ID   RAB4B_HUMAN             Reviewed;         213 AA.
AC   P61018; P22750; Q7Z514; Q9HBR6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   02-SEP-2026, entry version 180.
DE   RecName: Full=Ras-related protein Rab-4B {ECO:0000305};
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20338};
GN   Name=RAB4B {ECO:0000312|HGNC:HGNC:9782};
GN   Synonyms=RAB4 {ECO:0000303|PubMed:20534812}; ORFNames=PP1596;
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] (ISOFORM 1).
RA   Chu J.H., Yu L., Cui W.C., Bi A.D., Huang J., Zhao S.Y.;
RT   "Cloning and characterization of a novel human cDNA homologous to
RT   R.norvegicus rab4b mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hematopoietic stem cell;
RA   Huang C., Wu T., Xu S., Gu W., Wang Y., Han Z., Chen Z.;
RT   "Novel genes expressed in hematopoietic stem/progenitor cells from
RT   myelodysplastic syndrome patients.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
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).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RUFY1, AND MUTAGENESIS OF
RP   GLN-67.
RX   PubMed=20534812; DOI=10.1091/mbc.e10-01-0074;
RA   Yamamoto H., Koga H., Katoh Y., Takahashi S., Nakayama K., Shin H.W.;
RT   "Functional cross-talk between Rab14 and Rab4 through a dual effector,
RT   RUFY1/Rabip4.";
RL   Mol. Biol. Cell 21:2746-2755(2010).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10] {ECO:0007744|PDB:2O52}
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-183 IN COMPLEX WITH GDP AND
RP   MG(2+), AND COFACTOR.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human RAB4B in complex with GDP.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different set of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion (By similarity). RAB4B
CC       mediates endosomal tethering and fusion through the interaction with
CC       RUFY1 and RAB14 (PubMed:20534812). Acts as a regulator of platelet
CC       alpha-granule release during activation and aggregation of platelets
CC       (By similarity). {ECO:0000250|UniProtKB:P20338,
CC       ECO:0000250|UniProtKB:Q91ZR1, ECO:0000269|PubMed:20534812}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); 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:P20338};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P20338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.10};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP. Regulated
CC       by GTPase activating proteins (GAPs) which increase the GTP hydrolysis
CC       activity. Inhibited by GDP dissociation inhibitors (GDIs).
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Interacts (GTP-bound form) with RUFY1; the interaction allows
CC       endosomal tethering and fusion. {ECO:0000269|PubMed:20534812}.
CC   -!- INTERACTION:
CC       P61018; A0A087WZT3: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-10218066, EBI-12006120;
CC       P61018; O75419: CDC45; NbExp=3; IntAct=EBI-10218066, EBI-374969;
CC       P61018; O00471: EXOC5; NbExp=6; IntAct=EBI-10218066, EBI-949824;
CC       P61018; Q8NEG0: GARIN6; NbExp=3; IntAct=EBI-10218066, EBI-752049;
CC       P61018; Q15276: RABEP1; NbExp=3; IntAct=EBI-10218066, EBI-447043;
CC       P61018; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-10218066, EBI-2799833;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC       {ECO:0000269|PubMed:20534812}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P61018-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P61018-2; Sequence=VSP_013567;
CC   -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are
CC       characteristic of Rab GTPases and mediate the interactions with Rab
CC       downstream effectors. The switch regions undergo conformational changes
CC       upon nucleotide binding which drives interaction with specific sets of
CC       effector proteins, with most effectors only binding to GTP-bound Rab.
CC       {ECO:0000250|UniProtKB:P61106}.
CC   -!- PTM: Serotonylation of Gln-67 by TGM2 during activation and aggregation
CC       of platelets leads to constitutive activation of GTPase activity.
CC       {ECO:0000250|UniProtKB:Q91ZR1}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AF087861; AAP97171.1; -; mRNA.
DR   EMBL; AF165522; AAD45923.1; -; mRNA.
DR   EMBL; AF217985; AAG17228.1; -; mRNA.
DR   EMBL; AF498935; AAM21083.1; -; mRNA.
DR   EMBL; BC046927; AAH46927.1; -; mRNA.
DR   CCDS; CCDS33030.1; -. [P61018-1]
DR   RefSeq; NP_057238.3; NM_016154.5. [P61018-1]
DR   PDB; 2O52; X-ray; 2.20 A; A/B=6-183.
DR   AlphaFoldDB; P61018; -.
DR   SMR; P61018; -.
DR   BioGRID; 119816; 34.
DR   FunCoup; P61018; 1196.
DR   IntAct; P61018; 27.
DR   NDEx; IQUERY-CP-RAB4B; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000470246; -.
DR   iPTMnet; P61018; -.
DR   PhosphoSitePlus; P61018; -.
DR   SwissPalm; P61018; -.
DR   BioMuta; RAB4B; -.
DR   DMDM; 46577635; -.
DR   jPOST; P61018; -.
DR   MassIVE; P61018; -.
DR   PaxDb; 9606-ENSP00000470246; -.
DR   PeptideAtlas; P61018; -.
DR   ProteomicsDB; 57249; -. [P61018-1]
DR   ProteomicsDB; 57250; -. [P61018-2]
DR   Pumba; P61018; -.
DR   Antibodypedia; 48676; 98 antibodies from 18 providers.
DR   DNASU; 53916; -.
DR   Ensembl; ENST00000357052.8; ENSP00000349560.2; ENSG00000167578.19. [P61018-1]
DR   Ensembl; ENST00000594136.2; ENSP00000469872.1; ENSG00000171570.11. [P61018-1]
DR   Ensembl; ENST00000594800.5; ENSP00000470246.1; ENSG00000167578.19. [P61018-1]
DR   Ensembl; ENST00000858145.1; ENSP00000528204.1; ENSG00000167578.19. [P61018-1]
DR   Ensembl; ENST00000971035.1; ENSP00000641094.1; ENSG00000167578.19. [P61018-1]
DR   GeneID; 53916; -.
DR   KEGG; hsa:53916; -.
DR   MANE-Select; ENST00000357052.8; ENSP00000349560.2; NM_016154.5; NP_057238.3.
DR   UCSC; uc002opd.2; human. [P61018-1]
DR   AGR; HGNC:9782; -.
DR   ClinPGx; PA34142; -.
DR   CTD; 53916; -.
DR   DisGeNET; 53916; -.
DR   GeneCards; RAB4B; -.
DR   HGNC; HGNC:9782; RAB4B.
DR   HPA; ENSG00000167578; Tissue enhanced (brain).
DR   MIM; 612945; gene.
DR   OpenTargets; ENSG00000167578; -.
DR   VEuPathDB; HostDB:ENSG00000167578; -.
DR   eggNOG; KOG0086; Eukaryota.
DR   GeneTree; ENSGT00940000159399; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P61018; -.
DR   OMA; ASQNICI; -.
DR   OrthoDB; 9989112at2759; -.
DR   PAN-GO; P61018; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; P61018; -.
DR   PathwayCommons; P61018; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   Reactome; R-HSA-8875656; MET receptor recycling.
DR   SignaLink; P61018; -.
DR   Agora; ENSG00000167578; -.
DR   BioGRID-ORCS; 53916; 15 hits in 1155 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   EvolutionaryTrace; P61018; -.
DR   GenomeRNAi; 53916; -.
DR   Pharos; P61018; Tbio.
DR   PRO; PR:P61018; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P61018; protein.
DR   Bgee; ENSG00000167578; Expressed in C1 segment of cervical spinal cord and 97 other cell types or tissues.
DR   ExpressionAtlas; P61018; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProt.
DR   GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0003925; F:G protein activity; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProt.
DR   GO; GO:0098708; P:D-glucose import across plasma membrane; IMP:UniProtKB.
DR   GO; GO:0034498; P:early endosome to Golgi transport; IDA:UniProt.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProt.
DR   GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR   GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04113; Rab4; 1.
DR   FunFam; 3.40.50.300:FF:000280; Putative ras-related protein Rab-4B; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041819; Rab4.
DR   InterPro; IPR050209; Rab_GTPases_membrane_traffic.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PDBsum; 2O52; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell membrane; Endosome;
KW   GTP-binding; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW   Protein transport; Proteomics identification; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..213
FT                   /note="Ras-related protein Rab-4B"
FT                   /id="PRO_0000121099"
FT   MOTIF           39..44
FT                   /note="Switch 1"
FT                   /evidence="ECO:0000250|UniProtKB:P61106"
FT   MOTIF           65..74
FT                   /note="Switch 2"
FT                   /evidence="ECO:0000250|UniProtKB:P61106"
FT   BINDING         18
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         19
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         20
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         21
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         22
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         23
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         121
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         122
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         124
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         152
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   BINDING         153
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:2O52"
FT   BINDING         153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         67
FT                   /note="5-glutamyl serotonin"
FT                   /evidence="ECO:0000250|UniProtKB:Q91ZR1"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20338"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         213
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           211
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..5
FT                   /note="MAETY -> MSVSLPLTVMVRERDWIGIHLFSLYLSLPVGIPDFGSIWS
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_013567"
FT   MUTAGEN         67
FT                   /note="Q->L: GTP-locked. Interacts with RUFY1."
FT                   /evidence="ECO:0000269|PubMed:20534812"
FT   CONFLICT        4..6
FT                   /note="TYD -> DRH (in Ref. 1; AAP97171)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   STRAND          45..52
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           93..97
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           99..109
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           123..128
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           133..142
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           158..174
FT                   /evidence="ECO:0007829|PDB:2O52"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:2O52"
SQ   SEQUENCE   213 AA;  23587 MW;  0C3D76DC3285DB98 CRC64;
     MAETYDFLFK FLVIGSAGTG KSCLLHQFIE NKFKQDSNHT IGVEFGSRVV NVGGKTVKLQ
     IWDTAGQERF RSVTRSYYRG AAGALLVYDI TSRETYNSLA AWLTDARTLA SPNIVVILCG
     NKKDLDPERE VTFLEASRFA QENELMFLET SALTGENVEE AFLKCARTIL NKIDSGELDP
     ERMGSGIQYG DASLRQLRQP RSAQAVAPQP CGC
//