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Q9NP84 (TNR12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 12A
Alternative name(s):
Fibroblast growth factor-inducible immediate-early response protein 14
Short name=FGF-inducible 14
Tweak-receptor
Short name=TweakR
CD_antigen=CD266
Gene names
Name:TNFRSF12A
Synonyms:FN14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length129 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 TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins. Ref.5

Subunit structure

Associates with TRAF1 and TRAF2, and probably also with TRAF3.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Highly expressed in heart, placenta and kidney. Intermediate expression in lung, skeletal muscle and pancreas.

Induction

By FGF1 and phorbol ester.

Sequence similarities

Contains 1 TNFR-Cys repeat.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Cell adhesion
Differentiation
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular component movement

Traceable author statement. Source: ProtInc

multicellular organismal development

Traceable author statement. Source: ProtInc

positive regulation of apoptotic process

Inferred from direct assay PubMed 21525013. Source: UniProt

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21525013. Source: UniProtKB

substrate-dependent cell migration, cell attachment to substrate

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 21525013PubMed 23438059. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NP84-1)

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: Q9NP84-2)

The sequence of this isoform differs from the canonical sequence as follows:
     33-67: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 129102Tumor necrosis factor receptor superfamily member 12A
PRO_0000034611

Regions

Topological domain28 – 8053Extracellular Potential
Transmembrane81 – 10121Helical; Potential
Topological domain102 – 12928Cytoplasmic Potential
Repeat36 – 6732TNFR-Cys; atypical

Amino acid modifications

Disulfide bond36 ↔ 49 Ref.7
Disulfide bond52 ↔ 67 Ref.7
Disulfide bond55 ↔ 64 Ref.7

Natural variations

Alternative sequence33 – 6735Missing in isoform 2.
VSP_006519

Secondary structure

........... 129
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: BF3FDFB9C1E1C448

FASTA12913,911
        10         20         30         40         50         60 
MARGSLRRLL RLLVLGLWLA LLRSVAGEQA PGTAPCSRGS SWSADLDKCM DCASCRARPH 

        70         80         90        100        110        120 
SDFCLGCAAA PPAPFRLLWP ILGGALSLTF VLGLLSGFLV WRRCRRREKF TTPIEETGGE 


GCPAVALIQ 

« Hide

Isoform 2 [UniParc].

Checksum: E3C52B1308DC768F
Show »

FASTA9410,191

References

« Hide 'large scale' references
[1]"The Fn14 immediate-early response gene is induced during liver regeneration and highly expressed in both human and murine hepatocellular carcinomas."
Feng S.-L.Y., Guo Y., Factor V.M., Thorgeirsson S.S., Bell D.W., Testa J.R., Peifley K.A., Winkles J.A.
Am. J. Pathol. 156:1253-1261(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Human homologue of Fn14."
Tanaka S., Sugimachi K.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 1).
Tissue: Uterus.
[5]"A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis."
Wiley S.R., Cassiano L., Lofton T., Davis-Smith T., Winkles J.A., Lindner V., Liu H., Daniel T.O., Smith C.A., Fanslow W.C.
Immunity 15:837-846(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Solution structure of the STN_TNFRSF12A_TNFR domain of tumor necrosis factor receptor superfamily member 12A precursor."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 26-70.
[7]"Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily."
He F., Dang W., Saito K., Watanabe S., Kobayashi N., Guntert P., Kigawa T., Tanaka A., Muto Y., Yokoyama S.
Protein Sci. 18:650-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 26-70, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF191148 mRNA. Translation: AAF69108.1.
AB035480 mRNA. Translation: BAA94792.1.
AB035481 mRNA. Translation: BAB17850.1.
CH471112 Genomic DNA. Translation: EAW85429.1.
CH471112 Genomic DNA. Translation: EAW85430.1.
BC002718 mRNA. Translation: AAH02718.1.
CCDSCCDS10489.1. [Q9NP84-1]
RefSeqNP_057723.1. NM_016639.2. [Q9NP84-1]
UniGeneHs.355899.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQPNMR-A28-70[»]
2KMZNMR-A28-80[»]
2RPJNMR-A28-70[»]
ProteinModelPortalQ9NP84.
SMRQ9NP84. Positions 28-80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119478. 6 interactions.
IntActQ9NP84. 4 interactions.
MINTMINT-8415044.
STRING9606.ENSP00000326737.

Chemistry

GuidetoPHARMACOLOGY1884.

PTM databases

PhosphoSiteQ9NP84.

Polymorphism databases

DMDM21263626.

Proteomic databases

MaxQBQ9NP84.
PaxDbQ9NP84.
PeptideAtlasQ9NP84.
PRIDEQ9NP84.

Protocols and materials databases

DNASU51330.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326577; ENSP00000326737; ENSG00000006327. [Q9NP84-1]
ENST00000341627; ENSP00000343894; ENSG00000006327. [Q9NP84-2]
GeneID51330.
KEGGhsa:51330.
UCSCuc002csv.4. human. [Q9NP84-1]
uc002csw.4. human. [Q9NP84-2]

Organism-specific databases

CTD51330.
GeneCardsGC16P003141.
HGNCHGNC:18152. TNFRSF12A.
HPACAB015941.
HPA007853.
MIM605914. gene.
neXtProtNX_Q9NP84.
PharmGKBPA134976874.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39144.
HOGENOMHOG000154660.
HOVERGENHBG031553.
KOK05149.
OMASGLLVWR.
PhylomeDBQ9NP84.
TreeFamTF337901.

Gene expression databases

ArrayExpressQ9NP84.
BgeeQ9NP84.
CleanExHS_TNFRSF12A.
GenevestigatorQ9NP84.

Family and domain databases

InterProIPR022316. TNFR_12.
[Graphical view]
PfamPF12191. stn_TNFRSF12A. 1 hit.
[Graphical view]
PRINTSPR01962. TNFACTORR12.
ProDomPD336131. TNFR_12. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

ChiTaRSTNFRSF12A. human.
EvolutionaryTraceQ9NP84.
GeneWikiTNFRSF12A.
GenomeRNAi51330.
NextBio54743.
PROQ9NP84.
SOURCESearch...

Entry information

Entry nameTNR12_HUMAN
AccessionPrimary (citable) accession number: Q9NP84
Secondary accession number(s): D3DUA6, Q9HCS0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 114 of the entry and version 1 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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