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O00481

- BT3A1_HUMAN

UniProt

O00481 - BT3A1_HUMAN

Protein

Butyrophilin subfamily 3 member A1

Gene

BTN3A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (31 Oct 2006)
      Previous versions | rss
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    Functioni

    Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.4 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. activated T cell proliferation Source: UniProtKB
    2. cytokine secretion Source: UniProtKB
    3. interferon-gamma secretion Source: UniProtKB
    4. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Butyrophilin subfamily 3 member A1
    Alternative name(s):
    CD_antigen: CD277
    Gene namesi
    Name:BTN3A1
    Synonyms:BTF5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:1138. BTN3A1.

    Subcellular locationi

    Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25459.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 513484Butyrophilin subfamily 3 member A1PRO_0000014532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 1261 PublicationPROSITE-ProRule annotation
    Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
    Disulfide bondi166 ↔ 2201 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO00481.
    PaxDbiO00481.
    PRIDEiO00481.

    PTM databases

    PhosphoSiteiO00481.

    Expressioni

    Tissue specificityi

    Detected on T-cells, natural killer cells, dendritic cells and macrophages (at protein level). Ubiquitous. Highly expressed in heart, pancreas and lung, Moderately expressed in placenta, liver and muscle.4 Publications

    Gene expression databases

    ArrayExpressiO00481.
    BgeeiO00481.
    CleanExiHS_BTN3A1.
    GenevestigatoriO00481.

    Organism-specific databases

    HPAiHPA012565.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFF1P041553EBI-2809309,EBI-743871

    Protein-protein interaction databases

    BioGridi116294. 2 interactions.
    IntActiO00481. 2 interactions.
    STRINGi9606.ENSP00000289361.

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 343
    Beta strandi40 – 434
    Beta strandi48 – 569
    Beta strandi63 – 697
    Turni70 – 734
    Beta strandi74 – 807
    Helixi86 – 883
    Helixi91 – 933
    Beta strandi96 – 1005
    Helixi104 – 1063
    Beta strandi108 – 1158
    Helixi118 – 1203
    Beta strandi122 – 1309
    Beta strandi133 – 14311
    Beta strandi151 – 1588
    Beta strandi161 – 17313
    Beta strandi176 – 1805
    Beta strandi202 – 2109
    Beta strandi218 – 2247
    Turni225 – 2284
    Beta strandi229 – 2357
    Turni239 – 2413
    Helixi328 – 3369
    Beta strandi337 – 3393
    Helixi346 – 3483
    Beta strandi353 – 3553
    Beta strandi359 – 3646
    Beta strandi379 – 3813
    Beta strandi383 – 3875
    Beta strandi390 – 40011
    Beta strandi407 – 4137
    Helixi426 – 4283
    Beta strandi430 – 4367
    Turni437 – 4393
    Beta strandi440 – 4434
    Beta strandi458 – 4658
    Turni466 – 4694
    Beta strandi470 – 4756
    Turni476 – 4783
    Beta strandi481 – 4855
    Beta strandi494 – 4996
    Beta strandi508 – 5103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F80X-ray1.94A30-246[»]
    4F9LX-ray3.14A/B30-246[»]
    4F9PX-ray3.52A/B30-246[»]
    4JKWX-ray2.01A28-143[»]
    4K55X-ray1.91A28-143[»]
    4N7IX-ray1.40A328-513[»]
    4N7UX-ray1.46A328-513[»]
    ProteinModelPortaliO00481.
    SMRiO00481. Positions 30-243, 342-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 254225ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini272 – 513242CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei255 – 27117HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 139110Ig-like V-type 1Add
    BLAST
    Domaini145 – 23692Ig-like V-type 2Add
    BLAST
    Domaini322 – 513192B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG326834.
    HOGENOMiHOG000230860.
    HOVERGENiHBG050747.
    InParanoidiO00481.
    KOiK06712.
    OMAiNVQRKGW.
    OrthoDBiEOG73804F.
    PhylomeDBiO00481.
    TreeFamiTF331083.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR013162. CD80_C2-set.
    IPR008985. ConA-like_lec_gl_sf.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PfamiPF08205. C2-set_2. 1 hit.
    PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    PRINTSiPR01407. BUTYPHLNCDUF.
    SMARTiSM00409. IG. 1 hit.
    SM00589. PRY. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50835. IG_LIKE. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00481-1) [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

    MKMASFLAFL LLNFRVCLLL LQLLMPHSAQ FSVLGPSGPI LAMVGEDADL    50
    PCHLFPTMSA ETMELKWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL 100
    RDGITAGKAA LRIHNVTASD SGKYLCYFQD GDFYEKALVE LKVAALGSDL 150
    HVDVKGYKDG GIHLECRSTG WYPQPQIQWS NNKGENIPTV EAPVVADGVG 200
    LYAVAASVIM RGSSGEGVSC TIRSSLLGLE KTASISIADP FFRSAQRWIA 250
    ALAGTLPVLL LLLGGAGYFL WQQQEEKKTQ FRKKKREQEL REMAWSTMKQ 300
    EQSTRVKLLE ELRWRSIQYA SRGERHSAYN EWKKALFKPA DVILDPKTAN 350
    PILLVSEDQR SVQRAKEPQD LPDNPERFNW HYCVLGCESF ISGRHYWEVE 400
    VGDRKEWHIG VCSKNVQRKG WVKMTPENGF WTMGLTDGNK YRTLTEPRTN 450
    LKLPKPPKKV GVFLDYETGD ISFYNAVDGS HIHTFLDVSF SEALYPVFRI 500
    LTLEPTALTI CPA 513
    Length:513
    Mass (Da):57,677
    Last modified:October 31, 2006 - v3
    Checksum:i8D834D70526D1F6F
    GO
    Isoform 2 (identifier: O00481-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         340-352: ADVILDPKTANPI → GEEMLQMRLHFVK
         353-513: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:352
    Mass (Da):39,397
    Checksum:i274CA3723C653772
    GO
    Isoform 3 (identifier: O00481-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         340-513: ADVILDPKTA...EPTALTICPA → GPPIGQTQQQ...SWGPEEGGES

    Note: No experimental confirmation available.

    Show »
    Length:378
    Mass (Da):41,819
    Checksum:i274B31308FA9B73D
    GO
    Isoform 4 (identifier: O00481-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-194: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:461
    Mass (Da):52,019
    Checksum:i72FE04DA9664783D
    GO

    Sequence cautioni

    The sequence CAA69164.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131N → S in BAG58563. (PubMed:14702039)Curated
    Sequence conflicti25 – 251M → T in BAD97194. 1 PublicationCurated
    Sequence conflicti46 – 461E → K in BAG61334. (PubMed:14702039)Curated
    Sequence conflicti111 – 1111L → F in CAA69164. (PubMed:9382921)Curated
    Sequence conflicti118 – 1181A → G in CAA69164. (PubMed:9382921)Curated
    Sequence conflicti121 – 1222SG → RW in CAA69164. (PubMed:9382921)Curated
    Sequence conflicti130 – 1301D → G in BAG58563. (PubMed:14702039)Curated
    Sequence conflicti239 – 2391D → R in CAA69164. (PubMed:9382921)Curated
    Sequence conflicti254 – 2541G → R in AAB53430. (PubMed:9149941)Curated
    Sequence conflicti509 – 5091T → S in AAB53430. (PubMed:9149941)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → H.1 Publication
    Corresponds to variant rs56161420 [ dbSNP | Ensembl ].
    VAR_061305
    Natural varianti224 – 2241S → N.1 Publication
    Corresponds to variant rs1057933 [ dbSNP | Ensembl ].
    VAR_021170
    Natural varianti282 – 2821R → T.1 Publication
    Corresponds to variant rs41266839 [ dbSNP | Ensembl ].
    VAR_061306
    Natural varianti456 – 4561P → T.1 Publication
    Corresponds to variant rs4712990 [ dbSNP | Ensembl ].
    VAR_028788

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 19452Missing in isoform 4. 1 PublicationVSP_045062Add
    BLAST
    Alternative sequencei340 – 513174ADVIL…TICPA → GPPIGQTQQQTRGQGSPVAL SQESAQRTDSWGPEEGGES in isoform 3. 1 PublicationVSP_042034Add
    BLAST
    Alternative sequencei340 – 35213ADVIL…TANPI → GEEMLQMRLHFVK in isoform 2. 1 PublicationVSP_012714Add
    BLAST
    Alternative sequencei353 – 513161Missing in isoform 2. 1 PublicationVSP_012715Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07827 mRNA. Translation: CAA69164.1. Different initiation.
    U90552 mRNA. Translation: AAB53430.1.
    AK223474 mRNA. Translation: BAD97194.1.
    AK290193 mRNA. Translation: BAF82882.1.
    AK295720 mRNA. Translation: BAG58563.1.
    AK299327 mRNA. Translation: BAG61334.1.
    AL021917 Genomic DNA. Translation: CAC03424.3.
    AL021917 Genomic DNA. Translation: CAM28245.1.
    CH471087 Genomic DNA. Translation: EAW55566.1.
    CH471087 Genomic DNA. Translation: EAW55567.1.
    BC118586 mRNA. Translation: AAI18587.1.
    BC121800 mRNA. Translation: AAI21801.1.
    CCDSiCCDS4608.1. [O00481-1]
    CCDS4609.1. [O00481-2]
    CCDS47388.1. [O00481-4]
    CCDS47389.1. [O00481-3]
    RefSeqiNP_001138480.1. NM_001145008.1. [O00481-4]
    NP_001138481.1. NM_001145009.1. [O00481-3]
    NP_008979.3. NM_007048.5. [O00481-1]
    NP_919423.1. NM_194441.2. [O00481-2]
    XP_005248891.1. XM_005248834.2. [O00481-2]
    UniGeneiHs.191510.

    Genome annotation databases

    EnsembliENST00000289361; ENSP00000289361; ENSG00000026950. [O00481-1]
    ENST00000414912; ENSP00000406667; ENSG00000026950. [O00481-4]
    ENST00000425234; ENSP00000396684; ENSG00000026950. [O00481-3]
    ENST00000476549; ENSP00000420010; ENSG00000026950. [O00481-2]
    GeneIDi11119.
    KEGGihsa:11119.
    UCSCiuc003nhv.3. human. [O00481-1]
    uc010jqj.3. human. [O00481-2]
    uc011dkj.2. human. [O00481-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07827 mRNA. Translation: CAA69164.1 . Different initiation.
    U90552 mRNA. Translation: AAB53430.1 .
    AK223474 mRNA. Translation: BAD97194.1 .
    AK290193 mRNA. Translation: BAF82882.1 .
    AK295720 mRNA. Translation: BAG58563.1 .
    AK299327 mRNA. Translation: BAG61334.1 .
    AL021917 Genomic DNA. Translation: CAC03424.3 .
    AL021917 Genomic DNA. Translation: CAM28245.1 .
    CH471087 Genomic DNA. Translation: EAW55566.1 .
    CH471087 Genomic DNA. Translation: EAW55567.1 .
    BC118586 mRNA. Translation: AAI18587.1 .
    BC121800 mRNA. Translation: AAI21801.1 .
    CCDSi CCDS4608.1. [O00481-1 ]
    CCDS4609.1. [O00481-2 ]
    CCDS47388.1. [O00481-4 ]
    CCDS47389.1. [O00481-3 ]
    RefSeqi NP_001138480.1. NM_001145008.1. [O00481-4 ]
    NP_001138481.1. NM_001145009.1. [O00481-3 ]
    NP_008979.3. NM_007048.5. [O00481-1 ]
    NP_919423.1. NM_194441.2. [O00481-2 ]
    XP_005248891.1. XM_005248834.2. [O00481-2 ]
    UniGenei Hs.191510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F80 X-ray 1.94 A 30-246 [» ]
    4F9L X-ray 3.14 A/B 30-246 [» ]
    4F9P X-ray 3.52 A/B 30-246 [» ]
    4JKW X-ray 2.01 A 28-143 [» ]
    4K55 X-ray 1.91 A 28-143 [» ]
    4N7I X-ray 1.40 A 328-513 [» ]
    4N7U X-ray 1.46 A 328-513 [» ]
    ProteinModelPortali O00481.
    SMRi O00481. Positions 30-243, 342-498.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116294. 2 interactions.
    IntActi O00481. 2 interactions.
    STRINGi 9606.ENSP00000289361.

    PTM databases

    PhosphoSitei O00481.

    Proteomic databases

    MaxQBi O00481.
    PaxDbi O00481.
    PRIDEi O00481.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000289361 ; ENSP00000289361 ; ENSG00000026950 . [O00481-1 ]
    ENST00000414912 ; ENSP00000406667 ; ENSG00000026950 . [O00481-4 ]
    ENST00000425234 ; ENSP00000396684 ; ENSG00000026950 . [O00481-3 ]
    ENST00000476549 ; ENSP00000420010 ; ENSG00000026950 . [O00481-2 ]
    GeneIDi 11119.
    KEGGi hsa:11119.
    UCSCi uc003nhv.3. human. [O00481-1 ]
    uc010jqj.3. human. [O00481-2 ]
    uc011dkj.2. human. [O00481-3 ]

    Organism-specific databases

    CTDi 11119.
    GeneCardsi GC06P026402.
    HGNCi HGNC:1138. BTN3A1.
    HPAi HPA012565.
    MIMi 613593. gene.
    neXtProti NX_O00481.
    PharmGKBi PA25459.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326834.
    HOGENOMi HOG000230860.
    HOVERGENi HBG050747.
    InParanoidi O00481.
    KOi K06712.
    OMAi NVQRKGW.
    OrthoDBi EOG73804F.
    PhylomeDBi O00481.
    TreeFami TF331083.

    Miscellaneous databases

    GeneWikii Butyrophilin,_subfamily_3,_member_A1.
    GenomeRNAii 11119.
    NextBioi 42260.
    PROi O00481.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00481.
    Bgeei O00481.
    CleanExi HS_BTN3A1.
    Genevestigatori O00481.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR013162. CD80_C2-set.
    IPR008985. ConA-like_lec_gl_sf.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    Pfami PF08205. C2-set_2. 1 hit.
    PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00409. IG. 1 hit.
    SM00589. PRY. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, localization, and structure of new members of the butyrophilin gene family in the juxta-telomeric region of the major histocompatibility complex."
      Tazi-Ahnini R., Henry J., Offer C., Bouissou-Bouchouata C., Mather I.H., Pontarotti P.
      Immunogenetics 47:55-63(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASN-224.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "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] (ISOFORMS 1; 3 AND 4), VARIANTS HIS-15 AND THR-282.
      Tissue: Hippocampus and Thalamus.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Synovium.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1), VARIANT THR-456.
    8. "Stimulation of human butyrophilin 3 molecules results in negative regulation of cellular immunity."
      Yamashiro H., Yoshizaki S., Tadaki T., Egawa K., Seo N.
      J. Leukoc. Biol. 88:757-767(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, TISSUE SPECIFICITY.
    9. "CD277 is a negative co-stimulatory molecule universally expressed by ovarian cancer microenvironmental cells."
      Cubillos-Ruiz J.R., Martinez D., Scarlett U.K., Rutkowski M.R., Nesbeth Y.C., Camposeco-Jacobs A.L., Conejo-Garcia J.R.
      Oncotarget 1:329-338(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing by a major human gammadelta T-cell subset."
      Harly C., Guillaume Y., Nedellec S., Peigne C.M., Monkkonen H., Monkkonen J., Li J., Kuball J., Adams E.J., Netzer S., Dechanet-Merville J., Leger A., Herrmann T., Breathnach R., Olive D., Bonneville M., Scotet E.
      Blood 120:2269-2279(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "The molecular basis for modulation of human Vgamma9Vdelta2 T cell responses by CD277/butyrophilin-3 (BTN3A)-specific antibodies."
      Palakodeti A., Sandstrom A., Sundaresan L., Harly C., Nedellec S., Olive D., Scotet E., Bonneville M., Adams E.J.
      J. Biol. Chem. 287:32780-32790(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 30-246, FUNCTION, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-115.

    Entry informationi

    Entry nameiBT3A1_HUMAN
    AccessioniPrimary (citable) accession number: O00481
    Secondary accession number(s): A2A278
    , A8K2C8, B4DIQ1, B4DRM2, E9PGB4, E9PHG8, Q0P515, Q147X5, Q53F15, Q99420, Q9HCY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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 6
      Human chromosome 6: 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