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P22105

- TENX_HUMAN

UniProt

P22105 - TENX_HUMAN

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Protein

Tenascin-X

Gene
TNXB, HXBL, TNX, TNXB1, TNXB2, XB
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

Organism-specific databases

HGNCiHGNC:11976. TNXB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  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 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 42894266Tenascin-XPRO_0000007751Add
BLAST

Amino acid modifications

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

ArrayExpressiP22105.
BgeeiP22105.
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. 5 interactions.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22105.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili901 – 92222 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1748 – 17503Cell attachment site Reviewed prediction

Sequence similaritiesi

Belongs to the tenascin family.
Contains 19 EGF-like domains.

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

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.

« Hide

MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA     50
GVGSPSSQLY EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV 100
QALRVRLEIL EELVKGLKEQ CTGGCCPASA QAGTGQTDVR TLCSLHGVFD 150
LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP PSASGSCPDD CNDQGRCVRG 200
RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS GPDCSQRSCP 250
RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG 300
YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG 350
RCVDGRCVCW PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG 400
VRSCPGDCNQ RGRCEDGRCV CWPGYTGTDC GSRACPRDCR GRGRCENGVC 450
VCNAGYSGED CGVRSCPGDC RGRGRCESGR CMCWPGYTGR DCGTRACPGD 500
CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED GVCVCDAGYS 550
GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC 600
QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR 650
MCPADCRGRG RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA 700
GQCVCVEGFR GPDCAIQTCP GDCRGRGECH DGSCVCKDGY AGEDCGEARV 750
PSSASAYDQR GLAPGQEYQV TVRALRGTSW GLPASKTITT MIDGPQDLRV 800
VAVTPTTLEL GWLRPQAEVD RFVVSYVSAG NQRVRLEVPP EADGTLLTDL 850
MPGVEYVVTV TAERGRAVSY PASVRANTEE REEESPPRPS LSQPPRRPWG 900
NLTAELSRFR GTVQDLERHL RAHGYPLRAN QTYTSVARHI HEYLQRQVLG 950
SSADGALLVS LDGLRGQFER VVLRWRPQPP AEGPGGELTV PGTTRTVSLP 1000
DLRPGTTYHV EVHGVRAGQT SKSYAFITTT GPSTTQGAQA PLLQQRPQEL 1050
GELRVLGRDE TGRLRVVWTA QPDTFAYFQL RMRVPEGPGA HEEVLPGDVR 1100
QALVPPPPPG TPYELSLHGV PPGGKPSDPI IYQGIMDKDE EKPGKSSGPP 1150
RLGELTVTDR TSDSLLLRWT VPEGEFDSFV IQYKDRDGQP QVVPVEGPQR 1200
SAVITSLDPG RKYKFVLYGF VGKKRHGPLV AEAKILPQSD PSPGTPPHLG 1250
NLWVTDPTPD SLHLSWTVPE GQFDTFMVQY RDRDGRPQVV PVEGPERSFV 1300
VSSLDPDHKY RFTLFGIANK KRYGPLTADG TTAPERKEEP PRPEFLEQPL 1350
LGELTVTGVT PDSLRLSWTV AQGPFDSFMV QYKDAQGQPQ AVPVAGDENE 1400
VTVPGLDPDR KYKMNLYGLR GRQRVGPESV VAKTAPQEDV DETPSPTELG 1450
TEAPESPEEP LLGELTVTGS SPDSLSLFWT VPQGSFDSFT VQYKDRDGRP 1500
RAVRVGGKES EVTVGGLEPG HKYKMHLYGL HEGQRVGPVS AVGVTAPQQE 1550
ETPPATESPL EPRLGELTVT DVTPNSVGLS WTVPEGQFDS FIVQYKDKDG 1600
QPQVVPVAAD QREVTVYNLE PERKYKMNMY GLHDGQRMGP LSVVIVTAPA 1650
TEASKPPLEP RLGELTVTDI TPDSVGLSWT VPEGEFDSFV VQYKDRDGQP 1700
QVVPVAADQR EVTIPDLEPS RKYKFLLFGI QDGKRRSPVS VEAKTVARGD 1750
ASPGAPPRLG ELWVTDPTPD SLRLSWTVPE GQFDSFVVQF KDKDGPQVVP 1800
VEGHERSVTV TPLDAGRKYR FLLYGLLGKK RHGPLTADGT TEARSAMDDT 1850
GTKRPPKPRL GEELQVTTVT QNSVGLSWTV PEGQFDSFVV QYKDRDGQPQ 1900
VVPVEGSLRE VSVPGLDPAH RYKLLLYGLH HGKRVGPISA VAITAGREET 1950
ETETTAPTPP APEPHLGELT VEEATSHTLH LSWMVTEGEF DSFEIQYTDR 2000
DGQLQMVRIG GDRNDITLSG LESDHRYLVT LYGFSDGKHV GPVHVEALTV 2050
PEEEKPSEPP TATPEPPIKP RLGELTVTDA TPDSLSLSWT VPEGQFDHFL 2100
VQYRNGDGQP KAVRVPGHEE GVTISGLEPD HKYKMNLYGF HGGQRMGPVS 2150
VVGVTEPSME APEPAEEPLL GELTVTGSSP DSLSLSWTVP QGRFDSFTVQ 2200
YKDRDGRPQV VRVGGEESEV TVGGLEPGRK YKMHLYGLHE GRRVGPVSAV 2250
GVTAPEEESP DAPLAKLRLG QMTVRDITSD SLSLSWTVPE GQFDHFLVQF 2300
KNGDGQPKAV RVPGHEDGVT ISGLEPDHKY KMNLYGFHGG QRVGPVSAVG 2350
LTASTEPPTP EPPIKPRLEE LTVTDATPDS LSLSWTVPEG QFDHFLVQYK 2400
NGDGQPKATR VPGHEDRVTI SGLEPDNKYK MNLYGFHGGQ RVGPVSAIGV 2450
TEEETPSPTE PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS 2500
FTVQYKDRDG RPQVVRVGGE ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP 2550
VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP EEPLLGELTV TGSSPDSLSL 2600
SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL EPGRKYKMHL 2650
YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT 2700
PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH 2750
KYKMNLYGFH GGQRVGPISV IGVTEEETPS PTELSTEAPE PPEEPLLGEL 2800
TVTGSSPDSL SLSWTIPQGH FDSFTVQYKD RDGRPQVMRV RGEESEVTVG 2850
GLEPGRKYKM HLYGLHEGRR VGPVSTVGVT VPTTTPEPPN KPRLGELTVT 2900
DATPDSLSLS WMVPEGQFDH FLVQYRNGDG QPKVVRVPGH EDGVTISGLE 2950
PDHKYKMNLY GFHGGQRVGP ISVIGVTEEE TPAPTEPSTE APEPPEEPLL 3000
GELTVTGSSP DSLSLSWTIP QGRFDSFTVQ YKDRDGRPQV VRVRGEESEV 3050
TVGGLEPGCK YKMHLYGLHE GQRVGPVSAV GVTAPKDEAE TTQAVPTMTP 3100
EPPIKPRLGE LTVTDATPDS LSLSWMVPEG QFDHFLVQYR NGDGQPKAVR 3150
VPGHEDGVTI SGLEPDHKYK MNLYGFHGGQ RVGPVSAIGV TEEETPSPTE 3200
PSTEAPEAPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG 3250
QPQVVRVRGE ESEVTVGGLE PGRKYKMHLY GLHEGQRVGP VSTVGITAPL 3300
PTPLPVEPRL GELAVAAVTS DSVGLSWTVA QGPFDSFLVQ YRDAQGQPQA 3350
VPVSGDLRAV AVSGLDPARK YKFLLFGLQN GKRHGPVPVE ARTAPDTKPS 3400
PRLGELTVTD ATPDSVGLSW TVPEGEFDSF VVQYKDKDGR LQVVPVAANQ 3450
REVTVQGLEP SRKYRFLLYG LSGRKRLGPI SADSTTAPLE KELPPHLGEL 3500
TVAEETSSSL RLSWTVAQGP FDSFVVQYRD TDGQPRAVPV AADQRTVTVE 3550
DLEPGKKYKF LLYGLLGGKR LGPVSALGMT APEEDTPAPE LAPEAPEPPE 3600
EPRLGVLTVT DTTPDSMRLS WSVAQGPFDS FVVQYEDTNG QPQALLVDGD 3650
QSKILISGLE PSTPYRFLLY GLHEGKRLGP LSAEGTTGLA PAGQTSEESR 3700
PRLSQLSVTD VTTSSLRLNW EAPPGAFDSF LLRFGVPSPS TLEPHPRPLL 3750
QRELMVPGTR HSAVLRDLRS GTLYSLTLYG LRGPHKADSI QGTARTLSPV 3800
LESPRDLQFS EIRETSAKVN WMPPPSRADS FKVSYQLADG GEPQSVQVDG 3850
QARTQKLQGL IPGARYEVTV VSVRGFEESE PLTGFLTTVP DGPTQLRALN 3900
LTEGFAVLHW KPPQNPVDTY DVQVTAPGAP PLQAETPGSA VDYPLHDLVL 3950
HTNYTATVRG LRGPNLTSPA SITFTTGLEA PRDLEAKEVT PRTALLTWTE 4000
PPVRPAGYLL SFHTPGGQNQ EILLPGGITS HQLLGLFPST SYNARLQAMW 4050
GQSLLPPVST SFTTGGLRIP FPRDCGEEMQ NGAGASRTST IFLNGNRERP 4100
LNVFCDMETD GGGWLVFQRR MDGQTDFWRD WEDYAHGFGN ISGEFWLGNE 4150
ALHSLTQAGD YSMRVDLRAG DEAVFAQYDS FHVDSAAEYY RLHLEGYHGT 4200
AGDSMSYHSG SVFSARDRDP NSLLISCAVS YRGAWWYRNC HYANLNGLYG 4250
STVDHQGVSW YHWKGFEFSV PFTEMKLRPR NFRSPAGGG 4289

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

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. VSP_001418Add
BLAST
Alternative sequencei747 – 7471E → EEVPTIEGMRMHLLEETTVR TEWTPAPGPVDAYEIQFIPT TEGASPPFT in isoform 3. VSP_034569
Alternative sequencei878 – 1013136Missing in isoform 3. VSP_034570Add
BLAST
Alternative sequencei1014 – 103017GVRAG…FITTT → TGSSPLGLLGTTDEPPPS in isoform 3. VSP_034571Add
BLAST
Alternative sequencei1648 – 16481A → APLPPA in isoform 3. VSP_034572
Alternative sequencei2155 – 21551T → TAAEEETPSPT in isoform 3. VSP_034573
Alternative sequencei2353 – 23531A → APGKDEEMAPA in isoform 3. VSP_034574
Alternative sequencei2451 – 24511T → TAA in isoform 3. VSP_034575
Alternative sequencei2774 – 27741T → TAA in isoform 3. VSP_034576
Alternative sequencei2880 – 28801T → TEDEAETTQA in isoform 3. VSP_034578
Alternative sequencei2977 – 29771T → TAA in isoform 3. VSP_034577

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000375247; ENSP00000364396; ENSG00000168477. [P22105-3]
ENST00000451343; ENSP00000407685; ENSG00000168477. [P22105-2]
ENST00000546684; ENSP00000447694; ENSG00000236236.
ENST00000550539; ENSP00000448326; ENSG00000229353. [P22105-2]
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 5 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 ENST00000375247 ; ENSP00000364396 ; ENSG00000168477 . [P22105-3 ]
ENST00000451343 ; ENSP00000407685 ; ENSG00000168477 . [P22105-2 ]
ENST00000546684 ; ENSP00000447694 ; ENSG00000236236 .
ENST00000550539 ; ENSP00000448326 ; ENSG00000229353 . [P22105-2 ]
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

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

ArrayExpressi P22105.
Bgeei P22105.
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: September 3, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 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

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