-A3890-3991[»]
2CUINMR-A3699-3797[»]
2CUMNMR-A3978-4069[»]
ProteinModelPortaliP22105.
SMRiP22105. Positions 140-878, 983-4279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22105.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 16813EGF-like 1; incompletePROSITE-ProRule annotationAdd
BLAST
Domaini183 – 21331EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 24431EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini245 – 27531EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini276 – 30631EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini307 – 33731EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 36831EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini369 – 39931EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 43031EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini431 – 46131EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 49231EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini493 – 52331EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini524 – 55431EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini555 – 58531EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini586 – 61631EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini617 – 64731EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini648 – 67932EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini684 – 71431EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini715 – 74632EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini794 – 88188Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini940 – 103495Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1046 – 113893Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1151 – 124090Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1248 – 133689Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1350 – 143990Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini1461 – 155595Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1563 – 165492Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1656 – 175196Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1756 – 184691Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1860 – 195091Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini1965 – 205389Fibronectin type-III 12PROSITE-ProRule annotationAdd
BLAST
Domaini2071 – 216191Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini2169 – 225789Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini2268 – 235891Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini2367 – 245892Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini2468 – 256295Fibronectin type-III 17PROSITE-ProRule annotationAdd
BLAST
Domaini2579 – 267799Fibronectin type-III 18PROSITE-ProRule annotationAdd
BLAST
Domaini2685 – 278197Fibronectin type-III 19PROSITE-ProRule annotationAdd
BLAST
Domaini2791 – 288797Fibronectin type-III 20PROSITE-ProRule annotationAdd
BLAST
Domaini2888 – 298497Fibronectin type-III 21PROSITE-ProRule annotationAdd
BLAST
Domaini2994 – 308794Fibronectin type-III 22PROSITE-ProRule annotationAdd
BLAST
Domaini3107 – 319892Fibronectin type-III 23PROSITE-ProRule annotationAdd
BLAST
Domaini3213 – 330593Fibronectin type-III 24PROSITE-ProRule annotationAdd
BLAST
Domaini3309 – 340092Fibronectin type-III 25PROSITE-ProRule annotationAdd
BLAST
Domaini3402 – 349190Fibronectin type-III 26PROSITE-ProRule annotationAdd
BLAST
Domaini3496 – 358994Fibronectin type-III 27PROSITE-ProRule annotationAdd
BLAST
Domaini3598 – 369295Fibronectin type-III 28PROSITE-ProRule annotationAdd
BLAST
Domaini3702 – 379998Fibronectin type-III 29PROSITE-ProRule annotationAdd
BLAST
Domaini3803 – 389290Fibronectin type-III 30PROSITE-ProRule annotationAdd
BLAST
Domaini3893 – 397987Fibronectin type-III 31PROSITE-ProRule annotationAdd
BLAST
Domaini3980 – 407091Fibronectin type-III 32PROSITE-ProRule annotationAdd
BLAST
Domaini4066 – 4281216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili901 – 92222Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1748 – 17503Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the tenascin family.Curated
Contains 19 EGF-like domains.PROSITE-ProRule annotation
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
Contains 32 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00770000120463.
HOVERGENiHBG006855.
InParanoidiP22105.
KOiK06252.
PhylomeDBiP22105.
TreeFamiTF329915.

Family and domain databases

Gene3Di2.60.40.10. 32 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 31 hits.
PF12661. hEGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 9 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 32 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 31 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 18 hits.
PS01186. EGF_2. 19 hits.
PS50026. EGF_3. 8 hits.
PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 32 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform XB (identifier: P22105-1) [UniParc]FASTAAdd to Basket

Also known as: 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.

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        10         20         30         40         50
MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA
60 70 80 90 100
GVGSPSSQLY EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV
110 120 130 140 150
QALRVRLEIL EELVKGLKEQ CTGGCCPASA QAGTGQTDVR TLCSLHGVFD
160 170 180 190 200
LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP PSASGSCPDD CNDQGRCVRG
210 220 230 240 250
RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS GPDCSQRSCP
260 270 280 290 300
RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG
310 320 330 340 350
YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG
360 370 380 390 400
RCVDGRCVCW PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG
410 420 430 440 450
VRSCPGDCNQ RGRCEDGRCV CWPGYTGTDC GSRACPRDCR GRGRCENGVC
460 470 480 490 500
VCNAGYSGED CGVRSCPGDC RGRGRCESGR CMCWPGYTGR DCGTRACPGD
510 520 530 540 550
CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED GVCVCDAGYS
560 570 580 590 600
GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC
610 620 630 640 650
QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR
660 670 680 690 700
MCPADCRGRG RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA
710 720 730 740 750
GQCVCVEGFR GPDCAIQTCP GDCRGRGECH DGSCVCKDGY AGEDCGEARV
760 770 780 790 800
PSSASAYDQR GLAPGQEYQV TVRALRGTSW GLPASKTITT MIDGPQDLRV
810 820 830 840 850
VAVTPTTLEL GWLRPQAEVD RFVVSYVSAG NQRVRLEVPP EADGTLLTDL
860 870 880 890 900
MPGVEYVVTV TAERGRAVSY PASVRANTEE REEESPPRPS LSQPPRRPWG
910 920 930 940 950
NLTAELSRFR GTVQDLERHL RAHGYPLRAN QTYTSVARHI HEYLQRQVLG
960 970 980 990 1000
SSADGALLVS LDGLRGQFER VVLRWRPQPP AEGPGGELTV PGTTRTVSLP
1010 1020 1030 1040 1050
DLRPGTTYHV EVHGVRAGQT SKSYAFITTT GPSTTQGAQA PLLQQRPQEL
1060 1070 1080 1090 1100
GELRVLGRDE TGRLRVVWTA QPDTFAYFQL RMRVPEGPGA HEEVLPGDVR
1110 1120 1130 1140 1150
QALVPPPPPG TPYELSLHGV PPGGKPSDPI IYQGIMDKDE EKPGKSSGPP
1160 1170 1180 1190 1200
RLGELTVTDR TSDSLLLRWT VPEGEFDSFV IQYKDRDGQP QVVPVEGPQR
1210 1220 1230 1240 1250
SAVITSLDPG RKYKFVLYGF VGKKRHGPLV AEAKILPQSD PSPGTPPHLG
1260 1270 1280 1290 1300
NLWVTDPTPD SLHLSWTVPE GQFDTFMVQY RDRDGRPQVV PVEGPERSFV
1310 1320 1330 1340 1350
VSSLDPDHKY RFTLFGIANK KRYGPLTADG TTAPERKEEP PRPEFLEQPL
1360 1370 1380 1390 1400
LGELTVTGVT PDSLRLSWTV AQGPFDSFMV QYKDAQGQPQ AVPVAGDENE
1410 1420 1430 1440 1450
VTVPGLDPDR KYKMNLYGLR GRQRVGPESV VAKTAPQEDV DETPSPTELG
1460 1470 1480 1490 1500
TEAPESPEEP LLGELTVTGS SPDSLSLFWT VPQGSFDSFT VQYKDRDGRP
1510 1520 1530 1540 1550
RAVRVGGKES EVTVGGLEPG HKYKMHLYGL HEGQRVGPVS AVGVTAPQQE
1560 1570 1580 1590 1600
ETPPATESPL EPRLGELTVT DVTPNSVGLS WTVPEGQFDS FIVQYKDKDG
1610 1620 1630 1640 1650
QPQVVPVAAD QREVTVYNLE PERKYKMNMY GLHDGQRMGP LSVVIVTAPA
1660 1670 1680 1690 1700
TEASKPPLEP RLGELTVTDI TPDSVGLSWT VPEGEFDSFV VQYKDRDGQP
1710 1720 1730 1740 1750
QVVPVAADQR EVTIPDLEPS RKYKFLLFGI QDGKRRSPVS VEAKTVARGD
1760 1770 1780 1790 1800
ASPGAPPRLG ELWVTDPTPD SLRLSWTVPE GQFDSFVVQF KDKDGPQVVP
1810 1820 1830 1840 1850
VEGHERSVTV TPLDAGRKYR FLLYGLLGKK RHGPLTADGT TEARSAMDDT
1860 1870 1880 1890 1900
GTKRPPKPRL GEELQVTTVT QNSVGLSWTV PEGQFDSFVV QYKDRDGQPQ
1910 1920 1930 1940 1950
VVPVEGSLRE VSVPGLDPAH RYKLLLYGLH HGKRVGPISA VAITAGREET
1960 1970 1980 1990 2000
ETETTAPTPP APEPHLGELT VEEATSHTLH LSWMVTEGEF DSFEIQYTDR
2010 2020 2030 2040 2050
DGQLQMVRIG GDRNDITLSG LESDHRYLVT LYGFSDGKHV GPVHVEALTV
2060 2070 2080 2090 2100
PEEEKPSEPP TATPEPPIKP RLGELTVTDA TPDSLSLSWT VPEGQFDHFL
2110 2120 2130 2140 2150
VQYRNGDGQP KAVRVPGHEE GVTISGLEPD HKYKMNLYGF HGGQRMGPVS
2160 2170 2180 2190 2200
VVGVTEPSME APEPAEEPLL GELTVTGSSP DSLSLSWTVP QGRFDSFTVQ
2210 2220 2230 2240 2250
YKDRDGRPQV VRVGGEESEV TVGGLEPGRK YKMHLYGLHE GRRVGPVSAV
2260 2270 2280 2290 2300
GVTAPEEESP DAPLAKLRLG QMTVRDITSD SLSLSWTVPE GQFDHFLVQF
2310 2320 2330 2340 2350
KNGDGQPKAV RVPGHEDGVT ISGLEPDHKY KMNLYGFHGG QRVGPVSAVG
2360 2370 2380 2390 2400
LTASTEPPTP EPPIKPRLEE LTVTDATPDS LSLSWTVPEG QFDHFLVQYK
2410 2420 2430 2440 2450
NGDGQPKATR VPGHEDRVTI SGLEPDNKYK MNLYGFHGGQ RVGPVSAIGV
2460 2470 2480 2490 2500
TEEETPSPTE PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS
2510 2520 2530 2540 2550
FTVQYKDRDG RPQVVRVGGE ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP
2560 2570 2580 2590 2600
VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP EEPLLGELTV TGSSPDSLSL
2610 2620 2630 2640 2650
SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL EPGRKYKMHL
2660 2670 2680 2690 2700
YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT
2710 2720 2730 2740 2750
PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH
2760 2770 2780 2790 2800
KYKMNLYGFH GGQRVGPISV IGVTEEETPS PTELSTEAPE PPEEPLLGEL
2810 2820 2830 2840 2850
TVTGSSPDSL SLSWTIPQGH FDSFTVQYKD RDGRPQVMRV RGEESEVTVG
2860 2870 2880 2890 2900
GLEPGRKYKM HLYGLHEGRR VGPVSTVGVT VPTTTPEPPN KPRLGELTVT
2910 2920 2930 2940 2950
DATPDSLSLS WMVPEGQFDH FLVQYRNGDG QPKVVRVPGH EDGVTISGLE
2960 2970 2980 2990 3000
PDHKYKMNLY GFHGGQRVGP ISVIGVTEEE TPAPTEPSTE APEPPEEPLL
3010 3020 3030 3040 3050
GELTVTGSSP DSLSLSWTIP QGRFDSFTVQ YKDRDGRPQV VRVRGEESEV
3060 3070 3080 3090 3100
TVGGLEPGCK YKMHLYGLHE GQRVGPVSAV GVTAPKDEAE TTQAVPTMTP
3110 3120 3130 3140 3150
EPPIKPRLGE LTVTDATPDS LSLSWMVPEG QFDHFLVQYR NGDGQPKAVR
3160 3170 3180 3190 3200
VPGHEDGVTI SGLEPDHKYK MNLYGFHGGQ RVGPVSAIGV TEEETPSPTE
3210 3220 3230 3240 3250
PSTEAPEAPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG
3260 3270 3280 3290 3300
QPQVVRVRGE ESEVTVGGLE PGRKYKMHLY GLHEGQRVGP VSTVGITAPL
3310 3320 3330 3340 3350
PTPLPVEPRL GELAVAAVTS DSVGLSWTVA QGPFDSFLVQ YRDAQGQPQA
3360 3370 3380 3390 3400
VPVSGDLRAV AVSGLDPARK YKFLLFGLQN GKRHGPVPVE ARTAPDTKPS
3410 3420 3430 3440 3450
PRLGELTVTD ATPDSVGLSW TVPEGEFDSF VVQYKDKDGR LQVVPVAANQ
3460 3470 3480 3490 3500
REVTVQGLEP SRKYRFLLYG LSGRKRLGPI SADSTTAPLE KELPPHLGEL
3510 3520 3530 3540 3550
TVAEETSSSL RLSWTVAQGP FDSFVVQYRD TDGQPRAVPV AADQRTVTVE
3560 3570 3580 3590 3600
DLEPGKKYKF LLYGLLGGKR LGPVSALGMT APEEDTPAPE LAPEAPEPPE
3610 3620 3630 3640 3650
EPRLGVLTVT DTTPDSMRLS WSVAQGPFDS FVVQYEDTNG QPQALLVDGD
3660 3670 3680 3690 3700
QSKILISGLE PSTPYRFLLY GLHEGKRLGP LSAEGTTGLA PAGQTSEESR
3710 3720 3730 3740 3750
PRLSQLSVTD VTTSSLRLNW EAPPGAFDSF LLRFGVPSPS TLEPHPRPLL
3760 3770 3780 3790 3800
QRELMVPGTR HSAVLRDLRS GTLYSLTLYG LRGPHKADSI QGTARTLSPV
3810 3820 3830 3840 3850
LESPRDLQFS EIRETSAKVN WMPPPSRADS FKVSYQLADG GEPQSVQVDG
3860 3870 3880 3890 3900
QARTQKLQGL IPGARYEVTV VSVRGFEESE PLTGFLTTVP DGPTQLRALN
3910 3920 3930 3940 3950
LTEGFAVLHW KPPQNPVDTY DVQVTAPGAP PLQAETPGSA VDYPLHDLVL
3960 3970 3980 3990 4000
HTNYTATVRG LRGPNLTSPA SITFTTGLEA PRDLEAKEVT PRTALLTWTE
4010 4020 4030 4040 4050
PPVRPAGYLL SFHTPGGQNQ EILLPGGITS HQLLGLFPST SYNARLQAMW
4060 4070 4080 4090 4100
GQSLLPPVST SFTTGGLRIP FPRDCGEEMQ NGAGASRTST IFLNGNRERP
4110 4120 4130 4140 4150
LNVFCDMETD GGGWLVFQRR MDGQTDFWRD WEDYAHGFGN ISGEFWLGNE
4160 4170 4180 4190 4200
ALHSLTQAGD YSMRVDLRAG DEAVFAQYDS FHVDSAAEYY RLHLEGYHGT
4210 4220 4230 4240 4250
AGDSMSYHSG SVFSARDRDP NSLLISCAVS YRGAWWYRNC HYANLNGLYG
4260 4270 4280
STVDHQGVSW YHWKGFEFSV PFTEMKLRPR NFRSPAGGG

Note: No experimental confirmation available.

Length:4,289
Mass (Da):464,325
Last modified:March 2, 2010 - v3
Checksum:i3E26AA5923D1AAA2
GO
Isoform XB-short (identifier: P22105-2) [UniParc]FASTAAdd to Basket

Also known as: 2

The sequence of this isoform differs from the canonical sequence as follows:
     1-3616: Missing.

Show »
Length:673
Mass (Da):74,030
Checksum:i2A14010E8A633FA1
GO
Isoform 3 (identifier: P22105-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     747-747: E → EEVPTIEGMRMHLLEETTVRTEWTPAPGPVDAYEIQFIPTTEGASPPFT
     878-1013: Missing.
     1014-1030: GVRAGQTSKSYAFITTT → TGSSPLGLLGTTDEPPPS
     1648-1648: A → APLPPA
     2155-2155: T → TAAEEETPSPT
     2353-2353: A → APGKDEEMAPA
     2451-2451: T → TAA
     2774-2774: T → TAA
     2880-2880: T → TEDEAETTQA
     2977-2977: T → TAA

Note: No experimental confirmation available.

Show »
Length:4,242
Mass (Da):458,220
Checksum:i7E07AC46BF6F2599
GO

Sequence cautioni

The sequence AAH33740.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB89296.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI17414.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI17471.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI18078.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI18332.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAQ09268.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351G → GEQG in CAA50739. (PubMed:7686164)Curated
Sequence conflicti2789 – 27891P → R in AAB67981. (PubMed:14656967)Curated
Sequence conflicti2789 – 27891P → R in AAB47488. (PubMed:14656967)Curated
Sequence conflicti3836 – 38361Q → L in AAH33740. (PubMed:15489334)Curated
Sequence conflicti3922 – 39221V → I in AAI25115. (PubMed:15489334)Curated
Sequence conflicti3922 – 39221V → I in AAI25116. (PubMed:15489334)Curated
Sequence conflicti3922 – 39221V → I in BAD92249. 1 PublicationCurated
Sequence conflicti4019 – 40191N → T in AAI25115. (PubMed:15489334)Curated
Sequence conflicti4019 – 40191N → T in AAI25116. (PubMed:15489334)Curated
Sequence conflicti4019 – 40191N → T in BAD92249. 1 PublicationCurated
Sequence conflicti4038 – 40381P → G in AAB41287. (PubMed:8530023)Curated
Sequence conflicti4038 – 40381P → G in AAA35884. (PubMed:2475872)Curated
Sequence conflicti4049 – 40491M → T in AAI25116. (PubMed:15489334)Curated
Sequence conflicti4049 – 40491M → T in BAD92249. 1 PublicationCurated
Sequence conflicti4102 – 41021N → I in AAI25115. (PubMed:15489334)Curated
Sequence conflicti4163 – 41631M → I in AAB41287. (PubMed:8530023)Curated
Sequence conflicti4163 – 41631M → I in AAA35884. (PubMed:2475872)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291R → W in EDS3. 1 Publication
VAR_046499
Natural varianti302 – 3021T → A.1 Publication
Corresponds to variant rs1150752 [ dbSNP | Ensembl ].
VAR_044347
Natural varianti511 – 5111R → H.
Corresponds to variant rs204896 [ dbSNP | Ensembl ].
VAR_021908
Natural varianti641 – 6411G → C.
Corresponds to variant rs17201609 [ dbSNP | Ensembl ].
VAR_055781
Natural varianti650 – 6501R → H.
Corresponds to variant rs17201602 [ dbSNP | Ensembl ].
VAR_055782
Natural varianti825 – 8251S → A.
Corresponds to variant rs204900 [ dbSNP | Ensembl ].
VAR_055783
Natural varianti1195 – 11951V → M in EDS3. 1 Publication
VAR_046500
Natural varianti1248 – 12481H → R.
Corresponds to variant rs185819 [ dbSNP | Ensembl ].
VAR_024270
Natural varianti1987 – 19871E → K.
Corresponds to variant rs17207923 [ dbSNP | Ensembl ].
VAR_059276
Natural varianti2363 – 23631P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_020170
Natural varianti2425 – 24251P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_055784
Natural varianti2472 – 24721P → L.
Corresponds to variant rs12524664 [ dbSNP | Ensembl ].
VAR_059277
Natural varianti2555 – 25551G → S.
Corresponds to variant rs2269429 [ dbSNP | Ensembl ].
VAR_020171
Natural varianti2578 – 25781G → E.2 Publications
Corresponds to variant rs1009382 [ dbSNP | Ensembl ].
VAR_020172
Natural varianti4033 – 40331L → I.1 Publication
VAR_046501

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 36163616Missing in isoform XB-short. 2 PublicationsVSP_001418Add
BLAST
Alternative sequencei747 – 7471E → EEVPTIEGMRMHLLEETTVR TEWTPAPGPVDAYEIQFIPT TEGASPPFT in isoform 3. CuratedVSP_034569
Alternative sequencei878 – 1013136Missing in isoform 3. CuratedVSP_034570Add
BLAST
Alternative sequencei1014 – 103017GVRAG…FITTT → TGSSPLGLLGTTDEPPPS in isoform 3. CuratedVSP_034571Add
BLAST
Alternative sequencei1648 – 16481A → APLPPA in isoform 3. CuratedVSP_034572
Alternative sequencei2155 – 21551T → TAAEEETPSPT in isoform 3. CuratedVSP_034573
Alternative sequencei2353 – 23531A → APGKDEEMAPA in isoform 3. CuratedVSP_034574
Alternative sequencei2451 – 24511T → TAA in isoform 3. CuratedVSP_034575
Alternative sequencei2774 – 27741T → TAA in isoform 3. CuratedVSP_034576
Alternative sequencei2880 – 28801T → TEDEAETTQA in isoform 3. CuratedVSP_034578
Alternative sequencei2977 – 29771T → TAA in isoform 3. CuratedVSP_034577

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24488 mRNA. Translation: AAB41287.1.
AF019413 Genomic DNA. Translation: AAB67981.1.
U89337 Genomic DNA. Translation: AAB47488.1.
AL049547 Genomic DNA. Translation: CAB89296.1. Different initiation.
AL049547 Genomic DNA. Translation: CAB89300.1.
AL645922, AL662884, AL772248 Genomic DNA. Translation: CAQ09268.1. Sequence problems.
AL662828, AL662849 Genomic DNA. Translation: CAI17414.1. Sequence problems.
AL662849, AL662828 Genomic DNA. Translation: CAI17471.1. Sequence problems.
AL662884, AL645922, AL772248 Genomic DNA. Translation: CAI18332.1. Sequence problems.
AL772248, AL645922, AL662884 Genomic DNA. Translation: CAI18078.1. Sequence problems.
CH471081 Genomic DNA. Translation: EAX03574.1.
BC033740 mRNA. Translation: AAH33740.1. Different initiation.
BC125114 mRNA. Translation: AAI25115.1.
BC125115 mRNA. Translation: AAI25116.1.
BC130037 mRNA. Translation: AAI30038.1.
X71923 mRNA. Translation: CAA50739.1.
Y13782 mRNA. Translation: CAA74109.1.
Y13783 Genomic DNA. Translation: CAA74110.1.
U52696 mRNA. Translation: AAC50889.1.
AB209012 mRNA. Translation: BAD92249.1.
M25813 mRNA. Translation: AAA35884.1.
CCDSiCCDS4736.1. [P22105-2]
PIRiA40701.
A42175.
B42175.
D42175.
RefSeqiNP_061978.6. NM_019105.6. [P22105-3]
NP_115859.2. NM_032470.3. [P22105-2]
UniGeneiHs.485104.

Genome annotation databases

EnsembliENST00000451343; ENSP00000407685; ENSG00000168477. [P22105-2]
ENST00000546684; ENSP00000447694; ENSG00000236236.
ENST00000550539; ENSP00000448326; ENSG00000229353.
GeneIDi7148.
KEGGihsa:7148.
UCSCiuc003nzg.1. human. [P22105-2]
uc003nzl.2. human. [P22105-3]

Polymorphism databases

DMDMi290457668.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24488 mRNA. Translation: AAB41287.1 .
AF019413 Genomic DNA. Translation: AAB67981.1 .
U89337 Genomic DNA. Translation: AAB47488.1 .
AL049547 Genomic DNA. Translation: CAB89296.1 . Different initiation.
AL049547 Genomic DNA. Translation: CAB89300.1 .
AL645922 , AL662884 , AL772248 Genomic DNA. Translation: CAQ09268.1 . Sequence problems.
AL662828 , AL662849 Genomic DNA. Translation: CAI17414.1 . Sequence problems.
AL662849 , AL662828 Genomic DNA. Translation: CAI17471.1 . Sequence problems.
AL662884 , AL645922 , AL772248 Genomic DNA. Translation: CAI18332.1 . Sequence problems.
AL772248 , AL645922 , AL662884 Genomic DNA. Translation: CAI18078.1 . Sequence problems.
CH471081 Genomic DNA. Translation: EAX03574.1 .
BC033740 mRNA. Translation: AAH33740.1 . Different initiation.
BC125114 mRNA. Translation: AAI25115.1 .
BC125115 mRNA. Translation: AAI25116.1 .
BC130037 mRNA. Translation: AAI30038.1 .
X71923 mRNA. Translation: CAA50739.1 .
Y13782 mRNA. Translation: CAA74109.1 .
Y13783 Genomic DNA. Translation: CAA74110.1 .
U52696 mRNA. Translation: AAC50889.1 .
AB209012 mRNA. Translation: BAD92249.1 .
M25813 mRNA. Translation: AAA35884.1 .
CCDSi CCDS4736.1. [P22105-2 ]
PIRi A40701.
A42175.
B42175.
D42175.
RefSeqi NP_061978.6. NM_019105.6. [P22105-3 ]
NP_115859.2. NM_032470.3. [P22105-2 ]
UniGenei Hs.485104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CUH NMR - A 3890-3991 [» ]
2CUI NMR - A 3699-3797 [» ]
2CUM NMR - A 3978-4069 [» ]
ProteinModelPortali P22105.
SMRi P22105. Positions 140-878, 983-4279.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P22105. 7 interactions.

PTM databases

PhosphoSitei P22105.

Polymorphism databases

DMDMi 290457668.

Proteomic databases

MaxQBi P22105.
PRIDEi P22105.

Protocols and materials databases

DNASUi 7148.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000451343 ; ENSP00000407685 ; ENSG00000168477 . [P22105-2 ]
ENST00000546684 ; ENSP00000447694 ; ENSG00000236236 .
ENST00000550539 ; ENSP00000448326 ; ENSG00000229353 .
GeneIDi 7148.
KEGGi hsa:7148.
UCSCi uc003nzg.1. human. [P22105-2 ]
uc003nzl.2. human. [P22105-3 ]

Organism-specific databases

CTDi 7148.
GeneCardsi GC06M032008.
GC06Mn31966.
GC06Mo32000.
GeneReviewsi TNXB.
H-InvDB HIX0165968.
HIX0207682.
HGNCi HGNC:11976. TNXB.
HPAi CAB005373.
MIMi 130020. phenotype.
600985. gene.
606408. phenotype.
neXtProti NX_P22105.
Orphaneti 230839. Ehlers-Danlos syndrome due to tenascin-X deficiency.
285. Ehlers-Danlos syndrome, hypermobility type.
PharmGKBi PA36662.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00770000120463.
HOVERGENi HBG006855.
InParanoidi P22105.
KOi K06252.
PhylomeDBi P22105.
TreeFami TF329915.

Enzyme and pathway databases

Reactomei REACT_163906. ECM proteoglycans.

Miscellaneous databases

ChiTaRSi TNXB. human.
EvolutionaryTracei P22105.
GeneWikii Tenascin_X.
GenomeRNAii 7148.
NextBioi 27974.
PROi P22105.
SOURCEi Search...

Gene expression databases

Bgeei P22105.
ExpressionAtlasi P22105. baseline.
Genevestigatori P22105.

Family and domain databases

Gene3Di 2.60.40.10. 32 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view ]
Pfami PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 31 hits.
PF12661. hEGF. 7 hits.
[Graphical view ]
SMARTi SM00181. EGF. 9 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 32 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 31 hits.
SSF56496. SSF56496. 1 hit.
PROSITEi PS00022. EGF_1. 18 hits.
PS01186. EGF_2. 19 hits.
PS50026. EGF_3. 8 hits.
PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 32 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequences promoting the transcription of the human XA gene overlapping P450c21A correctly predict the presence of a novel, adrenal-specific, truncated form of tenascin-X."
    Tee M.K., Thomson A.A., Bristow J., Miller W.L.
    Genomics 28:171-178(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XB-SHORT).
    Tissue: Adrenal gland.
  2. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-2578.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-302 AND GLU-2578.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XB-SHORT), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3455-4289 (ISOFORMS XB/3).
  6. "Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B."
    Bristow J., Tee M.K., Gitelman S.E., Mellon S.H., Miller W.L.
    J. Cell Biol. 122:265-278(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-747 AND 1687-1944 (ISOFORMS XB/3).
    Tissue: Leukocyte.
  7. "Alternate promoters and alternate splicing of human tenascin-X, a gene with 5' and 3' ends buried in other genes."
    Speek M., Barry F., Miller W.L.
    Hum. Mol. Genet. 5:1749-1758(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-23 (ISOFORMS XB/3).
    Tissue: Fetal adrenal gland.
  8. "Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin."
    Matsumoto K., Arai M., Ishihara N., Ando A., Inoko H., Ikemura T.
    Genomics 12:485-491(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1148-1235; 2581-2668; 2687-2774 AND 2793-2880.
    Tissue: B-cell.
  9. "Identification and characterization of multiple species of tenascin-X in human serum."
    Egging D.F., Peeters A.C.T.M., Grebenchtchikov N., Geurts-Moespot A., Sweep C.G.J., den Heijer M., Schalkwijk J.
    FEBS J. 274:1280-1289(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1486-1494; 1525-1535; 2194-2202; 2498-2506; 2609-2617; 2821-2829; 2840-2857; 3024-3032; 3063-3073; 3238-3246; 3257-3274; 3277-3287; 3654-3666 AND 3678-3710 (ISOFORMS XB/3), INTERACTION WITH TROPOELASTIN, DEVELOPMENTAL STAGE.
  10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3406-4289 (ISOFORMS XB/3).
    Tissue: Brain.
  11. "Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus."
    Morel Y., Bristow J., Gitelman S.E., Miller W.L.
    Proc. Natl. Acad. Sci. U.S.A. 86:6582-6586(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3470-4289 (ISOFORMS XB/3).
  12. "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-3965.
    Tissue: Plasma.
  13. "Interactions of human tenascin-X domains with dermal extracellular matrix molecules."
    Egging D.F., van den Berkmortel F., Taylor G., Bristow J., Schalkwijk J.
    Arch. Dermatol. Res. 298:389-396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COLLAGEN AND TROPOELASTIN.
  14. "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-901 AND ASN-930.
    Tissue: Liver.
  15. "Solution structure of the 29th, 31st and 33rd fibronectin type-III domains of the human tenascin-X."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 3699-4069.
  16. Cited for: INVOLVEMENT IN EDSTNXD.
  17. "Elastic fiber abnormalities in hypermobility type Ehlers-Danlos syndrome patients with tenascin-X mutations."
    Zweers M.C., Dean W.B., van Kuppevelt T.H., Bristow J., Schalkwijk J.
    Clin. Genet. 67:330-334(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDS3 TRP-29 AND MET-1195, VARIANT ILE-4033.

Entry informationi

Entry nameiTENX_HUMAN
AccessioniPrimary (citable) accession number: P22105
Secondary accession number(s): P78530
, P78531, Q08424, Q08AM0, Q08AM1, Q59GU7, Q5SQD3, Q5ST74, Q7L8Q4, Q8N4R1, Q9NPK9, Q9UC10, Q9UC11, Q9UC12, Q9UC13, Q9UMG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: March 2, 2010
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 6
    Human chromosome 6: 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