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Entry version 192 (13 Feb 2019)
Sequence version 1 (20 Mar 1987)
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Protein

Histidine-rich glycoprotein

Gene

HRG

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding
Biological processAngiogenesis, Blood coagulation, Chemotaxis, Fibrinolysis, Hemostasis
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-75205 Dissolution of Fibrin Clot

Protein family/group databases

MEROPS protease database

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MEROPSi
I25.022

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histidine-rich glycoprotein
Alternative name(s):
Histidine-proline-rich glycoprotein
Short name:
HPRG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HRG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000113905.4

Human Gene Nomenclature Database

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HGNCi
HGNC:5181 HRG

Online Mendelian Inheritance in Man (OMIM)

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MIMi
142640 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P04196

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder characterized by a tendency to thrombosis.
See also OMIM:613116
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_063000103G → E in THPH11; HRG Tokushima 1; results in increased intracellular degradation and reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs121918122EnsemblClinVar.1
Natural variantiVAR_063001241C → R in THPH11; HRG Tokushima 2; results in increased intracellular degradation and reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs2276804Ensembl.1

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNET

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DisGeNETi
3273

MalaCards human disease database

More...
MalaCardsi
HRG
MIMi613116 phenotype

Open Targets

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OpenTargetsi
ENSG00000113905

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
217467 Hereditary thrombophilia due to congenital histidine-rich (poly-L) glycoprotein deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29455

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HRG

Domain mapping of disease mutations (DMDM)

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DMDMi
123523

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 181 PublicationAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000670919 – 525Histidine-rich glycoproteinAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi24 ↔ 504By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi63N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi78 ↔ 89By similarity
Disulfide bondi105 ↔ 126By similarity
Glycosylationi125N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi203 ↔ 417By similarity
Disulfide bondi218 ↔ 241By similarity
Glycosylationi344N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi345N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei439 – 440Cleavage; by plasminBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P04196

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P04196

PeptideAtlas

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PeptideAtlasi
P04196

PRoteomics IDEntifications database

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PRIDEi
P04196

ProteomicsDB human proteome resource

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ProteomicsDBi
51675

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P04196

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
805

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04196

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P04196

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000113905 Expressed in 84 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04196 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA050269
HPA054598

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 ATP5F1A; 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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109509, 30 interactors

Database of interacting proteins

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DIPi
DIP-47264N

Protein interaction database and analysis system

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IntActi
P04196, 14 interactors

Molecular INTeraction database

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MINTi
P04196

STRING: functional protein association networks

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STRINGi
9606.ENSP00000232003

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04196

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04196

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 136Cystatin 1Add BLAST118
Domaini137 – 254Cystatin 2Add BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni41 – 84Interaction with ATP5F1A1 PublicationAdd BLAST44
Regioni348 – 382Necessary for endothelial cell focal adhesions and anti-angiogenic activitiesAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi276 – 321Pro-richAdd BLAST46
Compositional biasi350 – 497His/Pro-rich (HRR)Add BLAST148

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IVJP Eukaryota
ENOG41117FH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153911

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000090255

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004597

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04196

Identification of Orthologs from Complete Genome Data

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OMAi
IQPFPQS

Database of Orthologous Groups

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OrthoDBi
715844at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P04196

TreeFam database of animal gene trees

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TreeFami
TF333729

Family and domain databases

Conserved Domains Database

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CDDi
cd00042 CY, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000010 Cystatin_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00031 Cystatin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00043 CY, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA2B124D6CE93114F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04885679S → L. Corresponds to variant dbSNP:rs4516605Ensembl.1
Natural variantiVAR_063000103G → E in THPH11; HRG Tokushima 1; results in increased intracellular degradation and reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs121918122EnsemblClinVar.1
Natural variantiVAR_020488118D → G. Corresponds to variant dbSNP:rs3733008Ensembl.1
Natural variantiVAR_022080180I → T. Corresponds to variant dbSNP:rs10770Ensembl.1
Natural variantiVAR_014528204P → S. Corresponds to variant dbSNP:rs9898Ensembl.1
Natural variantiVAR_063001241C → R in THPH11; HRG Tokushima 2; results in increased intracellular degradation and reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs2276804Ensembl.1
Natural variantiVAR_020489340H → R. Corresponds to variant dbSNP:rs2228243Ensembl.1
Natural variantiVAR_024427436G → R. Corresponds to variant dbSNP:rs2229331Ensembl.1
Natural variantiVAR_024428448R → C. Corresponds to variant dbSNP:rs1042445Ensembl.1
Natural variantiVAR_024429493N → I. Corresponds to variant dbSNP:rs1042464Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS3280.1

Protein sequence database of the Protein Information Resource

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PIRi
A01287 KGHUGH

NCBI Reference Sequences

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RefSeqi
NP_000403.1, NM_000412.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.1498

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000232003; ENSP00000232003; ENSG00000113905

Database of genes from NCBI RefSeq genomes

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GeneIDi
3273

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:3273

UCSC genome browser

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UCSCi
uc003fqq.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS3280.1
PIRiA01287 KGHUGH
RefSeqiNP_000403.1, NM_000412.4
UniGeneiHs.1498

3D structure databases

ProteinModelPortaliP04196
SMRiP04196
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109509, 30 interactors
DIPiDIP-47264N
IntActiP04196, 14 interactors
MINTiP04196
STRINGi9606.ENSP00000232003

Protein family/group databases

MEROPSiI25.022

PTM databases

GlyConnecti805
iPTMnetiP04196
PhosphoSitePlusiP04196

Polymorphism and mutation databases

BioMutaiHRG
DMDMi123523

2D gel databases

SWISS-2DPAGEiP04196

Proteomic databases

jPOSTiP04196
PaxDbiP04196
PeptideAtlasiP04196
PRIDEiP04196
ProteomicsDBi51675

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232003; ENSP00000232003; ENSG00000113905
GeneIDi3273
KEGGihsa:3273
UCSCiuc003fqq.5 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3273
DisGeNETi3273
EuPathDBiHostDB:ENSG00000113905.4

GeneCards: human genes, protein and diseases

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GeneCardsi
HRG
HGNCiHGNC:5181 HRG
HPAiHPA050269
HPA054598
MalaCardsiHRG
MIMi142640 gene
613116 phenotype
neXtProtiNX_P04196
OpenTargetsiENSG00000113905
Orphaneti217467 Hereditary thrombophilia due to congenital histidine-rich (poly-L) glycoprotein deficiency
PharmGKBiPA29455

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IVJP Eukaryota
ENOG41117FH LUCA
GeneTreeiENSGT00940000153911
HOGENOMiHOG000090255
HOVERGENiHBG004597
InParanoidiP04196
OMAiIQPFPQS
OrthoDBi715844at2759
PhylomeDBiP04196
TreeFamiTF333729

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-75205 Dissolution of Fibrin Clot

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
HRG human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
HRG_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
3273

Protein Ontology

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PROi
PR:P04196

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000113905 Expressed in 84 organ(s), highest expression level in liver
GenevisibleiP04196 HS

Family and domain databases

CDDicd00042 CY, 1 hit
InterProiView protein in InterPro
IPR000010 Cystatin_dom
PfamiView protein in Pfam
PF00031 Cystatin, 1 hit
SMARTiView protein in SMART
SM00043 CY, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHRG_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04196
Secondary accession number(s): B9EK35, D3DNU7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: February 13, 2019
This is version 192 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
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