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Q7Z6A9

- BTLA_HUMAN

UniProt

Q7Z6A9 - BTLA_HUMAN

Protein

B- and T-lymphocyte attenuator

Gene

BTLA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.1 Publication

    GO - Molecular functioni

    1. receptor activity Source: Ensembl

    GO - Biological processi

    1. immune response-regulating cell surface receptor signaling pathway Source: Ensembl
    2. negative regulation of alpha-beta T cell proliferation Source: Ensembl
    3. negative regulation of B cell proliferation Source: Ensembl
    4. T cell costimulation Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_19344. Costimulation by the CD28 family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B- and T-lymphocyte attenuator
    Alternative name(s):
    B- and T-lymphocyte-associated protein
    CD_antigen: CD272
    Gene namesi
    Name:BTLA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:21087. BTLA.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of plasma membrane Source: Ensembl
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi226 – 2261Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-257 and/or F-282. 2 Publications
    Mutagenesisi257 – 2571Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-282. 2 Publications
    Mutagenesisi282 – 2821Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-257. 2 Publications

    Organism-specific databases

    PharmGKBiPA134968341.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 289259B- and T-lymphocyte attenuatorPRO_0000014523Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 631 PublicationPROSITE-ProRule annotation
    Disulfide bondi58 ↔ 1151 PublicationPROSITE-ProRule annotation
    Disulfide bondi72 ↔ 791 PublicationPROSITE-ProRule annotation
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11.1 Publication
    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ7Z6A9.
    PRIDEiQ7Z6A9.

    PTM databases

    PhosphoSiteiQ7Z6A9.

    Expressioni

    Gene expression databases

    BgeeiQ7Z6A9.
    CleanExiHS_BTLA.
    GenevestigatoriQ7Z6A9.

    Organism-specific databases

    HPAiHPA047211.

    Interactioni

    Subunit structurei

    Interacts with tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. Interacts with TNFRSF14/HVEM.4 Publications

    Protein-protein interaction databases

    BioGridi127411. 2 interactions.
    DIPiDIP-48795N.
    IntActiQ7Z6A9. 3 interactions.
    MINTiMINT-8020099.
    STRINGi9606.ENSP00000333919.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 496
    Beta strandi54 – 618
    Beta strandi63 – 653
    Beta strandi68 – 747
    Beta strandi79 – 813
    Beta strandi87 – 915
    Beta strandi96 – 1049
    Helixi107 – 1093
    Beta strandi111 – 1199
    Beta strandi122 – 1254
    Beta strandi129 – 1346

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AW2X-ray2.80A/X26-137[»]
    ProteinModelPortaliQ7Z6A9.
    SMRiQ7Z6A9. Positions 34-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z6A9.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 157127ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini179 – 289111CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei158 – 17821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 132102Ig-like V-typeAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42530.
    HOGENOMiHOG000168895.
    HOVERGENiHBG080937.
    InParanoidiQ7Z6A9.
    KOiK06707.
    OMAiAAICVRS.
    OrthoDBiEOG7F513T.
    PhylomeDBiQ7Z6A9.
    TreeFamiTF337694.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z6A9-1) [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

    MKTLPAMLGT GKLFWVFFLI PYLDIWNIHG KESCDVQLYI KRQSEHSILA    50
    GDPFELECPV KYCANRPHVT WCKLNGTTCV KLEDRQTSWK EEKNISFFIL 100
    HFEPVLPNDN GSYRCSANFQ SNLIESHSTT LYVTDVKSAS ERPSKDEMAS 150
    RPWLLYRLLP LGGLPLLITT CFCLFCCLRR HQGKQNELSD TAGREINLVD 200
    AHLKSEQTEA STRQNSQVLL SETGIYDNDP DLCFRMQEGS EVYSNPCLEE 250
    NKPGIVYASL NHSVIGPNSR LARNVKEAPT EYASICVRS 289
    Length:289
    Mass (Da):32,834
    Last modified:May 18, 2010 - v3
    Checksum:iF4D1FF775D7D33F3
    GO
    Isoform 2 (identifier: Q7Z6A9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         135-182: Missing.

    Show »
    Length:241
    Mass (Da):27,317
    Checksum:i991AFF2495C3F612
    GO

    Sequence cautioni

    The sequence BAD18396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051V → M in AAP44003. (PubMed:12796776)Curated
    Sequence conflicti138 – 1381S → G in AAP44003. (PubMed:12796776)Curated
    Sequence conflicti148 – 1481M → V in AAP44003. (PubMed:12796776)Curated
    Sequence conflicti171 – 1711C → W in AAP44003. (PubMed:12796776)Curated
    Sequence conflicti219 – 2191L → P in BAD18396. (PubMed:14702039)Curated
    Sequence conflicti223 – 2231T → A in AAP44003. (PubMed:12796776)Curated
    Sequence conflicti243 – 2431Y → C in AAP44003. (PubMed:12796776)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241I → V.
    Corresponds to variant rs16859633 [ dbSNP | Ensembl ].
    VAR_056027
    Natural varianti157 – 1571R → S.3 Publications
    Corresponds to variant rs2931761 [ dbSNP | Ensembl ].
    VAR_027607
    Natural varianti267 – 2671P → L.5 Publications
    Corresponds to variant rs9288952 [ dbSNP | Ensembl ].
    VAR_027608

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei135 – 18248Missing in isoform 2. 3 PublicationsVSP_040305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY293286 mRNA. Translation: AAP44003.1.
    AY599411 mRNA. Translation: AAT44901.1.
    DQ198368 mRNA. Translation: ABA54407.1.
    AC092894 Genomic DNA. No translation available.
    BC107091 mRNA. Translation: AAI07092.1.
    BC107092 mRNA. Translation: AAI07093.1.
    AK131204 mRNA. Translation: BAD18396.1. Different initiation.
    CCDSiCCDS33819.1. [Q7Z6A9-1]
    CCDS43130.1. [Q7Z6A9-2]
    RefSeqiNP_001078826.1. NM_001085357.1. [Q7Z6A9-2]
    NP_861445.3. NM_181780.3.
    XP_005247193.1. XM_005247136.2. [Q7Z6A9-1]
    UniGeneiHs.445162.

    Genome annotation databases

    EnsembliENST00000334529; ENSP00000333919; ENSG00000186265. [Q7Z6A9-1]
    ENST00000383680; ENSP00000373178; ENSG00000186265. [Q7Z6A9-2]
    GeneIDi151888.
    KEGGihsa:151888.
    UCSCiuc003dza.4. human. [Q7Z6A9-1]
    uc003dzb.4. human. [Q7Z6A9-2]

    Polymorphism databases

    DMDMi296439425.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY293286 mRNA. Translation: AAP44003.1 .
    AY599411 mRNA. Translation: AAT44901.1 .
    DQ198368 mRNA. Translation: ABA54407.1 .
    AC092894 Genomic DNA. No translation available.
    BC107091 mRNA. Translation: AAI07092.1 .
    BC107092 mRNA. Translation: AAI07093.1 .
    AK131204 mRNA. Translation: BAD18396.1 . Different initiation.
    CCDSi CCDS33819.1. [Q7Z6A9-1 ]
    CCDS43130.1. [Q7Z6A9-2 ]
    RefSeqi NP_001078826.1. NM_001085357.1. [Q7Z6A9-2 ]
    NP_861445.3. NM_181780.3.
    XP_005247193.1. XM_005247136.2. [Q7Z6A9-1 ]
    UniGenei Hs.445162.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AW2 X-ray 2.80 A/X 26-137 [» ]
    ProteinModelPortali Q7Z6A9.
    SMRi Q7Z6A9. Positions 34-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127411. 2 interactions.
    DIPi DIP-48795N.
    IntActi Q7Z6A9. 3 interactions.
    MINTi MINT-8020099.
    STRINGi 9606.ENSP00000333919.

    PTM databases

    PhosphoSitei Q7Z6A9.

    Polymorphism databases

    DMDMi 296439425.

    Proteomic databases

    PaxDbi Q7Z6A9.
    PRIDEi Q7Z6A9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334529 ; ENSP00000333919 ; ENSG00000186265 . [Q7Z6A9-1 ]
    ENST00000383680 ; ENSP00000373178 ; ENSG00000186265 . [Q7Z6A9-2 ]
    GeneIDi 151888.
    KEGGi hsa:151888.
    UCSCi uc003dza.4. human. [Q7Z6A9-1 ]
    uc003dzb.4. human. [Q7Z6A9-2 ]

    Organism-specific databases

    CTDi 151888.
    GeneCardsi GC03M112182.
    HGNCi HGNC:21087. BTLA.
    HPAi HPA047211.
    MIMi 607925. gene.
    neXtProti NX_Q7Z6A9.
    PharmGKBi PA134968341.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42530.
    HOGENOMi HOG000168895.
    HOVERGENi HBG080937.
    InParanoidi Q7Z6A9.
    KOi K06707.
    OMAi AAICVRS.
    OrthoDBi EOG7F513T.
    PhylomeDBi Q7Z6A9.
    TreeFami TF337694.

    Enzyme and pathway databases

    Reactomei REACT_19344. Costimulation by the CD28 family.

    Miscellaneous databases

    EvolutionaryTracei Q7Z6A9.
    GeneWikii BTLA.
    GenomeRNAii 151888.
    NextBioi 86817.
    PROi Q7Z6A9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7Z6A9.
    CleanExi HS_BTLA.
    Genevestigatori Q7Z6A9.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF TYR-226; TYR-257 AND TYR-282, GLYCOSYLATION, FUNCTION, INTERACTION WITH PTPN6 AND PTPN11, VARIANTS SER-157 AND LEU-267.
    2. "Point mutations in the BTLA gene in multiple myeloma and other hematologic malignancies."
      Mao Y., Wang X., Wu H., Chen Y., Ge Y., Chen J., Zhang X.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-267.
    3. "Human BTLA mRNA alternate splice transcript lacking transmembrane encoding region."
      Oaks M.K., Tector M.F., Mewissen G.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-267.
      Tissue: Peripheral blood.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-289 (ISOFORM 1), VARIANTS SER-157 AND LEU-267.
    6. "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] OF 4-289 (ISOFORM 1), VARIANTS SER-157 AND LEU-267.
      Tissue: Trachea.
    7. "Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2."
      Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., Murphy K.M.
      Biochem. Biophys. Res. Commun. 312:1236-1243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-226; TYR-257 AND TYR-282, INTERACTION WITH PTPN6 AND PTPN11.
    8. "B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator."
      Sedy J.R., Gavrieli M., Potter K.G., Hurchla M.A., Lindsley R.C., Hildner K., Scheu S., Pfeffer K., Ware C.F., Murphy T.L., Murphy K.M.
      Nat. Immunol. 6:90-98(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14, PHOSPHORYLATION.
    9. "Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex."
      Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D., Hymowitz S.G.
      J. Biol. Chem. 280:39553-39561(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH TNFRSF14, DISULFIDE BONDS.

    Entry informationi

    Entry nameiBTLA_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z6A9
    Secondary accession number(s): Q3B831, Q3HS85, Q6ZNH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 105 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 3
      Human chromosome 3: 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