P16150 (LEUK_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 111.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Leukosialin Alternative name(s): Galactoglycoprotein Short name=GALGP Leukocyte sialoglycoprotein Sialophorin CD_antigen=CD43 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 400 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. |
| Subunit structure | Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX By similarity. |
| Subcellular location | |
| Tissue specificity | Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas. |
| Post-translational modification | Glycosylated; has a high content of sialic acid and O-linked carbohydrate structures. Ref.6 |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.6 | ||||||
| Chain | 20 – 400 | 381 | Leukosialin | PRO_0000021588 | |||||
Regions | |||||||||
| Topological domain | 20 – 253 | 234 | Extracellular Potential | ||||||
| Transmembrane | 254 – 276 | 23 | Helical; Potential | ||||||
| Topological domain | 277 – 400 | 124 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 291 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 341 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 351 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 355 | 1 | Phosphoserine Ref.7 Ref.9 | ||||||
| Modified residue | 368 | 1 | Phosphoserine Ref.10 | ||||||
| Glycosylation | 21 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 22 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 26 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 28 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 29 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 35 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 36 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 37 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 41 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 42 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 46 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 47 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 48 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 50 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 58 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 69 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 99 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 103 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 109 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 113 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 114 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 136 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 137 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 173 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 178 | 1 | O-linked (GalNAc...) Ref.6 | ||||||
| Glycosylation | 239 | 1 | N-linked (GlcNAc...) Ref.6 | ||||||
Natural variations | |||||||||
| Natural variant | 22 | 1 | T → I. Corresponds to variant rs2229653 [ dbSNP | Ensembl ]. | VAR_051091 | |||||
| Natural variant | 93 | 1 | T → A. Corresponds to variant rs2229654 [ dbSNP | Ensembl ]. | VAR_051092 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 2521952] [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: 2784859] [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: 2241892] [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: 1827122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
| [6] | "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: 1731338] [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. |
| [7] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, MASS SPECTROMETRY. Tissue: Platelet. |
| [8] | "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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, MASS SPECTROMETRY. Tissue: T-cell. |
| [9] | Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-355, MASS SPECTROMETRY. Tissue: T-cell. |
| [10] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-368, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [11] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J04168 mRNA. Translation: AAA59510.1. J04536 mRNA. Translation: AAB59540.1. X52075 Genomic DNA. Translation: CAA36294.1. M61827 Genomic DNA. Translation: AAA51949.1. BC012350 mRNA. Translation: AAH12350.1. |
| IPI | IPI00027430. |
| PIR | A39822. |
| RefSeq | NP_001025459.1. NM_001030288.1. NP_003114.1. NM_003123.3. |
| UniGene | Hs.632188. |
3D structure databases | |
| ProteinModelPortal | P16150. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P16150. |
PTM databases | |
| GlycoSuiteDB | P16150. |
| PhosphoSite | P16150. |
Polymorphism databases | |
| DMDM | 126213. |
Proteomic databases | |
| PeptideAtlas | P16150. |
| PRIDE | P16150. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000360121; ENSP00000353238; ENSG00000197471. ENST00000395389; ENSP00000378787; ENSG00000197471. |
| GeneID | 6693. |
| KEGG | hsa:6693. |
| UCSC | uc002dtm.1. human. |
Organism-specific databases | |
| CTD | 6693. |
| GeneCards | GC16P029581. |
| HGNC | HGNC:11249. SPN. |
| HPA | CAB002666. |
| MIM | 182160. gene. |
| neXtProt | NX_P16150. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG16992. |
| GeneTree | ENSGT00390000017626. |
| HOGENOM | HBG126784. |
| HOVERGEN | HBG006258. |
| InParanoid | P16150. |
| OMA | GSLAMEE. |
| OrthoDB | EOG4KSPK7. |
| PhylomeDB | P16150. |
Enzyme and pathway databases | |
| Reactome | REACT_604. Hemostasis. |
Gene expression databases | |
| ArrayExpress | P16150. |
| Bgee | P16150. |
| CleanEx | HS_SPN. |
| Genevestigator | P16150. |
Family and domain databases | |
| KO | K06477. |
| ProtoNet | Search... |
Other | |
| NextBio | 26089. |
| PMAP-CutDB | P16150. |
| SOURCE | Search... |
Entry information
| Entry name | LEUK_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P16150 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human cell differentiation molecules CD nomenclature of surface proteins of human leucocytes and list of entries |
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |

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