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T-cell-specific surface glycoprotein CD28 (TP44) (CD antigen CD28)

 CD28_HUMAN              Reviewed;         220 AA.
P10747; A8KAC1; Q13964; Q52M23; Q70WG0; Q8NI54; Q8NI55; Q8NI56;
Q8WXJ2; Q9BYV0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
27-SEP-2017, entry version 183.
RecName: Full=T-cell-specific surface glycoprotein CD28;
AltName: Full=TP44;
AltName: CD_antigen=CD28;
Flags: Precursor;
Name=CD28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2825196; DOI=10.1073/pnas.84.23.8573;
Aruffo A., Seed B.;
"Molecular cloning of a CD28 cDNA by a high-efficiency COS cell
expression system.";
Proc. Natl. Acad. Sci. U.S.A. 84:8573-8577(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), AND ALTERNATIVE
SPLICING.
PubMed=2162892;
Lee K.P., Taylor C., Petryniak B., Turka L.A., June C.H.,
Thompson C.B.;
"The genomic organization of the CD28 gene. Implications for the
regulation of CD28 mRNA expression and heterogeneity.";
J. Immunol. 145:344-352(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=11916166; DOI=10.1016/S0198-8859(01)00354-8;
Deshpande M., Venuprasad K., Parab P.B., Saha B., Mitra D.;
"A novel CD28 mRNA variant and simultaneous presence of various CD28
mRNA isoforms in human T lymphocytes.";
Hum. Immunol. 63:20-23(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 6), AND CHARACTERIZATION
(ISOFORM 3).
TISSUE=Peripheral blood T-cell;
PubMed=11877290; DOI=10.1182/blood.V99.6.2138;
Hanawa H., Ma Y., Mikolajczak S.A., Charles M.L., Yoshida T.,
Yoshida R., Strathdee C.A., Litchfield D.W., Ochi A.;
"A novel costimulatory signaling in human T lymphocytes by a splice
variant of CD28.";
Blood 99:2138-2145(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Gan S.U., Hare J., Krivoshchapov L., Hui K.M., Galea-Lauri J.,
Farzaneh F., Darling D.;
"New human CD28 isoforms generated by a novel splicing event in the
5'UTR.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Synovium, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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., 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178 (ISOFORM 1).
PubMed=11735222; DOI=10.1006/geno.2001.6655;
Ling V., Wu P.W., Finnerty H.F., Agostino M.J., Graham J.R., Chen S.,
Jussiff J.M., Fisk G.J., Miller C.P., Collins M.;
"Assembly and annotation of human chromosome 2q33 sequence containing
the CD28, CTLA4, and ICOS gene cluster: analysis by computational,
comparative, and microarray approaches.";
Genomics 78:155-168(2001).
[12]
FUNCTION.
PubMed=8617933;
Blotta M.H., Marshall J.D., DeKruyff R.H., Umetsu D.T.;
"Cross-linking of the CD40 ligand on human CD4+ T lymphocytes
generates a costimulatory signal that up-regulates IL-4 synthesis.";
J. Immunol. 156:3133-3140(1996).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[14]
FUNCTION (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), INTERACTION
WITH CD40LG (ISOFORM 3), AND PHOSPHORYLATION (ISOFORM 3).
PubMed=15067037; DOI=10.1084/jem.20031705;
Mikolajczak S.A., Ma B.Y., Yoshida T., Yoshida R., Kelvin D.J.,
Ochi A.;
"The modulation of CD40 ligand signaling by transmembrane CD28 splice
variant in human T cells.";
J. Exp. Med. 199:1025-1031(2004).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71 AND ASN-129.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND TYR-191, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-152 IN COMPLEX WITH THE
FAB FRAGMENT OF A MITOGENIC ANTIBODY, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-37 AND ASN-105.
PubMed=15696168; DOI=10.1038/ni1170;
Evans E.J., Esnouf R.M., Manso-Sancho R., Gilbert R.J., James J.R.,
Yu C., Fennelly J.A., Vowles C., Hanke T., Walse B., Hunig T.,
Sorensen P., Stuart D.I., Davis S.J.;
"Crystal structure of a soluble CD28-Fab complex.";
Nat. Immunol. 6:271-279(2005).
[18]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 189-196 IN COMPLEX WITH
GRB2, AND INTERACTION WITH GRB2.
PubMed=24098653; DOI=10.1371/journal.pone.0074482;
Higo K., Ikura T., Oda M., Morii H., Takahashi J., Abe R., Ito N.;
"High resolution crystal structure of the Grb2 SH2 domain with a
phosphopeptide derived from CD28.";
PLoS ONE 8:E74482-E74482(2013).
-!- FUNCTION: Involved in T-cell activation, the induction of cell
proliferation and cytokine production and promotion of T-cell
survival. Enhances the production of IL4 and IL10 in T-cells in
conjunction with TCR/CD3 ligation and CD40L costimulation
(PubMed:8617933). Isoform 3 enhances CD40L-mediated activation of
NF-kappa-B and kinases MAPK8 and PAK2 in T-cells
(PubMed:15067037). {ECO:0000269|PubMed:15067037,
ECO:0000269|PubMed:8617933}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with DUSP14. Binds
to CD80/B7-1 and CD86/B7-2/B70. Interacts with GRB2. Isoform 3
interacts with CD40LG (PubMed:15067037).
{ECO:0000269|PubMed:15067037, ECO:0000269|PubMed:15696168,
ECO:0000269|PubMed:24098653}.
-!- INTERACTION:
P27986:PIK3R1; NbExp=8; IntAct=EBI-4314301, EBI-79464;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell surface
{ECO:0000269|PubMed:15067037}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=P10747-1; Sequence=Displayed;
Name=2; Synonyms=CD28-S2;
IsoId=P10747-2; Sequence=VSP_002494;
Name=3; Synonyms=CD28i;
IsoId=P10747-3; Sequence=VSP_002495;
Name=4; Synonyms=CD28-S1;
IsoId=P10747-4; Sequence=VSP_002496;
Name=5;
IsoId=P10747-5; Sequence=VSP_002495, VSP_002497, VSP_002498;
Name=6; Synonyms=CD28-S3;
IsoId=P10747-6; Sequence=VSP_002495, VSP_002499;
Name=7;
IsoId=P10747-7; Sequence=VSP_047701;
-!- TISSUE SPECIFICITY: Expressed in T-cells and plasma cells, but not
in less mature B-cells.
-!- PTM: CD40LG induces tyrosine phosphorylation of isoform 3.
{ECO:0000269|PubMed:15067037}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CD28 entry;
URL="https://en.wikipedia.org/wiki/CD28";
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EMBL; J02988; AAA60581.1; -; mRNA.
EMBL; M37815; AAA51944.1; -; Genomic_DNA.
EMBL; M37812; AAA51944.1; JOINED; Genomic_DNA.
EMBL; M37813; AAA51944.1; JOINED; Genomic_DNA.
EMBL; M37814; AAA51944.1; JOINED; Genomic_DNA.
EMBL; M37815; AAA51945.1; -; Genomic_DNA.
EMBL; M37812; AAA51945.1; JOINED; Genomic_DNA.
EMBL; M37813; AAA51945.1; JOINED; Genomic_DNA.
EMBL; M37814; AAA51945.1; JOINED; Genomic_DNA.
EMBL; AJ295273; CAC29237.1; -; mRNA.
EMBL; AF222341; AAF33792.1; -; mRNA.
EMBL; AF222342; AAF33793.1; -; mRNA.
EMBL; AF222343; AAF33794.1; -; mRNA.
EMBL; AJ517504; CAD57003.1; -; mRNA.
EMBL; EF064755; ABK41938.1; -; Genomic_DNA.
EMBL; AK292986; BAF85675.1; -; mRNA.
EMBL; AK313313; BAG36118.1; -; mRNA.
EMBL; AC125238; AAY24123.1; -; Genomic_DNA.
EMBL; CH471063; EAW70348.1; -; Genomic_DNA.
EMBL; BC093698; AAH93698.1; -; mRNA.
EMBL; BC112085; AAI12086.1; -; mRNA.
EMBL; AF411057; AAL40931.1; -; Genomic_DNA.
CCDS; CCDS2361.1; -. [P10747-1]
CCDS; CCDS58749.1; -. [P10747-2]
PIR; A39983; RWHU28.
RefSeq; NP_001230006.1; NM_001243077.1. [P10747-4]
RefSeq; NP_001230007.1; NM_001243078.1. [P10747-2]
RefSeq; NP_006130.1; NM_006139.3. [P10747-1]
RefSeq; XP_011510496.1; XM_011512194.2. [P10747-7]
RefSeq; XP_011510499.1; XM_011512197.2. [P10747-3]
UniGene; Hs.443123; -.
PDB; 1YJD; X-ray; 2.70 A; C=17-152.
PDB; 3WA4; X-ray; 1.35 A; B=189-196.
PDB; 5AUL; X-ray; 1.10 A; B=189-196.
PDB; 5GJH; X-ray; 1.20 A; B/D=189-196.
PDB; 5GJI; X-ray; 0.90 A; B=189-196.
PDBsum; 1YJD; -.
PDBsum; 3WA4; -.
PDBsum; 5AUL; -.
PDBsum; 5GJH; -.
PDBsum; 5GJI; -.
ProteinModelPortal; P10747; -.
SMR; P10747; -.
BioGrid; 107378; 20.
CORUM; P10747; -.
DIP; DIP-6043N; -.
ELM; P10747; -.
IntAct; P10747; 7.
MINT; MINT-4656075; -.
STRING; 9606.ENSP00000324890; -.
ChEMBL; CHEMBL5191; -.
GuidetoPHARMACOLOGY; 2863; -.
iPTMnet; P10747; -.
PhosphoSitePlus; P10747; -.
BioMuta; CD28; -.
DMDM; 115973; -.
MaxQB; P10747; -.
PaxDb; P10747; -.
PeptideAtlas; P10747; -.
PRIDE; P10747; -.
Ensembl; ENST00000324106; ENSP00000324890; ENSG00000178562. [P10747-1]
Ensembl; ENST00000374481; ENSP00000363605; ENSG00000178562. [P10747-2]
Ensembl; ENST00000458610; ENSP00000393648; ENSG00000178562. [P10747-7]
GeneID; 940; -.
KEGG; hsa:940; -.
UCSC; uc002vah.6; human. [P10747-1]
CTD; 940; -.
DisGeNET; 940; -.
EuPathDB; HostDB:ENSG00000178562.17; -.
GeneCards; CD28; -.
HGNC; HGNC:1653; CD28.
HPA; HPA070003; -.
MalaCards; CD28; -.
MIM; 186760; gene.
neXtProt; NX_P10747; -.
OpenTargets; ENSG00000178562; -.
PharmGKB; PA26207; -.
eggNOG; ENOG410IXMM; Eukaryota.
eggNOG; ENOG410Z063; LUCA.
GeneTree; ENSGT00530000063873; -.
HOGENOM; HOG000276892; -.
HOVERGEN; HBG004094; -.
InParanoid; P10747; -.
KO; K06470; -.
OMA; VNGNYSH; -.
OrthoDB; EOG091G0IGY; -.
PhylomeDB; P10747; -.
TreeFam; TF335679; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-164939; Nef mediated downregulation of CD28 cell surface expression.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P10747; -.
SIGNOR; P10747; -.
ChiTaRS; CD28; human.
EvolutionaryTrace; P10747; -.
GeneWiki; CD28; -.
GenomeRNAi; 940; -.
PRO; PR:P10747; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000178562; -.
CleanEx; HS_CD28; -.
Genevisible; P10747; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:MGI.
GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; NAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:UniProtKB.
GO; GO:0042089; P:cytokine biosynthetic process; TAS:UniProtKB.
GO; GO:0006959; P:humoral immune response; TAS:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IDA:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; NAS:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; NAS:UniProtKB.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0045066; P:regulatory T cell differentiation; IDA:BHF-UCL.
GO; GO:0031295; P:T cell costimulation; TAS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR008093; CD28.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013106; Ig_V-set.
Pfam; PF15910; V-set_2; 1.
PRINTS; PR01717; CD28ANTIGEN.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 18
CHAIN 19 220 T-cell-specific surface glycoprotein
CD28.
/FTId=PRO_0000014652.
TOPO_DOM 19 152 Extracellular. {ECO:0000255}.
TRANSMEM 153 179 Helical. {ECO:0000255}.
TOPO_DOM 180 220 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 137 Ig-like V-type.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 191 191 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 209 209 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15696168}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15696168}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 40 112 {ECO:0000269|PubMed:15696168}.
DISULFID 66 86 {ECO:0000269|PubMed:15696168}.
VAR_SEQ 1 17 MLRLLLALNLFPSIQVT -> MPCGLSALIMCPKGMVAVVV
AVDDGDSQALA (in isoform 7).
{ECO:0000303|Ref.5}.
/FTId=VSP_047701.
VAR_SEQ 19 137 Missing (in isoform 2).
{ECO:0000303|PubMed:11877290}.
/FTId=VSP_002494.
VAR_SEQ 40 137 CKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYS
KTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPP
YLDNEKSNGTIIHVKG -> W (in isoform 4).
{ECO:0000303|PubMed:11877290}.
/FTId=VSP_002496.
VAR_SEQ 40 124 CKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYS
KTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPP
YLD -> Y (in isoform 3, isoform 5 and
isoform 6). {ECO:0000303|PubMed:11877290,
ECO:0000303|PubMed:11916166}.
/FTId=VSP_002495.
VAR_SEQ 138 139 KH -> EE (in isoform 5).
{ECO:0000303|PubMed:11916166}.
/FTId=VSP_002497.
VAR_SEQ 140 220 Missing (in isoform 5).
{ECO:0000303|PubMed:11916166}.
/FTId=VSP_002498.
VAR_SEQ 152 207 Missing (in isoform 6).
{ECO:0000303|PubMed:11877290}.
/FTId=VSP_002499.
STRAND 27 30 {ECO:0000244|PDB:1YJD}.
STRAND 35 43 {ECO:0000244|PDB:1YJD}.
STRAND 49 58 {ECO:0000244|PDB:1YJD}.
STRAND 64 74 {ECO:0000244|PDB:1YJD}.
STRAND 77 79 {ECO:0000244|PDB:1YJD}.
STRAND 81 83 {ECO:0000244|PDB:1YJD}.
STRAND 85 90 {ECO:0000244|PDB:1YJD}.
STRAND 92 101 {ECO:0000244|PDB:1YJD}.
HELIX 104 106 {ECO:0000244|PDB:1YJD}.
STRAND 108 121 {ECO:0000244|PDB:1YJD}.
STRAND 123 125 {ECO:0000244|PDB:1YJD}.
STRAND 131 134 {ECO:0000244|PDB:1YJD}.
SEQUENCE 220 AA; 25066 MW; 1D9B6552A5878D0F CRC64;
MLRLLLALNL FPSIQVTGNK ILVKQSPMLV AYDNAVNLSC KYSYNLFSRE FRASLHKGLD
SAVEVCVVYG NYSQQLQVYS KTGFNCDGKL GNESVTFYLQ NLYVNQTDIY FCKIEVMYPP
PYLDNEKSNG TIIHVKGKHL CPSPLFPGPS KPFWVLVVVG GVLACYSLLV TVAFIIFWVR
SKRSRLLHSD YMNMTPRRPG PTRKHYQPYA PPRDFAAYRS


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