RAB20_HUMAN
ID RAB20_HUMAN Reviewed; 234 AA.
AC Q9NX57; Q5T9X5; Q9NX49;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ras-related protein Rab-20;
GN Name=RAB20;
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=16613320; DOI=10.1016/j.humpath.2005.10.017;
RA Amillet J.-M., Ferbus D., Real F.X., Antony C., Muleris M., Gress T.M.,
RA Goubin G.;
RT "Characterization of human Rab20 overexpressed in exocrine pancreatic
RT carcinoma.";
RL Hum. Pathol. 37:256-263(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 FUNCTION, AND 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: Plays a role in apical endocytosis/recycling. Plays a role in
CC the maturation and acidification of phagosomes that engulf pathogens,
CC such as S.aureus and M.tuberculosis. Plays a role in the fusion of
CC phagosomes with lysosomes. {ECO:0000269|PubMed:21255211}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16613320}.
CC Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Highly enriched on
CC apical endocytic structures in polarized epithelial cells of kidney
CC proximal tubules (By similarity). Recruited to phagosomes containing
CC S.aureus or M.tuberculosis (PubMed:21255211).
CC {ECO:0000250|UniProtKB:P35295, ECO:0000269|PubMed:21255211}.
CC -!- TISSUE SPECIFICITY: Low or absent expression in normal pancreas and
CC stronger expression in 15 of 18 exocrine pancreatic adenocarcinomas (at
CC protein level). {ECO:0000269|PubMed:16613320}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ272065; CAC81247.1; -; mRNA.
DR EMBL; AK000436; BAA91163.1; -; mRNA.
DR EMBL; AK000446; BAA91171.1; -; mRNA.
DR EMBL; AL139385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09113.1; -; Genomic_DNA.
DR EMBL; BC026025; AAH26025.1; -; mRNA.
DR CCDS; CCDS9512.1; -.
DR RefSeq; NP_060287.1; NM_017817.2.
DR AlphaFoldDB; Q9NX57; -.
DR SMR; Q9NX57; -.
DR BioGRID; 120781; 18.
DR STRING; 9606.ENSP00000267328; -.
DR iPTMnet; Q9NX57; -.
DR PhosphoSitePlus; Q9NX57; -.
DR BioMuta; RAB20; -.
DR DMDM; 20139805; -.
DR EPD; Q9NX57; -.
DR jPOST; Q9NX57; -.
DR MassIVE; Q9NX57; -.
DR MaxQB; Q9NX57; -.
DR PaxDb; Q9NX57; -.
DR PeptideAtlas; Q9NX57; -.
DR PRIDE; Q9NX57; -.
DR ProteomicsDB; 83044; -.
DR Antibodypedia; 25565; 293 antibodies from 28 providers.
DR DNASU; 55647; -.
DR Ensembl; ENST00000267328.5; ENSP00000267328.3; ENSG00000139832.5.
DR GeneID; 55647; -.
DR KEGG; hsa:55647; -.
DR MANE-Select; ENST00000267328.5; ENSP00000267328.3; NM_017817.3; NP_060287.1.
DR UCSC; uc001vqy.4; human.
DR CTD; 55647; -.
DR DisGeNET; 55647; -.
DR GeneCards; RAB20; -.
DR HGNC; HGNC:18260; RAB20.
DR HPA; ENSG00000139832; Low tissue specificity.
DR neXtProt; NX_Q9NX57; -.
DR OpenTargets; ENSG00000139832; -.
DR PharmGKB; PA34110; -.
DR VEuPathDB; HostDB:ENSG00000139832; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000161024; -.
DR HOGENOM; CLU_041217_12_0_1; -.
DR InParanoid; Q9NX57; -.
DR OMA; HDCIYAL; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9NX57; -.
DR TreeFam; TF331574; -.
DR PathwayCommons; Q9NX57; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 55647; 13 hits in 1078 CRISPR screens.
DR GenomeRNAi; 55647; -.
DR Pharos; Q9NX57; Tbio.
DR PRO; PR:Q9NX57; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NX57; protein.
DR Bgee; ENSG00000139832; Expressed in secondary oocyte and 151 other tissues.
DR Genevisible; Q9NX57; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090383; P:phagosome acidification; IMP:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
DR CDD; cd04126; Rab20; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041836; Rab20.
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; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..234
FT /note="Ras-related protein Rab-20"
FT /id="PRO_0000121202"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..41
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 55..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 113..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 232
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 233
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 134
FT /note="N -> S (in dbSNP:rs426453)"
FT /id="VAR_017158"
FT CONFLICT 62
FT /note="F -> I (in Ref. 2; BAA91171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26277 MW; A0201E23BBF75DC8 CRC64;
MRKPDSKIVL LGDMNVGKTS LLQRYMERRF PDTVSTVGGA FYLKQWRSYN ISIWDTAGRE
QFHGLGSMYC RGAAAIILTY DVNHRQSLVE LEDRFLGLTD TASKDCLFAI VGNKVDLTEE
GALAGQEKEE CSPNMDAGDR VSPRAPKQVQ LEDAVALYKK ILKYKMLDEQ DVPAAEQMCF
ETSAKTGYNV DLLFETLFDL VVPMILQQRA ERPSHTVDIS SHKPPKRTRS GCCA
