GTPase HRas precursor - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

P20171 (RASH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GTPase HRas

Alternative name(s):
H-Ras-1
Transforming protein p21
c-H-ras
p21ras

Cleaved into the following chain:

GTPase HRas, N-terminally processed

Gene names

Name:	Hras1
Synonyms:	Hras

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Enzyme regulation	Alternate 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	Forms a signaling complex with RASGRP1 and DGKZ. In its GTP-bound form interacts with PLCE1. Interacts with TBC1D10C. Interacts with RGL3 and RASSF5. Interacts with HSPD1. Interacts with PDE6D. Interacts with IKZF3. Interacts with GNB2L1 By similarity. Found in a complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14. Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain). Ref.5 Ref.6 Ref.7
Subcellular location	Cell membrane. Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus By similarity. Golgi apparatus membrane; Lipid-anchor By similarity. Note: Shuttles between the plasma membrane and the Golgi apparatus By similarity. The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form. Ref.7
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 By similarity. 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 By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Ras family.
Sequence caution	The sequence AAH86608.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH99130.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell membrane Golgi apparatus Membrane
Disease	Proto-oncogene
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Palmitate Prenylation S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Ras protein signal transduction Inferred from mutant phenotype. Source: RGD apoptotic process Inferred from mutant phenotype. Source: RGD positive regulation of DNA replication Inferred from mutant phenotype. Source: RGD positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype. Source: RGD social behavior Inferred from expression pattern. Source: RGD
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: RGD plasma membrane Inferred from direct assay Ref.7. Source: UniProtKB soluble fraction Inferred from direct assay. Source: RGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 186

186

GTPase HRas

PRO_0000043000

Initiator methionine

Removed; alternate By similarity

Chain

2 – 186

185

GTPase HRas, N-terminally processed

PRO_0000326479

Propeptide

187 – 189

Removed in mature form By similarity

PRO_0000043001

Regions

Nucleotide binding

10 – 17

GTP

Nucleotide binding

57 – 61

GTP

Nucleotide binding

116 – 119

GTP

Region

166 – 185

Hypervariable region

Motif

32 – 40

Effector region

Amino acid modifications

Modified residue

N-acetylmethionine; in GTPase HRas; alternate By similarity

Modified residue

N-acetylthreonine; in GTPase HRas, N-terminally processed By similarity

Modified residue

118

S-nitrosocysteine By similarity

Modified residue

186

Cysteine methyl ester Ref.4

Lipidation

181

S-palmitoyl cysteine By similarity

Lipidation

184

S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate By similarity

Lipidation

184

S-palmitoyl cysteine; alternate

Lipidation

186

S-farnesyl cysteine Ref.4

Experimental info

Mutagenesis

N → G: Interacts and partially stimulates PLCE1; when associated with L-61. Ref.5

Mutagenesis

T → S: No interaction and stimulation of PLCE1; when associated with L-61. Ref.5

Mutagenesis

E → G: Reduced interaction and stimulation of PLCE1; when associated with L-61. Ref.5

Mutagenesis

D → N: Reduced interaction and stimulation of PLCE1; when associated with L-61. Ref.5

Mutagenesis

Y → C: No interaction and stimulation of PLCE1; when associated with L-61. Ref.5

Mutagenesis

Q → L: Constitutively active. Constitutively interacts and stimulates PLCE1 phospholipase activity. Reduced interaction and stimulation of PLCE1; when associated with G-37 and N-38. No interaction and stimulation of PLCE1; when associated with S-35 and C-40. Interacts and partially stimulates PLCE1; when associated with G-26. Interacts but does not stimulate PLCE1; when associated with S-186. Ref.5

Mutagenesis

186

C → S: Interacts but does not stimulate PLCE1; when associated with L-61. Ref.5

Sequence conflict

179

P → L in AAA42009. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P20171 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: EE6DC2D933E2856A
Show »

FASTA

189

21,298

        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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the two rat cellular rasH genes." Ruta M., Wolford R., Dhar R., Defeo-Jones D., Ellis R.W., Scolnick E.M. Mol. Cell. Biol. 6:1706-1710(1986) [PubMed: 3023901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Thymus.
[3]	"Nucleotide sequence and characterization of the 5' flanking region of the rat Ha-ras protooncogene." Damante G., Filetti S., Rapoport B. Proc. Natl. Acad. Sci. U.S.A. 84:774-778(1987) [PubMed: 3027702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
[4]	"Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases." Clarke S., Vogel J.P., Deschenes R.J., Stock J. Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988) [PubMed: 3290900] [Abstract] Cited for: ISOPRENYLATION AT CYS-186, CLEAVAGE, METHYLATION AT CYS-186.
[5]	"Phospholipase C(epsilon): a novel Ras effector." Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V. EMBO J. 20:743-754(2001) [PubMed: 11179219] [Abstract] Cited for: INTERACTION WITH PLCE1, MUTAGENESIS OF ASN-26; THR-35; GLU-37; ASP-38; TYR-40; GLN-61 AND CYS-186.
[6]	"Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras effector." Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J., Snider W.D., Siderovski D.P. PLoS ONE 4:E4884-E4884(2009) [PubMed: 19319189] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH BRAF; MAP2K1; MAPK3 AND RGS14, INTERACTION WITH RGS14.
[7]	"RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways." Shu F.J., Ramineni S., Hepler J.R. Cell. Signal. 22:366-376(2010) [PubMed: 19878719] [Abstract] Cited for: INTERACTION WITH RGS14, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13011 Genomic DNA. Translation: AAA42009.1. BC086608 mRNA. Translation: AAH86608.1. Different initiation. BC099130 mRNA. Translation: AAH99130.1. Different initiation. M15188 Genomic DNA. Translation: AAA42008.1.
IPI	IPI00196529.
PIR	A25229.
RefSeq	NP_001091711.1. NM_001098241.1. NP_001123913.1. NM_001130441.1.
UniGene	Rn.102180.
3D structure databases
ProteinModelPortal	P20171.
SMR	P20171. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4996514.
STRING	P20171.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	293621.
KEGG	rno:293621.
UCSC	BC086608. rat.
Organism-specific databases
CTD	3265.
RGD	2827. Hras.
Phylogenomic databases
eggNOG	maNOG09147.
HOVERGEN	HBG009351.
InParanoid	P20171.
PhylomeDB	P20171.
Enzyme and pathway databases
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
Genevestigator	P20171.
GermOnline	ENSRNOG00000016611. Rattus norvegicus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
KO	K02833.
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RASH_RAT

Accession

Primary (citable) accession number: P20171
Secondary accession number(s): Q4KLL6, Q5RJJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents