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CD30; tumor necrosis factor receptor superfamily member 8; CD30L receptor; lymphocyte activation antigen CD30; KI-1 antigen (TNFRSF8, D1S166E)
Function:
- receptor for TNFSF8/CD30L
- may play a role in the regulation of cellular growth & transformation of activated lymphoblasts
- regulates gene expression through activation of NF-kappa-B
- interacts with TRAF1, TRAF2, TRAF3 & TRAF5
- phosphorylated on Ser & Tyr
Structure: contains 6 TNFR-Cys repeats
Compartment:
- isoform long: cell membrane
- isoform short: cytoplasm
Alternative initiation: named isoforms=2
Expression:
- granulocytes
- plasma cells
- activated T cells & B cells
- NK cells
Pathology:
- expressed in:
a) lymphocytes infected with HIV, HTLV-1, EBV, HHV8 or hepatitis B virus
b) infectious mononucleosis
c) Reed-Sternberg cells
- CD30 is a cell surface marke for Hodgkin's disease
d) anaplastic large cell lymphomas ~90%
e) lymphomatoid papulosis
f) peripheral T cell lymphomas
g) embryonal carcinoma
Pharmacology:
- target of monoclonal antibody brentuximab, component of antineoplastic agent brentuximab vedotin used for treatment of Hodgkin's lymphoma & systemic anaplastic large cell lymphoma
Related
CD30 Ag in tissue
CD30 cells in specimen
Hodgkin's disease (Hodgkin's lymphoma)
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
tumor necrosis factor [TNF] receptor family
Properties
SIZE: MW = 64 kD
entity length = 595 aa
COMPARTMENT: plasma membrane
MOTIF: cysteine-rich region {N-TERMINAL}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
N-glycosylation site
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
cysteine-rich region {complement receptor type 2
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-20}
Sushi domain {21-659} (10)
MOTIF: cysteine residue {C23}
MODIFICATION: cysteine residue {C65}
cysteine residue {C51}
MODIFICATION: cysteine residue {C82}
cysteine residue {C65}
MODIFICATION: cysteine residue {C23}
cysteine residue {C82}
MODIFICATION: cysteine residue {C51}
Sushi domain {660-716}
MOTIF: cysteine residue {C662}
MODIFICATION: cysteine residue {C699}
N-glycosylation site {N682}
cysteine residue {C685}
MODIFICATION: cysteine residue {C714}
cysteine residue {C699}
MODIFICATION: cysteine residue {C662}
cysteine residue {C714}
MODIFICATION: cysteine residue {C685}
Sushi domain {717-781}
MOTIF: cysteine residue {C719}
MODIFICATION: cysteine residue {C762}
cysteine residue {C748}
MODIFICATION: cysteine residue {C779}
cysteine residue {C762}
MODIFICATION: cysteine residue {C719}
cysteine residue {C779}
MODIFICATION: cysteine residue {C748}
Sushi domain {786-845}
MOTIF: cysteine residue {C788}
MODIFICATION: cysteine residue {C830}
N-glycosylation site {N800}
cysteine residue {C816}
MODIFICATION: cysteine residue {C843}
N-glycosylation site {N823}
cysteine residue {C830}
MODIFICATION: cysteine residue {C788}
cysteine residue {C843}
MODIFICATION: cysteine residue {C816}
Sushi domain {849-909}
MOTIF: cysteine residue {C851}
MODIFICATION: cysteine residue {C894}
N-glycosylation site {N861}
cysteine residue {C880}
MODIFICATION: cysteine residue {C907}
cysteine residue {C894}
MODIFICATION: cysteine residue {C851}
cysteine residue {C907}
MODIFICATION: cysteine residue {C880}
Sushi domain {910-970}
MOTIF: N-glycosylation site {N911}
cysteine residue {C912}
MODIFICATION: cysteine residue {C955}
cysteine residue {C941}
MODIFICATION: cysteine residue {C968}
cysteine residue {C955}
MODIFICATION: cysteine residue {C912}
cysteine residue {C968}
MODIFICATION: cysteine residue {C941}
transmembrane domain {972-999}
Tyr phosphorylation site {Y1029}}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
N-glycosylation site
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
cysteine-rich region {integrin alpha-M
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-16}
FG-GAP {31-84}
MOTIF: cysteine residue {C66}
MODIFICATION: cysteine residue {C73}
cysteine residue {C73}
MODIFICATION: cysteine residue {C66}
FG-GAP {85-163}
MOTIF: N-glycosylation site {N86}
cysteine residue {C105}
MODIFICATION: cysteine residue {C123}
cysteine residue {C123}
MODIFICATION: cysteine residue {C105}
VWFA domain {164-350}
MOTIF: N-glycosylation site {N240}
FG-GAP {337-400}
MOTIF: N-glycosylation site {N391}
FG-GAP {401-452}
FG-GAP {454-515}
MOTIF: Ca+2-binding site
SITE: 465-473
N-glycosylation site {N469}
FG-GAP {517-575}
MOTIF: Ca+2-binding site
SITE: 529-537
FG-GAP {580-632}
MOTIF: Ca+2-binding site
SITE: 592-600
cysteine residue {C654}
MODIFICATION: cysteine residue {C711}
N-glycosylation site {N692}
N-glycosylation site {N696}
cysteine residue {C711}
MODIFICATION: cysteine residue {C654}
N-glycosylation site {N734}
cysteine residue {C770}
MODIFICATION: cysteine residue {C776}
cysteine residue {C776}
MODIFICATION: cysteine residue {C770}
N-glycosylation site {N801}
cysteine residue {C847}
MODIFICATION: cysteine residue {C864}
cysteine residue {C864}
MODIFICATION: cysteine residue {C847}
N-glycosylation site {N880}
N-glycosylation site {N900}
N-glycosylation site {N911}
N-glycosylation site {N940}
N-glycosylation site {N946}
N-glycosylation site {N978}
N-glycosylation site {N993}
cysteine residue {C998}
MODIFICATION: cysteine residue {C1022}
N-glycosylation site {N1021}
cysteine residue {C1022}
MODIFICATION: cysteine residue {C998}
cysteine residue {C1027}
MODIFICATION: cysteine residue {C1032}
cysteine residue {C1032}
MODIFICATION: cysteine residue {C1027}
N-glycosylation site {N1044}
N-glycosylation site {N1050}
N-glycosylation site {N1075}
transmembrane domain {1105-1128}
GFFKR {1131-1135}}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
cysteine-rich region {integrin alpha-X
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-19}
FG-GAP {34-87}
MOTIF: N-glycosylation site {N61}
cysteine residue {C69}
MODIFICATION: cysteine residue {C76}
cysteine residue {C76}
MODIFICATION: cysteine residue {C69}
consensus repeat {88}
SEQUENCE-IS: FG-GAP
N-glycosylation site {N89}
cysteine residue {C108}
MODIFICATION: cysteine residue {C126}
cysteine residue {C126}
MODIFICATION: cysteine residue {C108}
VWFA domain {165-351}
N-glycosylation site {N392}
consensus repeat {401}
SEQUENCE-IS: FG-GAP
FG-GAP {402-453}
FG-GAP {455-517}
MOTIF: Ca+2-binding site
SITE: 466-474
FG-GAP {518-576}
MOTIF: Ca+2-binding site
SITE: 530-538
FG-GAP {581-633}
MOTIF: Ca+2-binding site
SITE: 593-601
cysteine residue {C655}
MODIFICATION: cysteine residue {C712}
N-glycosylation site {N697}
cysteine residue {C712}
MODIFICATION: cysteine residue {C655}
N-glycosylation site {N735}
cysteine residue {C771}
MODIFICATION: cysteine residue {C777}
cysteine residue {C777}
MODIFICATION: cysteine residue {C771}
cysteine residue {C848}
MODIFICATION: cysteine residue {C863}
cysteine residue {C863}
MODIFICATION: cysteine residue {C848}
N-glycosylation site {N899}
N-glycosylation site {N939}
cysteine residue {C998}
MODIFICATION: cysteine residue {C1022}
cysteine residue {C1022}
MODIFICATION: cysteine residue {C998}
cysteine residue {C1027}
MODIFICATION: cysteine residue {C1032}
cysteine residue {C1032}
MODIFICATION: cysteine residue {C1027}
N-glycosylation site {N1050}
transmembrane domain {1108-1128}
GFFKR {1131-1135}}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
cysteine-rich region {CR5}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
cysteine-rich region {growth arrest & DNA-damage-inducible protein GADD45 gamma
COMPARTMENT: cell nucleus
MOTIF: binding site
FOR-BINDING-OF: proliferating cell nuclear antigen}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+14}
cysteine residue {X+14}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+16}
MODIFICATION: cysteine residue {X+29}
cysteine residue {X+19}
MODIFICATION: cysteine residue {X+34}
cysteine residue {X+29}
MODIFICATION: cysteine residue {X+16}
cysteine residue {X+34}
MODIFICATION: cysteine residue {X+19}
transmembrane domain
Database Correlations
OMIM 153243
UniProt P28908
Pfam PF00020
Entrez Gene 943
Kegg hsa:943
References
- Durkop H et al,
Molecular cloning and expression of a new member of the
nerve growth factor receptor family that is chararteristic
for Hodgkin's disease
Cell 68:421-7 1992
PMID: 1310894
- http://www.pathologyoutlines.com/cdmarkers.html
15 October 2002
- Entrez Gene :accession 943
- UniProt :accession P28908