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F5H4T5 (F5H4T5_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:TNFRSF1A Ensembl ENSP00000439981
OrganismHomo sapiens (Human) [Reference proteome] Ensembl ENSP00000439981
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length71 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000439981

Ontologies

Keywords
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to estradiol stimulus

Inferred from electronic annotation. Source: Compara

defense response to bacterium

Inferred from electronic annotation. Source: Compara

diterpenoid metabolic process

Inferred from electronic annotation. Source: Compara

flavonoid metabolic process

Inferred from electronic annotation. Source: Compara

inflammatory response

Inferred from electronic annotation. Source: Compara

negative regulation of gene expression

Inferred from electronic annotation. Source: Compara

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Compara

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Compara

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Compara

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Compara

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Compara

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Compara

protein heterooligomerization

Inferred from electronic annotation. Source: Compara

regulation of apoptotic process

Inferred from electronic annotation. Source: Compara

response to alkaloid

Inferred from electronic annotation. Source: Compara

response to amino acid stimulus

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to hypoxia

Inferred from electronic annotation. Source: Compara

response to lipopolysaccharide

Inferred from electronic annotation. Source: Compara

tetrapyrrole metabolic process

Inferred from electronic annotation. Source: Compara

   Cellular_componentaxon

Inferred from electronic annotation. Source: Compara

cell surface

Inferred from electronic annotation. Source: Compara

extracellular space

Inferred from electronic annotation. Source: Compara

membrane raft

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: Compara

protein complex

Inferred from electronic annotation. Source: Compara

   Molecular_functiontumor necrosis factor-activated receptor activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
F5H4T5 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: BCB26BFA5D9BED63

FASTA717,807
        10         20         30         40         50         60 
MGLSTVPDLL LPLVLLELLV GIYPSGVIGL VPHLGDREKR DSVCPQGKYI HPQNNSICCT 

        70 
KCHKGTYLYN D 

« Hide

References

« Hide 'large scale' references
[1]"The finished DNA sequence of human chromosome 12."
Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A., null.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006057 Genomic DNA. No translation available.
IPIIPI01014076.

3D structure databases

ProteinModelPortalF5H4T5.
SMRF5H4T5. Positions 41-71.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000543048; ENSP00000439981; ENSG00000067182.

Organism-specific databases

HGNCHGNC:11916. TNFRSF1A.
GenAtlasSearch...

Gene expression databases

ArrayExpressF5H4T5.
BgeeF5H4T5.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
[Graphical view]
PfamPF00020. TNFR_c6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF1A. human.
NextBio35508857.

Entry information

Entry nameF5H4T5_HUMAN
AccessionPrimary (citable) accession number: F5H4T5
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 3, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.