UniProt:P20171 Hras

chain
  • chain:1-186
  • initiator methionine:1
  • chain:2-186
  • propeptide:187-189
checksum EE6DC2D933E2856A
comment
  • FUNCTION Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)ACTIVITY 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 In its GTP-bound form interacts with PLCE1 (PubMed:11179219). Interacts with TBC1D10C (By similarity). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (PubMed:19319189). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (PubMed:19319189, PubMed:19878719). Forms a signaling complex with RASGRP1 and DGKZ (By similarity). Interacts with RASSF5 (By similarity). Interacts with PDE6D (By similarity). Interacts with IKZF3 (By similarity). Interacts with RACK1 (By similarity). 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 (By similarity). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex; SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS (By similarity). Interacts (in GTP-bound form) with Oog1 (By similarity). Interacts (GTP-bound form) with MAPKAP1/SIN1; inhibiting H-Ras/HRAS activity (By similarity).INTERACTION 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.PTM Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.PTM S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.PTM 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.PTM Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs).PTM Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes.SIMILARITY Belongs to the small GTPase superfamily. Ras family.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.
crossReference
databaseName UniProt
dbId 99637
description
  • recommendedName: GTPase HRas ecNumber evidence="2"3.6.5.2 alternativeName: H-Ras-1 alternativeName: Transforming protein p21 alternativeName: c-H-ras alternativeName: p21ras component recommendedName: GTPase HRas, N-terminally processed /component
displayName UniProt:P20171 Hras
geneName
  • Hras
  • Hras1
identifier P20171
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Cell membrane
  • Golgi apparatus
  • GTP-binding
  • Hydrolase
  • Isopeptide bond
  • Lipoprotein
  • Membrane
  • Methylation
  • Nucleotide-binding
  • Palmitate
  • Prenylation
  • Proto-oncogene
  • Reference proteome
  • S-nitrosylation
  • Ubl conjugation
modified [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
moleculeType Protein
name
  • Hras
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • RASH_RAT
  • Q4KLL6
  • Q5RJJ8
sequenceLength 189
species [Species:48895] Rattus norvegicus
stId uniprot:P20171
url http://purl.uniprot.org/uniprot/P20171
Cite Us!