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P07585

- PGS2_HUMAN

UniProt

P07585 - PGS2_HUMAN

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Protein
Decorin
Gene
DCN, SLRR1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

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 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 3014
PRO_0000032709Add
BLAST
Chaini31 – 359329Decorin
PRO_0000032710Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

BioGridi108002. 14 interactions.
STRINGi9606.ENSP00000052754.

Structurei

3D structure databases

ProteinModelPortaliP07585.
SMRiP07585. Positions 51-355.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

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

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.
VSP_006172Add
BLAST
Alternative sequencei72 – 754LDKV → CLPS in isoform E.
VSP_006175
Alternative sequencei73 – 219147Missing in isoform C.
VSP_006173Add
BLAST
Alternative sequencei76 – 359284Missing in isoform E.
VSP_006176Add
BLAST
Alternative sequencei109 – 295187Missing in isoform D.
VSP_006174Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371G → A AA sequence 1 Publication
Sequence conflicti45 – 451D → P AA sequence 1 Publication

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]
ENST00000228329; ENSP00000228329; ENSG00000011465. [P07585-2]
ENST00000303320; ENSP00000302031; ENSG00000011465. [P07585-4]
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.
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 ]
ENST00000228329 ; ENSP00000228329 ; ENSG00000011465 . [P07585-2 ]
ENST00000303320 ; ENSP00000302031 ; ENSG00000011465 . [P07585-4 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 166 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

Dasty 3

Similar proteinsi