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P13727

- PRG2_HUMAN

UniProt

P13727 - PRG2_HUMAN

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Protein
Bone marrow proteoglycan
Gene
PRG2, MBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA.1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: ProtInc
  2. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. immune response Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity

Keywords - Ligandi

Heparin-binding, Lectin

Protein family/group databases

MEROPSiI63.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Bone marrow proteoglycan
Short name:
BMPG
Alternative name(s):
Proteoglycan 2
Cleaved into the following chain:
Eosinophil granule major basic protein
Short name:
EMBP
Short name:
MBP
Alternative name(s):
Pregnancy-associated major basic protein
Gene namesi
Name:PRG2
Synonyms:MBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9362. PRG2.

Subcellular locationi

Chain Bone marrow proteoglycan : Secreted
Note: The proform is secreted.
Chain Eosinophil granule major basic protein : Cytoplasmic vesiclesecretory vesicle
Note: The proform is secreted. The mature protein is found in the matrix of the eosinophil's large specific granule (crystalloid core).

GO - Cellular componenti

  1. extracellular region Source: ProtInc
  2. extracellular vesicular exosome Source: UniProt
  3. transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33734.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16163 Publications
Add
BLAST
Chaini17 – 222206Bone marrow proteoglycan
PRO_0000259923Add
BLAST
Propeptidei17 – 10589Acidic
PRO_0000017385Add
BLAST
Chaini106 – 222117Eosinophil granule major basic protein
PRO_0000017386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231O-linked (GalNAc...); partial1 Publication
Glycosylationi24 – 241O-linked (GalNAc...)2 Publications
Glycosylationi25 – 251O-linked (GalNAc...)2 Publications
Glycosylationi34 – 341O-linked (GalNAc...); partial1 Publication
Disulfide bondi51 – 51Interchain (with C-461 in PAPPA)3 Publications
Glycosylationi62 – 621O-linked (Xyl...) (chondroitin sulfate)2 Publications
Glycosylationi86 – 861N-linked (GlcNAc...)2 Publications
Disulfide bondi125 ↔ 2203 Publications
Disulfide bondi169 – 169Interchain (with C-732 in PAPPA)3 Publications
Disulfide bondi197 ↔ 2123 Publications

Post-translational modificationi

Nitrated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration, Proteoglycan

Proteomic databases

PaxDbiP13727.
PRIDEiP13727.

Expressioni

Tissue specificityi

High levels of the proform in placenta and pregnancy serum; in placenta, localized to X cells of septa and anchoring villi. Lower levels in a variety of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow and colon.2 Publications

Developmental stagei

Levels of the proform increase in serum and placenta during pregnancy.2 Publications

Gene expression databases

CleanExiHS_MBP.
HS_PRG2.
GenevestigatoriP13727.

Organism-specific databases

HPAiHPA038515.

Interactioni

Subunit structurei

In pregnancy serum, the proform exists as a disulfide-linked 2:2 heterotetramer with PAPPA, as a disulfide-linked 2:2 heterotetramer with AGT, and as a complex (probably a 2:2:2 heterohexamer) with AGT and C3dg.6 Publications

Protein-protein interaction databases

BioGridi111544. 4 interactions.
IntActiP13727. 2 interactions.
MINTiMINT-1375191.
STRINGi9606.ENSP00000312134.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi109 – 1168
Helixi118 – 12912
Beta strandi130 – 1334
Helixi139 – 14911
Beta strandi153 – 16412
Beta strandi166 – 1683
Beta strandi171 – 1744
Beta strandi187 – 1893
Beta strandi196 – 2016
Turni202 – 2054
Beta strandi207 – 2104
Beta strandi216 – 2216

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8UX-ray1.80A/B106-222[»]
2BRSX-ray2.20A/B106-222[»]
ProteinModelPortaliP13727.
SMRiP13727. Positions 107-222.

Miscellaneous databases

EvolutionaryTraceiP13727.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 222119C-type lectin
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG266233.
HOGENOMiHOG000261603.
HOVERGENiHBG005583.
InParanoidiP13727.
KOiK10786.
OMAiFTCRRCY.
OrthoDBiEOG779P0F.
PhylomeDBiP13727.
TreeFamiTF336281.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR002352. Eosinophil_major_basic.
[Graphical view]
PANTHERiPTHR10068. PTHR10068. 1 hit.
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
PRINTSiPR00770. EMAJORBASICP.
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13727-1 [UniParc]FASTAAdd to Basket

« Hide

MKLPLLLALL FGAVSALHLR SETSTFETPL GAKTLPEDEE TPEQEMEETP    50
CRELEEEEEW GSGSEDASKK DGAVESISVP DMVDKNLTCP EEEDTVKVVG 100
IPGCQTCRYL LVRSLQTFSQ AWFTCRRCYR GNLVSIHNFN INYRIQCSVS 150
ALNQGQVWIG GRITGSGRCR RFQWVDGSRW NFAYWAAHQP WSRGGHCVAL 200
CTRGGHWRRA HCLRRLPFIC SY 222
Length:222
Mass (Da):25,206
Last modified:December 15, 2009 - v2
Checksum:iCDD545642555E2D0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036401
Natural varianti206 – 2061H → Y.7 Publications
Corresponds to variant rs536455 [ dbSNP | Ensembl ].
VAR_060729

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841D → H in AAA36203. 1 Publication
Sequence conflicti192 – 1921S → T in CAA81207. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00809 mRNA. Translation: CAA68751.1.
M36805 mRNA. Translation: AAA36203.1.
M34462 Genomic DNA. Translation: AAA35796.1.
M35670 mRNA. Translation: AAA35965.1.
X14088 mRNA. Translation: CAA32250.1.
X65787 mRNA. Translation: CAA46670.1.
Z26248 mRNA. Translation: CAA81207.1.
CR450311 mRNA. Translation: CAG29307.1.
AP000781 Genomic DNA. No translation available.
BC005929 mRNA. Translation: AAH05929.1.
CCDSiCCDS7955.1.
PIRiI54055. JL0085.
RefSeqiNP_001230174.1. NM_001243245.1.
NP_002719.3. NM_002728.4.
UniGeneiHs.512633.

Genome annotation databases

EnsembliENST00000311862; ENSP00000312134; ENSG00000186652.
ENST00000525955; ENSP00000433016; ENSG00000186652.
GeneIDi5553.
KEGGihsa:5553.
UCSCiuc001nkc.3. human.

Polymorphism databases

DMDMi281185479.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Major basic protein entry

Functional Glycomics Gateway - Glycan Binding

Eosinophil major basic protein

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00809 mRNA. Translation: CAA68751.1 .
M36805 mRNA. Translation: AAA36203.1 .
M34462 Genomic DNA. Translation: AAA35796.1 .
M35670 mRNA. Translation: AAA35965.1 .
X14088 mRNA. Translation: CAA32250.1 .
X65787 mRNA. Translation: CAA46670.1 .
Z26248 mRNA. Translation: CAA81207.1 .
CR450311 mRNA. Translation: CAG29307.1 .
AP000781 Genomic DNA. No translation available.
BC005929 mRNA. Translation: AAH05929.1 .
CCDSi CCDS7955.1.
PIRi I54055. JL0085.
RefSeqi NP_001230174.1. NM_001243245.1.
NP_002719.3. NM_002728.4.
UniGenei Hs.512633.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H8U X-ray 1.80 A/B 106-222 [» ]
2BRS X-ray 2.20 A/B 106-222 [» ]
ProteinModelPortali P13727.
SMRi P13727. Positions 107-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111544. 4 interactions.
IntActi P13727. 2 interactions.
MINTi MINT-1375191.
STRINGi 9606.ENSP00000312134.

Chemistry

DrugBanki DB00020. Sargramostim.

Protein family/group databases

MEROPSi I63.001.

Polymorphism databases

DMDMi 281185479.

Proteomic databases

PaxDbi P13727.
PRIDEi P13727.

Protocols and materials databases

DNASUi 5553.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311862 ; ENSP00000312134 ; ENSG00000186652 .
ENST00000525955 ; ENSP00000433016 ; ENSG00000186652 .
GeneIDi 5553.
KEGGi hsa:5553.
UCSCi uc001nkc.3. human.

Organism-specific databases

CTDi 5553.
GeneCardsi GC11M057154.
H-InvDB HIX0009634.
HGNCi HGNC:9362. PRG2.
HPAi HPA038515.
MIMi 605601. gene.
neXtProti NX_P13727.
PharmGKBi PA33734.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266233.
HOGENOMi HOG000261603.
HOVERGENi HBG005583.
InParanoidi P13727.
KOi K10786.
OMAi FTCRRCY.
OrthoDBi EOG779P0F.
PhylomeDBi P13727.
TreeFami TF336281.

Miscellaneous databases

ChiTaRSi PRG2. human.
EvolutionaryTracei P13727.
GeneWikii Major_basic_protein.
GenomeRNAii 5553.
NextBioi 21522.
PROi P13727.
SOURCEi Search...

Gene expression databases

CleanExi HS_MBP.
HS_PRG2.
Genevestigatori P13727.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR002352. Eosinophil_major_basic.
[Graphical view ]
PANTHERi PTHR10068. PTHR10068. 1 hit.
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
PRINTSi PR00770. EMAJORBASICP.
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Acidic precursor revealed in human eosinophil granule major basic protein cDNA."
    Barker R.L., Gleich G.J., Pease L.R.
    J. Exp. Med. 168:1493-1498(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
    Tissue: Promyelocyte.
  2. Barker R.L.
    Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 84.
  3. "Cloning and sequence analysis of the human gene encoding eosinophil major basic protein."
    Barker R.L., Loegering D.A., Arakawa K.C., Pease L.R., Gleich G.J.
    Gene 86:285-289(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-206.
  4. "Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein."
    McGrogan M., Simonsen C., Scott R., Giffith J., Ellis N., Kennedy J., Campanelli D., Nathan C., Gabay J.
    J. Exp. Med. 168:2295-2308(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
  5. "Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins."
    Yoshimatsu K., Ohya Y., Shikata Y., Seto T., Hasegawa Y., Tanaka I., Kawamura T., Kitoh K., Toyoshima S., Osawa T.
    Mol. Immunol. 29:537-546(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT TYR-206.
  6. "Human eosinophil major basic protein, a mediator of allergic inflammation, is expressed by alternative splicing from two promoters."
    Li M.S., Sun L., Satoh T., Fisher L.M., Spry C.J.
    Biochem. J. 305:921-927(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
    Tissue: Bone marrow.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-206.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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], VARIANT TYR-206.
    Tissue: Placenta.
  10. "Pro-major basic protein has three types of sugar chains at the pro-portion."
    Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K., Yoshida Y.
    Biochim. Biophys. Acta 1163:243-249(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-222, GLYCOSYLATION AT SER-24; THR-25; SER-62 AND ASN-86.
    Tissue: Liver.
  11. "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein."
    Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.
    J. Biol. Chem. 268:12243-12246(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-26; 47-52; 98-108; 172-179 AND 210-222, SUBUNIT, INTERCHAIN DISULFIDE BOND.
    Tissue: Serum.
  12. "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma."
    Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.
    J. Biol. Chem. 270:13645-13651(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-29, SUBUNIT, DEVELOPMENTAL STAGE.
    Tissue: Serum.
  13. "Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein."
    Wasmoen T.L., Bell M.P., Loegering D.A., Gleich G.J., Prendergast F.G., McKean D.J.
    J. Biol. Chem. 263:12559-12563(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 106-222.
  14. Cited for: PROTEIN SEQUENCE OF 106-125.
  15. "Eosinophil granule cationic proteins: major basic protein is distinct from the smaller subunit of eosinophil peroxidase."
    Weller P.F., Ackerman S.J., Smith J.A.
    J. Leukoc. Biol. 43:1-4(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 108-124.
  16. "Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA."
    Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.
    Biochemistry 33:1592-1598(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 172-179 AND 210-222, SUBUNIT.
    Tissue: Serum.
  17. "Evidence of eosinophil granule major basic protein in human placenta."
    Wasmoen T.L., McKean D.J., Benirschke K., Coulam C.B., Gleich G.J.
    J. Exp. Med. 170:2051-2063(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 177-196.
    Tissue: Placenta.
  18. "Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum."
    Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.
    Biochem. Mol. Biol. Int. 33:329-336(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
  19. "Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein."
    Oxvig C., Gleich G.J., Sottrup-Jensen L.
    FEBS Lett. 341:213-217(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  20. "Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta."
    Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T., Sottrup-Jensen L., Gleich G.J.
    Lab. Invest. 71:560-566(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  21. "Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein: expression in human reproductive and nonreproductive tissues."
    Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A., Gleich G.J., Sottrup-Jensen L., Haaning J.
    Biol. Reprod. 61:1083-1089(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  22. "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor."
    Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S., Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.
    J. Biol. Chem. 275:31128-31133(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  23. "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment sites."
    Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B., Kristensen L., Sottrup-Jensen L., Oxvig C.
    J. Biol. Chem. 278:2106-2117(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BONDS.
  24. Cited for: NITRATION.
  25. "Crystal structure of the eosinophil major basic protein at 1.8-A. An atypical lectin with a paradigm shift in specificity."
    Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L., Leonidas D.D., Gleich G.J., Acharya K.R.
    J. Biol. Chem. 276:26197-26203(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-222, HEPARIN-BINDING.
  26. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-179.

Entry informationi

Entry nameiPRG2_HUMAN
AccessioniPrimary (citable) accession number: P13727
Secondary accession number(s): P81448, Q14227, Q6ICT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 15, 2009
Last modified: September 3, 2014
This is version 156 of the entry and version 2 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

Miscellaneous

Binds heparin. Does not bind calcium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi