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Q5ZPR3 (CD276_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD276 antigen
Alternative name(s):
4Ig-B7-H3
B7 homolog 3
Short name=B7-H3
Costimulatory molecule
CD_antigen=CD276
Gene names
Name:CD276
Synonyms:B7H3
ORF Names:PSEC0249, UNQ309/PRO352
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling. Ref.1 Ref.2 Ref.8 Ref.9 Ref.11 Ref.13

Subunit structure

Interacts with TREML2 and this interaction enhances T-cell activation. Ref.14

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Tissue specificity

Ubiquitous but not detectable in peripheral blood lymphocytes or granulocytes. Weakly expressed in resting monocytes. Expressed in dendritic cells derived from monocytes. Expressed in epithelial cells of sinonasal tissue. Expressed in extravillous trophoblast cells and Hofbauer cells of the first trimester placenta and term placenta. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12

Induction

By bacterial lipopolysaccharides (LPS) in monocytes and by ionomycin in T and B-lymphocytes. Up-regulated in cells mediating rejection of human transplants. Ref.2 Ref.13

Miscellaneous

B7-H3 locus underwent genomic duplication leading to tandemly repeated immunoglobulin-like V and C domains (VC domains). The dominantly expressed human B7-H3 isoform containstandemly duplicated VC domains. In contrast, mouse B7-H3 transcript contains only one single VC domain form due to an exon structure corresponding to V domain-(pseudoexon C)-(pseudoexon V)-C domain. This duplication appearing in primates is suggested to be very recent supporting a model of multiple independent emergence of tandem VC repeats within human and monkey species.

Sequence similarities

Belongs to the immunoglobulin superfamily. BTN/MOG family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 Ig-like V-type (immunoglobulin-like) domains.

Sequence caution

The sequence BAC11344.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Inferred from direct assay Ref.14. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

immune response

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of interferon-gamma biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-2 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from direct assay Ref.1. Source: HGNC

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma biosynthetic process

Inferred from direct assay Ref.1. Source: HGNC

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Non-traceable author statement Ref.1. Source: HGNC

   Cellular_componentexternal side of plasma membrane

Non-traceable author statement PubMed 15188059. Source: HGNC

integral component of membrane

Non-traceable author statement PubMed 15188059. Source: HGNC

   Molecular_functionprotein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

receptor binding

Non-traceable author statement Ref.1. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5ZPR3-1)

Also known as: 4Ig-B7-H3;

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.
Note: Contains tandemly repeated immunoglobulin-like V and C domains.
Isoform 2 (identifier: Q5ZPR3-2)

Also known as: B7-H3;

The sequence of this isoform differs from the canonical sequence as follows:
     159-376: Missing.
Note: Minor transcript. Contains one single set of immunoglobulin-like V and C domains.
Isoform 3 (identifier: Q5ZPR3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     465-493: EALWVTVGLSVCLIALLVALAFVCWRKIK → GPASSAVPLSPAHPPHGSMCWSHWFSRGL
     494-534: Missing.
Note: Contains tandemly repeated immunoglobulin-like V and C domains.
Isoform 4 (identifier: Q5ZPR3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     528-534: DDGQEIA → GKDTWA
Note: Contains tandemly repeated immunoglobulin-like V and C domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.7
Chain29 – 534506CD276 antigen
PRO_0000045801

Regions

Topological domain29 – 466438Extracellular Potential
Transmembrane467 – 48721Helical; Potential
Topological domain488 – 53447Cytoplasmic Potential
Domain29 – 139111Ig-like V-type 1
Domain145 – 23894Ig-like C2-type 1
Domain243 – 357115Ig-like V-type 2
Domain363 – 45694Ig-like C2-type 2

Amino acid modifications

Modified residue5251Phosphoserine Ref.16
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Ref.17
Glycosylation4071N-linked (GlcNAc...) Ref.17
Glycosylation4331N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 122 By similarity
Disulfide bond165 ↔ 220 By similarity
Disulfide bond268 ↔ 340 By similarity
Disulfide bond383 ↔ 438 By similarity

Natural variations

Alternative sequence159 – 376218Missing in isoform 2.
VSP_017088
Alternative sequence465 – 49329EALWV…WRKIK → GPASSAVPLSPAHPPHGSMC WSHWFSRGL in isoform 3.
VSP_017089
Alternative sequence494 – 53441Missing in isoform 3.
VSP_017090
Alternative sequence528 – 5347DDGQEIA → GKDTWA in isoform 4.
VSP_017091
Natural variant971P → L.
Corresponds to variant rs7173448 [ dbSNP | Ensembl ].
VAR_049857
Natural variant1111R → S.
Corresponds to variant rs7173476 [ dbSNP | Ensembl ].
VAR_049858
Natural variant1371Q → L.
Corresponds to variant rs11574477 [ dbSNP | Ensembl ].
VAR_049859
Natural variant1601T → M. Ref.4 Ref.5
Corresponds to variant rs11574479 [ dbSNP | Ensembl ].
VAR_049860
Natural variant2671R → H.
Corresponds to variant rs11574483 [ dbSNP | Ensembl ].
VAR_049861
Natural variant2791A → T.
Corresponds to variant rs10083681 [ dbSNP | Ensembl ].
VAR_049862
Natural variant3151P → L.
Corresponds to variant rs7173448 [ dbSNP | Ensembl ].
VAR_049863
Natural variant3291R → S.
Corresponds to variant rs7173476 [ dbSNP | Ensembl ].
VAR_049864
Natural variant3781T → M.
Corresponds to variant rs11574479 [ dbSNP | Ensembl ].
VAR_049865

Experimental info

Sequence conflict3871R → Q in AAQ88709. Ref.3
Sequence conflict4731L → P in BAC11243. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (4Ig-B7-H3) [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 2181A064404C7939

FASTA53457,235
        10         20         30         40         50         60 
MLRRRGSPGM GVHVGAALGA LWFCLTGALE VQVPEDPVVA LVGTDATLCC SFSPEPGFSL 

        70         80         90        100        110        120 
AQLNLIWQLT DTKQLVHSFA EGQDQGSAYA NRTALFPDLL AQGNASLRLQ RVRVADEGSF 

       130        140        150        160        170        180 
TCFVSIRDFG SAAVSLQVAA PYSKPSMTLE PNKDLRPGDT VTITCSSYQG YPEAEVFWQD 

       190        200        210        220        230        240 
GQGVPLTGNV TTSQMANEQG LFDVHSILRV VLGANGTYSC LVRNPVLQQD AHSSVTITPQ 

       250        260        270        280        290        300 
RSPTGAVEVQ VPEDPVVALV GTDATLRCSF SPEPGFSLAQ LNLIWQLTDT KQLVHSFTEG 

       310        320        330        340        350        360 
RDQGSAYANR TALFPDLLAQ GNASLRLQRV RVADEGSFTC FVSIRDFGSA AVSLQVAAPY 

       370        380        390        400        410        420 
SKPSMTLEPN KDLRPGDTVT ITCSSYRGYP EAEVFWQDGQ GVPLTGNVTT SQMANEQGLF 

       430        440        450        460        470        480 
DVHSVLRVVL GANGTYSCLV RNPVLQQDAH GSVTITGQPM TFPPEALWVT VGLSVCLIAL 

       490        500        510        520        530 
LVALAFVCWR KIKQSCEEEN AGAEDQDGEG EGSKTALQPL KHSDSKEDDG QEIA 

« Hide

Isoform 2 (B7-H3) [UniParc].

Checksum: FF97007F191CCFA1
Show »

FASTA31633,791
Isoform 3 [UniParc].

Checksum: CD7C5591CC4822D2
Show »

FASTA49352,761
Isoform 4 [UniParc].

Checksum: BC38033295EBE978
Show »

FASTA53357,165

References

« Hide 'large scale' references
[1]"B7-H3: a costimulatory molecule for T cell activation and IFN-gamma production."
Chapoval A.I., Ni J., Lau J.S., Wilcox R.A., Flies D.B., Liu D., Dong H., Sica G.L., Zhu G., Tamada K., Chen L.
Nat. Immunol. 2:269-274(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
[2]"Molecular characterization of human 4Ig-B7-H3, a member of the B7 family with four Ig-like domains."
Steinberger P., Majdic O., Derdak S.V., Pfistershammer K., Kirchberger S., Klauser C., Zlabinger G., Pickl W.F., Stockl J., Knapp W.
J. Immunol. 172:2352-2359(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, INDUCTION.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"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. expand/collapse author list , 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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-534 (ISOFORM 1), VARIANT MET-160.
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-160.
[6]"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] (ISOFORM 3).
Tissue: Lung.
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-43.
[8]"Duplication of primate and rodent B7-H3 immunoglobulin V- and C-like domains: divergent history of functional redundancy and exon loss."
Ling V., Wu P.W., Spaulding V., Kieleczawa J., Luxenberg D., Carreno B.M., Collins M.
Genomics 82:365-377(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GENOMIC DOMAIN DUPLICATION.
[9]"Identification of 4Ig-B7-H3 as a neuroblastoma-associated molecule that exerts a protective role from an NK cell-mediated lysis."
Castriconi R., Dondero A., Augugliaro R., Cantoni C., Carnemolla B., Sementa A.R., Negri F., Conte R., Corrias M.V., Moretta L., Moretta A., Bottino C.
Proc. Natl. Acad. Sci. U.S.A. 101:12640-12645(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The immunomodulatory proteins B7-DC, B7-H2, and B7-H3 are differentially expressed across gestation in the human placenta."
Petroff M.G., Kharatyan E., Torry D.S., Holets L.
Am. J. Pathol. 167:465-473(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Constitutive and inducible expression of B7 family of ligands by human airway epithelial cells."
Kim J., Myers A.C., Chen L., Pardoll D.M., Truong-Tran Q.A., Lane A.P., McDyer J.F., Fortuno L., Schleimer R.P.
Am. J. Respir. Cell Mol. Biol. 33:280-289(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"B7-H3: another molecule marker for Mo-DCs?"
Zhang G.B., Dong Q.M., Xu Y., Yu G.H., Zhang X.G.
Cell. Mol. Immunol. 2:307-311(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"B7-H3 promotes acute and chronic allograft rejection."
Wang L., Fraser C.C., Kikly K., Wells A.D., Han R., Coyle A.J., Chen L., Hancock W.W.
Eur. J. Immunol. 35:428-438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[14]"Triggering receptor expressed on myeloid cell-like transcript 2 (TLT-2) is a counter-receptor for B7-H3 and enhances T cell responses."
Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.
Proc. Natl. Acad. Sci. U.S.A. 105:10495-10500(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TREML2.
[15]Erratum
Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.
Proc. Natl. Acad. Sci. U.S.A. 105:14744-14744(2008)
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322 AND ASN-407.
Tissue: Liver.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF302102 mRNA. Translation: AAK15438.1.
AJ583695 mRNA. Translation: CAE47548.1.
AY358343 mRNA. Translation: AAQ88709.1.
AK074849 mRNA. Translation: BAC11243.1.
AK074997 mRNA. Translation: BAC11344.1. Different initiation.
AK075549 mRNA. Translation: BAC11692.1.
BC062581 mRNA. Translation: AAH62581.1.
CCDSCCDS10251.1. [Q5ZPR3-2]
CCDS32288.1. [Q5ZPR3-1]
RefSeqNP_001019907.1. NM_001024736.1. [Q5ZPR3-1]
NP_079516.1. NM_025240.2. [Q5ZPR3-2]
XP_005254757.1. XM_005254700.2.
UniGeneHs.744915.

3D structure databases

ProteinModelPortalQ5ZPR3.
SMRQ5ZPR3. Positions 35-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123260. 2 interactions.
IntActQ5ZPR3. 1 interaction.
MINTMINT-5000152.
STRING9606.ENSP00000320084.

PTM databases

PhosphoSiteQ5ZPR3.

Polymorphism databases

DMDM74757248.

Proteomic databases

MaxQBQ5ZPR3.
PaxDbQ5ZPR3.
PRIDEQ5ZPR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318424; ENSP00000320058; ENSG00000103855. [Q5ZPR3-2]
ENST00000318443; ENSP00000320084; ENSG00000103855. [Q5ZPR3-1]
ENST00000537340; ENSP00000441087; ENSG00000103855.
ENST00000561213; ENSP00000452736; ENSG00000103855. [Q5ZPR3-4]
ENST00000564751; ENSP00000454940; ENSG00000103855. [Q5ZPR3-2]
GeneID80381.
KEGGhsa:80381.
UCSCuc002avu.1. human. [Q5ZPR3-4]
uc002avv.1. human. [Q5ZPR3-1]
uc002avw.1. human. [Q5ZPR3-2]

Organism-specific databases

CTD80381.
GeneCardsGC15P073976.
HGNCHGNC:19137. CD276.
HPACAB017826.
HPA009285.
HPA017139.
MIM605715. gene.
neXtProtNX_Q5ZPR3.
PharmGKBPA142672148.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85729.
HOVERGENHBG079786.
InParanoidQ5ZPR3.
KOK06746.
OMAAHSSVTI.
OrthoDBEOG7FBRH9.
PhylomeDBQ5ZPR3.
TreeFamTF331083.

Gene expression databases

ArrayExpressQ5ZPR3.
BgeeQ5ZPR3.
CleanExHS_CD276.
GenevestigatorQ5ZPR3.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF08205. C2-set_2. 2 hits.
PF07686. V-set. 2 hits.
[Graphical view]
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCD276.
GenomeRNAi80381.
NextBio70980.
PROQ5ZPR3.
SOURCESearch...

Entry information

Entry nameCD276_HUMAN
AccessionPrimary (citable) accession number: Q5ZPR3
Secondary accession number(s): Q6P5Y4 expand/collapse secondary AC list , Q6UXI2, Q8NBI8, Q8NC34, Q8NCB6, Q9BXR1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries