Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00481

- BT3A1_HUMAN

UniProt

O00481 - BT3A1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 - 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 254225ExtracellularSequence AnalysisAdd
BLAST
Transmembranei255 – 27117HelicalSequence AnalysisAdd
BLAST
Topological domaini272 – 513242CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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...)1 Publication
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

BgeeiO00481.
CleanExiHS_BTN3A1.
ExpressionAtlasiO00481. baseline and differential.
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. 4 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 – 343Combined sources
Beta strandi40 – 434Combined sources
Beta strandi48 – 569Combined sources
Beta strandi63 – 697Combined sources
Turni70 – 734Combined sources
Beta strandi74 – 807Combined sources
Helixi86 – 883Combined sources
Helixi91 – 933Combined sources
Beta strandi96 – 1005Combined sources
Helixi104 – 1063Combined sources
Beta strandi108 – 1158Combined sources
Helixi118 – 1203Combined sources
Beta strandi122 – 1309Combined sources
Beta strandi133 – 14311Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi161 – 17313Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi218 – 2247Combined sources
Turni225 – 2284Combined sources
Beta strandi229 – 2357Combined sources
Turni239 – 2413Combined sources
Helixi328 – 3369Combined sources
Beta strandi337 – 3393Combined sources
Helixi346 – 3483Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi359 – 3646Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 3875Combined sources
Beta strandi390 – 40011Combined sources
Beta strandi407 – 4137Combined sources
Helixi426 – 4283Combined sources
Beta strandi430 – 4367Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 4434Combined sources
Beta strandi458 – 4658Combined sources
Turni466 – 4694Combined sources
Beta strandi470 – 4756Combined sources
Turni476 – 4783Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi508 – 5103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 328-513.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118933.
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.
IPR013320. ConA-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR006574. PRY.
IPR003877. SPRY_dom.
[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

        10         20         30         40         50
MKMASFLAFL LLNFRVCLLL LQLLMPHSAQ FSVLGPSGPI LAMVGEDADL
60 70 80 90 100
PCHLFPTMSA ETMELKWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL
110 120 130 140 150
RDGITAGKAA LRIHNVTASD SGKYLCYFQD GDFYEKALVE LKVAALGSDL
160 170 180 190 200
HVDVKGYKDG GIHLECRSTG WYPQPQIQWS NNKGENIPTV EAPVVADGVG
210 220 230 240 250
LYAVAASVIM RGSSGEGVSC TIRSSLLGLE KTASISIADP FFRSAQRWIA
260 270 280 290 300
ALAGTLPVLL LLLGGAGYFL WQQQEEKKTQ FRKKKREQEL REMAWSTMKQ
310 320 330 340 350
EQSTRVKLLE ELRWRSIQYA SRGERHSAYN EWKKALFKPA DVILDPKTAN
360 370 380 390 400
PILLVSEDQR SVQRAKEPQD LPDNPERFNW HYCVLGCESF ISGRHYWEVE
410 420 430 440 450
VGDRKEWHIG VCSKNVQRKG WVKMTPENGF WTMGLTDGNK YRTLTEPRTN
460 470 480 490 500
LKLPKPPKKV GVFLDYETGD ISFYNAVDGS HIHTFLDVSF SEALYPVFRI
510
LTLEPTALTI CPA
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 328-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116294. 4 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.
GeneTreei ENSGT00760000118933.
HOGENOMi HOG000230860.
HOVERGENi HBG050747.
InParanoidi O00481.
KOi K06712.
OMAi NVQRKGW.
OrthoDBi EOG73804F.
PhylomeDBi O00481.
TreeFami TF331083.

Miscellaneous databases

ChiTaRSi BTN3A1. human.
GeneWikii Butyrophilin,_subfamily_3,_member_A1.
GenomeRNAii 11119.
NextBioi 42260.
PROi O00481.
SOURCEi Search...

Gene expression databases

Bgeei O00481.
CleanExi HS_BTN3A1.
ExpressionAtlasi O00481. baseline and differential.
Genevestigatori O00481.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013162. CD80_C2-set.
IPR013320. ConA-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR006574. PRY.
IPR003877. SPRY_dom.
[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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 132 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