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P10747

- CD28_HUMAN

UniProt

P10747 - CD28_HUMAN

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Protein
T-cell-specific surface glycoprotein CD28
Gene
CD28
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: UniProtKB
  2. coreceptor activity Source: UniProtKB
  3. identical protein binding Source: UniProtKB
  4. protease binding Source: BHF-UCL
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. T cell costimulation Source: Reactome
  3. apoptotic signaling pathway Source: Ensembl
  4. cell surface receptor signaling pathway Source: UniProtKB
  5. cytokine biosynthetic process Source: UniProtKB
  6. epidermal growth factor receptor signaling pathway Source: Reactome
  7. fibroblast growth factor receptor signaling pathway Source: Reactome
  8. humoral immune response Source: UniProtKB
  9. innate immune response Source: Reactome
  10. negative thymic T cell selection Source: Ensembl
  11. neurotrophin TRK receptor signaling pathway Source: Reactome
  12. phosphatidylinositol-mediated signaling Source: Reactome
  13. positive regulation of T cell proliferation Source: UniProtKB
  14. positive regulation of alpha-beta T cell proliferation Source: Ensembl
  15. positive regulation of inflammatory response to antigenic stimulus Source: Ensembl
  16. positive regulation of interleukin-2 biosynthetic process Source: UniProtKB
  17. positive regulation of isotype switching to IgG isotypes Source: Ensembl
  18. positive regulation of mitosis Source: UniProtKB
  19. positive regulation of signal transduction Source: GOC
  20. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  21. positive regulation of translation Source: UniProtKB
  22. positive regulation of viral genome replication Source: UniProtKB
  23. regulation of defense response to virus by virus Source: Reactome
  24. regulatory T cell differentiation Source: BHF-UCL
  25. viral process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11139. Nef mediated downregulation of CD28 cell surface expression.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19183. CD28 co-stimulation.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP10747.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell-specific surface glycoprotein CD28
Alternative name(s):
TP44
CD_antigen: CD28
Gene namesi
Name:CD28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1653. CD28.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 152134Extracellular Reviewed prediction
Add
BLAST
Transmembranei153 – 17927Helical; Reviewed prediction
Add
BLAST
Topological domaini180 – 22041Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. external side of plasma membrane Source: MGI
  3. integral component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26207.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818
Add
BLAST
Chaini19 – 220202T-cell-specific surface glycoprotein CD28
PRO_0000014652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)1 Publication
Disulfide bondi40 ↔ 1121 Publication
Disulfide bondi66 ↔ 861 Publication
Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi105 – 1051N-linked (GlcNAc...)1 Publication
Glycosylationi129 – 1291N-linked (GlcNAc...)1 Publication
Modified residuei189 – 1891Phosphoserine1 Publication
Modified residuei191 – 1911Phosphotyrosine1 Publication
Modified residuei209 – 2091Phosphotyrosine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP10747.
PaxDbiP10747.
PRIDEiP10747.

PTM databases

PhosphoSiteiP10747.

Expressioni

Tissue specificityi

Expressed in T-cells and plasma cells, but not in less mature B-cells.

Gene expression databases

ArrayExpressiP10747.
BgeeiP10747.
CleanExiHS_CD28.
GenevestigatoriP10747.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with DUSP14. Binds to CD80/B7-1 and CD86/B7-2/B70. Interacts with GRB2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R1P279868EBI-4314301,EBI-79464

Protein-protein interaction databases

BioGridi107378. 12 interactions.
DIPiDIP-6043N.
IntActiP10747. 7 interactions.
MINTiMINT-4656075.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 304
Beta strandi35 – 439
Beta strandi49 – 5810
Beta strandi64 – 7411
Beta strandi77 – 793
Beta strandi81 – 833
Beta strandi85 – 906
Beta strandi92 – 10110
Helixi104 – 1063
Beta strandi108 – 12114
Beta strandi123 – 1253
Beta strandi131 – 1344

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YJDX-ray2.70C17-152[»]
3WA4X-ray1.35B189-196[»]
ProteinModelPortaliP10747.
SMRiP10747. Positions 19-136.

Miscellaneous databases

EvolutionaryTraceiP10747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 137110Ig-like V-type
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG48152.
HOVERGENiHBG004094.
InParanoidiP10747.
KOiK06470.
OMAiAPTYANS.
OrthoDBiEOG7W6WMJ.
PhylomeDBiP10747.
TreeFamiTF335679.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR008093. CD28.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01717. CD28ANTIGEN.

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P10747-1) [UniParc]FASTAAdd to Basket

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

MLRLLLALNL FPSIQVTGNK ILVKQSPMLV AYDNAVNLSC KYSYNLFSRE    50
FRASLHKGLD SAVEVCVVYG NYSQQLQVYS KTGFNCDGKL GNESVTFYLQ 100
NLYVNQTDIY FCKIEVMYPP PYLDNEKSNG TIIHVKGKHL CPSPLFPGPS 150
KPFWVLVVVG GVLACYSLLV TVAFIIFWVR SKRSRLLHSD YMNMTPRRPG 200
PTRKHYQPYA PPRDFAAYRS 220
Length:220
Mass (Da):25,066
Last modified:July 1, 1989 - v1
Checksum:i1D9B6552A5878D0F
GO
Isoform 2 (identifier: P10747-2) [UniParc]FASTAAdd to Basket

Also known as: CD28-S2

The sequence of this isoform differs from the canonical sequence as follows:
     19-137: Missing.

Show »
Length:101
Mass (Da):11,528
Checksum:iF9B205F1D1BBFDC9
GO
Isoform 3 (identifier: P10747-3) [UniParc]FASTAAdd to Basket

Also known as: CD28i

The sequence of this isoform differs from the canonical sequence as follows:
     40-124: CKYSYNLFSR...EVMYPPPYLD → Y

Show »
Length:136
Mass (Da):15,369
Checksum:iC9AF33467706D2BE
GO
Isoform 4 (identifier: P10747-4) [UniParc]FASTAAdd to Basket

Also known as: CD28-S1

The sequence of this isoform differs from the canonical sequence as follows:
     40-137: CKYSYNLFSR...SNGTIIHVKG → W

Show »
Length:123
Mass (Da):14,014
Checksum:i3DE54211F2642520
GO
Isoform 5 (identifier: P10747-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-124: CKYSYNLFSR...EVMYPPPYLD → Y
     138-139: KH → EE
     140-220: Missing.

Show »
Length:55
Mass (Da):6,099
Checksum:iA2F24E0CFBD16D90
GO
Isoform 6 (identifier: P10747-6) [UniParc]FASTAAdd to Basket

Also known as: CD28-S3

The sequence of this isoform differs from the canonical sequence as follows:
     40-124: CKYSYNLFSR...EVMYPPPYLD → Y
     152-207: Missing.

Show »
Length:80
Mass (Da):8,823
Checksum:iC09D0EC41F748AFC
GO
Isoform 7 (identifier: P10747-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MLRLLLALNLFPSIQVT → MPCGLSALIMCPKGMVAVVVAVDDGDSQALA

Show »
Length:234
Mass (Da):26,186
Checksum:i02AD85397834E57E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717MLRLL…SIQVT → MPCGLSALIMCPKGMVAVVV AVDDGDSQALA in isoform 7.
VSP_047701Add
BLAST
Alternative sequencei19 – 137119Missing in isoform 2.
VSP_002494Add
BLAST
Alternative sequencei40 – 13798CKYSY…IHVKG → W in isoform 4.
VSP_002496Add
BLAST
Alternative sequencei40 – 12485CKYSY…PPYLD → Y in isoform 3, isoform 5 and isoform 6.
VSP_002495Add
BLAST
Alternative sequencei138 – 1392KH → EE in isoform 5.
VSP_002497
Alternative sequencei140 – 22081Missing in isoform 5.
VSP_002498Add
BLAST
Alternative sequencei152 – 20756Missing in isoform 6.
VSP_002499Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02988 mRNA. Translation: AAA60581.1.
M37815
, M37812, M37813, M37814 Genomic DNA. Translation: AAA51944.1.
M37815
, M37812, M37813, M37814 Genomic DNA. Translation: AAA51945.1.
AJ295273 mRNA. Translation: CAC29237.1.
AF222341 mRNA. Translation: AAF33792.1.
AF222342 mRNA. Translation: AAF33793.1.
AF222343 mRNA. Translation: AAF33794.1.
AJ517504 mRNA. Translation: CAD57003.1.
EF064755 Genomic DNA. Translation: ABK41938.1.
AK292986 mRNA. Translation: BAF85675.1.
AK313313 mRNA. Translation: BAG36118.1.
AC125238 Genomic DNA. Translation: AAY24123.1.
CH471063 Genomic DNA. Translation: EAW70348.1.
BC093698 mRNA. Translation: AAH93698.1.
BC112085 mRNA. Translation: AAI12086.1.
AF411057 Genomic DNA. Translation: AAL40931.1.
CCDSiCCDS2361.1. [P10747-1]
CCDS58749.1. [P10747-2]
PIRiA39983. RWHU28.
RefSeqiNP_001230006.1. NM_001243077.1. [P10747-4]
NP_001230007.1. NM_001243078.1. [P10747-2]
NP_006130.1. NM_006139.3. [P10747-1]
UniGeneiHs.443123.

Genome annotation databases

EnsembliENST00000324106; ENSP00000324890; ENSG00000178562. [P10747-1]
ENST00000374478; ENSP00000363602; ENSG00000178562. [P10747-2]
ENST00000374481; ENSP00000363605; ENSG00000178562. [P10747-3]
ENST00000458610; ENSP00000393648; ENSG00000178562. [P10747-7]
GeneIDi940.
KEGGihsa:940.
UCSCiuc002vah.4. human. [P10747-1]
uc010ftx.3. human. [P10747-2]
uc010zio.2. human. [P10747-4]

Polymorphism databases

DMDMi115973.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

CD28 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02988 mRNA. Translation: AAA60581.1 .
M37815
, M37812 , M37813 , M37814 Genomic DNA. Translation: AAA51944.1 .
M37815
, M37812 , M37813 , M37814 Genomic DNA. Translation: AAA51945.1 .
AJ295273 mRNA. Translation: CAC29237.1 .
AF222341 mRNA. Translation: AAF33792.1 .
AF222342 mRNA. Translation: AAF33793.1 .
AF222343 mRNA. Translation: AAF33794.1 .
AJ517504 mRNA. Translation: CAD57003.1 .
EF064755 Genomic DNA. Translation: ABK41938.1 .
AK292986 mRNA. Translation: BAF85675.1 .
AK313313 mRNA. Translation: BAG36118.1 .
AC125238 Genomic DNA. Translation: AAY24123.1 .
CH471063 Genomic DNA. Translation: EAW70348.1 .
BC093698 mRNA. Translation: AAH93698.1 .
BC112085 mRNA. Translation: AAI12086.1 .
AF411057 Genomic DNA. Translation: AAL40931.1 .
CCDSi CCDS2361.1. [P10747-1 ]
CCDS58749.1. [P10747-2 ]
PIRi A39983. RWHU28.
RefSeqi NP_001230006.1. NM_001243077.1. [P10747-4 ]
NP_001230007.1. NM_001243078.1. [P10747-2 ]
NP_006130.1. NM_006139.3. [P10747-1 ]
UniGenei Hs.443123.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YJD X-ray 2.70 C 17-152 [» ]
3WA4 X-ray 1.35 B 189-196 [» ]
ProteinModelPortali P10747.
SMRi P10747. Positions 19-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107378. 12 interactions.
DIPi DIP-6043N.
IntActi P10747. 7 interactions.
MINTi MINT-4656075.

Chemistry

ChEMBLi CHEMBL5191.

PTM databases

PhosphoSitei P10747.

Polymorphism databases

DMDMi 115973.

Proteomic databases

MaxQBi P10747.
PaxDbi P10747.
PRIDEi P10747.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324106 ; ENSP00000324890 ; ENSG00000178562 . [P10747-1 ]
ENST00000374478 ; ENSP00000363602 ; ENSG00000178562 . [P10747-2 ]
ENST00000374481 ; ENSP00000363605 ; ENSG00000178562 . [P10747-3 ]
ENST00000458610 ; ENSP00000393648 ; ENSG00000178562 . [P10747-7 ]
GeneIDi 940.
KEGGi hsa:940.
UCSCi uc002vah.4. human. [P10747-1 ]
uc010ftx.3. human. [P10747-2 ]
uc010zio.2. human. [P10747-4 ]

Organism-specific databases

CTDi 940.
GeneCardsi GC02P204535.
HGNCi HGNC:1653. CD28.
MIMi 186760. gene.
neXtProti NX_P10747.
PharmGKBi PA26207.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG48152.
HOVERGENi HBG004094.
InParanoidi P10747.
KOi K06470.
OMAi APTYANS.
OrthoDBi EOG7W6WMJ.
PhylomeDBi P10747.
TreeFami TF335679.

Enzyme and pathway databases

Reactomei REACT_11139. Nef mediated downregulation of CD28 cell surface expression.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19183. CD28 co-stimulation.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki P10747.

Miscellaneous databases

ChiTaRSi CD28. human.
EvolutionaryTracei P10747.
GeneWikii CD28.
GenomeRNAii 940.
NextBioi 3894.
PROi P10747.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10747.
Bgeei P10747.
CleanExi HS_CD28.
Genevestigatori P10747.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR008093. CD28.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view ]
Pfami PF07686. V-set. 1 hit.
[Graphical view ]
PRINTSi PR01717. CD28ANTIGEN.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system."
    Aruffo A., Seed B.
    Proc. Natl. Acad. Sci. U.S.A. 84:8573-8577(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The genomic organization of the CD28 gene. Implications for the regulation of CD28 mRNA expression and heterogeneity."
    Lee K.P., Taylor C., Petryniak B., Turka L.A., June C.H., Thompson C.B.
    J. Immunol. 145:344-352(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING.
  3. "A novel CD28 mRNA variant and simultaneous presence of various CD28 mRNA isoforms in human T lymphocytes."
    Deshpande M., Venuprasad K., Parab P.B., Saha B., Mitra D.
    Hum. Immunol. 63:20-23(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  4. "A novel costimulatory signaling in human T lymphocytes by a splice variant of CD28."
    Hanawa H., Ma Y., Mikolajczak S.A., Charles M.L., Yoshida T., Yoshida R., Strathdee C.A., Litchfield D.W., Ochi A.
    Blood 99:2138-2145(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 6), CHARACTERIZATION (ISOFORM 3).
    Tissue: Peripheral blood T-cell.
  5. "New human CD28 isoforms generated by a novel splicing event in the 5'UTR."
    Gan S.U., Hare J., Krivoshchapov L., Hui K.M., Galea-Lauri J., Farzaneh F., Darling D.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Synovium and Trachea.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
  11. "Assembly and annotation of human chromosome 2q33 sequence containing the CD28, CTLA4, and ICOS gene cluster: analysis by computational, comparative, and microarray approaches."
    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.
    Genomics 78:155-168(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178 (ISOFORM 1).
  12. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71 AND ASN-129.
    Tissue: Leukemic T-cell.
  14. "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-189 AND TYR-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-152 IN COMPLEX WITH THE FAB FRAGMENT OF A MITOGENIC ANTIBODY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-37 AND ASN-105.
  16. "High resolution crystal structure of the Grb2 SH2 domain with a phosphopeptide derived from CD28."
    Higo K., Ikura T., Oda M., Morii H., Takahashi J., Abe R., Ito N.
    PLoS ONE 8:E74482-E74482(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 189-196 IN COMPLEX WITH GRB2, INTERACTION WITH GRB2.

Entry informationi

Entry nameiCD28_HUMAN
AccessioniPrimary (citable) accession number: P10747
Secondary accession number(s): A8KAC1
, Q13964, Q52M23, Q70WG0, Q8NI54, Q8NI55, Q8NI56, Q8WXJ2, Q9BYV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 156 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

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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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