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   24-JAN-2024, entry version 187.
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   IntAct; Q9NX57; 1.
DR   STRING; 9606.ENSP00000267328; -.
DR   iPTMnet; Q9NX57; -.
DR   PhosphoSitePlus; Q9NX57; -.
DR   SwissPalm; Q9NX57; -.
DR   BioMuta; RAB20; -.
DR   DMDM; 20139805; -.
DR   EPD; Q9NX57; -.
DR   jPOST; Q9NX57; -.
DR   MassIVE; Q9NX57; -.
DR   MaxQB; Q9NX57; -.
DR   PaxDb; 9606-ENSP00000267328; -.
DR   PeptideAtlas; Q9NX57; -.
DR   ProteomicsDB; 83044; -.
DR   Pumba; Q9NX57; -.
DR   Antibodypedia; 25565; 326 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   AGR; HGNC:18260; -.
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; YNIAIWD; -.
DR   OrthoDB; 3910590at2759; -.
DR   PhylomeDB; Q9NX57; -.
DR   TreeFam; TF331574; -.
DR   PathwayCommons; Q9NX57; -.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 55647; 14 hits in 1156 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 153 other cell types or tissues.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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 type II interferon; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041836; Rab20.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24073; DRAB5-RELATED; 1.
DR   PANTHER; PTHR24073:SF941; RAS-RELATED PROTEIN RAB-20; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; Q9NX57; HS.
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
//