Reviewed, UniProtKB/Swiss-Prot P20171 (RASH_RAT)

Names and origin

Protein names

Recommended name:
    GTPase HRas
Alternative name(s):
    Transforming protein p21
    p21ras
    H-Ras-1
    c-H-ras
Cleaved into the following chain:
    1- Recommended name:
            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 By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus membrane; Lipid-anchor By similarity. Note: Shuttles between the plasma membrane and the Golgi apparatus By similarity.
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.
Sequence similarities	Belongs to the small GTPase superfamily. Ras family.

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
Gene Ontology (GO)
Biological process	Ras protein signal transduction Inferred from mutant phenotype. Source: RGD apoptosis Inferred from mutant phenotype. Source: RGD positive regulation of DNA replication Inferred from mutant phenotype. Source: RGD protein heterooligomerization Inferred from physical interaction. Source: RGD
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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	1	1	Removed; alternate By similarity
	Chain	2 – 186	185	GTPase HRas, N-terminally processed		PRO_0000326479
	Propeptide	187 – 189	3	Removed in mature form By similarity		PRO_0000043001
Regions
	Nucleotide binding	10 – 17	8	GTP
	Nucleotide binding	57 – 61	5	GTP
	Nucleotide binding	116 – 119	4	GTP
	Region	166 – 185	20	Hypervariable region
	Motif	32 – 40	9	Effector region
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in GTPase HRas; alternate By similarity
	Modified residue	2	1	N-acetylthreonine; in GTPase HRas, N-terminally processed By similarity
	Modified residue	118	1	S-nitrosocysteine By similarity
	Modified residue	186	1	Cysteine methyl ester Ref.3
	Lipidation	181	1	S-palmitoyl cysteine By similarity
	Lipidation	184	1	S-palmitoyl cysteine
	Lipidation	186	1	S-farnesyl cysteine
Experimental info
	Mutagenesis	26	1	N → G: Interacts and partially stimulates PLCE1; when associated with L-61. Ref.4
	Mutagenesis	35	1	T → S: No interaction and stimulation of PLCE1; when associated with L-61. Ref.4
	Mutagenesis	37	1	E → G: Reduced interaction and stimulation of PLCE1; when associated with L-61. Ref.4
	Mutagenesis	38	1	D → N: Reduced interaction and stimulation of PLCE1; when associated with L-61. Ref.4
	Mutagenesis	40	1	Y → C: No interaction and stimulation of PLCE1; when associated with L-61. Ref.4
	Mutagenesis	61	1	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.4
	Mutagenesis	186	1	C → S: Interacts but does not stimulate PLCE1; when associated with L-61. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P20171-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: EE6DD9B533E2856A	FASTA	189	21,314
	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 LNPPDESGLG CMSCKCVLS

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]	"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.
[3]	"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.
[4]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M13011 Genomic DNA. Translation: AAA42009.1. M15188 Genomic DNA. Translation: AAA42008.1.
IPI	IPI00196529.
PIR	A25229.
UniGene	Rn.102180 Rn.129785
3D structure databases
HSSP	HSSP built from PDB template 6Q21 based on UniProtKB P01112.
SMR	P20171. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
STRING	P20171.
Genome annotation databases
Ensembl	ENSRNOT00000022363; ENSRNOP00000022363; ENSRNOG00000016611; Rattus norvegicus. [Genome view]
UCSC	BC086608. rat.
Organism-specific databases
RGD	2827. Hras.
Phylogenomic databases
HOVERGEN	P20171.
Gene expression databases
Genevestigator	P20171.
GermOnline	ENSRNOG00000016611. Rattus norvegicus.
Family and domain databases
InterPro	IPR003577. GTPase_Ras. IPR013753. Ras. IPR001806. Ras_GTPase. IPR015592. Ras_Ras_related. IPR005225. Small_GTP_bd. [Graphical view]
PANTHER	PTHR11708:SF125. Ras_Ras_related. 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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	October 13, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)