RAB4B_HUMAN
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 03-AUG-2022, entry version 162.
DE RecName: Full=Ras-related protein Rab-4B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20338};
GN Name=RAB4B; 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 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 [7]
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-183 IN COMPLEX WITH GDP.
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: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state (By similarity). Protein transport. Probably
CC involved in vesicular traffic (By similarity). Acts as a regulator of
CC platelet alpha-granule release during activation and aggregation of
CC platelets (By similarity). {ECO:0000250|UniProtKB:P20338,
CC ECO:0000250|UniProtKB:Q91ZR1}.
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:P20338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20338};
CC -!- INTERACTION:
CC P61018; A0A087WZT3: BOLA2B; 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: FAM71C; 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}.
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 -!- 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_016154.4. [P61018-1]
DR PDB; 2O52; X-ray; 2.20 A; A/B=6-183.
DR PDBsum; 2O52; -.
DR AlphaFoldDB; P61018; -.
DR SMR; P61018; -.
DR BioGRID; 119816; 30.
DR IntAct; P61018; 23.
DR STRING; 9606.ENSP00000349560; -.
DR iPTMnet; P61018; -.
DR PhosphoSitePlus; P61018; -.
DR SwissPalm; P61018; -.
DR BioMuta; RAB4B; -.
DR DMDM; 46577635; -.
DR EPD; P61018; -.
DR jPOST; P61018; -.
DR MassIVE; P61018; -.
DR MaxQB; P61018; -.
DR PaxDb; P61018; -.
DR PeptideAtlas; P61018; -.
DR PRIDE; P61018; -.
DR ProteomicsDB; 57249; -. [P61018-1]
DR ProteomicsDB; 57250; -. [P61018-2]
DR Antibodypedia; 48676; 102 antibodies from 18 providers.
DR DNASU; 53916; -.
DR Ensembl; ENST00000357052.8; ENSP00000349560.2; ENSG00000167578.18. [P61018-1]
DR Ensembl; ENST00000594800.5; ENSP00000470246.1; ENSG00000167578.18. [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 CTD; 53916; -.
DR DisGeNET; 53916; -.
DR GeneCards; RAB4B; -.
DR HGNC; HGNC:9782; RAB4B.
DR HPA; ENSG00000167578; Low tissue specificity.
DR MIM; 612945; gene.
DR neXtProt; NX_P61018; -.
DR OpenTargets; ENSG00000167578; -.
DR PharmGKB; PA34142; -.
DR VEuPathDB; HostDB:ENSG00000167578; -.
DR eggNOG; KOG0086; Eukaryota.
DR GeneTree; ENSGT00940000159399; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61018; -.
DR OMA; LHHFIHN; -.
DR PhylomeDB; P61018; -.
DR TreeFam; TF300032; -.
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 BioGRID-ORCS; 53916; 13 hits in 1078 CRISPR screens.
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 95 other tissues.
DR ExpressionAtlas; P61018; baseline and differential.
DR Genevisible; P61018; HS.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046323; P:glucose import; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041819; Rab4.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; 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 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.9, ECO:0007744|PDB:2O52"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.9, ECO:0007744|PDB:2O52"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.9, ECO:0007744|PDB:2O52"
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 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 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
