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P28908

- TNR8_HUMAN

UniProt

P28908 - TNR8_HUMAN

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Protein
Tumor necrosis factor receptor superfamily member 8
Gene
TNFRSF8, CD30, D1S166E
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. cellular response to mechanical stimulus Source: UniProtKB
  2. negative regulation of cell proliferation Source: ProtInc
  3. positive regulation of TRAIL biosynthetic process Source: UniProtKB
  4. positive regulation of apoptotic process Source: UniProtKB
  5. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  6. 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:11923. TNFRSF8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 379361Extracellular Reviewed prediction
Add
BLAST
Transmembranei380 – 40728Helical; Reviewed prediction
Add
BLAST
Topological domaini408 – 595188Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36616.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 44 By similarity
Disulfide bondi45 ↔ 58 By similarity
Disulfide bondi48 ↔ 65 By similarity
Disulfide bondi69 ↔ 81 By similarity
Disulfide bondi84 ↔ 98 By similarity
Disulfide bondi87 ↔ 106 By similarity
Glycosylationi101 – 1011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi108 ↔ 122 By similarity
Disulfide bondi131 ↔ 149 By similarity
Disulfide bondi233 ↔ 240 By similarity
Disulfide bondi244 ↔ 256 By similarity
Disulfide bondi259 ↔ 273 By similarity
Disulfide bondi262 ↔ 281 By similarity
Glycosylationi276 – 2761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi283 ↔ 297 By similarity
Disulfide bondi289 ↔ 300 By similarity
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

ArrayExpressiP28908.
BgeeiP28908.
CleanExiHS_TNFRSF8.
GenevestigatoriP28908.

Organism-specific databases

HPAiCAB000016.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107381. 11 interactions.
DIPiDIP-2930N.
IntActiP28908. 3 interactions.
STRINGi9606.ENSP00000263932.

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP28908.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

Contains 6 TNFR-Cys repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45191.
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. Align

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

MRVLLAALGL LFLGALRAFP QDRPFEDTCH GNPSHYYDKA VRRCCYRCPM    50
GLFPTQQCPQ RPTDCRKQCE PDYYLDEADR CTACVTCSRD DLVEKTPCAW 100
NSSRVCECRP GMFCSTSAVN SCARCFFHSV CPAGMIVKFP GTAQKNTVCE 150
PASPGVSPAC ASPENCKEPS SGTIPQAKPT PVSPATSSAS TMPVRGGTRL 200
AQEAASKLTR APDSPSSVGR PSSDPGLSPT QPCPEGSGDC RKQCEPDYYL 250
DEAGRCTACV SCSRDDLVEK TPCAWNSSRT CECRPGMICA TSATNSCARC 300
VPYPICAAET VTKPQDMAEK DTTFEAPPLG TQPDCNPTPE NGEAPASTSP 350
TQSLLVDSQA SKTLPIPTSA PVALSSTGKP VLDAGPVLFW VILVLVVVVG 400
SSAFLLCHRR ACRKRIRQKL HLCYPVQTSQ PKLELVDSRP RRSSTQLRSG 450
ASVTEPVAEE RGLMSQPLME TCHSVGAAYL ESLPLQDASP AGGPSSPRDL 500
PEPRVSTEHT NNKIEKIYIM KADTVIVGTV KAELPEGRGL AGPAEPELEE 550
ELEADHTPHY PEQETEPPLG SCSDVMLSVE EEGKEDPLPT AASGK 595
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.
VSP_018900Add
BLAST
Alternative sequencei1 – 111111Missing in isoform 3.
VSP_055032Add
BLAST
Alternative sequencei446 – 4461Missing in isoform 3.
VSP_055033

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
PIRiA42086.
RefSeqiNP_001234.3. NM_001243.4. [P28908-1]
NP_001268359.2. NM_001281430.2.
UniGeneiHs.1314.

Genome annotation databases

EnsembliENST00000413146; ENSP00000398337; ENSG00000120949. [P28908-2]
ENST00000417814; ENSP00000390650; ENSG00000120949.
GeneIDi943.
KEGGihsa:943.
UCSCiuc001atq.3. human. [P28908-1]
uc001atr.3. human. [P28908-2]

Polymorphism databases

DMDMi115978.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS144.1. [P28908-1 ]
PIRi A42086.
RefSeqi NP_001234.3. NM_001243.4. [P28908-1 ]
NP_001268359.2. NM_001281430.2.
UniGenei Hs.1314.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D01 X-ray 2.00 G/H/I 576-583 [» ]
ProteinModelPortali P28908.
SMRi P28908. Positions 42-155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107381. 11 interactions.
DIPi DIP-2930N.
IntActi P28908. 3 interactions.
STRINGi 9606.ENSP00000263932.

Chemistry

ChEMBLi CHEMBL2364161.
GuidetoPHARMACOLOGYi 1877.

PTM databases

PhosphoSitei P28908.

Polymorphism databases

DMDMi 115978.

Proteomic databases

MaxQBi P28908.
PaxDbi P28908.
PRIDEi P28908.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000413146 ; ENSP00000398337 ; ENSG00000120949 . [P28908-2 ]
ENST00000417814 ; ENSP00000390650 ; ENSG00000120949 .
GeneIDi 943.
KEGGi hsa:943.
UCSCi uc001atq.3. human. [P28908-1 ]
uc001atr.3. human. [P28908-2 ]

Organism-specific databases

CTDi 943.
GeneCardsi GC01P012123.
H-InvDB HIX0200047.
HGNCi HGNC:11923. TNFRSF8.
HPAi CAB000016.
MIMi 153243. gene.
neXtProti NX_P28908.
PharmGKBi PA36616.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45191.
HOGENOMi HOG000220871.
HOVERGENi HBG005054.
InParanoidi P28908.
KOi K05145.
OrthoDBi EOG786H2Q.
PhylomeDBi P28908.
TreeFami TF331157.

Enzyme and pathway databases

SignaLinki P28908.

Miscellaneous databases

EvolutionaryTracei P28908.
GeneWikii CD30.
GenomeRNAii 943.
NextBioi 35481995.
PROi P28908.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28908.
Bgeei P28908.
CleanExi HS_TNFRSF8.
Genevestigatori P28908.

Family and domain databases

InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020416. TNFR_8.
[Graphical view ]
Pfami PF00020. TNFR_c6. 3 hits.
[Graphical view ]
PRINTSi PR01923. TNFACTORR8.
SMARTi SM00208. TNFR. 4 hits.
[Graphical view ]
PROSITEi PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 155 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

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