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Q92752

- TENR_HUMAN

UniProt

Q92752 - TENR_HUMAN

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Protein

Tenascin-R

Gene

TNR

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ92752.
CleanExiHS_TNR.
ExpressionAtlasiQ92752. baseline and differential.
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.
GeneTreeiENSGT00770000120463.
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

        10         20         30         40         50
MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG
60 70 80 90 100
IANYNTSSKE QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE
110 120 130 140 150
YMGQTSDHES QVTFTHRINF PKKACPCASS AQVLQELLSR IEMLEREVSV
160 170 180 190 200
LRDQCNANCC QESAATGQLD YIPHCSGHGN FSFESCGCIC NEGWFGKNCS
210 220 230 240 250
EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS SRGLCVDGEC
260 270 280 290 300
VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA
310 320 330 340 350
CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM
360 370 380 390 400
AVTEYVISYQ PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS
410 420 430 440 450
NILSLPITAK VATHLSTPQG LQFKTITETT VEVQWEPFSF SFDGWEISFI
460 470 480 490 500
PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY IVNVVALKEQ ARSPPTSASV
510 520 530 540 550
STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL VGGEGGRTTF
560 570 580 590 600
RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL
610 620 630 640 650
RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR
660 670 680 690 700
ATLTDLVPGT EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET
710 720 730 740 750
SISLIWTKAS GPIDHYRITF TPSSGIASEV TVPKDRTSYT LTDLEPGAEY
760 770 780 790 800
IISVTAERGR QQSLESTVDA FTGFRPISHL HFSHVTSSSV NITWSDPSPP
810 820 830 840 850
ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY IVNLVAVHGT
860 870 880 890 900
VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP
910 920 930 940 950
TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH
960 970 980 990 1000
TAMDNPVDLI ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD
1010 1020 1030 1040 1050
GVSEEFRLVD LLPSTHYTAT MYATNGPLTS GTISTNFSTL LDPPANLTAS
1060 1070 1080 1090 1100
EVTRQSALIS WQPPRAEIEN YVLTYKSTDG SRKELIVDAE DTWIRLEGLL
1110 1120 1130 1140 1150
ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ HLMNGDTLSG
1160 1170 1180 1190 1200
VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
1210 1220 1230 1240 1250
FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR
1260 1270 1280 1290 1300
NLYKLRIGSY NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY
1310 1320 1330 1340 1350
KNCHRTNLNG KYGESRHSQG INWYHWKGHE FSIPFVEMKM RPYNHRLMAG

RKRQSLQF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00770000120463.
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

Bgeei Q92752.
CleanExi HS_TNR.
ExpressionAtlasi Q92752. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 128 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