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O14836

- TR13B_HUMAN

UniProt

O14836 - TR13B_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 13B

Gene

TNFRSF13B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. receptor activity Source: ProtInc

    GO - Biological processi

    1. B cell homeostasis Source: Ensembl
    2. cell surface receptor signaling pathway Source: ProtInc
    3. negative regulation of B cell proliferation Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    SignaLinkiO14836.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 13B
    Alternative name(s):
    Transmembrane activator and CAML interactor
    CD_antigen: CD267
    Gene namesi
    Name:TNFRSF13B
    Synonyms:TACI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:18153. TNFRSF13B.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency, common variable, 2 (CVID2) [MIM:240500]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
    Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
    VAR_024027
    Natural varianti181 – 1811A → G in CVID2. 1 Publication
    VAR_024028
    Natural varianti202 – 2021R → H in CVID2. 1 Publication
    VAR_024029
    Immunoglobulin A deficiency 2 (IGAD2) [MIM:609529]: Selective deficiency of immunoglobulin A (IGAD) is the most common form of primary immunodeficiency, with an incidence of approximately 1 in 600 individuals in the western world. Individuals with symptomatic IGAD often have deficiency of IgG subclasses or decreased antibody response to carbohydrate antigens such as pneumococcal polysaccharide vaccine. Individuals with IGAD also suffer from recurrent sinopulmonary and gastrointestinal infections and have an increased incidence of autoimmune disorders and of lymphoid and non-lymphoid malignancies. In vitro studies have suggested that some individuals with IGAD have impaired isotype class switching to IgA and others may have a post-switch defect. IGAD and CVID have been known to coexist in families. Some individuals initially present with IGAD1 and then develop CVID. These observations suggest that some cases of IGAD and CVID may have a common etiology.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
    Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
    VAR_024027

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi240500. phenotype.
    609529. phenotype.
    Orphaneti1572. Common variable immunodeficiency.
    69127. Immunoglobulin A deficiency.
    PharmGKBiPA38509.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 293293Tumor necrosis factor receptor superfamily member 13BPRO_0000058931Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 47By similarity
    Disulfide bondi50 ↔ 62By similarity
    Disulfide bondi54 ↔ 66By similarity
    Disulfide bondi71 ↔ 86
    Disulfide bondi89 ↔ 100
    Disulfide bondi93 ↔ 104
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO14836.
    PaxDbiO14836.
    PRIDEiO14836.

    PTM databases

    PhosphoSiteiO14836.

    Expressioni

    Tissue specificityi

    Highly expressed in spleen, thymus, small intestine and peripheral blood leukocytes. Expressed in resting B-cells and activated T-cells, but not in resting T-cells.

    Gene expression databases

    ArrayExpressiO14836.
    BgeeiO14836.
    CleanExiHS_TNFRSF13B.
    GenevestigatoriO14836.

    Organism-specific databases

    HPAiHPA030453.

    Interactioni

    Subunit structurei

    Binds TRAF2, TRAF5 and TRAF6. Binds the NH2-terminal domain of CAMLG with its C-terminus.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYD88Q9983612EBI-519160,EBI-447677
    TNFSF13BQ9Y2757EBI-519160,EBI-519169

    Protein-protein interaction databases

    BioGridi117046. 11 interactions.
    DIPiDIP-6224N.
    IntActiO14836. 11 interactions.
    STRINGi9606.ENSP00000261652.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi73 – 753
    Beta strandi77 – 804
    Turni81 – 844
    Beta strandi85 – 884
    Helixi89 – 924
    Helixi98 – 1003
    Helixi101 – 1044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XU1X-ray1.90R/S/T68-109[»]
    1XUTNMR-A68-109[»]
    ProteinModelPortaliO14836.
    SMRiO14836. Positions 68-109.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14836.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 165165ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini187 – 293107CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei166 – 18621Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati33 – 6735TNFR-Cys 1Add
    BLAST
    Repeati70 – 10435TNFR-Cys 2Add
    BLAST

    Sequence similaritiesi

    Contains 2 TNFR-Cys repeats.Curated

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43611.
    HOGENOMiHOG000273905.
    HOVERGENiHBG058015.
    InParanoidiO14836.
    KOiK05150.
    OMAiCHTRTTV.
    OrthoDBiEOG7W6WMN.
    PhylomeDBiO14836.
    TreeFamiTF337993.

    Family and domain databases

    InterProiIPR015384. TACI_Cys-rich-dom.
    IPR022317. TNFR_13B.
    [Graphical view]
    PfamiPF09305. TACI-CRD2. 2 hits.
    [Graphical view]
    PRINTSiPR01963. TNFACTORR13B.
    PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14836-1) [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

    MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC    50
    KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC 100
    AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL 150
    PGLKLSADQV ALVYSTLGLC LCAVLCCFLV AVACFLKKRG DPCSCQPRSR 200
    PRQSPAKSSQ DHAMEAGSPV STSPEPVETC SFCFPECRAP TQESAVTPGT 250
    PDPTCAGRWG CHTRTTVLQP CPHIPDSGLG IVCVPAQEGG PGA 293
    Length:293
    Mass (Da):31,816
    Last modified:January 1, 1998 - v1
    Checksum:i411799F3DE17A5EB
    GO
    Isoform 2 (identifier: O14836-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         21-67: FPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCR → W

    Show »
    Length:247
    Mass (Da):26,664
    Checksum:i850E1F4C2578E8E6
    GO
    Isoform 3 (identifier: O14836-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         150-176: LPGLKLSADQVALVYSTLGLCLCAVLC → PRGCPAPGTRKSFWDKENFQGEGFHLG
         177-293: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:176
    Mass (Da):19,865
    Checksum:i4506764708AF788C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561H → N Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064758
    Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
    Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
    VAR_024027
    Natural varianti181 – 1811A → G in CVID2. 1 Publication
    VAR_024028
    Natural varianti202 – 2021R → H in CVID2. 1 Publication
    VAR_024029
    Natural varianti251 – 2511P → L.1 Publication
    Corresponds to variant rs34562254 [ dbSNP | Ensembl ].
    VAR_052353

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei21 – 6747FPQGL…AAFCR → W in isoform 2. 2 PublicationsVSP_013798Add
    BLAST
    Alternative sequencei150 – 17627LPGLK…CAVLC → PRGCPAPGTRKSFWDKENFQ GEGFHLG in isoform 3. 1 PublicationVSP_054184Add
    BLAST
    Alternative sequencei177 – 293117Missing in isoform 3. 1 PublicationVSP_054185Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023614 mRNA. Translation: AAC51790.1.
    AY302137 mRNA. Translation: AAP57629.1.
    AK301032 mRNA. Translation: BAH13394.1.
    AK313302 mRNA. Translation: BAG36107.1.
    CH471196 Genomic DNA. Translation: EAW55729.1.
    BC109392 mRNA. Translation: AAI09393.1.
    CCDSiCCDS11181.1. [O14836-1]
    RefSeqiNP_036584.1. NM_012452.2. [O14836-1]
    UniGeneiHs.158341.

    Genome annotation databases

    EnsembliENST00000261652; ENSP00000261652; ENSG00000240505. [O14836-1]
    ENST00000583789; ENSP00000462952; ENSG00000240505. [O14836-2]
    GeneIDi23495.
    KEGGihsa:23495.
    UCSCiuc002gqs.1. human. [O14836-1]
    uc002gqt.1. human. [O14836-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    TNFRSF13Bbase

    TNFRSF13B mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023614 mRNA. Translation: AAC51790.1 .
    AY302137 mRNA. Translation: AAP57629.1 .
    AK301032 mRNA. Translation: BAH13394.1 .
    AK313302 mRNA. Translation: BAG36107.1 .
    CH471196 Genomic DNA. Translation: EAW55729.1 .
    BC109392 mRNA. Translation: AAI09393.1 .
    CCDSi CCDS11181.1. [O14836-1 ]
    RefSeqi NP_036584.1. NM_012452.2. [O14836-1 ]
    UniGenei Hs.158341.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XU1 X-ray 1.90 R/S/T 68-109 [» ]
    1XUT NMR - A 68-109 [» ]
    ProteinModelPortali O14836.
    SMRi O14836. Positions 68-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117046. 11 interactions.
    DIPi DIP-6224N.
    IntActi O14836. 11 interactions.
    STRINGi 9606.ENSP00000261652.

    Chemistry

    GuidetoPHARMACOLOGYi 1885.

    PTM databases

    PhosphoSitei O14836.

    Proteomic databases

    MaxQBi O14836.
    PaxDbi O14836.
    PRIDEi O14836.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261652 ; ENSP00000261652 ; ENSG00000240505 . [O14836-1 ]
    ENST00000583789 ; ENSP00000462952 ; ENSG00000240505 . [O14836-2 ]
    GeneIDi 23495.
    KEGGi hsa:23495.
    UCSCi uc002gqs.1. human. [O14836-1 ]
    uc002gqt.1. human. [O14836-2 ]

    Organism-specific databases

    CTDi 23495.
    GeneCardsi GC17M016832.
    GeneReviewsi TNFRSF13B.
    H-InvDB HIX0173687.
    HGNCi HGNC:18153. TNFRSF13B.
    HPAi HPA030453.
    MIMi 240500. phenotype.
    604907. gene.
    609529. phenotype.
    neXtProti NX_O14836.
    Orphaneti 1572. Common variable immunodeficiency.
    69127. Immunoglobulin A deficiency.
    PharmGKBi PA38509.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43611.
    HOGENOMi HOG000273905.
    HOVERGENi HBG058015.
    InParanoidi O14836.
    KOi K05150.
    OMAi CHTRTTV.
    OrthoDBi EOG7W6WMN.
    PhylomeDBi O14836.
    TreeFami TF337993.

    Enzyme and pathway databases

    SignaLinki O14836.

    Miscellaneous databases

    ChiTaRSi TNFRSF13B. human.
    EvolutionaryTracei O14836.
    GeneWikii TNFRSF13B.
    GenomeRNAii 23495.
    NextBioi 35480074.
    PROi O14836.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14836.
    Bgeei O14836.
    CleanExi HS_TNFRSF13B.
    Genevestigatori O14836.

    Family and domain databases

    InterProi IPR015384. TACI_Cys-rich-dom.
    IPR022317. TNFR_13B.
    [Graphical view ]
    Pfami PF09305. TACI-CRD2. 2 hits.
    [Graphical view ]
    PRINTSi PR01963. TNFACTORR13B.
    PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily."
      von Buelow G.-U., Bram R.J.
      Science 278:138-141(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: B-cell.
    2. Zhou G., Ke R., Li H., Zheng G., Shen C., Lin L., Yang S.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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 AND 3), VARIANT LEU-251.
      Tissue: Spleen.
    4. 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).
    6. "Tumor necrosis factor (TNF) receptor superfamily member TACI is a high affinity receptor for TNF family members APRIL and BLyS."
      Wu Y., Bressette D., Carrell J.A., Kaufman T., Feng P., Taylor K., Gan Y., Cho Y.H., Garcia A.D., Gollatz E., Dimke D., LaFleur D., Migone T.S., Nardelli B., Wei P., Ruben S.M., Ullrich S.J., Olsen H.S.
      , Kanakaraj P., Moore P.A., Baker K.P.
      J. Biol. Chem. 275:35478-35485(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: FUNCTION.
    8. "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation."
      Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M., Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R., Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J.
      , Delaney J., Meng S.-Y., Boyle W.J., Hsu H.
      J. Exp. Med. 192:137-143(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2 AND TRAF5.
    9. "Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding."
      Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J., Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F., Starovasnik M.A.
      J. Biol. Chem. 280:7218-7227(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 68-109 IN COMPLEX WITH MOUSE TNFSF13, STRUCTURE BY NMR OF 68-109.
    10. "TACI is mutant in common variable immunodeficiency and IgA deficiency."
      Castigli E., Wilson S.A., Garibyan L., Rachid R., Bonilla F., Schneider L., Geha R.S.
      Nat. Genet. 37:829-834(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IGAD2 ARG-104, VARIANTS CVID2 ARG-104; GLY-181 AND HIS-202.
    11. Cited for: VARIANT ASN-56.

    Entry informationi

    Entry nameiTR13B_HUMAN
    AccessioniPrimary (citable) accession number: O14836
    Secondary accession number(s): B2R8B0
    , B7Z6V8, Q32LX4, Q7Z6F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 17
      Human chromosome 17: 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