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P20171

- RASH_RAT

UniProt

P20171 - RASH_RAT

Protein

GTPase HRas

Gene

Hras

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178GTP
    Nucleotide bindingi57 – 615GTP
    Nucleotide bindingi116 – 1194GTP

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. apoptotic process Source: RGD
    3. cell cycle arrest Source: Ensembl
    4. cell proliferation Source: Ensembl
    5. cellular senescence Source: Ensembl
    6. endocytosis Source: Ensembl
    7. GTP catabolic process Source: InterPro
    8. intrinsic apoptotic signaling pathway Source: Ensembl
    9. mitotic cell cycle checkpoint Source: Ensembl
    10. negative regulation of cell proliferation Source: Ensembl
    11. negative regulation of gene expression Source: Ensembl
    12. negative regulation of neuron apoptotic process Source: Ensembl
    13. negative regulation of Rho GTPase activity Source: Ensembl
    14. positive regulation of actin cytoskeleton reorganization Source: Ensembl
    15. positive regulation of cell migration Source: Ensembl
    16. positive regulation of DNA replication Source: RGD
    17. positive regulation of epithelial cell proliferation Source: Ensembl
    18. positive regulation of ERK1 and ERK2 cascade Source: RGD
    19. positive regulation of JNK cascade Source: Ensembl
    20. positive regulation of MAP kinase activity Source: Ensembl
    21. positive regulation of miRNA metabolic process Source: Ensembl
    22. positive regulation of Rac GTPase activity Source: Ensembl
    23. positive regulation of Rac protein signal transduction Source: Ensembl
    24. positive regulation of Ras protein signal transduction Source: MGI
    25. positive regulation of ruffle assembly Source: Ensembl
    26. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    27. positive regulation of wound healing Source: Ensembl
    28. protein heterooligomerization Source: RGD
    29. Ras protein signal transduction Source: RGD
    30. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    31. regulation of synaptic transmission, GABAergic Source: Ensembl
    32. social behavior Source: RGD
    33. striated muscle cell differentiation Source: Ensembl
    34. visual learning Source: Ensembl

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_195025. Signaling by SCF-KIT.
    REACT_195026. SHC1 events in ERBB4 signaling.
    REACT_195029. SHC1 events in ERBB2 signaling.
    REACT_195202. FCERI mediated MAPK activation.
    REACT_195203. GRB2 events in ERBB2 signaling.
    REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196848. EGFR Transactivation by Gastrin.
    REACT_198665. Signaling by FGFR mutants.
    REACT_199246. Activation of RAS in B cells.
    REACT_199249. Signaling by constitutively active EGFR.
    REACT_204559. SOS-mediated signalling.
    REACT_206819. Downstream signal transduction.
    REACT_212418. DAP12 signaling.
    REACT_79133. SHC-mediated cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTPase HRas
    Alternative name(s):
    H-Ras-1
    Transforming protein p21
    c-H-ras
    p21ras
    Cleaved into the following chain:
    Gene namesi
    Name:Hras
    Synonyms:Hras1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi2827. Hras.

    Subcellular locationi

    Cell membrane 1 Publication. Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Golgi apparatus By similarity. Golgi apparatus membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. Golgi membrane Source: UniProtKB-SubCell
    3. intracellular membrane-bounded organelle Source: RGD
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261N → G: Interacts and partially stimulates PLCE1; when associated with L-61. 1 Publication
    Mutagenesisi35 – 351T → S: No interaction and stimulation of PLCE1; when associated with L-61. 1 Publication
    Mutagenesisi37 – 371E → G: Reduced interaction and stimulation of PLCE1; when associated with L-61. 1 Publication
    Mutagenesisi38 – 381D → N: Reduced interaction and stimulation of PLCE1; when associated with L-61. 1 Publication
    Mutagenesisi40 – 401Y → C: No interaction and stimulation of PLCE1; when associated with L-61. 1 Publication
    Mutagenesisi61 – 611Q → 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. 1 Publication
    Mutagenesisi186 – 1861C → S: Interacts but does not stimulate PLCE1; when associated with L-61. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 186186GTPase HRasPRO_0000043000Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 186185GTPase HRas, N-terminally processedPRO_0000326479Add
    BLAST
    Propeptidei187 – 1893Removed in mature formBy similarityPRO_0000043001

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylthreonine; in GTPase HRas, N-terminally processedBy similarity
    Modified residuei118 – 1181S-nitrosocysteineBy similarity
    Lipidationi181 – 1811S-palmitoyl cysteineBy similarity
    Lipidationi184 – 1841S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity
    Lipidationi184 – 1841S-palmitoyl cysteine; alternateBy similarity
    Modified residuei186 – 1861Cysteine methyl ester1 Publication
    Lipidationi186 – 1861S-farnesyl cysteine1 Publication

    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 By similarity.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.By similarity
    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

    PaxDbiP20171.
    PRIDEiP20171.

    Expressioni

    Gene expression databases

    GenevestigatoriP20171.

    Interactioni

    Subunit structurei

    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, HRAS, MAP2K1, MAPK3 and RGS14. Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain). 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.By similarity

    Protein-protein interaction databases

    BioGridi254357. 5 interactions.
    IntActiP20171. 1 interaction.
    MINTiMINT-4996514.
    STRINGi10116.ENSRNOP00000022363.

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1110
    Helixi16 – 2510
    Beta strandi36 – 4611
    Beta strandi49 – 5810
    Helixi62 – 643
    Helixi68 – 725
    Beta strandi76 – 838
    Helixi87 – 915
    Helixi93 – 10412
    Beta strandi111 – 1166
    Helixi127 – 13711
    Beta strandi141 – 1433
    Turni146 – 1483
    Helixi152 – 16312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3V4FX-ray1.39A1-166[»]
    ProteinModelPortaliP20171.
    SMRiP20171. Positions 1-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 18520Hypervariable regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 409Effector region

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Ras family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00750000117221.
    HOGENOMiHOG000233973.
    HOVERGENiHBG009351.
    InParanoidiP20171.
    KOiK02833.
    OMAiGPEPRIS.
    OrthoDBiEOG7QVM41.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view]
    PANTHERiPTHR24070. PTHR24070. 1 hit.
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00173. RAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51421. RAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20171-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET    50
    CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI 100
    KRVKDSDDVP MVLVGNKCDL AARTVESRQA QDLARSYGIP YIETSAKTRQ 150
    GVEDAFYTLV REIRQHKLRK LNPPDESGPG CMSCKCVLS 189
    Length:189
    Mass (Da):21,298
    Last modified:July 27, 2011 - v2
    Checksum:iEE6DC2D933E2856A
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791P → L in AAA42009. (PubMed:3023901)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA25229.
    RefSeqiNP_001091711.1. NM_001098241.1.
    NP_001123913.1. NM_001130441.1.
    UniGeneiRn.102180.

    Genome annotation databases

    EnsembliENSRNOT00000022363; ENSRNOP00000022363; ENSRNOG00000016611.
    GeneIDi293621.
    KEGGirno:293621.
    UCSCiRGD:2827. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A25229.
    RefSeqi NP_001091711.1. NM_001098241.1.
    NP_001123913.1. NM_001130441.1.
    UniGenei Rn.102180.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3V4F X-ray 1.39 A 1-166 [» ]
    ProteinModelPortali P20171.
    SMRi P20171. Positions 1-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 254357. 5 interactions.
    IntActi P20171. 1 interaction.
    MINTi MINT-4996514.
    STRINGi 10116.ENSRNOP00000022363.

    Chemistry

    BindingDBi P20171.

    Proteomic databases

    PaxDbi P20171.
    PRIDEi P20171.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022363 ; ENSRNOP00000022363 ; ENSRNOG00000016611 .
    GeneIDi 293621.
    KEGGi rno:293621.
    UCSCi RGD:2827. rat.

    Organism-specific databases

    CTDi 3265.
    RGDi 2827. Hras.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00750000117221.
    HOGENOMi HOG000233973.
    HOVERGENi HBG009351.
    InParanoidi P20171.
    KOi K02833.
    OMAi GPEPRIS.
    OrthoDBi EOG7QVM41.

    Enzyme and pathway databases

    Reactomei REACT_195025. Signaling by SCF-KIT.
    REACT_195026. SHC1 events in ERBB4 signaling.
    REACT_195029. SHC1 events in ERBB2 signaling.
    REACT_195202. FCERI mediated MAPK activation.
    REACT_195203. GRB2 events in ERBB2 signaling.
    REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196848. EGFR Transactivation by Gastrin.
    REACT_198665. Signaling by FGFR mutants.
    REACT_199246. Activation of RAS in B cells.
    REACT_199249. Signaling by constitutively active EGFR.
    REACT_204559. SOS-mediated signalling.
    REACT_206819. Downstream signal transduction.
    REACT_212418. DAP12 signaling.
    REACT_79133. SHC-mediated cascade.

    Miscellaneous databases

    NextBioi 636547.

    Gene expression databases

    Genevestigatori P20171.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLCE1, MUTAGENESIS OF ASN-26; THR-35; GLU-37; ASP-38; TYR-40; GLN-61 AND CYS-186.
    6. 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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS14, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiRASH_RAT
    AccessioniPrimary (citable) accession number: P20171
    Secondary accession number(s): Q4KLL6, Q5RJJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3