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P22105

- TENX_HUMAN

UniProt

P22105 - TENX_HUMAN

Protein

Tenascin-X

Gene

TNXB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 3 (02 Mar 2010)
      Previous versions | rss
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    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

    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

    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

    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.
    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

    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.

    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:
    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

    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: October 1, 2014
    This is version 172 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