Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P01112 (RASH_HUMAN)

Protein

GTPase HRas

Gene

HRAS

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

Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151).4 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 17GTP8
Nucleotide bindingi57 – 61GTP5
Nucleotide bindingi116 – 119GTP4

<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

  • GDP binding Source: CAFA
  • GTPase activity Source: WormBase
  • GTP binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-112412 SOS-mediated signalling
R-HSA-1169092 Activation of RAS in B cells
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1250196 SHC1 events in ERBB2 signaling
R-HSA-1250347 SHC1 events in ERBB4 signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-167044 Signalling to RAS
R-HSA-171007 p38MAPK events
R-HSA-179812 GRB2 events in EGFR signaling
R-HSA-180336 SHC1 events in EGFR signaling
R-HSA-186763 Downstream signal transduction
R-HSA-1963640 GRB2 events in ERBB2 signaling
R-HSA-210993 Tie2 Signaling
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-2424491 DAP12 signaling
R-HSA-2428933 SHC-related events triggered by IGF1R
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654693 FRS-mediated FGFR1 signaling
R-HSA-5654699 SHC-mediated cascade:FGFR2
R-HSA-5654700 FRS-mediated FGFR2 signaling
R-HSA-5654704 SHC-mediated cascade:FGFR3
R-HSA-5654706 FRS-mediated FGFR3 signaling
R-HSA-5654712 FRS-mediated FGFR4 signaling
R-HSA-5654719 SHC-mediated cascade:FGFR4
R-HSA-5655253 Signaling by FGFR2 in disease
R-HSA-5655291 Signaling by FGFR4 in disease
R-HSA-5655302 Signaling by FGFR1 in disease
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5675221 Negative regulation of MAPK pathway
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802953 RAS signaling downstream of NF1 loss-of-function variants
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-74751 Insulin receptor signalling cascade
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8851805 MET activates RAS signaling
R-HSA-8853334 Signaling by FGFR3 fusions in cancer
R-HSA-8853338 Signaling by FGFR3 point mutants in cancer
R-HSA-9026519 Activated NTRK2 signals through RAS
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-9028731 Activated NTRK2 signals through FRS2 and FRS3
R-HSA-9034864 Activated NTRK3 signals through RAS

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P01112

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P01112

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01112

<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:
GTPase HRas
Alternative name(s):
H-Ras-1
Ha-Ras
Transforming protein p21
c-H-ras
p21ras
Cleaved into the following chain:
GTPase HRas, N-terminally processed
<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:HRAS
Synonyms:HRAS1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000174775.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:5173 HRAS

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		190020 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01112

<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

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

<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

Costello syndrome (CSTLO)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities.
See also OMIM:218040
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_02610612G → A in CSTLO. 3 PublicationsCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_04597512G → C in CSTLO. 2 PublicationsCorresponds to variant dbSNP:rs104894229EnsemblClinVar.1
Natural variantiVAR_06881612G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_04597612G → E in CSTLO. 1 Publication1
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229EnsemblClinVar.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_02610713G → C in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894228EnsemblClinVar.1
Natural variantiVAR_02610813G → D in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894226EnsemblClinVar.1
Natural variantiVAR_06881837E → EE in CSTLO. 1 Publication1
Natural variantiVAR_04597858T → I in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917758EnsemblClinVar.1
Natural variantiVAR_045981117K → R in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894227EnsemblClinVar.1
Natural variantiVAR_045982146A → T in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894231EnsemblClinVar.1
Natural variantiVAR_045983146A → V in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917759EnsemblClinVar.1
Congenital myopathy with excess of muscle spindles (CMEMS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionVariant of Costello syndrome.
See also OMIM:218040
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229EnsemblClinVar.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_04597722Q → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917757EnsemblClinVar.1
Natural variantiVAR_04598063E → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917756EnsemblClinVar.1
Thyroid cancer, non-medullary, 2 (NMTC2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms.
See also OMIM:188470
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04597961Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant dbSNP:rs28933406EnsemblClinVar.1
Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors.1 Publication
Bladder cancer (BLC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences.
See also OMIM:109800
Schimmelpenning-Feuerstein-Mims syndrome (SFM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis.
See also OMIM:163200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06881713G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant dbSNP:rs104894228EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi17S → N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. 2 Publications1
Mutagenesisi26N → G: Loss of interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi29V → A: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi32Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi34P → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi35T → S: Loss of interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi37E → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi38D → N: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi39S → C: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi59A → T: Loss of GTPase activity and creation of an autophosphorylation site. 1
Mutagenesisi61Q → I: Moderately increased transformation of cultured cell lines. 1 Publication1
Mutagenesisi61Q → V: Strongly increased transformation of cultured cell lines. 1 Publication1
Mutagenesisi83A → T: GTP-binding activity reduced by factor of 30. 1 Publication1
Mutagenesisi118C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. 2 Publications1
Mutagenesisi119D → N: Loss of GTP-binding activity. 1 Publication1
Mutagenesisi144T → I: GTP-binding activity reduced by factor of 25. 1 Publication1
Mutagenesisi164 – 165RQ → AV: Loss of GTP-binding activity. 1 Publication2
Mutagenesisi181C → S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184. 2 Publications1
Mutagenesisi184C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine stimulation of Ras-GTPase activity. Mainly localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-181. 3 Publications1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		3265

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		HRAS

MalaCards human disease database

More...MalaCardsi		HRAS
MIMi109800 phenotype
163200 phenotype
188470 phenotype
218040 phenotype

Open Targets

More...OpenTargetsi		ENSG00000174775

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

More...Orphaneti		3071 Costello syndrome
146 Differentiated thyroid carcinoma
2612 Linear nevus sebaceus syndrome
2874 Phakomatosis pigmentokeratotica
79414 Woolly hair nevus

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29444

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2167

Drug and drug target database

More...DrugBanki		DB04315 Guanosine-5'-Diphosphate
DB04137 Guanosine-5'-Triphosphate
DB03226 Trifluoroethanol

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2822

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HRAS

Domain mapping of disease mutations (DMDM)

More...DMDMi		131869

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000429961 – 186GTPase HRasAdd BLAST186
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00003264762 – 186GTPase HRas, N-terminally processedAdd BLAST185
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000042997187 – 189Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine; in GTPase HRas; alternate1 Publication1
Modified residuei2N-acetylthreonine; in GTPase HRas, N-terminally processed1 Publication1
Modified residuei118S-nitrosocysteine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi181S-palmitoyl cysteine4 Publications1
Lipidationi184S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication1
Lipidationi184S-palmitoyl cysteine; alternate4 Publications1
Modified residuei186Cysteine methyl ester1 Publication1
Lipidationi186S-farnesyl cysteine1 Publication1

<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

Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.
S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.
Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Prenylation, S-nitrosylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P01112

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P01112

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

More...PaxDbi		P01112

PeptideAtlas

More...PeptideAtlasi		P01112

PRoteomics IDEntifications database

More...PRIDEi		P01112

ProteomicsDB human proteome resource

More...ProteomicsDBi		12698 [P01112-2]
51321
51322 [P01112-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01112

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

More...PhosphoSitePlusi		P01112

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P01112

<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

Widely expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000174775 Expressed in 227 organ(s), highest expression level in skin of abdomen

CleanEx database of gene expression profiles

More...CleanExi		HS_HRAS

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P01112 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01112 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002015
HPA049830

<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

In its GTP-bound form interacts with PLCE1 (PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706). Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1 (PubMed:14500341). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (PubMed:10608844, PubMed:11598133).By similarity10 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		109501, 106 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-395 GTPase HRAS - Son of sevenless homolog 1 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P01112

Database of interacting proteins

More...DIPi		DIP-1050N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P01112

Protein interaction database and analysis system

More...IntActi		P01112, 62 interactors

Molecular INTeraction database

More...MINTi		P01112

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000309845

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P01112

<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

Secondary structure

1189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
121PX-ray1.54A1-166[»]
1AA9NMR-A1-171[»]
1AGPX-ray2.30A1-166[»]
1BKDX-ray2.80R1-166[»]
1CLUX-ray1.70A1-166[»]
1CRPNMR-A1-166[»]
1CRQNMR-A1-166[»]
1CRRNMR-A1-166[»]
1CTQX-ray1.26A1-166[»]
1GNPX-ray2.70A1-166[»]
1GNQX-ray2.50A1-166[»]
1GNRX-ray1.85A1-166[»]
1HE8X-ray3.00B1-166[»]
1IAQX-ray2.90A/B/C1-166[»]
1IOZX-ray2.00A1-171[»]
1JAHX-ray1.80A1-166[»]
1JAIX-ray1.80A1-166[»]
1K8RX-ray3.00A1-166[»]
1LF0X-ray1.70A1-166[»]
1LF5X-ray1.70A1-166[»]
1LFDX-ray2.10B/D1-167[»]
1NVUX-ray2.20Q/R1-166[»]
1NVVX-ray2.18Q/R1-166[»]
1NVWX-ray2.70Q/R1-166[»]
1NVXX-ray3.20Q/R1-166[»]
1P2SX-ray2.45A1-166[»]
1P2TX-ray2.00A1-166[»]
1P2UX-ray2.00A1-166[»]
1P2VX-ray2.30A1-166[»]
1PLJX-ray2.80A1-166[»]
1PLKX-ray2.80A1-166[»]
1PLLX-ray2.80A1-166[»]
1Q21X-ray2.20A1-171[»]
1QRAX-ray1.60A1-166[»]
1RVDX-ray1.90A1-166[»]
1WQ1X-ray2.50R1-166[»]
1XCMX-ray1.84A1-167[»]
1XD2X-ray2.70A/B1-166[»]
1XJ0X-ray1.70A1-166[»]
1ZVQX-ray2.00A1-166[»]
1ZW6X-ray1.50A1-166[»]
221PX-ray2.30A1-166[»]
2C5LX-ray1.90A/B1-166[»]
2CE2X-ray1.00X1-166[»]
2CL0X-ray1.80X1-166[»]
2CL6X-ray1.24X1-166[»]
2CL7X-ray1.25X1-166[»]
2CLCX-ray1.30X1-166[»]
2CLDX-ray1.22X1-166[»]
2EVWX-ray1.05X1-166[»]
2GDPmodel-A1-171[»]
2LCFNMR-A1-166[»]
2LWINMR-A1-166[»]
2N42NMR-A1-166[»]
2N46NMR-A1-166[»]
2Q21X-ray2.20A1-171[»]
2QUZX-ray1.49A1-166[»]
2RGAX-ray1.90A1-166[»]
2RGBX-ray1.35A1-166[»]
2RGCX-ray1.60A1-166[»]
2RGDX-ray2.00A1-166[»]
2RGEX-ray1.40A1-166[»]
2RGGX-ray1.45A1-166[»]
2UZIX-ray2.00R1-166[»]
2VH5X-ray2.70R1-166[»]
2X1VX-ray1.70A1-166[»]
3DDCX-ray1.80A1-166[»]
3I3SX-ray1.36R1-166[»]
3K8YX-ray1.30A1-166[»]
3K9LX-ray1.80A/B/C1-166[»]
3K9NX-ray2.00A1-166[»]
3KKMX-ray1.70A1-166[»]
3KKNX-ray2.09A1-166[»]
3KUDX-ray2.15A1-166[»]
3L8YX-ray2.02A1-166[»]
3L8ZX-ray1.44A1-166[»]
3LBHX-ray1.85A1-166[»]
3LBIX-ray2.09A1-166[»]
3LBNX-ray1.86A1-166[»]
3LO5X-ray2.57A/C/E1-166[»]
3OIUX-ray1.32A1-166[»]
3OIVX-ray1.84A1-166[»]
3OIWX-ray1.30A1-166[»]
3RRYX-ray1.60A1-166[»]
3RRZX-ray1.60A1-166[»]
3RS0X-ray1.40A1-166[»]
3RS2X-ray1.84A1-166[»]
3RS3X-ray1.52A1-166[»]
3RS4X-ray1.70A1-166[»]
3RS5X-ray1.68A1-166[»]
3RS7X-ray1.70A1-166[»]
3RSLX-ray1.70A1-166[»]
3RSOX-ray1.60A1-166[»]
3TGPX-ray1.31A1-166[»]
421PX-ray2.20A1-166[»]
4DLRX-ray1.32A1-166[»]
4DLSX-ray1.82A1-166[»]
4DLTX-ray1.70A1-166[»]
4DLUX-ray1.60A1-166[»]
4DLVX-ray1.57A1-166[»]
4DLWX-ray1.72A1-166[»]
4DLXX-ray1.73A1-166[»]
4DLYX-ray1.57A1-166[»]
4DLZX-ray1.66A1-166[»]
4DSTX-ray2.30A2-167[»]
4DSUX-ray1.70A2-167[»]
4EFLX-ray1.90A1-166[»]
4EFMX-ray1.90A1-166[»]
4EFNX-ray2.30A1-166[»]
4G0NX-ray2.45A1-166[»]
4G3XX-ray3.25A1-166[»]
4K81X-ray2.40B/D/F/H1-166[»]
4L9SX-ray1.61A1-166[»]
4L9WX-ray1.95A1-166[»]
4NYIX-ray2.96Q/R1-166[»]
4NYJX-ray2.85Q/R1-166[»]
4NYMX-ray3.55Q/R1-166[»]
4Q21X-ray2.00A1-189[»]
4RSGneutron diffraction1.91A1-166[»]
4URUX-ray2.83R1-166[»]
4URVX-ray2.58R1-166[»]
4URWX-ray2.76R1-166[»]
4URXX-ray2.49R1-166[»]
4URYX-ray2.47R1-166[»]
4URZX-ray2.24R1-166[»]
4US0X-ray2.17R1-166[»]
4US1X-ray2.65R1-166[»]
4US2X-ray2.48R1-166[»]
4XVQX-ray1.89A1-166[»]
4XVRX-ray2.03A1-166[»]
521PX-ray2.60A1-166[»]
5B2ZX-ray1.56A1-166[»]
5B30X-ray1.60A1-166[»]
5E95X-ray1.40A1-166[»]
5P21X-ray1.35A1-166[»]
5VBEX-ray1.57A1-166[»]
5VBZX-ray2.20A/B/C1-166[»]
5WDOX-ray1.65A1-166[»]
5WDPX-ray1.35A1-166[»]
5WDQX-ray1.25A1-166[»]
5WFOX-ray1.99Q/R1-166[»]
5WFPX-ray2.08Q/R1-166[»]
5WFQX-ray2.26Q/R1-166[»]
5WFRX-ray2.46Q/R1-166[»]
5WPLX-ray2.15A/D/G/J1-166[»]
5X9SX-ray2.50A1-166[»]
5ZC6NMR-A1-166[»]
621PX-ray2.40A1-166[»]
6AMBX-ray2.50A1-168[»]
6AXGX-ray3.30B/D/F/H/J/L1-166[»]
6BVIX-ray1.75A/C1-166[»]
6BVJX-ray1.75A/C1-166[»]
6BVKX-ray1.80A/C1-166[»]
6BVLX-ray1.75A/C1-166[»]
6BVMX-ray1.80A/C1-166[»]
6D55X-ray1.68A/C1-166[»]
6D56X-ray1.68A/C1-166[»]
6D59X-ray1.70A/C1-166[»]
6D5EX-ray1.75A/C1-166[»]
6D5GX-ray1.92A/C1-166[»]
6D5HX-ray1.80A/C1-166[»]
6D5JX-ray1.75A/C1-166[»]
6D5LX-ray1.70A/C1-166[»]
6D5MX-ray2.08Q/R1-166[»]
6D5VX-ray2.04Q/R1-166[»]
6Q21X-ray1.95A/B/C/D1-171[»]
721PX-ray2.00A1-166[»]
821PX-ray1.50A1-166[»]

Database of protein disorder

More...DisProti		DP00153

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P01112

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

More...SMRi		P01112

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P01112

<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

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>Regioni166 – 185Hypervariable regionAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi32 – 40Effector region9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0395 Eukaryota
COG1100 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155653

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233973

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG009351

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01112

KEGG Orthology (KO)

More...KOi		K02833

Identification of Orthologs from Complete Genome Data

More...OMAi		QHIPICL

Database of Orthologous Groups

More...OrthoDBi		1557546at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01112

TreeFam database of animal gene trees

More...TreeFami		TF312796

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type

The PANTHER Classification System

More...PANTHERi		PTHR24070 PTHR24070, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51421 RAS, 1 hit

<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>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P01112-1) [UniParc]FASTAAdd to basket
Also known as: H-Ras4A, p21

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET 
        60         70         80         90        100
CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI 
       110        120        130        140        150
KRVKDSDDVP MVLVGNKCDL AARTVESRQA QDLARSYGIP YIETSAKTRQ 
       160        170        180 
GVEDAFYTLV REIRQHKLRK LNPPDESGPG CMSCKCVLS
Length:189
Mass (Da):21,298
Last modified:July 21, 1986 - 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:iEE6DC2D933E2856A
GO
Isoform 2 (identifier: P01112-2) [UniParc]FASTAAdd to basket
Also known as: H-RasIDX, p19

The sequence of this isoform differs from the canonical sequence as follows:
     152-189: VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS → SRSGSSSSSGTLWDPPGPM

Show »
Length:170
Mass (Da):18,870
Checksum:iC3364C8DC783C191
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0J9YXG8A0A0J9YXG8_HUMAN
GTPase HRas
HRAS
14Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 6223±2 Da from positions 112 - 166. Determined by ESI. 1 Publication
Molecular mass is 6253±2 Da from positions 112 - 166. Determined by ESI. Includes one nitric oxide molecule.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02610612G → A in CSTLO. 3 PublicationsCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_04597512G → C in CSTLO. 2 PublicationsCorresponds to variant dbSNP:rs104894229EnsemblClinVar.1
Natural variantiVAR_06881612G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_04597612G → E in CSTLO. 1 Publication1
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229EnsemblClinVar.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230EnsemblClinVar.1
Natural variantiVAR_02610713G → C in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894228EnsemblClinVar.1
Natural variantiVAR_02610813G → D in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894226EnsemblClinVar.1
Natural variantiVAR_06881713G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant dbSNP:rs104894228EnsemblClinVar.1
Natural variantiVAR_04597722Q → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917757EnsemblClinVar.1
Natural variantiVAR_06881837E → EE in CSTLO. 1 Publication1
Natural variantiVAR_04597858T → I in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917758EnsemblClinVar.1
Natural variantiVAR_04597961Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant dbSNP:rs28933406EnsemblClinVar.1
Natural variantiVAR_00683861Q → L in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines. 1 PublicationCorresponds to variant dbSNP:rs121913233EnsemblClinVar.1
Natural variantiVAR_04598063E → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917756EnsemblClinVar.1
Natural variantiVAR_07825989S → C Found in a patient with severe fetal hydrops and pleural effusion; unknown pathological significance; decreased activation of Ras protein signal transduction. 1 PublicationCorresponds to variant dbSNP:rs755322824EnsemblClinVar.1
Natural variantiVAR_045981117K → R in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894227EnsemblClinVar.1
Natural variantiVAR_045982146A → T in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894231EnsemblClinVar.1
Natural variantiVAR_045983146A → V in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917759EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041597152 – 189VEDAF…KCVLS → SRSGSSSSSGTLWDPPGPM in isoform 2. 2 PublicationsAdd BLAST38

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J00277 Genomic DNA Translation: AAB02605.1
AJ437024 mRNA Translation: CAD24594.1
AF493916 mRNA Translation: AAM12630.1
CR536579 mRNA Translation: CAG38816.1
CR542271 mRNA Translation: CAG47067.1
BT019421 mRNA Translation: AAV38228.1
EF015887 Genomic DNA Translation: ABI97389.1
AB451336 mRNA Translation: BAG70150.1
AB451485 mRNA Translation: BAG70299.1
CH471158 Genomic DNA Translation: EAX02337.1
CH471158 Genomic DNA Translation: EAX02338.1
BC006499 mRNA Translation: AAH06499.1
BC095471 mRNA Translation: AAH95471.1
M17232 Genomic DNA Translation: AAA35685.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS7698.1 [P01112-1]
CCDS7699.1 [P01112-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A93299 TVHUH

NCBI Reference Sequences

More...RefSeqi		NP_001123914.1, NM_001130442.2 [P01112-1]
NP_001304983.1, NM_001318054.1
NP_005334.1, NM_005343.3 [P01112-1]
NP_789765.1, NM_176795.4 [P01112-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.37003

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000311189; ENSP00000309845; ENSG00000174775 [P01112-1]
ENST00000397594; ENSP00000380722; ENSG00000174775 [P01112-2]
ENST00000397596; ENSP00000380723; ENSG00000174775 [P01112-1]
ENST00000417302; ENSP00000388246; ENSG00000174775 [P01112-2]
ENST00000451590; ENSP00000407586; ENSG00000174775 [P01112-1]
ENST00000493230; ENSP00000434023; ENSG00000174775 [P01112-2]
ENST00000610977; ENSP00000480686; ENSG00000276536 [P01112-1]
ENST00000615062; ENSP00000482366; ENSG00000276536 [P01112-1]
ENST00000616241; ENSP00000480317; ENSG00000276536 [P01112-2]
ENST00000631404; ENSP00000488757; ENSG00000276536 [P01112-1]
ENST00000631967; ENSP00000488225; ENSG00000276536 [P01112-2]
ENST00000634098; ENSP00000488296; ENSG00000276536 [P01112-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3265

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3265

UCSC genome browser

More...UCSCi		uc010qvw.3 human [P01112-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00277 Genomic DNA Translation: AAB02605.1
AJ437024 mRNA Translation: CAD24594.1
AF493916 mRNA Translation: AAM12630.1
CR536579 mRNA Translation: CAG38816.1
CR542271 mRNA Translation: CAG47067.1
BT019421 mRNA Translation: AAV38228.1
EF015887 Genomic DNA Translation: ABI97389.1
AB451336 mRNA Translation: BAG70150.1
AB451485 mRNA Translation: BAG70299.1
CH471158 Genomic DNA Translation: EAX02337.1
CH471158 Genomic DNA Translation: EAX02338.1
BC006499 mRNA Translation: AAH06499.1
BC095471 mRNA Translation: AAH95471.1
M17232 Genomic DNA Translation: AAA35685.1
CCDSiCCDS7698.1 [P01112-1]
CCDS7699.1 [P01112-2]
PIRiA93299 TVHUH
RefSeqiNP_001123914.1, NM_001130442.2 [P01112-1]
NP_001304983.1, NM_001318054.1
NP_005334.1, NM_005343.3 [P01112-1]
NP_789765.1, NM_176795.4 [P01112-2]
UniGeneiHs.37003

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
121PX-ray1.54A1-166[»]
1AA9NMR-A1-171[»]
1AGPX-ray2.30A1-166[»]
1BKDX-ray2.80R1-166[»]
1CLUX-ray1.70A1-166[»]
1CRPNMR-A1-166[»]
1CRQNMR-A1-166[»]
1CRRNMR-A1-166[»]
1CTQX-ray1.26A1-166[»]
1GNPX-ray2.70A1-166[»]
1GNQX-ray2.50A1-166[»]
1GNRX-ray1.85A1-166[»]
1HE8X-ray3.00B1-166[»]
1IAQX-ray2.90A/B/C1-166[»]
1IOZX-ray2.00A1-171[»]
1JAHX-ray1.80A1-166[»]
1JAIX-ray1.80A1-166[»]
1K8RX-ray3.00A1-166[»]
1LF0X-ray1.70A1-166[»]
1LF5X-ray1.70A1-166[»]
1LFDX-ray2.10B/D1-167[»]
1NVUX-ray2.20Q/R1-166[»]
1NVVX-ray2.18Q/R1-166[»]
1NVWX-ray2.70Q/R1-166[»]
1NVXX-ray3.20Q/R1-166[»]
1P2SX-ray2.45A1-166[»]
1P2TX-ray2.00A1-166[»]
1P2UX-ray2.00A1-166[»]
1P2VX-ray2.30A1-166[»]
1PLJX-ray2.80A1-166[»]
1PLKX-ray2.80A1-166[»]
1PLLX-ray2.80A1-166[»]
1Q21X-ray2.20A1-171[»]
1QRAX-ray1.60A1-166[»]
1RVDX-ray1.90A1-166[»]
1WQ1X-ray2.50R1-166[»]
1XCMX-ray1.84A1-167[»]
1XD2X-ray2.70A/B1-166[»]
1XJ0X-ray1.70A1-166[»]
1ZVQX-ray2.00A1-166[»]
1ZW6X-ray1.50A1-166[»]
221PX-ray2.30A1-166[»]
2C5LX-ray1.90A/B1-166[»]
2CE2X-ray1.00X1-166[»]
2CL0X-ray1.80X1-166[»]
2CL6X-ray1.24X1-166[»]
2CL7X-ray1.25X1-166[»]
2CLCX-ray1.30X1-166[»]
2CLDX-ray1.22X1-166[»]
2EVWX-ray1.05X1-166[»]
2GDPmodel-A1-171[»]
2LCFNMR-A1-166[»]
2LWINMR-A1-166[»]
2N42NMR-A1-166[»]
2N46NMR-A1-166[»]
2Q21X-ray2.20A1-171[»]
2QUZX-ray1.49A1-166[»]
2RGAX-ray1.90A1-166[»]
2RGBX-ray1.35A1-166[»]
2RGCX-ray1.60A1-166[»]
2RGDX-ray2.00A1-166[»]
2RGEX-ray1.40A1-166[»]
2RGGX-ray1.45A1-166[»]
2UZIX-ray2.00R1-166[»]
2VH5X-ray2.70R1-166[»]
2X1VX-ray1.70A1-166[»]
3DDCX-ray1.80A1-166[»]
3I3SX-ray1.36R1-166[»]
3K8YX-ray1.30A1-166[»]
3K9LX-ray1.80A/B/C1-166[»]
3K9NX-ray2.00A1-166[»]
3KKMX-ray1.70A1-166[»]
3KKNX-ray2.09A1-166[»]
3KUDX-ray2.15A1-166[»]
3L8YX-ray2.02A1-166[»]
3L8ZX-ray1.44A1-166[»]
3LBHX-ray1.85A1-166[»]
3LBIX-ray2.09A1-166[»]
3LBNX-ray1.86A1-166[»]
3LO5X-ray2.57A/C/E1-166[»]
3OIUX-ray1.32A1-166[»]
3OIVX-ray1.84A1-166[»]
3OIWX-ray1.30A1-166[»]
3RRYX-ray1.60A1-166[»]
3RRZX-ray1.60A1-166[»]
3RS0X-ray1.40A1-166[»]
3RS2X-ray1.84A1-166[»]
3RS3X-ray1.52A1-166[»]
3RS4X-ray1.70A1-166[»]
3RS5X-ray1.68A1-166[»]
3RS7X-ray1.70A1-166[»]
3RSLX-ray1.70A1-166[»]
3RSOX-ray1.60A1-166[»]
3TGPX-ray1.31A1-166[»]
421PX-ray2.20A1-166[»]
4DLRX-ray1.32A1-166[»]
4DLSX-ray1.82A1-166[»]
4DLTX-ray1.70A1-166[»]
4DLUX-ray1.60A1-166[»]
4DLVX-ray1.57A1-166[»]
4DLWX-ray1.72A1-166[»]
4DLXX-ray1.73A1-166[»]
4DLYX-ray1.57A1-166[»]
4DLZX-ray1.66A1-166[»]
4DSTX-ray2.30A2-167[»]
4DSUX-ray1.70A2-167[»]
4EFLX-ray1.90A1-166[»]
4EFMX-ray1.90A1-166[»]
4EFNX-ray2.30A1-166[»]
4G0NX-ray2.45A1-166[»]
4G3XX-ray3.25A1-166[»]
4K81X-ray2.40B/D/F/H1-166[»]
4L9SX-ray1.61A1-166[»]
4L9WX-ray1.95A1-166[»]
4NYIX-ray2.96Q/R1-166[»]
4NYJX-ray2.85Q/R1-166[»]
4NYMX-ray3.55Q/R1-166[»]
4Q21X-ray2.00A1-189[»]
4RSGneutron diffraction1.91A1-166[»]
4URUX-ray2.83R1-166[»]
4URVX-ray2.58R1-166[»]
4URWX-ray2.76R1-166[»]
4URXX-ray2.49R1-166[»]
4URYX-ray2.47R1-166[»]
4URZX-ray2.24R1-166[»]
4US0X-ray2.17R1-166[»]
4US1X-ray2.65R1-166[»]
4US2X-ray2.48R1-166[»]
4XVQX-ray1.89A1-166[»]
4XVRX-ray2.03A1-166[»]
521PX-ray2.60A1-166[»]
5B2ZX-ray1.56A1-166[»]
5B30X-ray1.60A1-166[»]
5E95X-ray1.40A1-166[»]
5P21X-ray1.35A1-166[»]
5VBEX-ray1.57A1-166[»]
5VBZX-ray2.20A/B/C1-166[»]
5WDOX-ray1.65A1-166[»]
5WDPX-ray1.35A1-166[»]
5WDQX-ray1.25A1-166[»]
5WFOX-ray1.99Q/R1-166[»]
5WFPX-ray2.08Q/R1-166[»]
5WFQX-ray2.26Q/R1-166[»]
5WFRX-ray2.46Q/R1-166[»]
5WPLX-ray2.15A/D/G/J1-166[»]
5X9SX-ray2.50A1-166[»]
5ZC6NMR-A1-166[»]
621PX-ray2.40A1-166[»]
6AMBX-ray2.50A1-168[»]
6AXGX-ray3.30B/D/F/H/J/L1-166[»]
6BVIX-ray1.75A/C1-166[»]
6BVJX-ray1.75A/C1-166[»]
6BVKX-ray1.80A/C1-166[»]
6BVLX-ray1.75A/C1-166[»]
6BVMX-ray1.80A/C1-166[»]
6D55X-ray1.68A/C1-166[»]
6D56X-ray1.68A/C1-166[»]
6D59X-ray1.70A/C1-166[»]
6D5EX-ray1.75A/C1-166[»]
6D5GX-ray1.92A/C1-166[»]
6D5HX-ray1.80A/C1-166[»]
6D5JX-ray1.75A/C1-166[»]
6D5LX-ray1.70A/C1-166[»]
6D5MX-ray2.08Q/R1-166[»]
6D5VX-ray2.04Q/R1-166[»]
6Q21X-ray1.95A/B/C/D1-171[»]
721PX-ray2.00A1-166[»]
821PX-ray1.50A1-166[»]
DisProtiDP00153
ProteinModelPortaliP01112
SMRiP01112
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109501, 106 interactors
ComplexPortaliCPX-395 GTPase HRAS - Son of sevenless homolog 1 complex
CORUMiP01112
DIPiDIP-1050N
ELMiP01112
IntActiP01112, 62 interactors
MINTiP01112
STRINGi9606.ENSP00000309845

Chemistry databases

BindingDBiP01112
ChEMBLiCHEMBL2167
DrugBankiDB04315 Guanosine-5'-Diphosphate
DB04137 Guanosine-5'-Triphosphate
DB03226 Trifluoroethanol
GuidetoPHARMACOLOGYi2822

PTM databases

iPTMnetiP01112
PhosphoSitePlusiP01112
SwissPalmiP01112

Polymorphism and mutation databases

BioMutaiHRAS
DMDMi131869

Proteomic databases

EPDiP01112
jPOSTiP01112
PaxDbiP01112
PeptideAtlasiP01112
PRIDEiP01112
ProteomicsDBi12698 [P01112-2]
51321
51322 [P01112-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3265
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311189; ENSP00000309845; ENSG00000174775 [P01112-1]
ENST00000397594; ENSP00000380722; ENSG00000174775 [P01112-2]
ENST00000397596; ENSP00000380723; ENSG00000174775 [P01112-1]
ENST00000417302; ENSP00000388246; ENSG00000174775 [P01112-2]
ENST00000451590; ENSP00000407586; ENSG00000174775 [P01112-1]
ENST00000493230; ENSP00000434023; ENSG00000174775 [P01112-2]
ENST00000610977; ENSP00000480686; ENSG00000276536 [P01112-1]
ENST00000615062; ENSP00000482366; ENSG00000276536 [P01112-1]
ENST00000616241; ENSP00000480317; ENSG00000276536 [P01112-2]
ENST00000631404; ENSP00000488757; ENSG00000276536 [P01112-1]
ENST00000631967; ENSP00000488225; ENSG00000276536 [P01112-2]
ENST00000634098; ENSP00000488296; ENSG00000276536 [P01112-2]
GeneIDi3265
KEGGihsa:3265
UCSCiuc010qvw.3 human [P01112-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3265
DisGeNETi3265
EuPathDBiHostDB:ENSG00000174775.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		HRAS
GeneReviewsiHRAS
HGNCiHGNC:5173 HRAS
HPAiCAB002015
HPA049830
MalaCardsiHRAS
MIMi109800 phenotype
163200 phenotype
188470 phenotype
190020 gene
218040 phenotype
neXtProtiNX_P01112
OpenTargetsiENSG00000174775
Orphaneti3071 Costello syndrome
146 Differentiated thyroid carcinoma
2612 Linear nevus sebaceus syndrome
2874 Phakomatosis pigmentokeratotica
79414 Woolly hair nevus
PharmGKBiPA29444

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0395 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00940000155653
HOGENOMiHOG000233973
HOVERGENiHBG009351
InParanoidiP01112
KOiK02833
OMAiQHIPICL
OrthoDBi1557546at2759
PhylomeDBiP01112
TreeFamiTF312796

Enzyme and pathway databases

ReactomeiR-HSA-112412 SOS-mediated signalling
R-HSA-1169092 Activation of RAS in B cells
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1250196 SHC1 events in ERBB2 signaling
R-HSA-1250347 SHC1 events in ERBB4 signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-167044 Signalling to RAS
R-HSA-171007 p38MAPK events
R-HSA-179812 GRB2 events in EGFR signaling
R-HSA-180336 SHC1 events in EGFR signaling
R-HSA-186763 Downstream signal transduction
R-HSA-1963640 GRB2 events in ERBB2 signaling
R-HSA-210993 Tie2 Signaling
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-2424491 DAP12 signaling
R-HSA-2428933 SHC-related events triggered by IGF1R
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654693 FRS-mediated FGFR1 signaling
R-HSA-5654699 SHC-mediated cascade:FGFR2
R-HSA-5654700 FRS-mediated FGFR2 signaling
R-HSA-5654704 SHC-mediated cascade:FGFR3
R-HSA-5654706 FRS-mediated FGFR3 signaling
R-HSA-5654712 FRS-mediated FGFR4 signaling
R-HSA-5654719 SHC-mediated cascade:FGFR4
R-HSA-5655253 Signaling by FGFR2 in disease
R-HSA-5655291 Signaling by FGFR4 in disease
R-HSA-5655302 Signaling by FGFR1 in disease
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5675221 Negative regulation of MAPK pathway
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802953 RAS signaling downstream of NF1 loss-of-function variants
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-74751 Insulin receptor signalling cascade
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8851805 MET activates RAS signaling
R-HSA-8853334 Signaling by FGFR3 fusions in cancer
R-HSA-8853338 Signaling by FGFR3 point mutants in cancer
R-HSA-9026519 Activated NTRK2 signals through RAS
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-9028731 Activated NTRK2 signals through FRS2 and FRS3
R-HSA-9034864 Activated NTRK3 signals through RAS
SABIO-RKiP01112
SignaLinkiP01112
SIGNORiP01112

Miscellaneous databases

EvolutionaryTraceiP01112

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HRAS

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

More...GenomeRNAii		3265

Protein Ontology

More...PROi		PR:P01112

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000174775 Expressed in 227 organ(s), highest expression level in skin of abdomen
CleanExiHS_HRAS
ExpressionAtlasiP01112 baseline and differential
GenevisibleiP01112 HS

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type
PANTHERiPTHR24070 PTHR24070, 1 hit
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51421 RAS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...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 nameiRASH_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: P01112
Secondary accession number(s): B5BUA0
, Q14080, Q6FHV9, Q9BR65, Q9UCE2
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 16, 2019
This is version 239 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

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again