RAB2B_HUMAN
ID RAB2B_HUMAN Reviewed; 216 AA.
AC Q8WUD1; B2RD03; D3DS24; Q6NZ33;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ras-related protein Rab-2B {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000305|PubMed:26209634};
GN Name=RAB2B {ECO:0000312|HGNC:HGNC:20246};
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).
RX PubMed=12376746; DOI=10.1007/s100380200083;
RA Ni X., Ma Y., Cheng H., Jiang M., Guo L., Ji C., Gu S., Cao Y., Xie Y.,
RA Mao Y.;
RT "Molecular cloning and characterization of a novel human Rab (Rab2B)
RT gene.";
RL J. Hum. Genet. 47:548-551(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin, and Testis;
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, 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 [7]
RP FUNCTION, INTERACTION WITH GARIN4, AND CATALYTIC ACTIVITY.
RX PubMed=26209634; DOI=10.1074/jbc.m115.669242;
RA Aizawa M., Fukuda M.;
RT "Small GTPase Rab2B and Its Specific Binding Protein Golgi-associated Rab2B
RT Interactor-like 4 (GARI-L4) Regulate Golgi Morphology.";
RL J. Biol. Chem. 290:22250-22261(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 5-176 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB2B.";
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 active GTP-bound and inactive
CC GDP-bound states. In their active state, drive transport of vesicular
CC carriers from donor organelles to acceptor organelles to regulate the
CC membrane traffic that maintains organelle identity and morphology.
CC Regulates the compacted morphology of the Golgi (Probable). Promotes
CC cytosolic DNA-induced innate immune responses. Regulates IFN responses
CC against DNA viruses by regulating the CGAS-STING signaling axis (By
CC similarity). {ECO:0000250|UniProtKB:P59279,
CC ECO:0000305|PubMed:26209634}.
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:0000305|PubMed:26209634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:26209634};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000305}.
CC -!- SUBUNIT: Interacts (in GTP-bound form) with GARIN4 (via N-terminus)
CC (PubMed:26209634). Interacts (in GTP-bound form) with GARIN5A.
CC Interacts (in GTP-bound form) with GARIN1B (By similarity).
CC {ECO:0000250|UniProtKB:P59279, ECO:0000269|PubMed:26209634}.
CC -!- INTERACTION:
CC Q8WUD1; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-5542466, EBI-10173507;
CC Q8WUD1; Q9H2G9: BLZF1; NbExp=10; IntAct=EBI-5542466, EBI-2548012;
CC Q8WUD1; Q8IWE2: FAM114A1; NbExp=6; IntAct=EBI-5542466, EBI-2686288;
CC Q8WUD1; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-5542466, EBI-10973142;
CC Q8WUD1; Q8IYT1: FAM71A; NbExp=3; IntAct=EBI-5542466, EBI-20113335;
CC Q8WUD1; Q8NEG0: FAM71C; NbExp=8; IntAct=EBI-5542466, EBI-752049;
CC Q8WUD1; Q6NXP2-2: FAM71F2; NbExp=6; IntAct=EBI-5542466, EBI-12925824;
CC Q8WUD1; Q08379: GOLGA2; NbExp=6; IntAct=EBI-5542466, EBI-618309;
CC Q8WUD1; Q05084: ICA1; NbExp=4; IntAct=EBI-5542466, EBI-1046751;
CC Q8WUD1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-5542466, EBI-16439278;
CC Q8WUD1; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-5542466, EBI-745021;
CC Q8WUD1; O60806: TBX19; NbExp=3; IntAct=EBI-5542466, EBI-12096770;
CC Q8WUD1; Q6PKC3: TXNDC11; NbExp=3; IntAct=EBI-5542466, EBI-749812;
CC Q8WUD1; Q9H8Y1: VRTN; NbExp=5; IntAct=EBI-5542466, EBI-12894399;
CC Q8WUD1-2; P55212: CASP6; NbExp=3; IntAct=EBI-25835884, EBI-718729;
CC Q8WUD1-2; P22607: FGFR3; NbExp=3; IntAct=EBI-25835884, EBI-348399;
CC Q8WUD1-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-25835884, EBI-8285963;
CC Q8WUD1-2; P06396: GSN; NbExp=3; IntAct=EBI-25835884, EBI-351506;
CC Q8WUD1-2; O00291: HIP1; NbExp=3; IntAct=EBI-25835884, EBI-473886;
CC Q8WUD1-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25835884, EBI-21591415;
CC Q8WUD1-2; P62826: RAN; NbExp=3; IntAct=EBI-25835884, EBI-286642;
CC Q8WUD1-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-25835884, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P59279};
CC Lipid-anchor {ECO:0000250|UniProtKB:P59279}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P59279}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P59279}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P59279}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P59279}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P59279}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:P59279}. Note=Localized in the Golgi
CC apparatus in the round spermatids and in the acrosome in the elongating
CC spermatid. {ECO:0000250|UniProtKB:P59279}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUD1-2; Sequence=VSP_055829;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, prostate, lung, liver, thymus,
CC colon, pancreas, and skeletal muscle, and low levels in placenta. Not
CC detected in heart, brain, spleen, testis, ovary, small intestine and
CC leukocyte.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF468652; AAN86142.1; -; mRNA.
DR EMBL; AK296057; BAG58820.1; -; mRNA.
DR EMBL; AK315354; BAG37750.1; -; mRNA.
DR EMBL; CH471078; EAW66382.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66383.1; -; Genomic_DNA.
DR EMBL; BC020839; AAH20839.1; -; mRNA.
DR EMBL; BC066366; AAH66366.1; -; mRNA.
DR CCDS; CCDS9570.1; -. [Q8WUD1-1]
DR RefSeq; NP_001156852.1; NM_001163380.1.
DR RefSeq; NP_116235.2; NM_032846.3. [Q8WUD1-1]
DR RefSeq; XP_016877200.1; XM_017021711.1.
DR PDB; 2A5J; X-ray; 1.50 A; A=5-176.
DR PDBsum; 2A5J; -.
DR AlphaFoldDB; Q8WUD1; -.
DR SMR; Q8WUD1; -.
DR BioGRID; 124366; 67.
DR IntAct; Q8WUD1; 46.
DR STRING; 9606.ENSP00000380869; -.
DR iPTMnet; Q8WUD1; -.
DR PhosphoSitePlus; Q8WUD1; -.
DR SwissPalm; Q8WUD1; -.
DR BioMuta; RAB2B; -.
DR DMDM; 28436385; -.
DR EPD; Q8WUD1; -.
DR jPOST; Q8WUD1; -.
DR MassIVE; Q8WUD1; -.
DR MaxQB; Q8WUD1; -.
DR PaxDb; Q8WUD1; -.
DR PeptideAtlas; Q8WUD1; -.
DR PRIDE; Q8WUD1; -.
DR ProteomicsDB; 74657; -. [Q8WUD1-1]
DR Antibodypedia; 22150; 212 antibodies from 31 providers.
DR DNASU; 84932; -.
DR Ensembl; ENST00000397762.6; ENSP00000380869.1; ENSG00000129472.15. [Q8WUD1-1]
DR GeneID; 84932; -.
DR KEGG; hsa:84932; -.
DR MANE-Select; ENST00000397762.6; ENSP00000380869.1; NM_032846.4; NP_116235.2.
DR UCSC; uc010tlt.2; human. [Q8WUD1-1]
DR CTD; 84932; -.
DR DisGeNET; 84932; -.
DR GeneCards; RAB2B; -.
DR HGNC; HGNC:20246; RAB2B.
DR HPA; ENSG00000129472; Low tissue specificity.
DR MIM; 607466; gene.
DR neXtProt; NX_Q8WUD1; -.
DR OpenTargets; ENSG00000129472; -.
DR PharmGKB; PA134865942; -.
DR VEuPathDB; HostDB:ENSG00000129472; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000153886; -.
DR InParanoid; Q8WUD1; -.
DR OMA; VEEAFMI; -.
DR OrthoDB; 1271975at2759; -.
DR PhylomeDB; Q8WUD1; -.
DR TreeFam; TF300032; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; Q8WUD1; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q8WUD1; -.
DR BioGRID-ORCS; 84932; 15 hits in 1077 CRISPR screens.
DR ChiTaRS; RAB2B; human.
DR EvolutionaryTrace; Q8WUD1; -.
DR GenomeRNAi; 84932; -.
DR Pharos; Q8WUD1; Tbio.
DR PRO; PR:Q8WUD1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8WUD1; protein.
DR Bgee; ENSG00000129472; Expressed in pancreatic ductal cell and 184 other tissues.
DR ExpressionAtlas; Q8WUD1; baseline and differential.
DR Genevisible; Q8WUD1; HS.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; 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 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; Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..216
FT /note="Ras-related protein Rab-2B"
FT /id="PRO_0000121071"
FT REGION 189..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 13..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2A5J"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2A5J"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2A5J"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..76
FT /note="MTYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMVNIDG
FT KQIKLQIWDTAGQESFRSITRSYY -> MENKSNCKSGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_055829"
FT VARIANT 212
FT /note="N -> T (in dbSNP:rs17106411)"
FT /id="VAR_051709"
FT CONFLICT 168
FT /note="Y -> H (in Ref. 1; AAN86142)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2A5J"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:2A5J"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2A5J"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:2A5J"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:2A5J"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2A5J"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2A5J"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:2A5J"
SQ SEQUENCE 216 AA; 24214 MW; 80A73F6D259701D8 CRC64;
MTYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMVNI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLTSW LEDARQHSSS NMVIMLIGNK
SDLESRRDVK REEGEAFARE HGLIFMETSA KTACNVEEAF INTAKEIYRK IQQGLFDVHN
EANGIKIGPQ QSISTSVGPS ASQRNSRDIG SNSGCC
