RBL2B_HUMAN
ID RBL2B_HUMAN Reviewed; 228 AA.
AC Q9UNT1; Q5TZT8; Q96C33;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Rab-like protein 2B;
GN Name=RABL2B;
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=10444334; DOI=10.1006/geno.1999.5889;
RA Wong A.C., Shkolny D., Dorman A., Willingham D., Roe B.A., McDermid H.E.;
RT "Two novel human RAB genes with near identical sequence each map to a
RT telomere-associated region: the subtelomeric region of 22q13.3 and the
RT ancestral telomere band 2q13.";
RL Genomics 59:326-334(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, and Uterus;
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 TISSUE SPECIFICITY.
RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA Ormandy C.J., O'Bryan M.K.;
RT "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT transport, and tail assembly.";
RL PLoS Genet. 8:E1002969-E1002969(2012).
RN [6]
RP FUNCTION, INTERACTION WITH CEP19 AND THE IFT74-IFT81 HETERODIMER,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF SER-35 AND GLN-80, AND PHYLOGENETIC
RP ANALYSIS.
RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.;
RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
RT transport at the ciliary base.";
RL Dev. Cell 42:1-15(2017).
RN [7]
RP FUNCTION, INTERACTION WITH CEP19 AND THE IFT74-IFT81 HETERODIMER,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-35; ASP-73 AND GLN-80.
RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017;
RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and
RT participates in ciliary assembly.";
RL Mol. Biol. Cell 28:1652-1666(2017).
CC -!- FUNCTION: Small GTPase required for ciliation. Activated in a guanine
CC nucleotide exchange factor (GEF)-independent manner via its intrinsic
CC GDP for GTP nucleotide exchange ability (PubMed:28625565). Involved in
CC ciliary assembly by binding the intraflagellar transport (IFT) complex
CC B from the large pool pre-docked at the base of the cilium and thus
CC triggers its entry into the cilia (PubMed:28625565, PubMed:28428259).
CC {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565}.
CC -!- SUBUNIT: Interacts (in its GTP-bound form) with CEP19 (via residues
CC 121-150); this interaction is required for its localization to the
CC mother centriole and cilium basal body. Interacts (in its GTP-bound
CC form) with the intraflagellar transport (IFT) complex B (via the IFT74-
CC IFT81 heterodimer) (PubMed:28625565, PubMed:28428259). Binding to CEP19
CC and the IFT74-IFT81 heterodimer is mutually exclusive
CC (PubMed:28428259). {ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565}.
CC -!- INTERACTION:
CC Q9UNT1-2; Q96LK0: CEP19; NbExp=3; IntAct=EBI-12256104, EBI-741885;
CC Q9UNT1-2; P22607: FGFR3; NbExp=3; IntAct=EBI-12256104, EBI-348399;
CC Q9UNT1-2; P06396: GSN; NbExp=3; IntAct=EBI-12256104, EBI-351506;
CC Q9UNT1-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12256104, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:28428259}. Cytoplasm
CC {ECO:0000269|PubMed:28625565}. Note=Localizes on the mother centriole.
CC Localizes slightly apical to the subdistal appendage, but below the
CC distal appendage. {ECO:0000269|PubMed:28625565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UNT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNT1-2; Sequence=VSP_005532;
CC Name=3;
CC IsoId=Q9UNT1-3; Sequence=VSP_041061;
CC -!- TISSUE SPECIFICITY: Expressed in the testis.
CC {ECO:0000269|PubMed:23055941}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF095352; AAD51379.1; -; mRNA.
DR EMBL; BT020037; AAV38840.1; -; mRNA.
DR EMBL; AC002055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014879; AAH14879.1; -; mRNA.
DR EMBL; BC024281; AAH24281.1; -; mRNA.
DR EMBL; BC075856; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14102.1; -. [Q9UNT1-1]
DR CCDS; CCDS33683.1; -. [Q9UNT1-2]
DR CCDS; CCDS46738.1; -. [Q9UNT1-3]
DR RefSeq; NP_001003789.1; NM_001003789.1. [Q9UNT1-2]
DR RefSeq; NP_001124391.1; NM_001130919.1. [Q9UNT1-2]
DR RefSeq; NP_001124392.1; NM_001130920.1. [Q9UNT1-2]
DR RefSeq; NP_001124393.1; NM_001130921.1. [Q9UNT1-2]
DR RefSeq; NP_001124394.1; NM_001130922.1. [Q9UNT1-1]
DR RefSeq; NP_001124395.1; NM_001130923.1. [Q9UNT1-3]
DR RefSeq; NP_009012.1; NM_007081.2. [Q9UNT1-1]
DR RefSeq; XP_005261956.1; XM_005261899.2.
DR RefSeq; XP_011528977.1; XM_011530675.1.
DR RefSeq; XP_016884036.1; XM_017028547.1. [Q9UNT1-3]
DR RefSeq; XP_016884037.1; XM_017028548.1.
DR RefSeq; XP_016884038.1; XM_017028549.1.
DR RefSeq; XP_016884041.1; XM_017028552.1. [Q9UNT1-2]
DR RefSeq; XP_016884042.1; XM_017028553.1.
DR RefSeq; XP_016884043.1; XM_017028554.1.
DR RefSeq; XP_016884044.1; XM_017028555.1. [Q9UNT1-2]
DR RefSeq; XP_016884045.1; XM_017028556.1. [Q9UNT1-1]
DR RefSeq; XP_016884046.1; XM_017028557.1.
DR RefSeq; XP_016884047.1; XM_017028558.1.
DR AlphaFoldDB; Q9UNT1; -.
DR SMR; Q9UNT1; -.
DR BioGRID; 116329; 10.
DR IntAct; Q9UNT1; 8.
DR STRING; 9606.ENSP00000378958; -.
DR iPTMnet; Q9UNT1; -.
DR PhosphoSitePlus; Q9UNT1; -.
DR BioMuta; RABL2B; -.
DR DMDM; 12229940; -.
DR EPD; Q9UNT1; -.
DR jPOST; Q9UNT1; -.
DR MassIVE; Q9UNT1; -.
DR MaxQB; Q9UNT1; -.
DR PeptideAtlas; Q9UNT1; -.
DR PRIDE; Q9UNT1; -.
DR ProteomicsDB; 85329; -. [Q9UNT1-1]
DR ProteomicsDB; 85330; -. [Q9UNT1-2]
DR ProteomicsDB; 85331; -. [Q9UNT1-3]
DR Antibodypedia; 28876; 51 antibodies from 21 providers.
DR DNASU; 11158; -.
DR Ensembl; ENST00000354869.8; ENSP00000346940.3; ENSG00000079974.19. [Q9UNT1-2]
DR Ensembl; ENST00000395593.7; ENSP00000378958.3; ENSG00000079974.19. [Q9UNT1-3]
DR Ensembl; ENST00000395595.8; ENSP00000378960.3; ENSG00000079974.19. [Q9UNT1-2]
DR Ensembl; ENST00000395598.7; ENSP00000378962.3; ENSG00000079974.19. [Q9UNT1-1]
DR Ensembl; ENST00000435118.5; ENSP00000401906.1; ENSG00000079974.19. [Q9UNT1-1]
DR Ensembl; ENST00000691320.1; ENSP00000509250.1; ENSG00000079974.19. [Q9UNT1-2]
DR GeneID; 11158; -.
DR KEGG; hsa:11158; -.
DR MANE-Select; ENST00000691320.1; ENSP00000509250.1; NM_001130919.3; NP_001124391.1. [Q9UNT1-2]
DR UCSC; uc003bnk.2; human. [Q9UNT1-1]
DR CTD; 11158; -.
DR DisGeNET; 11158; -.
DR GeneCards; RABL2B; -.
DR HGNC; HGNC:9800; RABL2B.
DR HPA; ENSG00000079974; Tissue enhanced (epididymis).
DR MIM; 605413; gene.
DR neXtProt; NX_Q9UNT1; -.
DR OpenTargets; ENSG00000079974; -.
DR PharmGKB; PA34160; -.
DR VEuPathDB; HostDB:ENSG00000079974; -.
DR GeneTree; ENSGT00940000156551; -.
DR HOGENOM; CLU_041217_13_1_1; -.
DR InParanoid; Q9UNT1; -.
DR OMA; DGYKPQQ; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9UNT1; -.
DR TreeFam; TF329398; -.
DR PathwayCommons; Q9UNT1; -.
DR SignaLink; Q9UNT1; -.
DR BioGRID-ORCS; 11158; 21 hits in 991 CRISPR screens.
DR GenomeRNAi; 11158; -.
DR Pharos; Q9UNT1; Tdark.
DR PRO; PR:Q9UNT1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UNT1; protein.
DR Bgee; ENSG00000079974; Expressed in right uterine tube and 94 other tissues.
DR ExpressionAtlas; Q9UNT1; baseline and differential.
DR Genevisible; Q9UNT1; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR CDD; cd04124; RabL2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041835; RabL2.
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 Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; GTP-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..228
FT /note="Rab-like protein 2B"
FT /id="PRO_0000121264"
FT REGION 200..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 136
FT /note="D -> DA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_005532"
FT VAR_SEQ 168
FT /note="K -> KVWLTAEVASK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041061"
FT MUTAGEN 35
FT /note="S->N: GDP-locked form; mild defects in ciliary
FT assembly. Loss of interaction with the intraflagellar
FT transport (IFT) complex B via the IFT74-IFT81 heterodimer.
FT Loss of interaction with CEP19. Loss of localization to the
FT centrosome. Loss of localization to the base of the
FT cilium."
FT /evidence="ECO:0000269|PubMed:28428259,
FT ECO:0000269|PubMed:28625565"
FT MUTAGEN 73
FT /note="D->G: Mild defects in ciliary assembly. Loss of
FT interaction with the intraflagellar transport (IFT) complex
FT B via the IFT74-IFT81 heterodimer. Interacts with CEP19."
FT /evidence="ECO:0000269|PubMed:28428259"
FT MUTAGEN 80
FT /note="Q->L: GTP-locked form; interacts with the
FT intraflagellar transport (IFT) complex B via the IFT74-
FT IFT81 heterodimer. Localizes to the base of the cilium and
FT accumulates within the cilium and at the tip in specific
FT puncta."
FT /evidence="ECO:0000269|PubMed:28428259,
FT ECO:0000269|PubMed:28625565"
SQ SEQUENCE 228 AA; 26101 MW; C2F4335FA0AAFD61 CRC64;
MAEDKTKPSE LDQGKYDADD NVKIICLGDS AVGKSKLMER FLMDGFQPQQ LSTYALTLYK
HTATVDGRTI LVDFWDTAGQ ERFQSMHASY YHKAHACIMV FDVQRKVTYR NLSTWYTELR
EFRPEIPCIV VANKIDDINV TQKSFNFAKK FSLPLYFVSA ADGTNVVKLF NDAIRLAVSY
KQNSQDFMDE IFQELENFSL EQEEEDVPDQ EQSSSIETPS EEAASPHS
