RASK_RAT
ID RASK_RAT Reviewed; 189 AA.
AC P08644; P46203; P97914;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=GTPase KRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=K-Ras 2;
DE AltName: Full=Ki-Ras;
DE AltName: Full=c-K-ras;
DE AltName: Full=c-Ki-ras;
DE Contains:
DE RecName: Full=GTPase KRas, N-terminally processed;
DE Flags: Precursor;
GN Name=Kras; Synonyms=Kras2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), MUTAGENESIS, AND FUNCTION.
RC STRAIN=Noble; TISSUE=Kidney;
RX PubMed=8058308;
RA Higinbotham K.G., Rice J.M., Buzard G.S., Perantoni A.O.;
RT "Activation of the K-ras gene by insertion mutations in chemically induced
RT rat renal mesenchymal tumors.";
RL Oncogene 9:2455-2459(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RX PubMed=3023884; DOI=10.1128/mcb.6.4.1349-1351.1986;
RA Tahira T., Hayashi K., Ochiai M., Tsuchida N., Nagao M., Sugimura T.;
RT "Structure of the c-Ki-ras gene in a rat fibrosarcoma induced by 1,8-
RT dinitropyrene.";
RL Mol. Cell. Biol. 6:1349-1351(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-37.
RX PubMed=3009041;
RA Iritani A., Katayama N., Tahira T., Hayashi K., Tsuchida N.;
RT "Nucleotide sequence of exon I of the rat c-K-ras gene.";
RL Bull. Tokyo Med. Dent. Univ. 33:35-40(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND FUNCTION.
RX PubMed=3110778; DOI=10.1073/pnas.84.14.4974;
RA McMahon G., Davis E., Wogan G.N.;
RT "Characterization of c-Ki-ras oncogene alleles by direct sequencing of
RT enzymatically amplified DNA from carcinogen-induced tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4974-4978(1987).
RN [6]
RP INTERACTION WITH PHLPP.
RX PubMed=12594205; DOI=10.1074/jbc.m213214200;
RA Shimizu K., Okada M., Nagai K., Fukada Y.;
RT "Suprachiasmatic nucleus circadian oscillatory protein, a novel binding
RT partner of K-Ras in the membrane rafts, negatively regulates MAPK
RT pathway.";
RL J. Biol. Chem. 278:14920-14925(2003).
RN [7]
RP INTERACTION WITH RGS14.
RX PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A.,
RA Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J.,
RA Snider W.D., Siderovski D.P.;
RT "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT effector.";
RL PLoS ONE 4:E4884-E4884(2009).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity (By similarity). Plays an important role in the regulation of
CC cell proliferation (PubMed:3110778). Plays a role in promoting
CC oncogenic events by inducing transcriptional silencing of tumor
CC suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:P01116,
CC ECO:0000269|PubMed:3110778}.
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). Interaction with SOS1 promotes exchange of bound GDP by GTP.
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- SUBUNIT: Interacts with SOS1 (By similarity). Interacts (when
CC farnesylated) with PDE6D; this promotes dissociation from the cell
CC membrane (By similarity). Interacts with PHLPP. Interacts (active GTP-
CC bound form preferentially) with RGS14. Interacts with (when
CC farnesylated) with GPR31 (By similarity). Interacts with RAP1GDS1 (By
CC similarity). {ECO:0000250|UniProtKB:P01116,
CC ECO:0000269|PubMed:12594205, ECO:0000269|PubMed:19319189}.
CC -!- SUBUNIT: [Isoform 2B]: Interacts (when farnesylated) with GPR31.
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01116};
CC Lipid-anchor {ECO:0000250|UniProtKB:P01116}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P01116}. Endomembrane system
CC {ECO:0000250|UniProtKB:P01116}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane
CC {ECO:0000250|UniProtKB:P01116}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ in the C-terminal region which is encoded by
CC two alternative exons (IVA and IVB).;
CC Name=2A;
CC IsoId=P08644-1; Sequence=Displayed;
CC Name=2B;
CC IsoId=P08644-2, P46203-1;
CC Sequence=VSP_011144, VSP_011145;
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.
CC -!- PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at
CC Lys-170 in a non-degradative manner, leading to inhibit Ras signaling
CC by decreasing Ras association with membranes.
CC {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: Palmitoylated at Lys-182, Lys-184 and Lys-185. Lysine-
CC depalmitoylation by SIRT2 promotes its localization to endomembranes in
CC endocytic pathways. {ECO:0000250|UniProtKB:P01116}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; U09793; AAB60458.1; -; mRNA.
DR EMBL; AABR03032592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M12260; AAA42011.1; -; Genomic_DNA.
DR EMBL; M12259; AAA42011.1; JOINED; Genomic_DNA.
DR EMBL; M54870; AAA40937.1; -; Genomic_DNA.
DR EMBL; M16970; AAA41494.1; -; Genomic_DNA.
DR PIR; I58402; I58402.
DR RefSeq; NP_113703.1; NM_031515.3. [P08644-2]
DR RefSeq; XP_008761576.1; XM_008763354.2. [P08644-2]
DR RefSeq; XP_017447931.1; XM_017592442.1. [P08644-1]
DR RefSeq; XP_017447932.1; XM_017592443.1. [P08644-1]
DR PDB; 1N4S; X-ray; 2.60 A; M/N/O/P/Q/R=185-188.
DR PDBsum; 1N4S; -.
DR AlphaFoldDB; P08644; -.
DR BMRB; P08644; -.
DR SMR; P08644; -.
DR BioGRID; 246680; 11.
DR IntAct; P08644; 1.
DR MINT; P08644; -.
DR STRING; 10116.ENSRNOP00000012588; -.
DR iPTMnet; P08644; -.
DR PhosphoSitePlus; P08644; -.
DR SwissPalm; P08644; -.
DR jPOST; P08644; -.
DR PaxDb; P08644; -.
DR PRIDE; P08644; -.
DR GeneID; 24525; -.
DR KEGG; rno:24525; -.
DR UCSC; RGD:2981; rat. [P08644-1]
DR CTD; 3845; -.
DR RGD; 2981; Kras.
DR VEuPathDB; HostDB:ENSRNOG00000069406; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P08644; -.
DR OMA; CCSGCVV; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P08644; -.
DR TreeFam; TF312796; -.
DR Reactome; R-RNO-1169092; Activation of RAS in B cells.
DR Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-171007; p38MAPK events.
DR Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
DR Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-RNO-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-RNO-8851805; MET activates RAS signaling.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-RNO-9648002; RAS processing.
DR Reactome; R-RNO-9674555; Signaling by CSF3 (G-CSF).
DR PRO; PR:P08644; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009338; Expressed in duodenum and 19 other tissues.
DR ExpressionAtlas; P08644; baseline and differential.
DR Genevisible; P08644; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0019002; F:GMP binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0030275; F:LRR domain binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:RGD.
DR GO; GO:0038002; P:endocrine signaling; ISO:RGD.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0021897; P:forebrain astrocyte development; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000774; P:positive regulation of cellular senescence; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0035900; P:response to isolation stress; IEP:RGD.
DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Prenylation; Proto-oncogene;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase KRas"
FT /id="PRO_0000326483"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT CHAIN 2..186
FT /note="GTPase KRas, N-terminally processed"
FT /id="PRO_0000082644"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT /id="PRO_0000281294"
FT REGION 166..185
FT /note="Hypervariable region"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 59..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase KRas, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 180
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 182
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 184
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 185
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT VAR_SEQ 151..153
FT /note="RVE -> GVD (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:8058308"
FT /id="VSP_011144"
FT VAR_SEQ 165..189
FT /note="QYRLKKISKEEKTPGCVKIKKCVIM -> KHKEKMSKDGKKKKKKSRTRCIV
FT M (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:8058308"
FT /id="VSP_011145"
FT CONFLICT 12
FT /note="G -> C (in Ref. 3; AAA42011)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> H (in Ref. 3; AAA42011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21656 MW; 97345422E01D2C81 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QELARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC
VKIKKCVIM
