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Q92752

- TENR_HUMAN

UniProt

Q92752 - TENR_HUMAN

Protein

Tenascin-R

Gene

TNR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance By similarity.By similarity

    GO - Biological processi

    1. associative learning Source: Ensembl
    2. axon guidance Source: ProtInc
    3. cell adhesion Source: ProtInc
    4. extracellular matrix organization Source: Reactome
    5. locomotory exploration behavior Source: Ensembl
    6. long-term synaptic potentiation Source: Ensembl
    7. negative regulation of axon extension involved in regeneration Source: Ensembl
    8. negative regulation of cell-cell adhesion Source: Ensembl
    9. negative regulation of synaptic transmission Source: Ensembl
    10. neuromuscular process controlling balance Source: Ensembl
    11. neuron cell-cell adhesion Source: Ensembl
    12. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    13. positive regulation of transmission of nerve impulse Source: Ensembl
    14. synapse organization Source: Ensembl
    15. telencephalon cell migration Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_163906. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tenascin-R
    Short name:
    TN-R
    Alternative name(s):
    Janusin
    Restrictin
    Gene namesi
    Name:TNR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11953. TNR.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. cytoplasm Source: HPA
    3. extracellular region Source: Reactome
    4. membrane raft Source: Ensembl
    5. nucleus Source: HPA
    6. perineuronal net Source: Ensembl
    7. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36642.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 13581327Tenascin-RPRO_0000007747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361O-linked (GalNAc...)1 Publication
    Glycosylationi37 – 371O-linked (GalNAc...)1 Publication
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi292 ↔ 301PROSITE-ProRule annotation
    Disulfide bondi297 ↔ 312PROSITE-ProRule annotation
    Disulfide bondi314 ↔ 323PROSITE-ProRule annotation
    Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi581 – 5811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi874 – 8741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1036 – 10361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1046 – 10461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1261 – 12611N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure By similarity. O-glycosylated on Thr-36 or Thr-37 with a core 1 or possibly core 8 glycan.By similarity1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan

    Proteomic databases

    PaxDbiQ92752.
    PRIDEiQ92752.

    PTM databases

    PhosphoSiteiQ92752.

    Expressioni

    Tissue specificityi

    Brain specific.1 Publication

    Gene expression databases

    ArrayExpressiQ92752.
    BgeeiQ92752.
    CleanExiHS_TNR.
    GenevestigatoriQ92752.

    Organism-specific databases

    HPAiCAB022343.
    HPA027134.
    HPA027150.
    HPA029859.

    Interactioni

    Subunit structurei

    Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi112997. 3 interactions.
    IntActiQ92752. 1 interaction.
    STRINGi9606.ENSP00000263525.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92752.
    SMRiQ92752. Positions 503-771.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini188 – 19912EGF-like 1Add
    BLAST
    Domaini219 – 23012EGF-like 2Add
    BLAST
    Domaini250 – 26112EGF-like 3Add
    BLAST
    Domaini281 – 29212EGF-like 4Add
    BLAST
    Domaini312 – 32312EGF-like 5Add
    BLAST
    Domaini328 – 42093Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 50585Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini506 – 59590Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini596 – 68792Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini688 – 77790Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini778 – 86588Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini866 – 95590Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini956 – 104287Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1043 – 113088Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1129 – 1344216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili127 – 15731Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi155 – 314160Cys-richAdd
    BLAST

    Domaini

    The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B By similarity.By similarity

    Sequence similaritiesi

    Belongs to the tenascin family.Curated
    Contains 5 EGF-like domains.Curated
    Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
    Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG311251.
    HOGENOMiHOG000234355.
    HOVERGENiHBG008949.
    InParanoidiQ92752.
    KOiK06252.
    OMAiKACPCAS.
    OrthoDBiEOG7X9G60.
    PhylomeDBiQ92752.
    TreeFamiTF329915.

    Family and domain databases

    Gene3Di2.60.40.10. 9 hits.
    3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProiIPR013032. EGF-like_CS.
    IPR013111. EGF_extracell.
    IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF07974. EGF_2. 2 hits.
    PF00147. Fibrinogen_C. 1 hit.
    PF00041. fn3. 9 hits.
    [Graphical view]
    SMARTiSM00186. FBG. 1 hit.
    SM00060. FN3. 9 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 5 hits.
    SSF56496. SSF56496. 1 hit.
    PROSITEiPS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 4 hits.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    PS50853. FN3. 9 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92752-1) [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.

    « Hide

    MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG     50
    IANYNTSSKE QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE 100
    YMGQTSDHES QVTFTHRINF PKKACPCASS AQVLQELLSR IEMLEREVSV 150
    LRDQCNANCC QESAATGQLD YIPHCSGHGN FSFESCGCIC NEGWFGKNCS 200
    EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS SRGLCVDGEC 250
    VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA 300
    CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM 350
    AVTEYVISYQ PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS 400
    NILSLPITAK VATHLSTPQG LQFKTITETT VEVQWEPFSF SFDGWEISFI 450
    PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY IVNVVALKEQ ARSPPTSASV 500
    STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL VGGEGGRTTF 550
    RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL 600
    RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR 650
    ATLTDLVPGT EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET 700
    SISLIWTKAS GPIDHYRITF TPSSGIASEV TVPKDRTSYT LTDLEPGAEY 750
    IISVTAERGR QQSLESTVDA FTGFRPISHL HFSHVTSSSV NITWSDPSPP 800
    ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY IVNLVAVHGT 850
    VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP 900
    TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH 950
    TAMDNPVDLI ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD 1000
    GVSEEFRLVD LLPSTHYTAT MYATNGPLTS GTISTNFSTL LDPPANLTAS 1050
    EVTRQSALIS WQPPRAEIEN YVLTYKSTDG SRKELIVDAE DTWIRLEGLL 1100
    ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ HLMNGDTLSG 1150
    VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG 1200
    FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR 1250
    NLYKLRIGSY NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY 1300
    KNCHRTNLNG KYGESRHSQG INWYHWKGHE FSIPFVEMKM RPYNHRLMAG 1350
    RKRQSLQF 1358
    Length:1,358
    Mass (Da):149,562
    Last modified:November 2, 2010 - v3
    Checksum:iE4DE356B44D117E7
    GO
    Isoform 2 (identifier: Q92752-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         773-862: Missing.

    Show »
    Length:1,268
    Mass (Da):139,695
    Checksum:iE4EB4095284A4E29
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti629 – 6291S → I in CAA66709. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171I → V.2 Publications
    Corresponds to variant rs859398 [ dbSNP | Ensembl ].
    VAR_021479
    Natural varianti128 – 1281A → S.
    Corresponds to variant rs2239819 [ dbSNP | Ensembl ].
    VAR_021906
    Natural varianti293 – 2931G → S.
    Corresponds to variant rs3752516 [ dbSNP | Ensembl ].
    VAR_021907
    Natural varianti302 – 3021S → N.
    Corresponds to variant rs35736986 [ dbSNP | Ensembl ].
    VAR_055780
    Natural varianti643 – 6431R → K.
    Corresponds to variant rs859427 [ dbSNP | Ensembl ].
    VAR_030737

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei773 – 86290Missing in isoform 2. 1 PublicationVSP_012993Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z67996 mRNA. Translation: CAA91947.1.
    X98085 mRNA. Translation: CAA66709.1.
    AL021919 Genomic DNA. No translation available.
    AL023285 Genomic DNA. No translation available.
    AL136530 Genomic DNA. No translation available.
    Z94057, Z94055 Genomic DNA. Translation: CAI21650.1.
    Z94055, Z94057 Genomic DNA. Translation: CAI19943.1.
    CCDSiCCDS1318.1. [Q92752-1]
    RefSeqiNP_003276.3. NM_003285.2. [Q92752-1]
    UniGeneiHs.659864.

    Genome annotation databases

    EnsembliENST00000263525; ENSP00000263525; ENSG00000116147. [Q92752-1]
    ENST00000367674; ENSP00000356646; ENSG00000116147. [Q92752-1]
    GeneIDi7143.
    KEGGihsa:7143.
    UCSCiuc001gkp.1. human. [Q92752-1]

    Polymorphism databases

    DMDMi311033534.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z67996 mRNA. Translation: CAA91947.1 .
    X98085 mRNA. Translation: CAA66709.1 .
    AL021919 Genomic DNA. No translation available.
    AL023285 Genomic DNA. No translation available.
    AL136530 Genomic DNA. No translation available.
    Z94057 , Z94055 Genomic DNA. Translation: CAI21650.1 .
    Z94055 , Z94057 Genomic DNA. Translation: CAI19943.1 .
    CCDSi CCDS1318.1. [Q92752-1 ]
    RefSeqi NP_003276.3. NM_003285.2. [Q92752-1 ]
    UniGenei Hs.659864.

    3D structure databases

    ProteinModelPortali Q92752.
    SMRi Q92752. Positions 503-771.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112997. 3 interactions.
    IntActi Q92752. 1 interaction.
    STRINGi 9606.ENSP00000263525.

    PTM databases

    PhosphoSitei Q92752.

    Polymorphism databases

    DMDMi 311033534.

    Proteomic databases

    PaxDbi Q92752.
    PRIDEi Q92752.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263525 ; ENSP00000263525 ; ENSG00000116147 . [Q92752-1 ]
    ENST00000367674 ; ENSP00000356646 ; ENSG00000116147 . [Q92752-1 ]
    GeneIDi 7143.
    KEGGi hsa:7143.
    UCSCi uc001gkp.1. human. [Q92752-1 ]

    Organism-specific databases

    CTDi 7143.
    GeneCardsi GC01M175291.
    H-InvDB HIX0028854.
    HGNCi HGNC:11953. TNR.
    HPAi CAB022343.
    HPA027134.
    HPA027150.
    HPA029859.
    MIMi 601995. gene.
    neXtProti NX_Q92752.
    PharmGKBi PA36642.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311251.
    HOGENOMi HOG000234355.
    HOVERGENi HBG008949.
    InParanoidi Q92752.
    KOi K06252.
    OMAi KACPCAS.
    OrthoDBi EOG7X9G60.
    PhylomeDBi Q92752.
    TreeFami TF329915.

    Enzyme and pathway databases

    Reactomei REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    GeneWikii Tenascin-R.
    GenomeRNAii 7143.
    NextBioi 27961.
    PROi Q92752.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92752.
    Bgeei Q92752.
    CleanExi HS_TNR.
    Genevestigatori Q92752.

    Family and domain databases

    Gene3Di 2.60.40.10. 9 hits.
    3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProi IPR013032. EGF-like_CS.
    IPR013111. EGF_extracell.
    IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF07974. EGF_2. 2 hits.
    PF00147. Fibrinogen_C. 1 hit.
    PF00041. fn3. 9 hits.
    [Graphical view ]
    SMARTi SM00186. FBG. 1 hit.
    SM00060. FN3. 9 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 5 hits.
    SSF56496. SSF56496. 1 hit.
    PROSITEi PS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 4 hits.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    PS50853. FN3. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human tenascin-R: complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24."
      Carnemolla B., Leprini A., Borsi L., Querze G., Urbini S., Zardi L.
      J. Biol. Chem. 271:8157-8160(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT VAL-17.
      Tissue: Brain.
    2. "Isolation of the gene for neural cell adhesion molecule tenascin-R and fine mapping relative to loci in 1q25-31."
      Williams H., Schachner M., Wang B., Goodfellow P., Kenwrick S.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-17.
      Tissue: Brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-37, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.

    Entry informationi

    Entry nameiTENR_HUMAN
    AccessioniPrimary (citable) accession number: Q92752
    Secondary accession number(s): C9J563, Q15568, Q5R3G0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 126 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3