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P07585

- PGS2_HUMAN

UniProt

P07585 - PGS2_HUMAN

Protein

Decorin

Gene

DCN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    May affect the rate of fibrils formation.

    GO - Molecular functioni

    1. extracellular matrix binding Source: Ensembl
    2. glycosaminoglycan binding Source: Ensembl
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. chondroitin sulfate biosynthetic process Source: Reactome
    4. chondroitin sulfate catabolic process Source: Reactome
    5. chondroitin sulfate metabolic process Source: Reactome
    6. dermatan sulfate biosynthetic process Source: Reactome
    7. extracellular matrix disassembly Source: Reactome
    8. extracellular matrix organization Source: Reactome
    9. glycosaminoglycan metabolic process Source: Reactome
    10. kidney development Source: Ensembl
    11. organ morphogenesis Source: ProtInc
    12. peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan Source: Ensembl
    13. placenta development Source: Ensembl
    14. response to lipopolysaccharide Source: Ensembl
    15. response to mechanical stimulus Source: Ensembl
    16. skeletal muscle tissue development Source: Ensembl
    17. small molecule metabolic process Source: Reactome
    18. wound healing Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_120800. Dermatan sulfate biosynthesis.
    REACT_120888. CS/DS degradation.
    REACT_120989. Chondroitin sulfate biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_163906. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Decorin
    Alternative name(s):
    Bone proteoglycan II
    PG-S2
    PG40
    Gene namesi
    Name:DCN
    Synonyms:SLRR1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2705. DCN.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type VI trimer Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. Golgi lumen Source: Reactome
    5. lysosomal lumen Source: Reactome
    6. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Corneal dystrophy, congenital stromal (CSCD) [MIM:610048]: A corneal dystrophy characterized by congenital corneal opacification consisting of a large number of flakes and spots throughout all layers of the stroma. It results in progressive, painless visual loss. Corneal erosions and photophobia are absent.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Corneal dystrophy

    Organism-specific databases

    MIMi610048. phenotype.
    Orphaneti101068. Congenital stromal corneal dystrophy.
    PharmGKBiPA27177.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 30142 PublicationsPRO_0000032709Add
    BLAST
    Chaini31 – 359329DecorinPRO_0000032710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341O-linked (Xyl...) (glycosaminoglycan)1 Publication
    Disulfide bondi54 ↔ 60By similarity
    Disulfide bondi58 ↔ 67By similarity
    Glycosylationi211 – 2111N-linked (GlcNAc...)1 Publication
    Glycosylationi262 – 2621N-linked (GlcNAc...)1 Publication
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi313 ↔ 346By similarity

    Post-translational modificationi

    The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan

    Proteomic databases

    PaxDbiP07585.
    PRIDEiP07585.

    PTM databases

    PhosphoSiteiP07585.

    Miscellaneous databases

    PMAP-CutDBP07585.

    Expressioni

    Gene expression databases

    ArrayExpressiP07585.
    BgeeiP07585.
    CleanExiHS_DCN.
    GenevestigatoriP07585.

    Organism-specific databases

    HPAiCAB017118.
    HPA003315.

    Interactioni

    Subunit structurei

    Binds to type I and type II collagen, fibronectin and TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108002. 14 interactions.
    IntActiP07585. 4 interactions.
    STRINGi9606.ENSP00000052754.

    Structurei

    3D structure databases

    ProteinModelPortaliP07585.
    SMRiP07585. Positions 51-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati73 – 9321LRR 1Add
    BLAST
    Repeati94 – 11724LRR 2Add
    BLAST
    Repeati118 – 14124LRR 3Add
    BLAST
    Repeati142 – 16221LRR 4Add
    BLAST
    Repeati163 – 18624LRR 5Add
    BLAST
    Repeati187 – 21226LRR 6Add
    BLAST
    Repeati213 – 23321LRR 7Add
    BLAST
    Repeati234 – 25724LRR 8Add
    BLAST
    Repeati258 – 28124LRR 9Add
    BLAST
    Repeati282 – 30423LRR 10Add
    BLAST
    Repeati305 – 33430LRR 11Add
    BLAST
    Repeati335 – 35925LRR 12Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi54 – 6714Cys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 12 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000261690.
    HOVERGENiHBG016052.
    InParanoidiP07585.
    KOiK04660.
    OMAiPLGPVCP.
    OrthoDBiEOG76739V.
    PhylomeDBiP07585.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR028549. Decorin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view]
    PANTHERiPTHR24369:SF5. PTHR24369:SF5. 1 hit.
    PfamiPF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002490. SLRP_I. 1 hit.
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 8 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P07585-1) [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

    MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL    50
    GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD 100
    FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK 150
    TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK 200
    KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL 250
    GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH 300
    NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR 350
    SAIQLGNYK 359
    Length:359
    Mass (Da):39,747
    Last modified:April 1, 1988 - v1
    Checksum:iFF511E871A1A52DD
    GO
    Isoform B (identifier: P07585-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         71-179: Missing.

    Show »
    Length:250
    Mass (Da):27,353
    Checksum:i5AA599BE479F68D9
    GO
    Isoform C (identifier: P07585-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-219: Missing.

    Show »
    Length:212
    Mass (Da):23,278
    Checksum:i0BCF8BC8CBA92CA9
    GO
    Isoform D (identifier: P07585-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         109-295: Missing.

    Show »
    Length:172
    Mass (Da):19,243
    Checksum:i7EA011E351163971
    GO
    Isoform E (identifier: P07585-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-75: LDKV → CLPS
         76-359: Missing.

    Show »
    Length:75
    Mass (Da):8,266
    Checksum:i781856DC9E377479
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371G → A AA sequence (PubMed:3597437)Curated
    Sequence conflicti45 – 451D → P AA sequence (PubMed:3597437)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti268 – 2681T → M.1 Publication
    Corresponds to variant rs3138268 [ dbSNP | Ensembl ].
    VAR_014351
    Natural varianti273 – 2731E → Q.
    Corresponds to variant rs1803344 [ dbSNP | Ensembl ].
    VAR_011975

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei71 – 179109Missing in isoform B. 1 PublicationVSP_006172Add
    BLAST
    Alternative sequencei72 – 754LDKV → CLPS in isoform E. 1 PublicationVSP_006175
    Alternative sequencei73 – 219147Missing in isoform C. 1 PublicationVSP_006173Add
    BLAST
    Alternative sequencei76 – 359284Missing in isoform E. 1 PublicationVSP_006176Add
    BLAST
    Alternative sequencei109 – 295187Missing in isoform D. 1 PublicationVSP_006174Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14219 mRNA. Translation: AAB00774.1.
    L01131
    , L01125, L01126, L01127, L01129, L01130 Genomic DNA. Translation: AAA52301.1. Sequence problems.
    AH005442 Genomic DNA. Translation: AAB60901.1.
    AF138300 mRNA. Translation: AAD44713.1.
    AF138301 mRNA. Translation: AAF61437.1.
    AF138302 mRNA. Translation: AAD44714.1.
    AF138303 mRNA. Translation: AAF61438.1.
    AF138304 mRNA. Translation: AAD44715.1.
    BT019800 mRNA. Translation: AAV38603.1.
    AF491944 Genomic DNA. Translation: AAL92176.1.
    BC005322 mRNA. Translation: AAH05322.1.
    CCDSiCCDS44951.1. [P07585-5]
    CCDS9039.1. [P07585-1]
    CCDS9040.1. [P07585-2]
    CCDS9041.1. [P07585-3]
    CCDS9042.1. [P07585-4]
    PIRiA45016. NBHUC8.
    B28457.
    RefSeqiNP_001911.1. NM_001920.3. [P07585-1]
    NP_598010.1. NM_133503.2. [P07585-1]
    NP_598011.1. NM_133504.2. [P07585-2]
    NP_598012.1. NM_133505.2. [P07585-3]
    NP_598013.1. NM_133506.2. [P07585-4]
    NP_598014.1. NM_133507.2. [P07585-5]
    XP_005268750.1. XM_005268693.1. [P07585-1]
    XP_006719333.1. XM_006719270.1. [P07585-1]
    UniGeneiHs.156316.

    Genome annotation databases

    EnsembliENST00000052754; ENSP00000052754; ENSG00000011465. [P07585-1]
    ENST00000393155; ENSP00000376862; ENSG00000011465. [P07585-1]
    ENST00000420120; ENSP00000413723; ENSG00000011465. [P07585-2]
    ENST00000425043; ENSP00000401021; ENSG00000011465. [P07585-3]
    ENST00000441303; ENSP00000399815; ENSG00000011465. [P07585-4]
    ENST00000456569; ENSP00000398514; ENSG00000011465. [P07585-5]
    ENST00000547568; ENSP00000447674; ENSG00000011465. [P07585-3]
    ENST00000552962; ENSP00000447654; ENSG00000011465. [P07585-1]
    GeneIDi1634.
    KEGGihsa:1634.
    UCSCiuc001tbo.3. human. [P07585-2]
    uc001tbp.3. human. [P07585-3]
    uc001tbq.3. human. [P07585-4]
    uc001tbr.3. human. [P07585-5]
    uc001tbt.3. human. [P07585-1]

    Polymorphism databases

    DMDMi129951.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14219 mRNA. Translation: AAB00774.1 .
    L01131
    , L01125 , L01126 , L01127 , L01129 , L01130 Genomic DNA. Translation: AAA52301.1 . Sequence problems.
    AH005442 Genomic DNA. Translation: AAB60901.1 .
    AF138300 mRNA. Translation: AAD44713.1 .
    AF138301 mRNA. Translation: AAF61437.1 .
    AF138302 mRNA. Translation: AAD44714.1 .
    AF138303 mRNA. Translation: AAF61438.1 .
    AF138304 mRNA. Translation: AAD44715.1 .
    BT019800 mRNA. Translation: AAV38603.1 .
    AF491944 Genomic DNA. Translation: AAL92176.1 .
    BC005322 mRNA. Translation: AAH05322.1 .
    CCDSi CCDS44951.1. [P07585-5 ]
    CCDS9039.1. [P07585-1 ]
    CCDS9040.1. [P07585-2 ]
    CCDS9041.1. [P07585-3 ]
    CCDS9042.1. [P07585-4 ]
    PIRi A45016. NBHUC8.
    B28457.
    RefSeqi NP_001911.1. NM_001920.3. [P07585-1 ]
    NP_598010.1. NM_133503.2. [P07585-1 ]
    NP_598011.1. NM_133504.2. [P07585-2 ]
    NP_598012.1. NM_133505.2. [P07585-3 ]
    NP_598013.1. NM_133506.2. [P07585-4 ]
    NP_598014.1. NM_133507.2. [P07585-5 ]
    XP_005268750.1. XM_005268693.1. [P07585-1 ]
    XP_006719333.1. XM_006719270.1. [P07585-1 ]
    UniGenei Hs.156316.

    3D structure databases

    ProteinModelPortali P07585.
    SMRi P07585. Positions 51-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108002. 14 interactions.
    IntActi P07585. 4 interactions.
    STRINGi 9606.ENSP00000052754.

    PTM databases

    PhosphoSitei P07585.

    Polymorphism databases

    DMDMi 129951.

    Proteomic databases

    PaxDbi P07585.
    PRIDEi P07585.

    Protocols and materials databases

    DNASUi 1634.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000052754 ; ENSP00000052754 ; ENSG00000011465 . [P07585-1 ]
    ENST00000393155 ; ENSP00000376862 ; ENSG00000011465 . [P07585-1 ]
    ENST00000420120 ; ENSP00000413723 ; ENSG00000011465 . [P07585-2 ]
    ENST00000425043 ; ENSP00000401021 ; ENSG00000011465 . [P07585-3 ]
    ENST00000441303 ; ENSP00000399815 ; ENSG00000011465 . [P07585-4 ]
    ENST00000456569 ; ENSP00000398514 ; ENSG00000011465 . [P07585-5 ]
    ENST00000547568 ; ENSP00000447674 ; ENSG00000011465 . [P07585-3 ]
    ENST00000552962 ; ENSP00000447654 ; ENSG00000011465 . [P07585-1 ]
    GeneIDi 1634.
    KEGGi hsa:1634.
    UCSCi uc001tbo.3. human. [P07585-2 ]
    uc001tbp.3. human. [P07585-3 ]
    uc001tbq.3. human. [P07585-4 ]
    uc001tbr.3. human. [P07585-5 ]
    uc001tbt.3. human. [P07585-1 ]

    Organism-specific databases

    CTDi 1634.
    GeneCardsi GC12M091472.
    GeneReviewsi DCN.
    HGNCi HGNC:2705. DCN.
    HPAi CAB017118.
    HPA003315.
    MIMi 125255. gene.
    610048. phenotype.
    neXtProti NX_P07585.
    Orphaneti 101068. Congenital stromal corneal dystrophy.
    PharmGKBi PA27177.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000261690.
    HOVERGENi HBG016052.
    InParanoidi P07585.
    KOi K04660.
    OMAi PLGPVCP.
    OrthoDBi EOG76739V.
    PhylomeDBi P07585.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_120800. Dermatan sulfate biosynthesis.
    REACT_120888. CS/DS degradation.
    REACT_120989. Chondroitin sulfate biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    ChiTaRSi DCN. human.
    GeneWikii Decorin.
    GenomeRNAii 1634.
    NextBioi 6702.
    PMAP-CutDB P07585.
    PROi P07585.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07585.
    Bgeei P07585.
    CleanExi HS_DCN.
    Genevestigatori P07585.

    Family and domain databases

    InterProi IPR028549. Decorin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view ]
    PANTHERi PTHR24369:SF5. PTHR24369:SF5. 1 hit.
    Pfami PF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002490. SLRP_I. 1 hit.
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA."
      Krusius T., Ruoslahti E.
      Proc. Natl. Acad. Sci. U.S.A. 83:7683-7687(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human decorin gene: intron-exon junctions and chromosomal localization."
      Vetter U., Vogel W., Just W., Young M.F., Fisher L.W.
      Genomics 15:161-168(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lung.
    3. "The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5' untranslated region, and mapping of the gene to chromosome 12q23."
      Danielson K.G., Fazzio A., Cohen I.R., Cannizzaro L., Iozzo R.V.
      Genomics 15:146-160(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
    4. "Alternative splicing of human decorin."
      Cs-Szabo G., Glant T.T.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    6. SeattleSNPs variation discovery resource
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-268.
    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: Liver.
    8. "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II."
      Roughley P.J., White R.J.
      Biochem. J. 262:823-827(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-50.
    9. "Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
      Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
      J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-49.
    10. "Congenital stromal dystrophy of the cornea caused by a mutation in the decorin gene."
      Bredrup C., Knappskog P.M., Majewski J., Rodahl E., Boman H.
      Invest. Ophthalmol. Vis. Sci. 46:420-426(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CONGENITAL STROMAL CORNEAL DYSTROPHY.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-211 AND ASN-262.
      Tissue: Liver.

    Entry informationi

    Entry nameiPGS2_HUMAN
    AccessioniPrimary (citable) accession number: P07585
    Secondary accession number(s): Q9P0Z0
    , Q9P0Z1, Q9Y5N8, Q9Y5N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 167 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 chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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