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P16150

- LEUK_HUMAN

UniProt

P16150 - LEUK_HUMAN

Protein

Leukosialin

Gene

SPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    One of the major glycoproteins of thymocytes and T lymphocytes. Plays a role in the physicochemical properties of the T-cell surface and in lectin binding. Presents carbohydrate ligands to selectins. Has an extended rodlike structure that could protrude above the glycocalyx of the cell and allow multiple glycan chains to be accessible for binding. Is a counter-receptor for SN/Siglec-1 By similarity. During T-cell activation is actively removed from the T-cell-APC (antigen-presenting cell) contact site thus suggesting a negative regulatory role in adaptive immune response By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: MTBBASE
    2. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. apoptotic signaling pathway Source: Ensembl
    2. blood coagulation Source: Reactome
    3. cell surface receptor signaling pathway Source: Ensembl
    4. cellular defense response Source: ProtInc
    5. chemotaxis Source: ProtInc
    6. defense response to bacterium Source: MGI
    7. establishment or maintenance of cell polarity Source: ProtInc
    8. immune response Source: ProtInc
    9. leukocyte migration Source: Reactome
    10. negative regulation of cell adhesion Source: ProtInc
    11. negative regulation of T cell proliferation Source: Ensembl
    12. negative regulation of type IV hypersensitivity Source: Ensembl
    13. negative thymic T cell selection Source: Ensembl
    14. positive regulation of T cell proliferation Source: Ensembl
    15. positive regulation of tumor necrosis factor biosynthetic process Source: MGI
    16. regulation of defense response to virus Source: Ensembl
    17. response to protozoan Source: Ensembl
    18. signal transduction Source: ProtInc
    19. T cell costimulation Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    REACT_12560. Basigin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leukosialin
    Alternative name(s):
    Galactoglycoprotein
    Short name:
    GALGP
    Leukocyte sialoglycoprotein
    Sialophorin
    CD_antigen: CD43
    Gene namesi
    Name:SPN
    Synonyms:CD43
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11249. SPN.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. cell surface Source: UniProtKB
    3. external side of plasma membrane Source: Ensembl
    4. extracellular space Source: MGI
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of plasma membrane Source: ProtInc
    7. membrane Source: UniProtKB
    8. plasma membrane Source: Reactome
    9. uropod Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36079.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 400381LeukosialinPRO_0000021588Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211O-linked (GalNAc...)1 Publication
    Glycosylationi22 – 221O-linked (GalNAc...)1 Publication
    Glycosylationi26 – 261O-linked (GalNAc...)1 Publication
    Glycosylationi28 – 281O-linked (GalNAc...)1 Publication
    Glycosylationi29 – 291O-linked (GalNAc...)1 Publication
    Glycosylationi35 – 351O-linked (GalNAc...)1 Publication
    Glycosylationi36 – 361O-linked (GalNAc...)1 Publication
    Glycosylationi37 – 371O-linked (GalNAc...)1 Publication
    Glycosylationi41 – 411O-linked (GalNAc...)1 Publication
    Glycosylationi42 – 421O-linked (GalNAc...)1 Publication
    Glycosylationi46 – 461O-linked (GalNAc...)1 Publication
    Glycosylationi47 – 471O-linked (GalNAc...)1 Publication
    Glycosylationi48 – 481O-linked (GalNAc...)1 Publication
    Glycosylationi50 – 501O-linked (GalNAc...)1 Publication
    Glycosylationi58 – 581O-linked (GalNAc...)1 Publication
    Glycosylationi69 – 691O-linked (GalNAc...)1 Publication
    Glycosylationi99 – 991O-linked (GalNAc...)1 Publication
    Glycosylationi103 – 1031O-linked (GalNAc...)1 Publication
    Glycosylationi109 – 1091O-linked (GalNAc...)1 Publication
    Glycosylationi113 – 1131O-linked (GalNAc...)1 Publication
    Glycosylationi114 – 1141O-linked (GalNAc...)1 Publication
    Glycosylationi136 – 1361O-linked (GalNAc...)1 Publication
    Glycosylationi137 – 1371O-linked (GalNAc...)1 Publication
    Glycosylationi173 – 1731O-linked (GalNAc...)1 Publication
    Glycosylationi178 – 1781O-linked (GalNAc...)1 Publication
    Glycosylationi239 – 2391N-linked (GlcNAc...)1 Publication
    Modified residuei291 – 2911Phosphoserine1 Publication
    Modified residuei351 – 3511Phosphoserine1 Publication
    Modified residuei355 – 3551Phosphoserine2 Publications
    Modified residuei368 – 3681Phosphoserine1 Publication

    Post-translational modificationi

    Glycosylated; has a high content of sialic acid and O-linked carbohydrate structures.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP16150.
    PaxDbiP16150.
    PeptideAtlasiP16150.
    PRIDEiP16150.

    PTM databases

    PhosphoSiteiP16150.
    UniCarbKBiP16150.

    Miscellaneous databases

    PMAP-CutDBP16150.

    Expressioni

    Tissue specificityi

    Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas.

    Gene expression databases

    ArrayExpressiP16150.
    BgeeiP16150.
    CleanExiHS_SPN.
    GenevestigatoriP16150.

    Organism-specific databases

    HPAiCAB002666.
    HPA055244.

    Interactioni

    Subunit structurei

    Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX By similarity.By similarity

    Protein-protein interaction databases

    BioGridi112571. 4 interactions.
    STRINGi9606.ENSP00000353238.

    Structurei

    3D structure databases

    ProteinModelPortaliP16150.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 253234ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini277 – 400124CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei254 – 27623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47487.
    HOGENOMiHOG000294199.
    HOVERGENiHBG006258.
    InParanoidiP16150.
    KOiK06477.
    OMAiGSLAMEE.
    OrthoDBiEOG7HXCVB.
    PhylomeDBiP16150.
    TreeFamiTF337688.

    Sequencei

    Sequence statusi: Complete.

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

    P16150-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATLLLLLGV LVVSPDALGS TTAVQTPTSG EPLVSTSEPL SSKMYTTSIT    50
    SDPKADSTGD QTSALPPSTS INEGSPLWTS IGASTGSPLP EPTTYQEVSI 100
    KMSSVPQETP HATSHPAVPI TANSLGSHTV TGGTITTNSP ETSSRTSGAP 150
    VTTAASSLET SRGTSGPPLT MATVSLETSK GTSGPPVTMA TDSLETSTGT 200
    TGPPVTMTTG SLEPSSGASG PQVSSVKLST MMSPTTSTNA STVPFRNPDE 250
    NSRGMLPVAV LVALLAVIVL VALLLLWRRR QKRRTGALVL SRGGKRNGVV 300
    DAWAGPAQVP EEGAVTVTVG GSGGDKGSGF PDGEGSSRRP TLTTFFGRRK 350
    SRQGSLAMEE LKSGSGPSLK GEEEPLVASE DGAVDAPAPD EPEGGDGAAP 400
    Length:400
    Mass (Da):40,322
    Last modified:April 1, 1990 - v1
    Checksum:iC9C9AB8435D5E1FE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221T → I.
    Corresponds to variant rs2229653 [ dbSNP | Ensembl ].
    VAR_051091
    Natural varianti93 – 931T → A.
    Corresponds to variant rs2229654 [ dbSNP | Ensembl ].
    VAR_051092

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04168 mRNA. Translation: AAA59510.1.
    J04536 mRNA. Translation: AAB59540.1.
    X52075 Genomic DNA. Translation: CAA36294.1.
    M61827 Genomic DNA. Translation: AAA51949.1.
    AK292626 mRNA. Translation: BAF85315.1.
    AK313750 mRNA. Translation: BAG36490.1.
    CH471238 Genomic DNA. Translation: EAW80015.1.
    BC012350 mRNA. Translation: AAH12350.1.
    CCDSiCCDS10650.1.
    PIRiA39822.
    RefSeqiNP_001025459.1. NM_001030288.2.
    NP_003114.1. NM_003123.4.
    XP_005276570.1. XM_005276513.1.
    UniGeneiHs.632188.

    Genome annotation databases

    EnsembliENST00000360121; ENSP00000353238; ENSG00000197471.
    ENST00000395389; ENSP00000378787; ENSG00000197471.
    ENST00000563039; ENSP00000455266; ENSG00000197471.
    GeneIDi101929889.
    6693.
    KEGGihsa:101929889.
    hsa:6693.
    UCSCiuc002dtm.4. human.

    Polymorphism databases

    DMDMi126213.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04168 mRNA. Translation: AAA59510.1 .
    J04536 mRNA. Translation: AAB59540.1 .
    X52075 Genomic DNA. Translation: CAA36294.1 .
    M61827 Genomic DNA. Translation: AAA51949.1 .
    AK292626 mRNA. Translation: BAF85315.1 .
    AK313750 mRNA. Translation: BAG36490.1 .
    CH471238 Genomic DNA. Translation: EAW80015.1 .
    BC012350 mRNA. Translation: AAH12350.1 .
    CCDSi CCDS10650.1.
    PIRi A39822.
    RefSeqi NP_001025459.1. NM_001030288.2.
    NP_003114.1. NM_003123.4.
    XP_005276570.1. XM_005276513.1.
    UniGenei Hs.632188.

    3D structure databases

    ProteinModelPortali P16150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112571. 4 interactions.
    STRINGi 9606.ENSP00000353238.

    PTM databases

    PhosphoSitei P16150.
    UniCarbKBi P16150.

    Polymorphism databases

    DMDMi 126213.

    Proteomic databases

    MaxQBi P16150.
    PaxDbi P16150.
    PeptideAtlasi P16150.
    PRIDEi P16150.

    Protocols and materials databases

    DNASUi 6693.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360121 ; ENSP00000353238 ; ENSG00000197471 .
    ENST00000395389 ; ENSP00000378787 ; ENSG00000197471 .
    ENST00000563039 ; ENSP00000455266 ; ENSG00000197471 .
    GeneIDi 101929889.
    6693.
    KEGGi hsa:101929889.
    hsa:6693.
    UCSCi uc002dtm.4. human.

    Organism-specific databases

    CTDi 6693.
    GeneCardsi GC16P029674.
    HGNCi HGNC:11249. SPN.
    HPAi CAB002666.
    HPA055244.
    MIMi 182160. gene.
    neXtProti NX_P16150.
    PharmGKBi PA36079.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47487.
    HOGENOMi HOG000294199.
    HOVERGENi HBG006258.
    InParanoidi P16150.
    KOi K06477.
    OMAi GSLAMEE.
    OrthoDBi EOG7HXCVB.
    PhylomeDBi P16150.
    TreeFami TF337688.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_12560. Basigin interactions.

    Miscellaneous databases

    GeneWikii CD43.
    NextBioi 26089.
    PMAP-CutDB P16150.
    PROi P16150.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16150.
    Bgeei P16150.
    CleanExi HS_SPN.
    Genevestigatori P16150.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNAs encoding human leukosialin and localization of the leukosialin gene to chromosome 16."
      Pallant A., Eskenazi A., Mattei M.-G., Fournier R.E.K., Carlsson S.R., Fukuda M., Frelinger J.G.
      Proc. Natl. Acad. Sci. U.S.A. 86:1328-1332(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular characterization of sialophorin (CD43), the lymphocyte surface sialoglycoprotein defective in Wiskott-Aldrich syndrome."
      Shelley C.S., Remold-O'Donnell E., Davis A.E. III, Bruns G.A.P., Rosen F.S., Carroll M.C., Whitehead D.A.S.
      Proc. Natl. Acad. Sci. U.S.A. 86:2819-2823(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure of the human sialophorin (CD43) gene. Identification of features atypical of genes encoding integral membrane proteins."
      Shelley C.S., Remold-O'Donnell E., Rosen F.S., Whitehead D.A.S.
      Biochem. J. 270:569-576(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "A short, novel promoter sequence confers the expression of human leukosialin, a major sialoglycoprotein on leukocytes."
      Kudo S., Fukuda M.
      J. Biol. Chem. 266:8483-8489(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
      Tissue: Spleen and Thymus.
    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].
      Tissue: Kidney.
    8. "Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin)."
      Schmid K., Hediger M.A., Brossmer R., Collins J.H., Haupt H., Marti T., Offner G.D., Schaller J., Takagaki K., Walsh M.T., Schwick H.G., Rose F.S., Remold-O'Donnell E.
      Proc. Natl. Acad. Sci. U.S.A. 89:663-667(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-245, GLYCOSYLATION AT THR-21; THR-22; THR-26; THR-28; SER-29; SER-35; THR-36; SER-37; SER-41; SER-42; THR-46; THR-47; SER-48; THR-50; THR-58; THR-69; SER-99; SER-103; THR-109; THR-113; SER-114; THR-136; THR-137; THR-173; THR-178 AND ASN-239.
    9. "Phosphorylation of the major leukocyte surface sialoglycoprotein, leukosialin, is increased by phorbol 12-myristate 13-acetate."
      Piller V., Piller F., Fukuda M.
      J. Biol. Chem. 264:18824-18831(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-291 AND SER-351.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Carrascal M., Abian J.
      Submitted (JAN-2008) to UniProtKB
      Cited for: PHOSPHORYLATION AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLEUK_HUMAN
    AccessioniPrimary (citable) accession number: P16150
    Secondary accession number(s): A8K9B1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 137 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 16
      Human chromosome 16: 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

    External Data

    Dasty 3