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Protein

Tumor necrosis factor receptor superfamily member 8

Gene

TNFRSF8

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

Functioni

Receptor for TNFSF8/CD30L. May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B.

GO - Molecular functioni

  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • cellular response to mechanical stimulus Source: UniProtKB
  • negative regulation of cell proliferation Source: ProtInc
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of TRAIL biosynthetic process Source: UniProtKB
  • positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

SignaLinkiP28908.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 8
Alternative name(s):
CD30L receptor
Ki-1 antigen
Lymphocyte activation antigen CD30
CD_antigen: CD30
Gene namesi
Name:TNFRSF8
Synonyms:CD30, D1S166E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11923. TNFRSF8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 379361ExtracellularSequence AnalysisAdd
BLAST
Transmembranei380 – 40728HelicalSequence AnalysisAdd
BLAST
Topological domaini408 – 595188CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36616.

Chemistry

DrugBankiDB08870. Brentuximab vedotin.

Polymorphism and mutation databases

BioMutaiTNFRSF8.
DMDMi115978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 595577Tumor necrosis factor receptor superfamily member 8PRO_0000034573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 44PROSITE-ProRule annotation
Disulfide bondi45 ↔ 58PROSITE-ProRule annotation
Disulfide bondi48 ↔ 65PROSITE-ProRule annotation
Disulfide bondi69 ↔ 81PROSITE-ProRule annotation
Disulfide bondi84 ↔ 98PROSITE-ProRule annotation
Disulfide bondi87 ↔ 106PROSITE-ProRule annotation
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi108 ↔ 122PROSITE-ProRule annotation
Disulfide bondi131 ↔ 149PROSITE-ProRule annotation
Disulfide bondi233 ↔ 240PROSITE-ProRule annotation
Disulfide bondi244 ↔ 256PROSITE-ProRule annotation
Disulfide bondi259 ↔ 273PROSITE-ProRule annotation
Disulfide bondi262 ↔ 281PROSITE-ProRule annotation
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi283 ↔ 297PROSITE-ProRule annotation
Disulfide bondi289 ↔ 300PROSITE-ProRule annotation
Modified residuei452 – 4521Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated on serine and tyrosine residues.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP28908.
PaxDbiP28908.
PRIDEiP28908.

PTM databases

PhosphoSiteiP28908.

Expressioni

Gene expression databases

BgeeiP28908.
CleanExiHS_TNFRSF8.
ExpressionAtlasiP28908. baseline and differential.
GenevisibleiP28908. HS.

Organism-specific databases

HPAiCAB000016.
HPA032081.
HPA032082.

Interactioni

Subunit structurei

Interacts with TRAF1, TRAF2, TRAF3 and TRAF5.5 Publications

Protein-protein interaction databases

BioGridi107381. 32 interactions.
DIPiDIP-2930N.
IntActiP28908. 3 interactions.
STRINGi9606.ENSP00000263932.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D01X-ray2.00G/H/I576-583[»]
ProteinModelPortaliP28908.
SMRiP28908. Positions 42-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28908.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 6639TNFR-Cys 1Add
BLAST
Repeati68 – 10639TNFR-Cys 2Add
BLAST
Repeati107 – 15044TNFR-Cys 3Add
BLAST
Repeati205 – 24137TNFR-Cys 4Add
BLAST
Repeati243 – 28139TNFR-Cys 5Add
BLAST
Repeati282 – 32544TNFR-Cys 6Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi347 – 37731Pro/Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Contains 6 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45191.
GeneTreeiENSGT00510000049215.
HOGENOMiHOG000220871.
HOVERGENiHBG005054.
InParanoidiP28908.
KOiK05145.
OrthoDBiEOG786H2Q.
PhylomeDBiP28908.
TreeFamiTF331157.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020416. TNFR_8.
[Graphical view]
PfamiPF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01923. TNFACTORR8.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P28908-1) [UniParc]FASTAAdd to basket

Also known as: Long

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
MRVLLAALGL LFLGALRAFP QDRPFEDTCH GNPSHYYDKA VRRCCYRCPM
60 70 80 90 100
GLFPTQQCPQ RPTDCRKQCE PDYYLDEADR CTACVTCSRD DLVEKTPCAW
110 120 130 140 150
NSSRVCECRP GMFCSTSAVN SCARCFFHSV CPAGMIVKFP GTAQKNTVCE
160 170 180 190 200
PASPGVSPAC ASPENCKEPS SGTIPQAKPT PVSPATSSAS TMPVRGGTRL
210 220 230 240 250
AQEAASKLTR APDSPSSVGR PSSDPGLSPT QPCPEGSGDC RKQCEPDYYL
260 270 280 290 300
DEAGRCTACV SCSRDDLVEK TPCAWNSSRT CECRPGMICA TSATNSCARC
310 320 330 340 350
VPYPICAAET VTKPQDMAEK DTTFEAPPLG TQPDCNPTPE NGEAPASTSP
360 370 380 390 400
TQSLLVDSQA SKTLPIPTSA PVALSSTGKP VLDAGPVLFW VILVLVVVVG
410 420 430 440 450
SSAFLLCHRR ACRKRIRQKL HLCYPVQTSQ PKLELVDSRP RRSSTQLRSG
460 470 480 490 500
ASVTEPVAEE RGLMSQPLME TCHSVGAAYL ESLPLQDASP AGGPSSPRDL
510 520 530 540 550
PEPRVSTEHT NNKIEKIYIM KADTVIVGTV KAELPEGRGL AGPAEPELEE
560 570 580 590
ELEADHTPHY PEQETEPPLG SCSDVMLSVE EEGKEDPLPT AASGK
Length:595
Mass (Da):63,747
Last modified:December 1, 1992 - v1
Checksum:i7A407CC78A6E0BC8
GO
Isoform 2 (identifier: P28908-2) [UniParc]FASTAAdd to basket

Also known as: Cytoplasmic, Short, C30V

The sequence of this isoform differs from the canonical sequence as follows:
     1-463: Missing.

Show »
Length:132
Mass (Da):14,088
Checksum:i211648B504B6313F
GO
Isoform 3 (identifier: P28908-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.
     446-446: Missing.

Show »
Length:483
Mass (Da):50,935
Checksum:i8EA95A0BEA6BD315
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti273 – 2731C → F.
Corresponds to variant rs2230624 [ dbSNP | Ensembl ].
VAR_054213
Natural varianti273 – 2731C → Y.1 Publication
VAR_018753
Natural varianti297 – 2971C → R.1 Publication
Corresponds to variant rs1763642 [ dbSNP | Ensembl ].
VAR_055257
Natural varianti314 – 3141P → S.
Corresponds to variant rs2275170 [ dbSNP | Ensembl ].
VAR_055258
Natural varianti402 – 4021S → G.1 Publication
Corresponds to variant rs2230625 [ dbSNP | Ensembl ].
VAR_018754
Natural varianti466 – 4661Q → R.
Corresponds to variant rs35511003 [ dbSNP | Ensembl ].
VAR_055259

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 463463Missing in isoform 2. 2 PublicationsVSP_018900Add
BLAST
Alternative sequencei1 – 111111Missing in isoform 3. 1 PublicationVSP_055032Add
BLAST
Alternative sequencei446 – 4461Missing in isoform 3. 1 PublicationVSP_055033

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83554 mRNA. Translation: AAA51947.1.
S75768 mRNA. Translation: AAD14188.1.
D86042 mRNA. Translation: BAA12973.1.
AJ289159 Genomic DNA. Translation: CAC16652.1.
AY498860 Genomic DNA. Translation: AAR32099.1.
AL357835 Genomic DNA. No translation available.
BC063482 mRNA. Translation: AAH63482.2.
BC136400 mRNA. Translation: AAI36401.1.
CCDSiCCDS144.1. [P28908-1]
CCDS59989.1. [P28908-3]
PIRiA42086.
RefSeqiNP_001234.3. NM_001243.4. [P28908-1]
NP_001268359.2. NM_001281430.2. [P28908-3]
UniGeneiHs.1314.

Genome annotation databases

EnsembliENST00000263932; ENSP00000263932; ENSG00000120949. [P28908-1]
ENST00000413146; ENSP00000398337; ENSG00000120949. [P28908-2]
ENST00000417814; ENSP00000390650; ENSG00000120949. [P28908-3]
GeneIDi943.
KEGGihsa:943.
UCSCiuc001atq.3. human. [P28908-1]
uc001atr.3. human. [P28908-2]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83554 mRNA. Translation: AAA51947.1.
S75768 mRNA. Translation: AAD14188.1.
D86042 mRNA. Translation: BAA12973.1.
AJ289159 Genomic DNA. Translation: CAC16652.1.
AY498860 Genomic DNA. Translation: AAR32099.1.
AL357835 Genomic DNA. No translation available.
BC063482 mRNA. Translation: AAH63482.2.
BC136400 mRNA. Translation: AAI36401.1.
CCDSiCCDS144.1. [P28908-1]
CCDS59989.1. [P28908-3]
PIRiA42086.
RefSeqiNP_001234.3. NM_001243.4. [P28908-1]
NP_001268359.2. NM_001281430.2. [P28908-3]
UniGeneiHs.1314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D01X-ray2.00G/H/I576-583[»]
ProteinModelPortaliP28908.
SMRiP28908. Positions 42-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107381. 32 interactions.
DIPiDIP-2930N.
IntActiP28908. 3 interactions.
STRINGi9606.ENSP00000263932.

Chemistry

ChEMBLiCHEMBL2364161.
DrugBankiDB08870. Brentuximab vedotin.
GuidetoPHARMACOLOGYi1877.

PTM databases

PhosphoSiteiP28908.

Polymorphism and mutation databases

BioMutaiTNFRSF8.
DMDMi115978.

Proteomic databases

MaxQBiP28908.
PaxDbiP28908.
PRIDEiP28908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263932; ENSP00000263932; ENSG00000120949. [P28908-1]
ENST00000413146; ENSP00000398337; ENSG00000120949. [P28908-2]
ENST00000417814; ENSP00000390650; ENSG00000120949. [P28908-3]
GeneIDi943.
KEGGihsa:943.
UCSCiuc001atq.3. human. [P28908-1]
uc001atr.3. human. [P28908-2]

Organism-specific databases

CTDi943.
GeneCardsiGC01P012123.
H-InvDBHIX0200047.
HGNCiHGNC:11923. TNFRSF8.
HPAiCAB000016.
HPA032081.
HPA032082.
MIMi153243. gene.
neXtProtiNX_P28908.
PharmGKBiPA36616.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45191.
GeneTreeiENSGT00510000049215.
HOGENOMiHOG000220871.
HOVERGENiHBG005054.
InParanoidiP28908.
KOiK05145.
OrthoDBiEOG786H2Q.
PhylomeDBiP28908.
TreeFamiTF331157.

Enzyme and pathway databases

SignaLinkiP28908.

Miscellaneous databases

EvolutionaryTraceiP28908.
GeneWikiiCD30.
GenomeRNAii943.
NextBioi35481995.
PROiP28908.
SOURCEiSearch...

Gene expression databases

BgeeiP28908.
CleanExiHS_TNFRSF8.
ExpressionAtlasiP28908. baseline and differential.
GenevisibleiP28908. HS.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020416. TNFR_8.
[Graphical view]
PfamiPF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01923. TNFACTORR8.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a new member of the nerve growth factor receptor family that is characteristic for Hodgkin's disease."
    Duerkop H., Latza U., Hummel M., Eitelbach F., Seed B., Stein H.
    Cell 68:421-427(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphoid tissue.
  2. "Opposite effects of the CD30 ligand are not due to CD30 mutations: results from cDNA cloning and sequence comparison of the CD30 antigen from different sources."
    Jung W., Krueger S., Renner C., Gause A., Sahin U., Trumper L., Pfreundschuh M.
    Mol. Immunol. 31:1329-1334(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "A variant CD30 protein lacking extracellular and transmembrane domains is induced in HL-60 by tetradecanoylphorbol acetate and is expressed in alveolar macrophages."
    Horie R., Ito K., Tatewaki M., Nagai M., Aizawa S., Higashihara M., Ishida T., Inoue J., Takizawa H., Watanabe T.
    Blood 88:2422-2432(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Structure of the Hodgkin's disease associated human CD30 gene and the influence of a microsatellite region on its expression in CD30+ cell lines."
    Durkop H., Oberbarnscheidt M., Latza U., Bulfone-Paus S.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    Tissue: Placenta.
  5. NIEHS SNPs program
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-273 AND GLY-402.
  6. "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], VARIANT ARG-297.
  7. "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 2 AND 3).
    Tissue: Blood and Testis.
  8. "T cell receptor-dependent cell death of T cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors."
    Lee S.Y., Park C.G., Choi Y.
    J. Exp. Med. 183:669-674(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF1 AND TRAF2.
  9. "Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other members of the TNF receptor superfamily."
    Boucher L.-M., Marengere L.E., Lu Y., Thukral S., Mak T.W.
    Biochem. Biophys. Res. Commun. 233:592-600(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF3.
  10. "Cloning and characterization of a cDNA encoding the human homolog of tumor necrosis factor receptor-associated factor 5 (TRAF5)."
    Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M., Yamamoto T., Inoue J.
    Gene 207:135-140(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF5.
  11. "Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2 are involved in CD30-mediated NFkappaB activation."
    Aizawa S., Nakano H., Ishida T., Horie R., Nagai M., Ito K., Yagita H., Okumura K., Inoue J., Watanabe T.
    J. Biol. Chem. 272:2042-2045(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF5.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The structural basis for the recognition of diverse receptor sequences by TRAF2."
    Ye H., Park Y.C., Kreishman M., Kieff E., Wu H.
    Mol. Cell 4:321-330(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 576-583 IN COMPLEX WITH TRAF2, INTERACTION WITH TRAF2.

Entry informationi

Entry nameiTNR8_HUMAN
AccessioniPrimary (citable) accession number: P28908
Secondary accession number(s): B1AN79
, B9EGD9, D3YTD8, Q6P4D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 24, 2015
This is version 162 of the entry and version 1 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

Miscellaneous

Most specific Hodgkin disease associated antigen.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.