RAB7B_HUMAN
ID RAB7B_HUMAN Reviewed; 199 AA.
AC Q96AH8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ras-related protein Rab-7b;
GN Name=RAB7B;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15144907; DOI=10.1016/j.bbrc.2004.04.115;
RA Yang M., Chen T., Han C., Li N., Wan T., Cao X.;
RT "Rab7b, a novel lysosome-associated small GTPase, is involved in monocytic
RT differentiation of human acute promyelocytic leukemia cells.";
RL Biochem. Biophys. Res. Commun. 318:792-799(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [3]
RP REVIEW ON FUNCTION.
RX PubMed=21057625; DOI=10.4161/cib.3.5.12341;
RA Bucci C., Bakke O., Progida C.;
RT "Rab7b and receptors trafficking.";
RL Commun. Integr. Biol. 3:401-404(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20375062; DOI=10.1242/jcs.051474;
RA Progida C., Cogli L., Piro F., De Luca A., Bakke O., Bucci C.;
RT "Rab7b controls trafficking from endosomes to the TGN.";
RL J. Cell Sci. 123:1480-1491(2010).
RN [5]
RP FUNCTION.
RX PubMed=20953574; DOI=10.1007/s00109-010-0689-z;
RA He D., Chen T., Yang M., Zhu X., Wang C., Cao X., Cai Z.;
RT "Small Rab GTPase Rab7b promotes megakaryocytic differentiation by
RT enhancing IL-6 production and STAT3-GATA-1 association.";
RL J. Mol. Med. 89:137-150(2011).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
CC -!- FUNCTION: Controls vesicular trafficking from endosomes to the trans-
CC Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and
CC can suppress TLR9-triggered TNFA, IL6, and IFNB production in
CC macrophages by promoting TLR9 lysosomal degradation. Also negatively
CC regulates TLR4 signaling in macrophages by promoting lysosomal
CC degradation of TLR4. Promotes megakaryocytic differentiation by
CC increasing NF-kappa-B-dependent IL6 production and subsequently
CC enhancing the association of STAT3 with GATA1. Not involved in the
CC regulation of the EGF- and EGFR degradation pathway.
CC {ECO:0000269|PubMed:20375062, ECO:0000269|PubMed:20953574}.
CC -!- INTERACTION:
CC Q96AH8; Q92624: APPBP2; NbExp=3; IntAct=EBI-3924400, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:20375062}.
CC Lysosome {ECO:0000269|PubMed:15144907, ECO:0000269|PubMed:20375062}.
CC Golgi apparatus {ECO:0000269|PubMed:20375062}. Golgi apparatus, trans-
CC Golgi network {ECO:0000269|PubMed:20375062}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or
CC M.tuberculosis. {ECO:0000269|PubMed:21255211}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung, skeletal muscle
CC and peripheral blood leukocyte. {ECO:0000269|PubMed:15144907}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY094596; AAM22519.1; -; mRNA.
DR EMBL; BC017092; AAH17092.1; -; mRNA.
DR CCDS; CCDS73011.1; -.
DR RefSeq; NP_001157994.1; NM_001164522.2.
DR RefSeq; NP_796377.3; NM_177403.5.
DR AlphaFoldDB; Q96AH8; -.
DR SMR; Q96AH8; -.
DR BioGRID; 130725; 15.
DR IntAct; Q96AH8; 7.
DR STRING; 9606.ENSP00000479762; -.
DR PhosphoSitePlus; Q96AH8; -.
DR BioMuta; RAB7B; -.
DR DMDM; 50401122; -.
DR EPD; Q96AH8; -.
DR jPOST; Q96AH8; -.
DR MassIVE; Q96AH8; -.
DR PeptideAtlas; Q96AH8; -.
DR PRIDE; Q96AH8; -.
DR ProteomicsDB; 75966; -.
DR TopDownProteomics; Q96AH8; -.
DR Antibodypedia; 72889; 143 antibodies from 19 providers.
DR DNASU; 338382; -.
DR Ensembl; ENST00000617070.5; ENSP00000482499.1; ENSG00000276600.5.
DR Ensembl; ENST00000617991.4; ENSP00000479762.1; ENSG00000276600.5.
DR Ensembl; ENST00000623597.3; ENSP00000485468.1; ENSG00000276600.5.
DR GeneID; 338382; -.
DR KEGG; hsa:338382; -.
DR MANE-Select; ENST00000617070.5; ENSP00000482499.1; NM_001164522.3; NP_001157994.1.
DR UCSC; uc031vlc.2; human.
DR CTD; 338382; -.
DR DisGeNET; 338382; -.
DR GeneCards; RAB7B; -.
DR HGNC; HGNC:30513; RAB7B.
DR HPA; ENSG00000276600; Tissue enhanced (skin).
DR neXtProt; NX_Q96AH8; -.
DR OpenTargets; ENSG00000276600; -.
DR PharmGKB; PA134940117; -.
DR VEuPathDB; HostDB:ENSG00000276600; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000161943; -.
DR InParanoid; Q96AH8; -.
DR OMA; ASSWCKE; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q96AH8; -.
DR PathwayCommons; Q96AH8; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q96AH8; -.
DR BioGRID-ORCS; 338382; 0 hits in 64 CRISPR screens.
DR ChiTaRS; RAB7B; human.
DR GeneWiki; RAB7B; -.
DR GenomeRNAi; 338382; -.
DR Pharos; Q96AH8; Tbio.
DR PRO; PR:Q96AH8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96AH8; protein.
DR Bgee; ENSG00000276600; Expressed in upper arm skin and 123 other tissues.
DR ExpressionAtlas; Q96AH8; baseline and differential.
DR Genevisible; Q96AH8; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0034499; P:late endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IBA:GO_Central.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 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 Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding; Lipoprotein;
KW Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..199
FT /note="Ras-related protein Rab-7b"
FT /id="PRO_0000121125"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEA8"
FT LIPID 198
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 22511 MW; 161C41ABC0EBA529 CRC64;
MNPRKKVDLK LIIVGAIGVG KTSLLHQYVH KTFYEEYQTT LGASILSKII ILGDTTLKLQ
IWDTGGQERF RSMVSTFYKG SDGCILAFDV TDLESFEALD IWRGDVLAKI VPMEQSYPMV
LLGNKIDLAD RKVPQEVAQG WCREKDIPYF EVSAKNDINV VQAFEMLASR ALSRYQSILE
NHLTESIKLS PDQSRSRCC
