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Protein

Tenascin-X

Gene

TNXB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:11976. TNXB.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • intracellular Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Tenascin-X deficiency (TNXD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionTNXD 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.

See also OMIM:606408
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4072 – 40721R → C in TNXD. 1 Publication
VAR_072582
Vesicoureteral reflux 8 (VUR8)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease belonging to the group of congenital anomalies of the kidney and urinary tract. It is characterized by the reflux of urine from the bladder into the ureters and sometimes into the kidneys, and is a risk factor for urinary tract infections. Primary disease results from a developmental defect of the ureterovesical junction. In combination with intrarenal reflux, the resulting inflammatory reaction may result in renal injury or scarring, also called reflux nephropathy. Extensive renal scarring impairs renal function and may predispose patients to hypertension, proteinuria, renal insufficiency and end-stage renal disease.

See also OMIM:615963
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1244 – 12441T → R in VUR8. 1 Publication
VAR_072580
Natural varianti3210 – 32101V → I in VUR8; shows significantly impaired migration in a wound-healing assay; associated with decreased expression of phosphorylated PTK2 protein. 1 Publication
VAR_072581

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

MIMi130020. phenotype.
606408. phenotype.
615963. phenotype.
Orphaneti230839. Ehlers-Danlos syndrome due to tenascin-X deficiency.
285. Ehlers-Danlos syndrome, hypermobility type.
289365. Familial vesicoureteral reflux.
PharmGKBiPA36662.

Polymorphism and mutation databases

BioMutaiTNXB.
DMDMi290457668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 42424219Tenascin-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
Glycosylationi3853 – 38531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3906 – 39061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3918 – 39181N-linked (GlcNAc...)By similarity
Disulfide bondi4028 ↔ 4058By similarity
Glycosylationi4093 – 40931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4180 ↔ 4193By 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.
GenevisibleiP22105. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BANPQ8N9N54EBI-2821024,EBI-744695

Protein-protein interaction databases

BioGridi113001. 3 interactions.
IntActiP22105. 7 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUHNMR-A3843-3944[»]
2CUINMR-A3652-3750[»]
2CUMNMR-A3931-4022[»]
ProteinModelPortaliP22105.
SMRiP22105. Positions 3700-3798, 3894-4072.
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
Domaini959 – 105193Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini1064 – 115390Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1161 – 124989Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1263 – 135290Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1374 – 146895Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1476 – 157297Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini1574 – 166996Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1674 – 176491Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1778 – 186891Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1883 – 197189Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1989 – 2089101Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini2097 – 218589Fibronectin type-III 12PROSITE-ProRule annotationAdd
BLAST
Domaini2196 – 2296101Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini2305 – 239894Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini2408 – 250295Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini2519 – 261799Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini2625 – 272399Fibronectin type-III 17PROSITE-ProRule annotationAdd
BLAST
Domaini2733 – 2838106Fibronectin type-III 18PROSITE-ProRule annotationAdd
BLAST
Domaini2839 – 293799Fibronectin type-III 19PROSITE-ProRule annotationAdd
BLAST
Domaini2947 – 304094Fibronectin type-III 20PROSITE-ProRule annotationAdd
BLAST
Domaini3060 – 315192Fibronectin type-III 21PROSITE-ProRule annotationAdd
BLAST
Domaini3166 – 325893Fibronectin type-III 22PROSITE-ProRule annotationAdd
BLAST
Domaini3262 – 335392Fibronectin type-III 23PROSITE-ProRule annotationAdd
BLAST
Domaini3355 – 344490Fibronectin type-III 24PROSITE-ProRule annotationAdd
BLAST
Domaini3449 – 354294Fibronectin type-III 25PROSITE-ProRule annotationAdd
BLAST
Domaini3551 – 364595Fibronectin type-III 26PROSITE-ProRule annotationAdd
BLAST
Domaini3655 – 375298Fibronectin type-III 27PROSITE-ProRule annotationAdd
BLAST
Domaini3756 – 384590Fibronectin type-III 28PROSITE-ProRule annotationAdd
BLAST
Domaini3846 – 393287Fibronectin type-III 29PROSITE-ProRule annotationAdd
BLAST
Domaini3933 – 402391Fibronectin type-III 30PROSITE-ProRule annotationAdd
BLAST
Domaini4019 – 4234216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1666 – 16683Cell 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 30 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. FN3_dom.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: P22105-1) [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.

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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 AGEDCGEEVP
760 770 780 790 800
TIEGMRMHLL EETTVRTEWT PAPGPVDAYE IQFIPTTEGA SPPFTARVPS
810 820 830 840 850
SASAYDQRGL APGQEYQVTV RALRGTSWGL PASKTITTMI DGPQDLRVVA
860 870 880 890 900
VTPTTLELGW LRPQAEVDRF VVSYVSAGNQ RVRLEVPPEA DGTLLTDLMP
910 920 930 940 950
GVEYVVTVTA ERGRAVSYPA SVRANTGSSP LGLLGTTDEP PPSGPSTTQG
960 970 980 990 1000
AQAPLLQQRP QELGELRVLG RDETGRLRVV WTAQPDTFAY FQLRMRVPEG
1010 1020 1030 1040 1050
PGAHEEVLPG DVRQALVPPP PPGTPYELSL HGVPPGGKPS DPIIYQGIMD
1060 1070 1080 1090 1100
KDEEKPGKSS GPPRLGELTV TDRTSDSLLL RWTVPEGEFD SFVIQYKDRD
1110 1120 1130 1140 1150
GQPQVVPVEG PQRSAVITSL DPGRKYKFVL YGFVGKKRHG PLVAEAKILP
1160 1170 1180 1190 1200
QSDPSPGTPP HLGNLWVTDP TPDSLHLSWT VPEGQFDTFM VQYRDRDGRP
1210 1220 1230 1240 1250
QVVPVEGPER SFVVSSLDPD HKYRFTLFGI ANKKRYGPLT ADGTTAPERK
1260 1270 1280 1290 1300
EEPPRPEFLE QPLLGELTVT GVTPDSLRLS WTVAQGPFDS FMVQYKDAQG
1310 1320 1330 1340 1350
QPQAVPVAGD ENEVTVPGLD PDRKYKMNLY GLRGRQRVGP ESVVAKTAPQ
1360 1370 1380 1390 1400
EDVDETPSPT ELGTEAPESP EEPLLGELTV TGSSPDSLSL FWTVPQGSFD
1410 1420 1430 1440 1450
SFTVQYKDRD GRPRAVRVGG KESEVTVGGL EPGHKYKMHL YGLHEGQRVG
1460 1470 1480 1490 1500
PVSAVGVTAP QQEETPPATE SPLEPRLGEL TVTDVTPNSV GLSWTVPEGQ
1510 1520 1530 1540 1550
FDSFIVQYKD KDGQPQVVPV AADQREVTVY NLEPERKYKM NMYGLHDGQR
1560 1570 1580 1590 1600
MGPLSVVIVT APLPPAPATE ASKPPLEPRL GELTVTDITP DSVGLSWTVP
1610 1620 1630 1640 1650
EGEFDSFVVQ YKDRDGQPQV VPVAADQREV TIPDLEPSRK YKFLLFGIQD
1660 1670 1680 1690 1700
GKRRSPVSVE AKTVARGDAS PGAPPRLGEL WVTDPTPDSL RLSWTVPEGQ
1710 1720 1730 1740 1750
FDSFVVQFKD KDGPQVVPVE GHERSVTVTP LDAGRKYRFL LYGLLGKKRH
1760 1770 1780 1790 1800
GPLTADGTTE ARSAMDDTGT KRPPKPRLGE ELQVTTVTQN SVGLSWTVPE
1810 1820 1830 1840 1850
GQFDSFVVQY KDRDGQPQVV PVEGSLREVS VPGLDPAHRY KLLLYGLHHG
1860 1870 1880 1890 1900
KRVGPISAVA ITAGREETET ETTAPTPPAP EPHLGELTVE EATSHTLHLS
1910 1920 1930 1940 1950
WMVTEGEFDS FEIQYTDRDG QLQMVRIGGD RNDITLSGLE SDHRYLVTLY
1960 1970 1980 1990 2000
GFSDGKHVGP VHVEALTVPE EEKPSEPPTA TPEPPIKPRL GELTVTDATP
2010 2020 2030 2040 2050
DSLSLSWTVP EGQFDHFLVQ YRNGDGQPKA VRVPGHEEGV TISGLEPDHK
2060 2070 2080 2090 2100
YKMNLYGFHG GQRMGPVSVV GVTAAEEETP SPTEPSMEAP EPAEEPLLGE
2110 2120 2130 2140 2150
LTVTGSSPDS LSLSWTVPQG RFDSFTVQYK DRDGRPQVVR VGGEESEVTV
2160 2170 2180 2190 2200
GGLEPGRKYK MHLYGLHEGR RVGPVSAVGV TAPEEESPDA PLAKLRLGQM
2210 2220 2230 2240 2250
TVRDITSDSL SLSWTVPEGQ FDHFLVQFKN GDGQPKAVRV PGHEDGVTIS
2260 2270 2280 2290 2300
GLEPDHKYKM NLYGFHGGQR VGPVSAVGLT APGKDEEMAP ASTEPPTPEP
2310 2320 2330 2340 2350
PIKPRLEELT VTDATPDSLS LSWTVPEGQF DHFLVQYKNG DGQPKATRVP
2360 2370 2380 2390 2400
GHEDRVTISG LEPDNKYKMN LYGFHGGQRV GPVSAIGVTA AEEETPSPTE
2410 2420 2430 2440 2450
PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG
2460 2470 2480 2490 2500
RPQVVRVGGE ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ
2510 2520 2530 2540 2550
EDVDETPSPT EPGTEAPGPP EEPLLGELTV TGSSPDSLSL SWTVPQGRFD
2560 2570 2580 2590 2600
SFTVQYKDRD GRPQAVRVGG QESKVTVRGL EPGRKYKMHL YGLHEGRRLG
2610 2620 2630 2640 2650
PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT PDSLSLSWTV
2660 2670 2680 2690 2700
PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH
2710 2720 2730 2740 2750
GGQRVGPISV IGVTAAEEET PSPTELSTEA PEPPEEPLLG ELTVTGSSPD
2760 2770 2780 2790 2800
SLSLSWTIPQ GHFDSFTVQY KDRDGRPQVM RVRGEESEVT VGGLEPGRKY
2810 2820 2830 2840 2850
KMHLYGLHEG RRVGPVSTVG VTEDEAETTQ AVPTTTPEPP NKPRLGELTV
2860 2870 2880 2890 2900
TDATPDSLSL SWMVPEGQFD HFLVQYRNGD GQPKVVRVPG HEDGVTISGL
2910 2920 2930 2940 2950
EPDHKYKMNL YGFHGGQRVG PISVIGVTAA EEETPAPTEP STEAPEPPEE
2960 2970 2980 2990 3000
PLLGELTVTG SSPDSLSLSW TIPQGRFDSF TVQYKDRDGR PQVVRVRGEE
3010 3020 3030 3040 3050
SEVTVGGLEP GCKYKMHLYG LHEGQRVGPV SAVGVTAPKD EAETTQAVPT
3060 3070 3080 3090 3100
MTPEPPIKPR LGELTVTDAT PDSLSLSWMV PEGQFDHFLV QYRNGDGQPK
3110 3120 3130 3140 3150
AVRVPGHEDG VTISGLEPDH KYKMNLYGFH GGQRVGPVSA IGVTEEETPS
3160 3170 3180 3190 3200
PTEPSTEAPE APEEPLLGEL TVTGSSPDSL SLSWTVPQGR FDSFTVQYKD
3210 3220 3230 3240 3250
RDGQPQVVRV RGEESEVTVG GLEPGRKYKM HLYGLHEGQR VGPVSTVGIT
3260 3270 3280 3290 3300
APLPTPLPVE PRLGELAVAA VTSDSVGLSW TVAQGPFDSF LVQYRDAQGQ
3310 3320 3330 3340 3350
PQAVPVSGDL RAVAVSGLDP ARKYKFLLFG LQNGKRHGPV PVEARTAPDT
3360 3370 3380 3390 3400
KPSPRLGELT VTDATPDSVG LSWTVPEGEF DSFVVQYKDK DGRLQVVPVA
3410 3420 3430 3440 3450
ANQREVTVQG LEPSRKYRFL LYGLSGRKRL GPISADSTTA PLEKELPPHL
3460 3470 3480 3490 3500
GELTVAEETS SSLRLSWTVA QGPFDSFVVQ YRDTDGQPRA VPVAADQRTV
3510 3520 3530 3540 3550
TVEDLEPGKK YKFLLYGLLG GKRLGPVSAL GMTAPEEDTP APELAPEAPE
3560 3570 3580 3590 3600
PPEEPRLGVL TVTDTTPDSM RLSWSVAQGP FDSFVVQYED TNGQPQALLV
3610 3620 3630 3640 3650
DGDQSKILIS GLEPSTPYRF LLYGLHEGKR LGPLSAEGTT GLAPAGQTSE
3660 3670 3680 3690 3700
ESRPRLSQLS VTDVTTSSLR LNWEAPPGAF DSFLLRFGVP SPSTLEPHPR
3710 3720 3730 3740 3750
PLLQRELMVP GTRHSAVLRD LRSGTLYSLT LYGLRGPHKA DSIQGTARTL
3760 3770 3780 3790 3800
SPVLESPRDL QFSEIRETSA KVNWMPPPSR ADSFKVSYQL ADGGEPQSVQ
3810 3820 3830 3840 3850
VDGQARTQKL QGLIPGARYE VTVVSVRGFE ESEPLTGFLT TVPDGPTQLR
3860 3870 3880 3890 3900
ALNLTEGFAV LHWKPPQNPV DTYDVQVTAP GAPPLQAETP GSAVDYPLHD
3910 3920 3930 3940 3950
LVLHTNYTAT VRGLRGPNLT SPASITFTTG LEAPRDLEAK EVTPRTALLT
3960 3970 3980 3990 4000
WTEPPVRPAG YLLSFHTPGG QNQEILLPGG ITSHQLLGLF PSTSYNARLQ
4010 4020 4030 4040 4050
AMWGQSLLPP VSTSFTTGGL RIPFPRDCGE EMQNGAGASR TSTIFLNGNR
4060 4070 4080 4090 4100
ERPLNVFCDM ETDGGGWLVF QRRMDGQTDF WRDWEDYAHG FGNISGEFWL
4110 4120 4130 4140 4150
GNEALHSLTQ AGDYSMRVDL RAGDEAVFAQ YDSFHVDSAA EYYRLHLEGY
4160 4170 4180 4190 4200
HGTAGDSMSY HSGSVFSARD RDPNSLLISC AVSYRGAWWY RNCHYANLNG
4210 4220 4230 4240
LYGSTVDHQG VSWYHWKGFE FSVPFTEMKL RPRNFRSPAG GG
Note: No experimental confirmation available.
Length:4,242
Mass (Da):458,220
Last modified:June 24, 2015 - v4
Checksum:i7E07AC46BF6F2599
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:
     1-3569: Missing.

Show »
Length:673
Mass (Da):74,030
Checksum:i2A14010E8A633FA1
GO
Isoform 4 (identifier: P22105-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2823-2823: E → APE

Note: No experimental confirmation available. May be due to competing acceptor splice site in exon 24.
Show »
Length:4,244
Mass (Da):458,388
Checksum:i45A3D29FDF133DBA
GO
Isoform 5 (identifier: P22105-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: G → GEQG

Note: No experimental confirmation available. May be due to competing donor splice site in exon 1.
Show »
Length:4,245
Mass (Da):458,535
Checksum:iA004E187A210F3D8
GO

Sequence cautioni

The sequence AAB47488.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAB67981.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB89296.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3789 – 37891Q → L in AAH33740 (PubMed:15489334).Curated
Sequence conflicti3875 – 38751V → I in AAI25115 (PubMed:15489334).Curated
Sequence conflicti3875 – 38751V → I in AAI25116 (PubMed:15489334).Curated
Sequence conflicti3875 – 38751V → I in BAD92249 (Ref. 10) Curated
Sequence conflicti3972 – 39721N → T in AAI25115 (PubMed:15489334).Curated
Sequence conflicti3972 – 39721N → T in AAI25116 (PubMed:15489334).Curated
Sequence conflicti3972 – 39721N → T in BAD92249 (Ref. 10) Curated
Sequence conflicti3991 – 39911P → G in AAB41287 (PubMed:8530023).Curated
Sequence conflicti3991 – 39911P → G in AAA35884 (PubMed:2475872).Curated
Sequence conflicti4002 – 40021M → T in AAI25116 (PubMed:15489334).Curated
Sequence conflicti4002 – 40021M → T in BAD92249 (Ref. 10) Curated
Sequence conflicti4055 – 40551N → I in AAI25115 (PubMed:15489334).Curated
Sequence conflicti4116 – 41161M → I in AAB41287 (PubMed:8530023).Curated
Sequence conflicti4116 – 41161M → 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 varianti873 – 8731S → A.
Corresponds to variant rs204900 [ dbSNP | Ensembl ].
VAR_055783
Natural varianti1108 – 11081V → M in EDS3. 1 Publication
VAR_046500
Natural varianti1161 – 11611H → R.
Corresponds to variant rs185819 [ dbSNP | Ensembl ].
VAR_024270
Natural varianti1244 – 12441T → R in VUR8. 1 Publication
VAR_072580
Natural varianti1905 – 19051E → K.
Corresponds to variant rs17207923 [ dbSNP | Ensembl ].
VAR_059276
Natural varianti2301 – 23011P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_020170
Natural varianti2363 – 23631P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_055784
Natural varianti2412 – 24121P → L.
Corresponds to variant rs12524664 [ dbSNP | Ensembl ].
VAR_059277
Natural varianti2495 – 24951G → S.
Corresponds to variant rs2269429 [ dbSNP | Ensembl ].
VAR_020171
Natural varianti2518 – 25181G → E.2 Publications
Corresponds to variant rs1009382 [ dbSNP | Ensembl ].
VAR_020172
Natural varianti3210 – 32101V → I in VUR8; shows significantly impaired migration in a wound-healing assay; associated with decreased expression of phosphorylated PTK2 protein. 1 Publication
VAR_072581
Natural varianti3986 – 39861L → I.1 Publication
VAR_046501
Natural varianti4072 – 40721R → C in TNXD. 1 Publication
VAR_072582

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 35693569Missing in isoform XB-short. 2 PublicationsVSP_001418Add
BLAST
Alternative sequencei135 – 1351G → GEQG in isoform 5. VSP_057718
Alternative sequencei2823 – 28231E → APE in isoform 4. VSP_057719

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24488 mRNA. Translation: AAB41287.1.
AF019413 Genomic DNA. Translation: AAB67981.1. Sequence problems.
U89337 Genomic DNA. Translation: AAB47488.1. Sequence problems.
AL049547 Genomic DNA. Translation: CAB89296.1. Sequence problems.
AL049547 Genomic DNA. Translation: CAB89300.1.
AL645922 Genomic DNA. No translation available.
AL662828 Genomic DNA. No translation available.
AL662849 Genomic DNA. No translation available.
AL662884 Genomic DNA. No translation available.
AL772248 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03574.1.
BC033740 mRNA. Translation: AAH33740.1.
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]

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. Sequence problems.
U89337 Genomic DNA. Translation: AAB47488.1. Sequence problems.
AL049547 Genomic DNA. Translation: CAB89296.1. Sequence problems.
AL049547 Genomic DNA. Translation: CAB89300.1.
AL645922 Genomic DNA. No translation available.
AL662828 Genomic DNA. No translation available.
AL662849 Genomic DNA. No translation available.
AL662884 Genomic DNA. No translation available.
AL772248 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03574.1.
BC033740 mRNA. Translation: AAH33740.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUHNMR-A3843-3944[»]
2CUINMR-A3652-3750[»]
2CUMNMR-A3931-4022[»]
ProteinModelPortaliP22105.
SMRiP22105. Positions 3700-3798, 3894-4072.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113001. 3 interactions.
IntActiP22105. 7 interactions.

PTM databases

PhosphoSiteiP22105.

Polymorphism and mutation databases

BioMutaiTNXB.
DMDMi290457668.

Proteomic databases

MaxQBiP22105.
PRIDEiP22105.

Protocols and materials databases

DNASUi7148.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi7148.
GeneCardsiGC06M032008.
GC06Mn31966.
GC06Mo32000.
GeneReviewsiTNXB.
H-InvDBHIX0165968.
HIX0207682.
HGNCiHGNC:11976. TNXB.
HPAiCAB005373.
MIMi130020. phenotype.
600985. gene.
606408. phenotype.
615963. phenotype.
neXtProtiNX_P22105.
Orphaneti230839. Ehlers-Danlos syndrome due to tenascin-X deficiency.
285. Ehlers-Danlos syndrome, hypermobility type.
289365. Familial vesicoureteral reflux.
PharmGKBiPA36662.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiTNXB. human.
EvolutionaryTraceiP22105.
GeneWikiiTenascin_X.
GenomeRNAii7148.
NextBioi27974.
PROiP22105.
SOURCEiSearch...

Gene expression databases

BgeeiP22105.
ExpressionAtlasiP22105. baseline.
GenevisibleiP22105. HS.

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. FN3_dom.
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]
ProtoNetiSearch...

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-2518.
  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-2518.
  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).
  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 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 1605-1862 (ISOFORMS 3/4/5).
    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 3/4/5).
    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 1061-1148; 2521-2607; 2627-2714 AND 2735-2821.
    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 1399-1407; 1438-1448; 2122-2130; 2438-2446; 2549-2557; 2763-2771; 2782-2799; 2977-2985; 3016-3026; 3191-3199; 3210-3227 AND 3230-3240 (ISOFORMS 3/4/5), PROTEIN SEQUENCE OF 3607-3619 AND 3631-3663 (ISOFORMS XB-SHORT/3/4/5), 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 3358-4242 (ISOFORMS 3/4/5).
    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 3423-4242 (ISOFORMS 3/4/5).
  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-3918.
    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 3652-4022.
  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-1108, VARIANT ILE-3986.
  18. Cited for: VARIANT TNXD CYS-4072.
  19. Cited for: VARIANTS VUR8 ARG-1244 AND ILE-3210.

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: June 24, 2015
Last modified: June 24, 2015
This is version 180 of the entry and version 4 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

Caution

There are two genes for TN-X: TNXA and TNXB. TNXA can sometimes recombine with TNXB.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.