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P04196

- HRG_HUMAN

UniProt

P04196 - HRG_HUMAN

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Protein

Histidine-rich glycoprotein

Gene

HRG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis.14 Publications

Cofactori

Zn2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei439 – 4402Cleavage; by plasminBy similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase inhibitor activity Source: InterPro
  2. heme binding Source: UniProtKB
  3. heparan sulfate proteoglycan binding Source: UniProtKB
  4. heparin binding Source: UniProtKB
  5. immunoglobulin binding Source: UniProtKB
  6. metal ion binding Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. serine-type endopeptidase inhibitor activity Source: Ensembl
  9. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. blood coagulation Source: Reactome
  3. chemotaxis Source: UniProtKB-KW
  4. defense response to fungus Source: UniProtKB
  5. fibrinolysis Source: Reactome
  6. heme export Source: Ensembl
  7. negative regulation of angiogenesis Source: UniProtKB
  8. negative regulation of blood vessel endothelial cell migration Source: UniProtKB
  9. negative regulation of cell adhesion Source: UniProtKB
  10. negative regulation of cell adhesion mediated by integrin Source: UniProtKB
  11. negative regulation of cell growth Source: UniProtKB
  12. negative regulation of cell proliferation Source: UniProtKB
  13. negative regulation of endothelial cell chemotaxis Source: UniProtKB
  14. negative regulation of fibrinolysis Source: Ensembl
  15. negative regulation of lamellipodium assembly Source: UniProtKB
  16. negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
  17. platelet activation Source: UniProtKB
  18. platelet degranulation Source: Reactome
  19. positive regulation of apoptotic process Source: UniProtKB
  20. positive regulation of blood vessel remodeling Source: UniProtKB
  21. positive regulation of focal adhesion assembly Source: UniProtKB
  22. positive regulation of immune response to tumor cell Source: UniProtKB
  23. regulation of actin cytoskeleton organization Source: UniProtKB
  24. regulation of blood coagulation Source: UniProtKB
  25. regulation of gene expression Source: UniProtKB
  26. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  27. regulation of platelet activation Source: UniProtKB
  28. regulation of protein complex assembly Source: UniProtKB
  29. regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
  30. response to organic cyclic compound Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Blood coagulation, Chemotaxis, Fibrinolysis, Hemostasis

Keywords - Ligandi

Copper, Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.

Protein family/group databases

MEROPSiI25.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine-rich glycoprotein
Alternative name(s):
Histidine-proline-rich glycoprotein
Short name:
HPRG
Gene namesi
Name:HRG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:5181. HRG.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. endolysosome Source: Ensembl
  3. extracellular region Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. phagolysosome membrane Source: Ensembl
  6. plasma membrane Source: Reactome
  7. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11) [MIM:613116]: A hemostatic disorder characterized by a tendency to thrombosis.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031G → E in THPH11; HRG Tokushima 1; results in increased intracellular degradation and reduced protein secretion. 1 Publication
VAR_063000
Natural varianti241 – 2411C → R in THPH11; HRG Tokushima 2; results in increased intracellular degradation and reduced protein secretion. 1 Publication
VAR_063001

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

MIMi613116. phenotype.
Orphaneti217467. Hereditary thrombophilia due to congenital histidine-rich (poly-L) glycoprotein deficiency.
PharmGKBiPA29455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 525507Histidine-rich glycoproteinPRO_0000006709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 504By similarity
Glycosylationi63 – 631N-linked (GlcNAc...)2 Publications
Disulfide bondi78 ↔ 89By similarity
Disulfide bondi105 ↔ 126By similarity
Glycosylationi125 – 1251N-linked (GlcNAc...)2 Publications
Disulfide bondi203 ↔ 417By similarity
Disulfide bondi218 ↔ 241By similarity
Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tether plasminogen to the cell surface. On platelet activation, releases a 33 kDa antiangiogenic peptide which encompasses the HRR. Also cleaved in the C-terminal by plasmin.3 Publications
N-glycosylated.3 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP04196.
PeptideAtlasiP04196.
PRIDEiP04196.

2D gel databases

SWISS-2DPAGEP04196.

PTM databases

PhosphoSiteiP04196.

Expressioni

Tissue specificityi

Expressed in macrophages and in malignant cells. Expressed by the liver and secreted in plasma (at protein level).3 Publications

Gene expression databases

BgeeiP04196.
CleanExiHS_HRG.
GenevestigatoriP04196.

Organism-specific databases

HPAiHPA050269.
HPA054598.

Interactioni

Subunit structurei

Interacts (via the HRR domain) with TPM1; the interaction appears to contribute to the antiangiogenic properties of the HRR domain. Interacts with THBS2; the interaction blocks the antiangiogenic effect of THBS2 with CD36 (By similarity). Interacts with THBS1 (via the TSP type I repeats); the interaction blocks the antiangiogenic effect of THBS1 with CD3. Interacts with PLG (via its Kringle domains); the interaction tethers PLG to the cell surface and enhances its activation. Interacts with HPSE; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts (via the HRR domain) with TMP1; the interaction partially mediates the antiangiogenic properties of HRG. Interacts with kappa and lambda light chains of IgG molecules. Interacts with ATP5A1; the interaction occurs on the surface of T-cells and alters their cell morphology in concert with CONA. Binds IgG molecules containing kappa and lambda light chains and inhibits the formation of insoluble immunoglobulin complexes. Interacts with F12; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding to HRG, inhibits factor XII autoactivation and contact-initiated coagulation.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RCHY1Q96PM53EBI-3915012,EBI-947779
SPy_2034Q99XU04EBI-3915012,EBI-8852705From a different organism.

Protein-protein interaction databases

BioGridi109509. 8 interactions.
DIPiDIP-47264N.
IntActiP04196. 11 interactions.
STRINGi9606.ENSP00000232003.

Structurei

3D structure databases

ProteinModelPortaliP04196.
SMRiP04196. Positions 141-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 136118Cystatin 1Add
BLAST
Domaini137 – 254118Cystatin 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 8444Interaction with ATP5A1Add
BLAST
Regioni348 – 38235Necessary for endothelial cell focal adhesions and anti-angiogenic activitiesAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi276 – 32146Pro-richAdd
BLAST
Compositional biasi350 – 497148His/Pro-rich (HRR)Add
BLAST

Domaini

The His/Pro-rich (HRR) region contains approximately 12 tandem internal repeats of the 5-residue G[H/P][H/P]PH consensus sequence. HRR binds heparan sulfate and possesses antiangiogenic, antibacterial and antifungal properties through binding Candida cells, and preferentially lysing the ergosterol-containing liposomes at low pH. The tandem repeats also bind divalent metal ions and heme.
The cystatin domains can also bind heparan sulfate. Binding is enhanced in the presence of zinc ions.

Sequence similaritiesi

Contains 2 cystatin domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG75740.
GeneTreeiENSGT00730000111384.
HOGENOMiHOG000090255.
HOVERGENiHBG004597.
InParanoidiP04196.
OMAiRTNYYVD.
OrthoDBiEOG7HXCSK.
PhylomeDBiP04196.
TreeFamiTF333729.

Family and domain databases

InterProiIPR000010. Prot_inh_cystat.
[Graphical view]
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04196-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALIAALLL ITLQYSCAVS PTDCSAVEPE AEKALDLINK RRRDGYLFQL
60 70 80 90 100
LRIADAHLDR VENTTVYYLV LDVQESDCSV LSRKYWNDCE PPDSRRPSEI
110 120 130 140 150
VIGQCKVIAT RHSHESQDLR VIDFNCTTSS VSSALANTKD SPVLIDFFED
160 170 180 190 200
TERYRKQANK ALEKYKEEND DFASFRVDRI ERVARVRGGE GTGYFVDFSV
210 220 230 240 250
RNCPRHHFPR HPNVFGFCRA DLFYDVEALD LESPKNLVIN CEVFDPQEHE
260 270 280 290 300
NINGVPPHLG HPFHWGGHER SSTTKPPFKP HGSRDHHHPH KPHEHGPPPP
310 320 330 340 350
PDERDHSHGP PLPQGPPPLL PMSCSSCQHA TFGTNGAQRH SHNNNSSDLH
360 370 380 390 400
PHKHHSHEQH PHGHHPHAHH PHEHDTHRQH PHGHHPHGHH PHGHHPHGHH
410 420 430 440 450
PHGHHPHCHD FQDYGPCDPP PHNQGHCCHG HGPPPGHLRR RGPGKGPRPF
460 470 480 490 500
HCRQIGSVYR LPPLRKGEVL PLPEANFPSF PLPHHKHPLK PDNQPFPQSV
510 520
SESCPGKFKS GFPQVSMFFT HTFPK
Length:525
Mass (Da):59,578
Last modified:March 20, 1987 - v1
Checksum:iA2B124D6CE93114F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791S → L.
Corresponds to variant rs4516605 [ dbSNP | Ensembl ].
VAR_048856
Natural varianti103 – 1031G → E in THPH11; HRG Tokushima 1; results in increased intracellular degradation and reduced protein secretion. 1 Publication
VAR_063000
Natural varianti118 – 1181D → G.
Corresponds to variant rs3733008 [ dbSNP | Ensembl ].
VAR_020488
Natural varianti180 – 1801I → T.
Corresponds to variant rs10770 [ dbSNP | Ensembl ].
VAR_022080
Natural varianti204 – 2041P → S.
Corresponds to variant rs9898 [ dbSNP | Ensembl ].
VAR_014528
Natural varianti241 – 2411C → R in THPH11; HRG Tokushima 2; results in increased intracellular degradation and reduced protein secretion. 1 Publication
VAR_063001
Natural varianti340 – 3401H → R.
Corresponds to variant rs2228243 [ dbSNP | Ensembl ].
VAR_020489
Natural varianti436 – 4361G → R.
Corresponds to variant rs2229331 [ dbSNP | Ensembl ].
VAR_024427
Natural varianti448 – 4481R → C.
Corresponds to variant rs1042445 [ dbSNP | Ensembl ].
VAR_024428
Natural varianti493 – 4931N → I.
Corresponds to variant rs1042464 [ dbSNP | Ensembl ].
VAR_024429

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13149 mRNA. Translation: AAA52694.1.
AB005803 Genomic DNA. Translation: BAA21613.1.
CH471052 Genomic DNA. Translation: EAW78183.1.
CH471052 Genomic DNA. Translation: EAW78184.1.
BC069574 mRNA. Translation: AAH69574.1.
BC150591 mRNA. Translation: AAI50592.1.
Z17218 Genomic DNA. Translation: CAA78925.1.
CCDSiCCDS3280.1.
PIRiA01287. KGHUGH.
RefSeqiNP_000403.1. NM_000412.3.
UniGeneiHs.1498.

Genome annotation databases

EnsembliENST00000232003; ENSP00000232003; ENSG00000113905.
GeneIDi3273.
KEGGihsa:3273.
UCSCiuc003fqq.3. human.

Polymorphism databases

DMDMi123523.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13149 mRNA. Translation: AAA52694.1 .
AB005803 Genomic DNA. Translation: BAA21613.1 .
CH471052 Genomic DNA. Translation: EAW78183.1 .
CH471052 Genomic DNA. Translation: EAW78184.1 .
BC069574 mRNA. Translation: AAH69574.1 .
BC150591 mRNA. Translation: AAI50592.1 .
Z17218 Genomic DNA. Translation: CAA78925.1 .
CCDSi CCDS3280.1.
PIRi A01287. KGHUGH.
RefSeqi NP_000403.1. NM_000412.3.
UniGenei Hs.1498.

3D structure databases

ProteinModelPortali P04196.
SMRi P04196. Positions 141-254.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109509. 8 interactions.
DIPi DIP-47264N.
IntActi P04196. 11 interactions.
STRINGi 9606.ENSP00000232003.

Protein family/group databases

MEROPSi I25.022.

PTM databases

PhosphoSitei P04196.

Polymorphism databases

DMDMi 123523.

2D gel databases

SWISS-2DPAGE P04196.

Proteomic databases

PaxDbi P04196.
PeptideAtlasi P04196.
PRIDEi P04196.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000232003 ; ENSP00000232003 ; ENSG00000113905 .
GeneIDi 3273.
KEGGi hsa:3273.
UCSCi uc003fqq.3. human.

Organism-specific databases

CTDi 3273.
GeneCardsi GC03P186378.
HGNCi HGNC:5181. HRG.
HPAi HPA050269.
HPA054598.
MIMi 142640. gene.
613116. phenotype.
neXtProti NX_P04196.
Orphaneti 217467. Hereditary thrombophilia due to congenital histidine-rich (poly-L) glycoprotein deficiency.
PharmGKBi PA29455.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75740.
GeneTreei ENSGT00730000111384.
HOGENOMi HOG000090255.
HOVERGENi HBG004597.
InParanoidi P04196.
OMAi RTNYYVD.
OrthoDBi EOG7HXCSK.
PhylomeDBi P04196.
TreeFami TF333729.

Enzyme and pathway databases

Reactomei REACT_641. Dissolution of Fibrin Clot.

Miscellaneous databases

GeneWikii HRG_(gene).
GenomeRNAii 3273.
NextBioi 12999.
PROi P04196.
SOURCEi Search...

Gene expression databases

Bgeei P04196.
CleanExi HS_HRG.
Genevestigatori P04196.

Family and domain databases

InterProi IPR000010. Prot_inh_cystat.
[Graphical view ]
Pfami PF00031. Cystatin. 1 hit.
[Graphical view ]
SMARTi SM00043. CY. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA."
    Koide T., Foster D.C., Yoshitake S., Davie E.W.
    Biochemistry 25:2220-2225(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Wakabayashi S., Takahashi K., Tokunaga F., Koide T.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Testis.
  5. "Evidence for the absence of intron H of the histidine-rich glycoprotein (HRG) gene: genetic mapping and in situ localization of HRG to chromosome 3q28-q29."
    Hennis B.C., Frants R.R., Bakker E., Vossen R.H., van der Poort E.W., Blonden L.A., Cox S., Khan P.M., Spurr N.K., Kluft C.
    Genomics 19:195-197(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-247.
  6. Cited for: PROTEIN SEQUENCE OF 19-27.
    Tissue: Plasma.
  7. "Human serum histidine-rich glycoprotein. I. Interactions with heme, metal ions and organic ligands."
    Morgan W.T.
    Biochim. Biophys. Acta 535:319-333(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME- AND METAL-BINDING.
  8. "Differential binding of histidine-rich glycoprotein (HRG) to human IgG subclasses and IgG molecules containing kappa and lambda light chains."
    Gorgani N.N., Parish C.R., Altin J.G.
    J. Biol. Chem. 274:29633-29640(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IMMUNOGLOBULIN G SUBCLASSES.
  9. "Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1."
    Simantov R., Febbraio M., Crombie R., Asch A.S., Nachman R.L., Silverstein R.L.
    J. Clin. Invest. 107:45-52(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THBS1, FUNCTION.
  10. "Histidine-proline-rich glycoprotein has potent antiangiogenic activity mediated through the histidine-proline-rich domain."
    Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., Parry G.C., Shaw D.E., Zhang J.C., Rabbani S.A., McCrae K.R., Mazar A.P., Morgan W.T., Donate F.
    Cancer Res. 62:5344-5350(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF HIS/PRO-RICH DOMAIN.
  11. "A fragment of histidine-rich glycoprotein is a potent inhibitor of tumor vascularization."
    Olsson A.K., Larsson H., Dixelius J., Johansson I., Lee C., Oellig C., Bjork I., Claesson-Welsh L.
    Cancer Res. 64:599-605(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A NEGATIVE REGULATOR OF ANGIOGENESIS, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
  12. "Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities."
    Donate F., Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., Tel-Tsur Z., Shaw D.E., Morgan W.T., Mazar A.P.
    Cancer Res. 64:5812-5817(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE HIS/PRO-RICH REGION, INTERACTION WITH TPM1.
  13. "Histidine-rich glycoprotein binds to cell-surface heparan sulfate via its N-terminal domain following Zn2+ chelation."
    Jones A.L., Hulett M.D., Parish C.R.
    J. Biol. Chem. 279:30114-30122(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEPARAN SULFATE-BINDING, METAL-BINDING.
  14. "Plasminogen is tethered with high affinity to the cell surface by the plasma protein, histidine-rich glycoprotein."
    Jones A.L., Hulett M.D., Altin J.G., Hogg P., Parish C.R.
    J. Biol. Chem. 279:38267-38276(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLG, FUNCTION.
  15. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-63; ASN-125 AND ASN-344.
    Tissue: Plasma.
  16. "Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein."
    Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I., Claesson-Welsh L.
    Cancer Res. 66:2089-2097(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE HIS/PRO-RICH REGION AS A NEGATIVE REGULATOR OF ANGIOGENESIS.
  17. "The anti-angiogenic His/Pro-rich fragment of histidine-rich glycoprotein binds to endothelial cell heparan sulfate in a Zn2+-dependent manner."
    Vanwildemeersch M., Olsson A.K., Gottfridsson E., Claesson-Welsh L., Lindahl U., Spillmann D.
    J. Biol. Chem. 281:10298-10304(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE HIS/PRO-RICH REGION AS A NEGATIVE REGULATOR OF ANGIOGENESIS, COFACTOR, ZINC-BINDING, HEPARIN- AND HEPARAN SULFATE-BINDING.
  18. "Regulation of histidine-rich glycoprotein (HRG) function via plasmin-mediated proteolytic cleavage."
    Poon I.K., Olsson A.K., Hulett M.D., Parish C.R.
    Biochem. J. 424:27-37(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, HEPARAN SULFATE-BINDING, INTERACTION WITH PLG, FUNCTION.
  19. "High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells."
    Ohta T., Ikemoto Y., Usami A., Koide T., Wakabayashi S.
    Biochim. Biophys. Acta 1788:1099-1107(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATP5A1, FUNCTION, GLYCOSYLATION AT ASN-63, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "Histidine-rich glycoprotein and concanavalin A synergistically stimulate the phosphatidylinositol 3-kinase-independent signaling pathway in leukocytes leading to increased cell adhesion and changes in cell morphology."
    Ohta T., Ikemoto Y., Saeki K., Koide T., Wakabayashi S.
    Cell. Immunol. 259:5-12(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Probing the Cu(2+) and Zn(2+) binding affinity of histidine-rich glycoprotein."
    Jancso A., Kolozsi A., Gyurcsik B., Nagy N.V., Gajda T.
    J. Inorg. Biochem. 103:1634-1643(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING.
  22. "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-125.
    Tissue: Liver.
  23. "Activated platelets provide a functional microenvironment for the antiangiogenic fragment of histidine-rich glycoprotein."
    Thulin A., Ringvall M., Dimberg A., Karehed K., Vaisanen T., Vaisanen M.R., Hamad O., Wang J., Bjerkvig R., Nilsson B., Pihlajaniemi T., Akerud H., Pietras K., Jahnen-Dechent W., Siegbahn A., Olsson A.K.
    Mol. Cancer Res. 7:1792-1802(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  24. "Histidine-rich glycoprotein binds heparanase and regulates its enzymatic activity and cell surface interactions."
    Poon I.K., Yee D.Y., Jones A.L., Wood R.J., Davis D.S., Freeman C., Parish C.R., Hulett M.D.
    Int. J. Biochem. Cell Biol. 42:1507-1516(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPSE.
  25. "Histidine-rich glycoprotein functions cooperatively with cell surface heparan sulfate on phagocytes to promote necrotic cell uptake."
    Poon I.K., Parish C.R., Hulett M.D.
    J. Leukoc. Biol. 88:559-569(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HEPARIN- AND HEPARAN SULFATE-BINDING.
  26. "Histidine-rich glycoprotein binds factor XIIa with high affinity and inhibits contact-initiated coagulation."
    Macquarrie J.L., Stafford A.R., Yau J.W., Leslie B.A., Vu T.T., Fredenburgh J.C., Weitz J.I.
    Blood 117:4134-4141(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH F12, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  27. Cited for: FUNCTION AS A TUMOR SUPPRESSOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  28. "HRG Tokushima: molecular and cellular characterization of histidine-rich glycoprotein (HRG) deficiency."
    Shigekiyo T., Yoshida H., Matsumoto K., Azuma H., Wakabayashi S., Saito S., Fujikawa K., Koide T.
    Blood 91:128-133(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH11 GLU-103, CHARACTERIZATION OF VARIANT THPH11 GLU-103.
  29. "Histidine-rich glycoprotein (HRG) Tokushima 2: novel HRG deficiency, molecular and cellular characterization."
    Shigekiyo T., Yoshida H., Kanagawa Y., Satoh K., Wakabayashi S., Matsumoto T., Koide T.
    Thromb. Haemost. 84:675-679(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH11 ARG-241, CHARACTERIZATION OF VARIANT THPH11 ARG-241.

Entry informationi

Entry nameiHRG_HUMAN
AccessioniPrimary (citable) accession number: P04196
Secondary accession number(s): B9EK35, D3DNU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 26, 2014
This is version 155 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 3
    Human chromosome 3: 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