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Q92956 (TNR14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 14
Alternative name(s):
Herpes virus entry mediator A
Short name=Herpesvirus entry mediator A
Short name=HveA
Tumor necrosis factor receptor-like 2
Short name=TR2
CD_antigen=CD270
Gene names
Name:TNFRSF14
Synonyms:HVEA, HVEM
ORF Names:UNQ329/PRO509
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells. Ref.1

Subunit structure

Interacts with TRAF2, TRAF3 and TRAF5. Interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 1 (HHV-2) envelope glycoprotein D; functions as an entry receptor for these viruses. Ref.13 Ref.14 Ref.15

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Tissue specificity

Widely expressed, with the highest expression in lung, spleen and thymus.

Post-translational modification

N-glycosylated. Ref.17

Sequence similarities

Contains 3 TNFR-Cys repeats.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHost cell receptor for virus entry
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Traceable author statement Ref.13. Source: ProtInc

defense response to Gram-negative bacterium

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement Ref.14. Source: ProtInc

negative regulation of alpha-beta T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

tumor necrosis factor-mediated signaling pathway

Traceable author statement Ref.13. Source: GOC

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred by curator Ref.13. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10318773Ref.13Ref.14PubMed 9462508. Source: IntAct

tumor necrosis factor-activated receptor activity

Traceable author statement Ref.13. Source: ProtInc

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92956-1)

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.
Isoform 2 (identifier: Q92956-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: MEPPGDWGPP...SKCLQCQMCD → MVSRPPRTPLSPSSWT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Ref.12
Chain39 – 283245Tumor necrosis factor receptor superfamily member 14
PRO_0000034590

Regions

Topological domain39 – 202164Extracellular Potential
Transmembrane203 – 22321Helical; Potential
Topological domain224 – 28360Cytoplasmic Potential
Repeat42 – 7534TNFR-Cys 1
Repeat78 – 11942TNFR-Cys 2
Repeat121 – 16242TNFR-Cys 3

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Ref.17
Glycosylation1731N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 53
Disulfide bond54 ↔ 67
Disulfide bond57 ↔ 75
Disulfide bond78 ↔ 93
Disulfide bond96 ↔ 111
Disulfide bond99 ↔ 119
Disulfide bond121 ↔ 138
Disulfide bond127 ↔ 135

Natural variations

Alternative sequence1 – 100100MEPPG…CQMCD → MVSRPPRTPLSPSSWT in isoform 2.
VSP_054186
Natural variant171K → R. Ref.4 Ref.6 Ref.8
Corresponds to variant rs4870 [ dbSNP | Ensembl ].
VAR_013007
Natural variant1171A → T. Ref.8
Corresponds to variant rs2234163 [ dbSNP | Ensembl ].
VAR_018955
Natural variant1741G → E. Ref.8
Corresponds to variant rs11573986 [ dbSNP | Ensembl ].
VAR_018956
Natural variant2411V → I. Ref.4 Ref.8
Corresponds to variant rs2234167 [ dbSNP | Ensembl ].
VAR_013440

Experimental info

Sequence conflict1351C → R in AAH29848. Ref.10

Secondary structure

......................... 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 46CE13C2C70242C1

FASTA28330,392
        10         20         30         40         50         60 
MEPPGDWGPP PWRSTPKTDV LRLVLYLTFL GAPCYAPALP SCKEDEYPVG SECCPKCSPG 

        70         80         90        100        110        120 
YRVKEACGEL TGTVCEPCPP GTYIAHLNGL SKCLQCQMCD PAMGLRASRN CSRTENAVCG 

       130        140        150        160        170        180 
CSPGHFCIVQ DGDHCAACRA YATSSPGQRV QKGGTESQDT LCQNCPPGTF SPNGTLEECQ 

       190        200        210        220        230        240 
HQTKCSWLVT KAGAGTSSSH WVWWFLSGSL VIVIVCSTVG LIICVKRRKP RGDVVKVIVS 

       250        260        270        280 
VQRKRQEAEG EATVIEALQA PPDVTTVAVE ETIPSFTGRS PNH 

« Hide

Isoform 2 [UniParc].

Checksum: B14A3275B16BBD66
Show »

FASTA19921,351

References

« Hide 'large scale' references
[1]"Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family."
Montgomery R.I., Warner M.S., Lum B.J., Spear P.G.
Cell 87:427-436(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A RECEPTOR FOR HHV-1.
Tissue: Cervix adenocarcinoma.
[2]"A newly identified member of the tumor necrosis factor receptor superfamily with a wide tissue distribution and involvement in lymphocyte activation."
Kwon B.S., Tan K.B., Ni J., Oh K.-O., Lee Z.H., Kim K.K., Kim Y.-J., Wang S., Gentz R., Yu G.-L., Harrop J., Lyn S.D., Silverman C., Porter T.G., Truneh A., Young P.R.
J. Biol. Chem. 272:14272-14276(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Zhang W., Wan T., Cao X.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Search for polymorphisms in the genes for herpesvirus entry mediator, Nectin-1, and Nectin-2 in immune seronegative individuals."
Struyf F., Posavad C.M., Keyaerts E., Van Ranst M., Corey L., Spear P.G.
J. Infect. Dis. 185:36-44(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-17 AND ILE-241.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[6]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-17.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]NIEHS SNPs program
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-17; THR-117; GLU-174 AND ILE-241.
[9]"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. expand/collapse author list , 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].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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] (ISOFORMS 1 AND 2).
Tissue: Skin.
[12]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-53.
[13]"ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5."
Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.
J. Biol. Chem. 272:13471-13474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF2 AND TRAF5.
[14]"Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1."
Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.
J. Biol. Chem. 272:14029-14032(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF3 AND TRAF5.
[15]"Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
[16]"Herpes simplex virus glycoprotein D bound to the human receptor HveA."
Carfi A., Willis S.H., Whitbeck J.C., Krummenacher C., Cohen G.H., Eisenberg R.J., Wiley D.C.
Mol. Cell 8:169-179(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 39-200 IN COMPLEX WITH HUMAN HERPESVIRUS 1 GLYCOPROTEIN.
[17]"Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex."
Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D., Hymowitz S.G.
J. Biol. Chem. 280:39553-39561(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH BTLA, GLYCOSYLATION AT ASN-110.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70321 mRNA. Translation: AAB58354.1.
U81232 mRNA. Translation: AAD00505.1.
AF153978 mRNA. Translation: AAF75588.1.
AF373877 mRNA. Translation: AAL47717.1.
AF373878 mRNA. Translation: AAL47718.1.
AY358879 mRNA. Translation: AAQ89238.1.
AK124010 mRNA. Translation: BAG53992.1.
CR456909 mRNA. Translation: CAG33190.1.
AY466111 Genomic DNA. Translation: AAR23264.1.
AL139246 Genomic DNA. Translation: CAX30824.1.
CH471183 Genomic DNA. Translation: EAW56089.1.
CH471183 Genomic DNA. Translation: EAW56090.1.
BC002794 mRNA. Translation: AAH02794.1.
BC029848 mRNA. Translation: AAH29848.1.
CCDSCCDS44046.1.
RefSeqNP_003811.2. NM_003820.2. [Q92956-1]
UniGeneHs.512898.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMAX-ray2.65B39-199[»]
2AW2X-ray2.80B/Y39-142[»]
4FHQX-ray2.25A39-162[»]
ProteinModelPortalQ92956.
SMRQ92956. Positions 39-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114298. 30 interactions.
DIPDIP-34779N.
DIP-6233N.
IntActQ92956. 29 interactions.
MINTMINT-208002.
STRING9606.ENSP00000347948.

Chemistry

GuidetoPHARMACOLOGY1887.

Polymorphism databases

DMDM13878821.

Proteomic databases

PaxDbQ92956.
PRIDEQ92956.

Protocols and materials databases

DNASU8764.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355716; ENSP00000347948; ENSG00000157873.
GeneID8764.
KEGGhsa:8764.
UCSCuc001ajr.3. human. [Q92956-1]

Organism-specific databases

CTD8764.
GeneCardsGC01P002487.
HGNCHGNC:11912. TNFRSF14.
HPACAB026150.
CAB030007.
HPA006404.
MIM602746. gene.
neXtProtNX_Q92956.
PharmGKBPA36605.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40150.
HOGENOMHOG000065766.
HOVERGENHBG072084.
InParanoidQ92956.
KOK05152.
OMASPGHFCI.
PhylomeDBQ92956.
TreeFamTF331157.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ92956.

Gene expression databases

ArrayExpressQ92956.
BgeeQ92956.
CleanExHS_TNFRSF14.
GenevestigatorQ92956.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022332. TNFR_14.
[Graphical view]
PfamPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSPR01965. TNFACTORR14.
SMARTSM00208. TNFR. 3 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF14. human.
EvolutionaryTraceQ92956.
GeneWikiTNFRSF14.
GenomeRNAi8764.
NextBio32872.
PROQ92956.
SOURCESearch...

Entry information

Entry nameTNR14_HUMAN
AccessionPrimary (citable) accession number: Q92956
Secondary accession number(s): B3KW30 expand/collapse secondary AC list , B9DI89, Q6IB95, Q8N634, Q8WXR1, Q96J31, Q9UM65
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries