RAB23_HUMAN
ID RAB23_HUMAN Reviewed; 237 AA.
AC Q9ULC3; B2R9I5; Q68DJ6; Q8NI06; Q9P023;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Ras-related protein Rab-23;
DE Flags: Precursor;
GN Name=RAB23; ORFNames=HSPC137;
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].
RC TISSUE=Fetal brain;
RA Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.;
RT "Human mRNA for RAB23 protein.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle;
RA Ikeda A., Yamashita M.;
RT "Expression of RAB-23 in human hair follicle.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-207.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-207.
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 (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [10]
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 [11]
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).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22452336; DOI=10.1111/j.1462-5822.2012.01792.x;
RA Nozawa T., Aikawa C., Goda A., Maruyama F., Hamada S., Nakagawa I.;
RT "The small GTPases Rab9A and Rab23 function at distinct steps in autophagy
RT during group A Streptococcus infection.";
RL Cell. Microbiol. 14:1149-1165(2012).
RN [13]
RP INTERACTION WITH SUFU, FUNCTION, GTPASE ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22365972; DOI=10.1016/j.cellsig.2012.02.004;
RA Chi S., Xie G., Liu H., Chen K., Zhang X., Li C., Xie J.;
RT "Rab23 negatively regulates Gli1 transcriptional factor in a Su(Fu)-
RT dependent manner.";
RL Cell. Signal. 24:1222-1228(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP VARIANTS VAL-13 DEL; ARG-40 AND ALA-101, AND VARIANT CRPT1 ARG-85.
RX PubMed=17503333; DOI=10.1086/518047;
RA Jenkins D., Seelow D., Jehee F.S., Perlyn C.A., Alonso L.G., Bueno D.F.,
RA Donnai D., Josifiova D., Mathijssen I.M.J., Morton J.E.V., Orstavik K.H.,
RA Sweeney E., Wall S.A., Marsh J.L., Nuernberg P., Passos-Bueno M.R.,
RA Wilkie A.O.M.;
RT "RAB23 mutations in Carpenter syndrome imply an unexpected role for
RT hedgehog signaling in cranial-suture development and obesity.";
RL Am. J. Hum. Genet. 80:1162-1170(2007).
RN [16]
RP VARIANTS CRPT1 LYS-12 AND TYR-79 DEL.
RX PubMed=21412941; DOI=10.1002/humu.21457;
RA Jenkins D., Baynam G., De Catte L., Elcioglu N., Gabbett M.T., Hudgins L.,
RA Hurst J.A., Jehee F.S., Oley C., Wilkie A.O.;
RT "Carpenter syndrome: extended RAB23 mutation spectrum and analysis of
RT nonsense-mediated mRNA decay.";
RL Hum. Mutat. 32:E2069-E2078(2011).
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. Together with SUFU, prevents
CC nuclear import of GLI1, and thereby inhibits GLI1 transcription factor
CC activity. Regulates GLI1 in differentiating chondrocytes. Likewise,
CC regulates GLI3 proteolytic processing and modulates GLI2 and GLI3
CC transcription factor activity. Plays a role in autophagic vacuole
CC assembly, and mediates defense against pathogens, such as S.aureus, by
CC promoting their capture by autophagosomes that then merge with
CC lysosomes. {ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:22452336}.
CC -!- SUBUNIT: Interacts with SUFU. {ECO:0000269|PubMed:22365972}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35288};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P35288}. Cytoplasm
CC {ECO:0000269|PubMed:22365972}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:22452336}. Endosome membrane {ECO:0000250,
CC ECO:0000250|UniProtKB:P35288}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane
CC {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 -!- DISEASE: Carpenter syndrome 1 (CRPT1) [MIM:201000]: A rare autosomal
CC recessive disorder characterized by acrocephaly with variable
CC synostosis of the sagittal, lambdoid, and coronal sutures; peculiar
CC facies; brachydactyly of the hands with syndactyly; preaxial
CC polydactyly and syndactyly of the feet; congenital heart defects;
CC growth retardation; intellectual disability; hypogenitalism; and
CC obesity. In addition, cerebral malformations, oral and dental
CC abnormalities, coxa valga, genu valgum, hydronephrosis, precocious
CC puberty, and hearing loss may be observed.
CC {ECO:0000269|PubMed:17503333, ECO:0000269|PubMed:21412941}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB034244; BAA87324.1; -; mRNA.
DR EMBL; AB025427; BAB40309.1; -; mRNA.
DR EMBL; AF161486; AAF29101.1; -; mRNA.
DR EMBL; AF498951; AAM21099.1; -; mRNA.
DR EMBL; AK313796; BAG36532.1; -; mRNA.
DR EMBL; AY585189; AAT79492.1; -; mRNA.
DR EMBL; CR749371; CAH18224.1; -; mRNA.
DR EMBL; AL031321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04476.1; -; Genomic_DNA.
DR EMBL; BC015021; AAH15021.1; -; mRNA.
DR CCDS; CCDS4962.1; -.
DR RefSeq; NP_001265595.1; NM_001278666.1.
DR RefSeq; NP_001265596.1; NM_001278667.1.
DR RefSeq; NP_001265597.1; NM_001278668.1.
DR RefSeq; NP_057361.3; NM_016277.4.
DR RefSeq; NP_899050.1; NM_183227.2.
DR AlphaFoldDB; Q9ULC3; -.
DR SMR; Q9ULC3; -.
DR BioGRID; 119694; 51.
DR IntAct; Q9ULC3; 11.
DR MINT; Q9ULC3; -.
DR STRING; 9606.ENSP00000417610; -.
DR iPTMnet; Q9ULC3; -.
DR PhosphoSitePlus; Q9ULC3; -.
DR SwissPalm; Q9ULC3; -.
DR BioMuta; RAB23; -.
DR DMDM; 12643897; -.
DR EPD; Q9ULC3; -.
DR jPOST; Q9ULC3; -.
DR MassIVE; Q9ULC3; -.
DR MaxQB; Q9ULC3; -.
DR PaxDb; Q9ULC3; -.
DR PeptideAtlas; Q9ULC3; -.
DR PRIDE; Q9ULC3; -.
DR ProteomicsDB; 84975; -.
DR Antibodypedia; 31144; 309 antibodies from 34 providers.
DR DNASU; 51715; -.
DR Ensembl; ENST00000317483.4; ENSP00000320413.3; ENSG00000112210.12.
DR Ensembl; ENST00000468148.6; ENSP00000417610.1; ENSG00000112210.12.
DR GeneID; 51715; -.
DR KEGG; hsa:51715; -.
DR MANE-Select; ENST00000468148.6; ENSP00000417610.1; NM_016277.5; NP_057361.3.
DR UCSC; uc003pds.5; human.
DR CTD; 51715; -.
DR DisGeNET; 51715; -.
DR GeneCards; RAB23; -.
DR HGNC; HGNC:14263; RAB23.
DR HPA; ENSG00000112210; Tissue enhanced (smooth).
DR MalaCards; RAB23; -.
DR MIM; 201000; phenotype.
DR MIM; 606144; gene.
DR neXtProt; NX_Q9ULC3; -.
DR OpenTargets; ENSG00000112210; -.
DR Orphanet; 65759; Carpenter syndrome.
DR PharmGKB; PA34113; -.
DR VEuPathDB; HostDB:ENSG00000112210; -.
DR eggNOG; KOG4252; Eukaryota.
DR GeneTree; ENSGT00940000155064; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9ULC3; -.
DR OMA; RQIQVNG; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9ULC3; -.
DR TreeFam; TF317494; -.
DR PathwayCommons; Q9ULC3; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q9ULC3; -.
DR SIGNOR; Q9ULC3; -.
DR BioGRID-ORCS; 51715; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; RAB23; human.
DR GeneWiki; RAB23; -.
DR GenomeRNAi; 51715; -.
DR Pharos; Q9ULC3; Tbio.
DR PRO; PR:Q9ULC3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9ULC3; protein.
DR Bgee; ENSG00000112210; Expressed in cauda epididymis and 185 other tissues.
DR ExpressionAtlas; Q9ULC3; baseline and differential.
DR Genevisible; Q9ULC3; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:UniProtKB.
DR CDD; cd04106; Rab23_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034114; Rab23.
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 Cell membrane; Craniosynostosis; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Disease variant; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..234
FT /note="Ras-related protein Rab-23"
FT /id="PRO_0000121211"
FT PROPEP 235..237
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370771"
FT REGION 188..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 188..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 234
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 12
FT /note="M -> K (in CRPT1)"
FT /evidence="ECO:0000269|PubMed:21412941"
FT /id="VAR_065294"
FT VARIANT 13
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:17503333"
FT /id="VAR_034900"
FT VARIANT 40
FT /note="K -> R (in dbSNP:rs45442500)"
FT /evidence="ECO:0000269|PubMed:17503333"
FT /id="VAR_034901"
FT VARIANT 79
FT /note="Missing (in CRPT1)"
FT /evidence="ECO:0000269|PubMed:21412941"
FT /id="VAR_065295"
FT VARIANT 85
FT /note="C -> R (in CRPT1)"
FT /evidence="ECO:0000269|PubMed:17503333"
FT /id="VAR_034902"
FT VARIANT 101
FT /note="S -> A (in dbSNP:rs45479896)"
FT /evidence="ECO:0000269|PubMed:17503333"
FT /id="VAR_034903"
FT VARIANT 207
FT /note="G -> S (in dbSNP:rs1040461)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_017159"
FT CONFLICT 95
FT /note="E -> G (in Ref. 3; AAF29101)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="K -> R (in Ref. 3; AAF29101)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="K -> N (in Ref. 3; AAF29101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26659 MW; B9CB96E94DDF6036 CRC64;
MLEEDMEVAI KMVVVGNGAV GKSSMIQRYC KGIFTKDYKK TIGVDFLERQ IQVNDEDVRL
MLWDTAGQEE FDAITKAYYR GAQACVLVFS TTDRESFEAV SSWREKVVAE VGDIPTVLVQ
NKIDLLDDSC IKNEEAEALA KRLKLRFYRT SVKEDLNVNE VFKYLAEKYL QKLKQQIAED
PELTHSSSNK IGVFNTSGGS HSGQNSGTLN GGDVINLRPN KQRTKKNRNP FSSCSIP
