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P01112 (RASH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 190. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTPase HRas
Alternative name(s):
H-Ras-1
Ha-Ras
Transforming protein p21
c-H-ras
p21ras

Cleaved into the following chain:

  1. GTPase HRas, N-terminally processed
Gene names
Name:HRAS
Synonyms:HRAS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Ref.4 Ref.20 Ref.40

Enzyme regulation

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).

Subunit structure

In its GTP-bound form interacts with PLCE1. Interacts with TBC1D10C. Interacts with RGL3. Interacts with HSPD1. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) By similarity. Forms a signaling complex with RASGRP1 and DGKZ. Interacts with RASSF5. Interacts with PDE6D. Interacts with IKZF3. Interacts with GNB2L1. 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. Ref.4 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.31

Subcellular location

Cell membrane. Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note: The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form By similarity. Shuttles between the plasma membrane and the Golgi apparatus. Ref.4 Ref.30

Isoform 2: Nucleus. Cytoplasm. Cytoplasmperinuclear region. Note: Colocalizes with GNB2L1 to the perinuclear region. Ref.4 Ref.30

Tissue specificity

Widely expressed. Ref.4

Post-translational modification

Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. Ref.18 Ref.19 Ref.29 Ref.30

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. Ref.18 Ref.19 Ref.29 Ref.30

Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs) By similarity. Ref.12

Involvement in disease

Faciocutaneoskeletal syndrome (FCSS) [MIM:218040]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28 Ref.45 Ref.46 Ref.47 Ref.48 Ref.50 Ref.51 Ref.52

Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.49

Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A rare type of thyroid cancer accounting for only about 3-10% of all differentiated thyroid cancers. These neoplasms are considered a variant of follicular carcinoma of the thyroid and are referred to as follicular carcinoma, oxyphilic type.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

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.

Bladder cancer (BLC) [MIM:109800]: A 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Defects in HRAS are the cause of oral squamous cell carcinoma (OSCC). Ref.43

Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.53

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Mass spectrometry

Molecular mass is 6223±2 Da from positions 112 - 166. Determined by ESI. Ref.20

Molecular mass is 6253±2 Da from positions 112 - 166. Determined by ESI. Includes one nitric oxide molecule. Ref.20

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Proto-oncogene
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Palmitate
Prenylation
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

GTP catabolic process

Inferred from electronic annotation. Source: InterPro

MAPK cascade

Traceable author statement. Source: Reactome

Ras protein signal transduction

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

activation of MAPKK activity

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell cycle arrest

Inferred from direct assay PubMed 9054499. Source: BHF-UCL

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 9020890. Source: ProtInc

cellular senescence

Inferred from direct assay PubMed 9054499. Source: BHF-UCL

chemotaxis

Traceable author statement PubMed 10848592. Source: ProtInc

endocytosis

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Inferred from direct assay PubMed 9054499. Source: BHF-UCL

negative regulation of Rho GTPase activity

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from direct assay PubMed 9054499. Source: BHF-UCL

negative regulation of gene expression

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ morphogenesis

Traceable author statement PubMed 10848592. Source: ProtInc

positive regulation of DNA replication

Inferred from direct assay PubMed 9765203. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 22065586. Source: BHF-UCL

positive regulation of JNK cascade

Inferred from direct assay PubMed 22065586. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of MAPK cascade

Inferred from direct assay PubMed 9765203. Source: BHF-UCL

positive regulation of Rac GTPase activity

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin cytoskeleton reorganization

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 9765203. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 20154697. Source: BHF-UCL

positive regulation of miRNA metabolic process

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 22065586. Source: BHF-UCL

positive regulation of ruffle assembly

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 22065586PubMed 23027131. Source: BHF-UCL

positive regulation of wound healing

Inferred from direct assay PubMed 23027131. Source: BHF-UCL

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement PubMed 8607982. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

social behavior

Inferred from electronic annotation. Source: Ensembl

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.4. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Traceable author statement PubMed 10842192. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from direct assay Ref.4. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.37. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.21Ref.22Ref.23Ref.24Ref.26Ref.4PubMed 2122974PubMed 22020336. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BRAPQ7Z5693EBI-350145,EBI-349900
Pik3caP423372EBI-350145,EBI-641748From a different organism.
PIK3CDO003292EBI-350145,EBI-718309
PIK3CDO00329-22EBI-350145,EBI-6470902
Rabac1Q9Z0S94EBI-350145,EBI-476965From a different organism.
RAF1P0404914EBI-350145,EBI-365996
Rapgef4Q9EQZ63EBI-350145,EBI-772212From a different organism.
RASSF1Q9NS23-22EBI-350145,EBI-438698
RASSF5Q8WWW02EBI-350145,EBI-367390
Rassf5Q5EBH111EBI-350145,EBI-960530From a different organism.
Rassf5Q5EBH1-23EBI-350145,EBI-960547From a different organism.
RIN1Q136715EBI-350145,EBI-366017
SOS1Q078898EBI-350145,EBI-297487

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01112-1)

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.
Isoform 2 (identifier: P01112-2)

Also known as: H-RasIDX; p19;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 186186GTPase HRas
PRO_0000042996
Initiator methionine11Removed; alternate Ref.12
Chain2 – 186185GTPase HRas, N-terminally processed
PRO_0000326476
Propeptide187 – 1893Removed in mature form
PRO_0000042997

Regions

Nucleotide binding10 – 178GTP
Nucleotide binding57 – 615GTP
Nucleotide binding116 – 1194GTP
Region166 – 18520Hypervariable region
Motif32 – 409Effector region

Amino acid modifications

Modified residue11N-acetylmethionine; in GTPase HRas; alternate Ref.12
Modified residue21N-acetylthreonine; in GTPase HRas, N-terminally processed Ref.12
Modified residue1181S-nitrosocysteine Ref.20
Modified residue1861Cysteine methyl ester Ref.19
Lipidation1811S-palmitoyl cysteine Ref.18 Ref.19 Ref.29 Ref.30
Lipidation1841S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate
Lipidation1841S-palmitoyl cysteine; alternate Ref.18 Ref.19 Ref.29 Ref.30
Lipidation1861S-farnesyl cysteine Ref.19

Natural variations

Alternative sequence152 – 18938VEDAF…KCVLS → SRSGSSSSSGTLWDPPGPM in isoform 2.
VSP_041597
Natural variant121G → A in FCSS. Ref.45 Ref.46 Ref.47
VAR_026106
Natural variant121G → C in FCSS. Ref.47 Ref.51
VAR_045975
Natural variant121G → D in FCSS; severe mutation. Ref.51
VAR_068816
Natural variant121G → E in FCSS. Ref.47
VAR_045976
Natural variant121G → S in FCSS, OSCC and CMEMS. Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49
VAR_006837
Natural variant121G → V in FCSS, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane; loss of interaction with and recruitment to plasma membrane of PLCE1 when associated with F-32; loss of interaction with PLCE1 when associated with G-26, F-32 and S-35; no effect on interaction with PLCE1 when associated with A-29, G-34, G-37, N-38 and C-39; no effect on subcellular location of isoform 2. Ref.23 Ref.28 Ref.45 Ref.49
VAR_006836
Natural variant131G → C in FCSS. Ref.46
VAR_026107
Natural variant131G → D in FCSS. Ref.45
VAR_026108
Natural variant131G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. Ref.53
VAR_068817
Natural variant221Q → K in CMEMS. Ref.49
VAR_045977
Natural variant371E → EE in FCSS. Ref.52
VAR_068818
Natural variant581T → I in FCSS. Ref.50
VAR_045978
Natural variant611Q → K in follicular thyroid carcinoma samples; somatic mutation; increases transformation of cultured cell lines. Ref.41 Ref.44
Corresponds to variant rs28933406 [ dbSNP | Ensembl ].
VAR_045979
Natural variant611Q → L in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines. Ref.41
VAR_006838
Natural variant631E → K in CMEMS. Ref.49
VAR_045980
Natural variant1171K → R in FCSS. Ref.47
VAR_045981
Natural variant1461A → T in FCSS. Ref.48
VAR_045982
Natural variant1461A → V in FCSS. Ref.50
VAR_045983

Experimental info

Mutagenesis171S → N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. Ref.4 Ref.17 Ref.23
Mutagenesis261N → G: Loss of interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis291V → A: No effect on interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis321Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis341P → G: No effect on interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis351T → S: Loss of interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis371E → G: No effect on interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis381D → N: No effect on interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis391S → C: No effect on interaction with PLCE1; when associated with V-12. Ref.17 Ref.23
Mutagenesis591A → T: Loss of GTPase activity and creation of an autophosphorylation site. Ref.17
Mutagenesis611Q → I: Moderately increased transformation of cultured cell lines. Ref.17 Ref.41
Mutagenesis611Q → V: Strongly increased transformation of cultured cell lines. Ref.17 Ref.41
Mutagenesis831A → T: GTP-binding activity reduced by factor of 30. Ref.16 Ref.17
Mutagenesis1181C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. Ref.17 Ref.20 Ref.40
Mutagenesis1191D → N: Loss of GTP-binding activity. Ref.16 Ref.17
Mutagenesis1441T → I: GTP-binding activity reduced by factor of 25. Ref.16 Ref.17
Mutagenesis164 – 1652RQ → AV: Loss of GTP-binding activity. Ref.17
Mutagenesis1811C → S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184. Ref.17 Ref.19 Ref.30
Mutagenesis1841C → 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. Ref.17 Ref.19 Ref.27 Ref.30

Secondary structure

.................................. 189
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (H-Ras4A) (p21) [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: EE6DC2D933E2856A

FASTA18921,298
        10         20         30         40         50         60 
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG 

        70         80         90        100        110        120 
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL 

       130        140        150        160        170        180 
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG 


CMSCKCVLS 

« Hide

Isoform 2 (H-RasIDX) (p19) [UniParc].

Checksum: C3364C8DC783C191
Show »

FASTA17018,870

References

« Hide 'large scale' references
[1]"Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue."
Capon D.J., Chen E.Y., Levinson A.D., Seeburg P.H., Goeddel D.V.
Nature 302:33-37(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene."
Reddy E.P.
Science 220:1061-1063(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient."
Sekiya T., Fushimi M., Hori H., Hirohashi S., Nishimura S., Sugimura T.
Proc. Natl. Acad. Sci. U.S.A. 81:4771-4775(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus."
Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C., Guinovart J.J., Bach-Elias M.
Cancer Res. 63:5178-5187(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GNB2L1, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, MUTAGENESIS OF SER-17.
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]NIEHS SNPs program
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Lung carcinoma.
[12]Bienvenut W.V., Calvo F., Kolch W.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-41; 43-117; 129-161 AND 170-185, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Mechanism of activation of a human oncogene."
Tabin C.J., Bradley S.M., Bargmann C.I., Weinberg R.A., Papageorge A.G., Scolnick E.M., Dhar R., Lowy D.R., Chang E.H.
Nature 300:143-149(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
[14]"Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay."
Honkawa H., Masahashi W., Hashimoto S., Hashimoto-Gotoh T.
Mol. Cell. Biol. 7:2933-2940(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[15]"Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP."
Loew A., Sprinzl M., Faulhammer H.G.
Eur. J. Biochem. 215:473-479(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 108-117 AND 132-153.
[16]"Isolation of ras GTP-binding mutants using an in situ colony-binding assay."
Feig L.A., Pan B.-T., Roberts T.M., Cooper G.M.
Proc. Natl. Acad. Sci. U.S.A. 83:4607-4611(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ALA-83; ASP-119 AND THR-144.
[17]"Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities."
Lacal J.C., Anderson P.S., Aaronson S.A.
EMBO J. 5:679-687(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 164-ARG-GLN-165.
[18]"All ras proteins are polyisoprenylated but only some are palmitoylated."
Hancock J.F., Magee A.I., Childs J.E., Marshall C.J.
Cell 57:1167-1177(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-181 AND CYS-184.
[19]"Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes."
Dudler T., Gelb M.H.
J. Biol. Chem. 271:11541-11547(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-181 AND CYS-184, ISOPRENYLATION AT CYS-186, METHYLATION AT CYS-186, MUTAGENESIS OF CYS-181 AND CYS-184.
[20]"A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction."
Lander H.M., Hajjar D.P., Hempstead B.L., Mirza U.A., Chait B.T., Campbell S., Quilliam L.A.
J. Biol. Chem. 272:4323-4326(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-118, FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF CYS-118.
[21]"Aiolos transcription factor controls cell death in T cells by regulating Bcl-2 expression and its cellular localization."
Romero F., Martinez-A C., Camonis J., Rebollo A.
EMBO J. 18:3419-3430(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKZF3.
[22]"RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans."
Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T., Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.
J. Biol. Chem. 274:37815-37820(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAPGEF2.
[23]"Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLCE1, CHARACTERIZATION OF VARIANT VAL-12, MUTAGENESIS OF SER-17; ASN-26; VAL-29; TYR-32; PRO-34; THR-35; GLU-37; ASP-38 AND SER-39.
[24]"Nedd4 regulates ubiquitination and stability of the guanine-nucleotide exchange factor CNrasGEF."
Pham N., Rotin D.
J. Biol. Chem. 276:46995-47003(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAPGEF2.
[25]"Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism."
Topham M.K., Prescott S.M.
J. Cell Biol. 152:1135-1143(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RASGRP1 AND DGKZ.
[26]"The complex of Arl2-GTP and PDE delta: from structure to function."
Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.
EMBO J. 21:2095-2106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE6D.
[27]"The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras."
Oliva J.L., Perez-Sala D., Castrillo A., Martinez N., Canada F.J., Bosca L., Rojas J.M.
Proc. Natl. Acad. Sci. U.S.A. 100:4772-4777(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPIDATION AT CYS-184, MUTAGENESIS OF CYS-184.
[28]"Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease."
Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.
J. Biol. Chem. 280:1790-1796(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF FCSS VARIANT VAL-12.
[29]"DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras."
Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K., Deschenes R.J., Linder M.E.
J. Biol. Chem. 280:31141-31148(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-181 AND CYS-184.
[30]"An acylation cycle regulates localization and activity of palmitoylated Ras isoforms."
Rocks O., Peyker A., Kahms M., Verveer P.J., Koerner C., Lumbierres M., Kuhlmann J., Waldmann H., Wittinghofer A., Bastiaens P.I.H.
Science 307:1746-1752(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-181 AND CYS-184, MUTAGENESIS OF CYS-181 AND CYS-184, SUBCELLULAR LOCATION.
[31]"Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin."
Pan F., Sun L., Kardian D.B., Whartenby K.A., Pardoll D.M., Liu J.O.
Nature 445:433-436(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D10C.
[32]"Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21."
de Vos A.M., Tong L., Milburn M.V., Matias P.M., Jancarik J., Noguchi S., Nishimura S., Miura K., Ohtsuka E., Kim S.-H.
Science 239:888-893(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[33]"Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation."
Pai E.F., Kabsch W., Krengel U., Holmes K.C., John J., Wittinghofer A.
Nature 341:209-214(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[34]"Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35-A resolution: implications for the mechanism of GTP hydrolysis."
Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W., Wittinghofer A.
EMBO J. 9:2351-2359(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[35]"Crystal structures at 2.2-A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP."
Tong L.A., de Vos A.M., Milburn M.V., Kim S.H.
J. Mol. Biol. 217:503-516(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[36]"Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy."
Kraulis P.J., Domaille P.J., Campbell-Burk S.L., van Aken T., Laue E.D.
Biochemistry 33:3515-3531(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-166.
[37]"The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants."
Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A.
Science 277:333-338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASGAP.
[38]"The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins."
Scheidig A.J., Burmester C., Goody R.S.
Structure 7:1311-1324(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
[39]"The structural basis for the transition from Ras-GTP to Ras-GDP."
Hall B.E., Bar-Sagi D., Nassar N.
Proc. Natl. Acad. Sci. U.S.A. 99:12138-12142(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP ANALOGS.
[40]"Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange."
Williams J.G., Pappu K., Campbell S.L.
Proc. Natl. Acad. Sci. U.S.A. 100:6376-6381(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-166, S-NITROSYLATION, FUNCTION, MUTAGENESIS OF CYS-118, IDENTIFICATION BY MASS SPECTROMETRY.
[41]"Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf."
Buhrman G., Wink G., Mattos C.
Structure 15:1618-1629(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP ANALOG, CHARACTERIZATION OF VARIANTS LEU-61 AND LYS-61, MUTAGENESIS OF GLN-61.
[42]"Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II."
Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A., Khokhlatchev A., Herrmann C.
EMBO J. 27:1995-2005(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASSF5.
[43]"The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma."
Sakai E., Rikimaru K., Ueda M., Matsumoto Y., Ishii N., Enomoto S., Yamamoto H., Tsuchida N.
Int. J. Cancer 52:867-872(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OSCC SER-12.
[44]"RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma."
Nikiforova M.N., Lynch R.A., Biddinger P.W., Alexander E.K., Dorn G.W. II, Tallini G., Kroll T.G., Nikiforov Y.E.
J. Clin. Endocrinol. Metab. 88:2318-2326(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-61, INVOLVEMENT IN SUSCEPTIBILITY TO HURTHLE CELL THYROID CARCINOMA.
[45]"Germline mutations in HRAS proto-oncogene cause Costello syndrome."
Aoki Y., Niihori T., Kawame H., Kurosawa K., Ohashi H., Tanaka Y., Filocamo M., Kato K., Suzuki Y., Kure S., Matsubara Y.
Nat. Genet. 37:1038-1040(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS ALA-12; SER-12; VAL-12 AND ASP-13.
[46]"HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation."
Gripp K.W., Lin A.E., Stabley D.L., Nicholson L., Scott C.I. Jr., Doyle D., Aoki Y., Matsubara Y., Zackai E.H., Lapunzina P., Gonzalez-Meneses A., Holbrook J., Agresta C.A., Gonzalez I.L., Sol-Church K.
Am. J. Med. Genet. A 140:1-7(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS ALA-12; SER-12 AND CYS-13.
[47]"Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases."
Kerr B., Delrue M.-A., Sigaudy S., Perveen R., Marche M., Burgelin I., Stef M., Tang B., Eden O.B., O'Sullivan J., De Sandre-Giovannoli A., Reardon W., Brewer C., Bennett C., Quarell O., M'Cann E., Donnai D., Stewart F. expand/collapse author list , Hennekam R., Cave H., Verloes A., Philip N., Lacombe D., Levy N., Arveiler B., Black G.
J. Med. Genet. 43:401-405(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS SER-12; CYS-12; GLU-12; ALA-12 AND ARG-117.
[48]"Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome."
Zampino G., Pantaleoni F., Carta C., Cobellis G., Vasta I., Neri C., Pogna E.A., De Feo E., Delogu A., Sarkozy A., Atzeri F., Selicorni A., Rauen K.A., Cytrynbaum C.S., Weksberg R., Dallapiccola B., Ballabio A., Gelb B.D., Neri G., Tartaglia M.
Hum. Mutat. 28:265-272(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS SER-12 AND THR-146.
[49]"Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation."
van der Burgt I., Kupsky W., Stassou S., Nadroo A., Barroso C., Diem A., Kratz C.P., Dvorsky R., Ahmadian M.R., Zenker M.
J. Med. Genet. 44:459-462(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMEMS VAL-12; SER-12; LYS-22 AND LYS-63.
[50]"Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype?"
Gripp K.W., Innes A.M., Axelrad M.E., Gillan T.L., Parboosingh J.S., Davies C., Leonard N.J., Lapointe M., Doyle D., Catalano S., Nicholson L., Stabley D.L., Sol-Church K.
Am. J. Med. Genet. A 146:683-690(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS ILE-58 AND VAL-146.
[51]"Severe neonatal manifestations of Costello syndrome."
Lo I.F., Brewer C., Shannon N., Shorto J., Tang B., Black G., Soo M.T., Ng D.K., Lam S.T., Kerr B.
J. Med. Genet. 45:167-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCSS ASP-12 AND CYS-12.
[52]"Duplication of Glu37 in the switch I region of HRAS impairs effector/GAP binding and underlies Costello syndrome by promoting enhanced growth factor-dependent MAPK and AKT activation."
Gremer L., De Luca A., Merbitz-Zahradnik T., Dallapiccola B., Morlot S., Tartaglia M., Kutsche K., Ahmadian M.R., Rosenberger G.
Hum. Mol. Genet. 19:790-802(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FCSS GLU-37 INS.
[53]"Postzygotic HRAS and KRAS mutations cause nevus sebaceous and Schimmelpenning syndrome."
Groesser L., Herschberger E., Ruetten A., Ruivenkamp C., Lopriore E., Zutt M., Langmann T., Singer S., Klingseisen L., Schneider-Brachert W., Toll A., Real F.X., Landthaler M., Hafner C.
Nat. Genet. 44:783-787(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SFM ARG-13, CHARACTERIZATION OF VARIANT SFM ARG-13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7698.1. [P01112-1]
CCDS7699.1. [P01112-2]
PIRTVHUH. A93299.
RefSeqNP_001123914.1. NM_001130442.1. [P01112-1]
NP_005334.1. NM_005343.2. [P01112-1]
NP_789765.1. NM_176795.3. [P01112-2]
XP_006718280.1. XM_006718217.1. [P01112-2]
XP_006725199.1. XM_006725136.1. [P01112-2]
UniGeneHs.37003.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
521PX-ray2.60A1-166[»]
5P21X-ray1.35A1-166[»]
621PX-ray2.40A1-166[»]
6Q21X-ray1.95A/B/C/D1-171[»]
721PX-ray2.00A1-166[»]
821PX-ray1.50A1-166[»]
DisProtDP00153.
ProteinModelPortalP01112.
SMRP01112. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109501. 58 interactions.
DIPDIP-1050N.
IntActP01112. 27 interactions.
MINTMINT-5002362.
STRING9606.ENSP00000309845.

Chemistry

BindingDBP01112.
ChEMBLCHEMBL2167.
DrugBankDB00605. Sulindac.

PTM databases

PhosphoSiteP01112.

Polymorphism databases

DMDM131869.

Proteomic databases

MaxQBP01112.
PaxDbP01112.
PRIDEP01112.

Protocols and materials databases

DNASU3265.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311189; 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]
GeneID3265.
KEGGhsa:3265.
UCSCuc001lpv.3. human. [P01112-1]
uc010qvw.2. human. [P01112-2]

Organism-specific databases

CTD3265.
GeneCardsGC11M000522.
GeneReviewsHRAS.
HGNCHGNC:5173. HRAS.
HPACAB002015.
MIM109800. phenotype.
163200. phenotype.
190020. gene.
218040. phenotype.
607464. phenotype.
neXtProtNX_P01112.
Orphanet3071. Costello syndrome.
2612. Linear nevus sebaceus syndrome.
2874. Phakomatosis pigmentokeratotica.
PharmGKBPA29444.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidP01112.
KOK02833.
OMAYPCIRRP.
OrthoDBEOG7QVM41.
PhylomeDBP01112.
TreeFamTF312796.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP01112.

Gene expression databases

ArrayExpressP01112.
BgeeP01112.
CleanExHS_HRAS.
GenevestigatorP01112.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01112.
GeneWikiHRAS.
GenomeRNAi3265.
NextBio12961.
PROP01112.
SOURCESearch...

Entry information

Entry nameRASH_HUMAN
AccessionPrimary (citable) accession number: P01112
Secondary accession number(s): B5BUA0 expand/collapse secondary AC list , Q14080, Q6FHV9, Q9BR65, Q9UCE2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 190 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM