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P13727

- PRG2_HUMAN

UniProt

P13727 - PRG2_HUMAN

Protein

Bone marrow proteoglycan

Gene

PRG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      Previous versions | rss
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    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

    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

    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 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)1 PublicationPROSITE-ProRule annotation
    Glycosylationi62 – 621O-linked (Xyl...) (chondroitin sulfate)2 Publications
    Glycosylationi86 – 861N-linked (GlcNAc...)2 Publications
    Disulfide bondi125 ↔ 2201 PublicationPROSITE-ProRule annotation
    Disulfide bondi169 – 169Interchain (with C-732 in PAPPA)1 PublicationPROSITE-ProRule annotation
    Disulfide bondi197 ↔ 2121 PublicationPROSITE-ProRule annotation

    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.
    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.5 Publications

    Protein-protein interaction databases

    BioGridi111544. 4 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 – 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.
    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.
    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]

    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. Align

    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

    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
    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:
    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.
    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.
    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.
    ENST00000533605; ENSP00000433231; ENSG00000186652.
    GeneIDi5553.
    KEGGihsa:5553.
    UCSCiuc001nkc.3. human.
    uc001nkd.3. human.

    Polymorphism databases

    DMDMi281185479.

    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:
    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 .
    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 .
    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 .
    ENST00000533605 ; ENSP00000433231 ; ENSG00000186652 .
    GeneIDi 5553.
    KEGGi hsa:5553.
    UCSCi uc001nkc.3. human.
    uc001nkd.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

    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: October 1, 2014
    This is version 157 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