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Protein

Bone marrow proteoglycan

Gene

PRG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • carbohydrate binding Source: ProtInc
  • heparin binding Source: UniProtKB-KW

GO - Biological processi

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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9362. PRG2.

Subcellular locationi

Bone marrow proteoglycan :
Eosinophil granule major basic protein :

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: ProtInc
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33734.

Chemistry

DrugBankiDB00020. Sargramostim.

Polymorphism and mutation databases

BioMutaiPRG2.
DMDMi281185479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16163 PublicationsAdd
BLAST
Chaini17 – 222206Bone marrow proteoglycanPRO_0000259923Add
BLAST
Propeptidei17 – 10589Acidic2 PublicationsPRO_0000017385Add
BLAST
Chaini106 – 222117Eosinophil granule major basic proteinPRO_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)PROSITE-ProRule annotation1 Publication
Glycosylationi62 – 621O-linked (Xyl...) (chondroitin sulfate)2 Publications
Glycosylationi86 – 861N-linked (GlcNAc...)2 Publications
Disulfide bondi125 ↔ 220PROSITE-ProRule annotation1 Publication
Disulfide bondi169 – 169Interchain (with C-732 in PAPPA)PROSITE-ProRule annotation1 Publication
Disulfide bondi197 ↔ 212PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Nitrated.1 Publication

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.
GenevisibleiP13727. HS.

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.5 Publications

Protein-protein interaction databases

BioGridi111544. 51 interactions.
IntActiP13727. 2 interactions.
MINTiMINT-1375191.
STRINGi9606.ENSP00000312134.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi109 – 1168Combined sources
Helixi118 – 12912Combined sources
Beta strandi130 – 1334Combined sources
Helixi139 – 14911Combined sources
Beta strandi153 – 16412Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi196 – 2016Combined sources
Turni202 – 2054Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi216 – 2216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8UX-ray1.80A/B106-222[»]
2BRSX-ray2.20A/B106-222[»]
4QXXX-ray1.45Z131-135[»]
ProteinModelPortaliP13727.
SMRiP13727. Positions 107-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13727.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 222119C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG266233.
GeneTreeiENSGT00440000039859.
HOGENOMiHOG000261603.
HOVERGENiHBG005583.
InParanoidiP13727.
KOiK10786.
OMAiGHWRRAH.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13727-1) [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

        10         20         30         40         50
MKLPLLLALL FGAVSALHLR SETSTFETPL GAKTLPEDEE TPEQEMEETP
60 70 80 90 100
CRELEEEEEW GSGSEDASKK DGAVESISVP DMVDKNLTCP EEEDTVKVVG
110 120 130 140 150
IPGCQTCRYL LVRSLQTFSQ AWFTCRRCYR GNLVSIHNFN INYRIQCSVS
160 170 180 190 200
ALNQGQVWIG GRITGSGRCR RFQWVDGSRW NFAYWAAHQP WSRGGHCVAL
210 220
CTRGGHWRRA HCLRRLPFIC SY
Length:222
Mass (Da):25,206
Last modified:December 15, 2009 - v2
Checksum:iCDD545642555E2D0
GO
Isoform 2 (identifier: P13727-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     112-122: Missing.

Show »
Length:211
Mass (Da):23,901
Checksum:i56CDF739284A3DE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841D → H in AAA36203 (PubMed:3171483).Curated
Sequence conflicti190 – 1901P → L in BAG35128 (PubMed:14702039).Curated
Sequence conflicti192 – 1921S → T in CAA81207 (PubMed:7531438).Curated

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.8 Publications
Corresponds to variant rs536455 [ dbSNP | Ensembl ].
VAR_060729

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei112 – 12211Missing in isoform 2. 1 PublicationVSP_056735Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
AK312195 mRNA. Translation: BAG35128.1.
CR450311 mRNA. Translation: CAG29307.1.
DQ846874 mRNA. Translation: ABI63361.1.
AP000781 Genomic DNA. No translation available.
BC005929 mRNA. Translation: AAH05929.1.
CCDSiCCDS58133.1. [P13727-2]
CCDS7955.1. [P13727-1]
PIRiI54055. JL0085.
RefSeqiNP_001230174.1. NM_001243245.2. [P13727-2]
NP_001289855.1. NM_001302926.1. [P13727-1]
NP_001289856.1. NM_001302927.1. [P13727-1]
NP_002719.3. NM_002728.5. [P13727-1]
UniGeneiHs.512633.

Genome annotation databases

EnsembliENST00000311862; ENSP00000312134; ENSG00000186652.
ENST00000525955; ENSP00000433016; ENSG00000186652.
ENST00000533605; ENSP00000433231; ENSG00000186652. [P13727-2]
GeneIDi5553.
KEGGihsa:5553.
UCSCiuc001nkc.3. human. [P13727-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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:
EMBLi
GenBanki
DDBJi
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.
AK312195 mRNA. Translation: BAG35128.1.
CR450311 mRNA. Translation: CAG29307.1.
DQ846874 mRNA. Translation: ABI63361.1.
AP000781 Genomic DNA. No translation available.
BC005929 mRNA. Translation: AAH05929.1.
CCDSiCCDS58133.1. [P13727-2]
CCDS7955.1. [P13727-1]
PIRiI54055. JL0085.
RefSeqiNP_001230174.1. NM_001243245.2. [P13727-2]
NP_001289855.1. NM_001302926.1. [P13727-1]
NP_001289856.1. NM_001302927.1. [P13727-1]
NP_002719.3. NM_002728.5. [P13727-1]
UniGeneiHs.512633.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8UX-ray1.80A/B106-222[»]
2BRSX-ray2.20A/B106-222[»]
4QXXX-ray1.45Z131-135[»]
ProteinModelPortaliP13727.
SMRiP13727. Positions 107-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111544. 51 interactions.
IntActiP13727. 2 interactions.
MINTiMINT-1375191.
STRINGi9606.ENSP00000312134.

Chemistry

DrugBankiDB00020. Sargramostim.

Protein family/group databases

MEROPSiI63.001.

Polymorphism and mutation databases

BioMutaiPRG2.
DMDMi281185479.

Proteomic databases

PaxDbiP13727.
PRIDEiP13727.

Protocols and materials databases

DNASUi5553.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311862; ENSP00000312134; ENSG00000186652.
ENST00000525955; ENSP00000433016; ENSG00000186652.
ENST00000533605; ENSP00000433231; ENSG00000186652. [P13727-2]
GeneIDi5553.
KEGGihsa:5553.
UCSCiuc001nkc.3. human. [P13727-1]

Organism-specific databases

CTDi5553.
GeneCardsiGC11M057154.
H-InvDBHIX0009634.
HGNCiHGNC:9362. PRG2.
HPAiHPA038515.
MIMi605601. gene.
neXtProtiNX_P13727.
PharmGKBiPA33734.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266233.
GeneTreeiENSGT00440000039859.
HOGENOMiHOG000261603.
HOVERGENiHBG005583.
InParanoidiP13727.
KOiK10786.
OMAiGHWRRAH.
OrthoDBiEOG779P0F.
PhylomeDBiP13727.
TreeFamiTF336281.

Miscellaneous databases

ChiTaRSiPRG2. human.
EvolutionaryTraceiP13727.
GeneWikiiMajor_basic_protein.
GenomeRNAii5553.
NextBioi21522.
PROiP13727.
SOURCEiSearch...

Gene expression databases

CleanExiHS_MBP.
HS_PRG2.
GenevisibleiP13727. HS.

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]
ProtoNetiSearch...

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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), VARIANT TYR-206.
    Tissue: Bone marrow.
  7. "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] (ISOFORM 1), VARIANT TYR-206.
    Tissue: Placenta.
  8. "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] (ISOFORM 1), VARIANT TYR-206.
  9. "A computer system platform used to predict novel genes."
    Yu Z., Zheng Z., Tang T., Fu Y.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: PROTEIN SEQUENCE OF 106-125.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. Cited for: NITRATION.
  27. "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.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-179.

Entry informationi

Entry nameiPRG2_HUMAN
AccessioniPrimary (citable) accession number: P13727
Secondary accession number(s): A6XMW0
, B2R5I1, P81448, Q14227, Q6ICT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 15, 2009
Last modified: July 22, 2015
This is version 166 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.