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RASE_HUMAN
ID   RASE_HUMAN              Reviewed;         233 AA.
AC   Q7Z444;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=GTPase ERas;
DE            Short=E-Ras;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE   AltName: Full=Embryonic stem cell-expressed Ras;
DE   Flags: Precursor;
GN   Name=ERAS; Synonyms=HRAS2, HRASP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12774123; DOI=10.1038/nature01646;
RA   Takahashi K., Mitsui K., Yamanaka S.;
RT   "Role of Eras in promoting tumor-like properties in mouse embryonic stem
RT   cells.";
RL   Nature 423:541-545(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity. Plays an important role in the tumor-like growth properties
CC       of embryonic stem cells (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P01116};
CC   -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine nucleotide-
CC       exchange factor (GEF) and inactivated by a GTPase-activating protein
CC       (GAP).
CC   -!- SUBUNIT: Interacts with PIK3CD. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q7Z444; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-13351543, EBI-14103818;
CC       Q7Z444; O43711: TLX3; NbExp=3; IntAct=EBI-13351543, EBI-3939165;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AB093575; BAC76997.1; -; mRNA.
DR   EMBL; BC101642; AAI01643.1; -; mRNA.
DR   EMBL; BC101644; AAI01645.1; -; mRNA.
DR   CCDS; CCDS35246.1; -.
DR   RefSeq; NP_853510.1; NM_181532.3.
DR   AlphaFoldDB; Q7Z444; -.
DR   SMR; Q7Z444; -.
DR   BioGRID; 109502; 4.
DR   IntAct; Q7Z444; 2.
DR   STRING; 9606.ENSP00000339136; -.
DR   PhosphoSitePlus; Q7Z444; -.
DR   BioMuta; ERAS; -.
DR   DMDM; 74723320; -.
DR   MassIVE; Q7Z444; -.
DR   PaxDb; Q7Z444; -.
DR   PeptideAtlas; Q7Z444; -.
DR   PRIDE; Q7Z444; -.
DR   Antibodypedia; 25880; 433 antibodies from 31 providers.
DR   DNASU; 3266; -.
DR   Ensembl; ENST00000338270.1; ENSP00000339136.1; ENSG00000187682.2.
DR   Ensembl; ENST00000636362.1; ENSP00000490793.1; ENSG00000187682.2.
DR   GeneID; 3266; -.
DR   KEGG; hsa:3266; -.
DR   MANE-Select; ENST00000636362.1; ENSP00000490793.1; NM_181532.3; NP_853510.1.
DR   UCSC; uc064zbl.1; human.
DR   CTD; 3266; -.
DR   DisGeNET; 3266; -.
DR   GeneCards; ERAS; -.
DR   HGNC; HGNC:5174; ERAS.
DR   HPA; ENSG00000187682; Tissue enhanced (brain).
DR   MIM; 300437; gene.
DR   neXtProt; NX_Q7Z444; -.
DR   OpenTargets; ENSG00000187682; -.
DR   PharmGKB; PA29448; -.
DR   VEuPathDB; HostDB:ENSG00000187682; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000162901; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q7Z444; -.
DR   OMA; KAMCRCG; -.
DR   OrthoDB; 1259506at2759; -.
DR   PhylomeDB; Q7Z444; -.
DR   TreeFam; TF312796; -.
DR   PathwayCommons; Q7Z444; -.
DR   SignaLink; Q7Z444; -.
DR   BioGRID-ORCS; 3266; 9 hits in 698 CRISPR screens.
DR   ChiTaRS; ERAS; human.
DR   GenomeRNAi; 3266; -.
DR   Pharos; Q7Z444; Tbio.
DR   PRO; PR:Q7Z444; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q7Z444; protein.
DR   Bgee; ENSG00000187682; Expressed in hypothalamus and 72 other tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT   CHAIN           1..230
FT                   /note="GTPase ERas"
FT                   /id="PRO_0000247538"
FT   PROPEP          231..233
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000247539"
FT   MOTIF           70..78
FT                   /note="Effector region"
FT   BINDING         48..55
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         95..99
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         230
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           226
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           228
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           230
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  25287 MW;  D5451F95978E7823 CRC64;
     MELPTKPGTF DLGLATWSPS FQGETHRAQA RRRDVGRQLP EYKAVVVGAS GVGKSALTIQ
     LNHQCFVEDH DPTIQDSYWK ELTLDSGDCI LNVLDTAGQA IHRALRDQCL AVCDGVLGVF
     ALDDPSSLIQ LQQIWATWGP HPAQPLVLVG NKCDLVTTAG DAHAAAAALA HSWGAHFVET
     SAKTRQGVEE AFSLLVHEIQ RVQEAMAKEP MARSCREKTR HQKATCHCGC SVA
 
 
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