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Protein

Ras-related protein Rab-20

Gene

RAB20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi55 – 595GTPBy similarity
Nucleotide bindingi113 – 1164GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • intracellular protein transport Source: GO_Central
  • metabolic process Source: GOC
  • phagosome acidification Source: UniProtKB
  • phagosome-lysosome fusion Source: UniProtKB
  • Rab protein signal transduction Source: GO_Central
  • regulation of endocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-20
Gene namesi
Name:RAB20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:18260. RAB20.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34110.

Polymorphism and mutation databases

BioMutaiRAB20.
DMDMi20139805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Ras-related protein Rab-20PRO_0000121202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi232 – 2321S-geranylgeranyl cysteineBy similarity
Lipidationi233 – 2331S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9NX57.
PaxDbiQ9NX57.
PRIDEiQ9NX57.

PTM databases

PhosphoSiteiQ9NX57.

Expressioni

Tissue specificityi

Low or absent expression in normal pancreas and stronger expression in 15 of 18 exocrine pancreatic adenocarcinomas (at protein level).1 Publication

Gene expression databases

BgeeiQ9NX57.
CleanExiHS_RAB20.
GenevisibleiQ9NX57. HS.

Organism-specific databases

HPAiHPA052111.
HPA068647.

Interactioni

Protein-protein interaction databases

BioGridi120781. 2 interactions.
STRINGi9606.ENSP00000267328.

Structurei

3D structure databases

ProteinModelPortaliQ9NX57.
SMRiQ9NX57. Positions 7-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi33 – 419Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG097927.
InParanoidiQ9NX57.
KOiK07911.
OMAiMRKPDGK.
OrthoDBiEOG78D7MT.
PhylomeDBiQ9NX57.
TreeFamiTF331574.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NX57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKPDSKIVL LGDMNVGKTS LLQRYMERRF PDTVSTVGGA FYLKQWRSYN
60 70 80 90 100
ISIWDTAGRE QFHGLGSMYC RGAAAIILTY DVNHRQSLVE LEDRFLGLTD
110 120 130 140 150
TASKDCLFAI VGNKVDLTEE GALAGQEKEE CSPNMDAGDR VSPRAPKQVQ
160 170 180 190 200
LEDAVALYKK ILKYKMLDEQ DVPAAEQMCF ETSAKTGYNV DLLFETLFDL
210 220 230
VVPMILQQRA ERPSHTVDIS SHKPPKRTRS GCCA
Length:234
Mass (Da):26,277
Last modified:October 1, 2000 - v1
Checksum:iA0201E23BBF75DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621F → I in BAA91171 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341N → S.
Corresponds to variant rs426453 [ dbSNP | Ensembl ].
VAR_017158

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272065 mRNA. Translation: CAC81247.1.
AK000436 mRNA. Translation: BAA91163.1.
AK000446 mRNA. Translation: BAA91171.1.
AL139385 Genomic DNA. Translation: CAI17006.1.
CH471085 Genomic DNA. Translation: EAX09113.1.
BC026025 mRNA. Translation: AAH26025.1.
CCDSiCCDS9512.1.
RefSeqiNP_060287.1. NM_017817.2.
UniGeneiHs.743563.

Genome annotation databases

EnsembliENST00000267328; ENSP00000267328; ENSG00000139832.
GeneIDi55647.
KEGGihsa:55647.
UCSCiuc001vqy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272065 mRNA. Translation: CAC81247.1.
AK000436 mRNA. Translation: BAA91163.1.
AK000446 mRNA. Translation: BAA91171.1.
AL139385 Genomic DNA. Translation: CAI17006.1.
CH471085 Genomic DNA. Translation: EAX09113.1.
BC026025 mRNA. Translation: AAH26025.1.
CCDSiCCDS9512.1.
RefSeqiNP_060287.1. NM_017817.2.
UniGeneiHs.743563.

3D structure databases

ProteinModelPortaliQ9NX57.
SMRiQ9NX57. Positions 7-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120781. 2 interactions.
STRINGi9606.ENSP00000267328.

PTM databases

PhosphoSiteiQ9NX57.

Polymorphism and mutation databases

BioMutaiRAB20.
DMDMi20139805.

Proteomic databases

MaxQBiQ9NX57.
PaxDbiQ9NX57.
PRIDEiQ9NX57.

Protocols and materials databases

DNASUi55647.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267328; ENSP00000267328; ENSG00000139832.
GeneIDi55647.
KEGGihsa:55647.
UCSCiuc001vqy.3. human.

Organism-specific databases

CTDi55647.
GeneCardsiGC13M111175.
HGNCiHGNC:18260. RAB20.
HPAiHPA052111.
HPA068647.
neXtProtiNX_Q9NX57.
PharmGKBiPA34110.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG097927.
InParanoidiQ9NX57.
KOiK07911.
OMAiMRKPDGK.
OrthoDBiEOG78D7MT.
PhylomeDBiQ9NX57.
TreeFamiTF331574.

Miscellaneous databases

GenomeRNAii55647.
NextBioi60342.
PROiQ9NX57.

Gene expression databases

BgeeiQ9NX57.
CleanExiHS_RAB20.
GenevisibleiQ9NX57. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human Rab20 overexpressed in exocrine pancreatic carcinoma."
    Amillet J.-M., Ferbus D., Real F.X., Antony C., Muleris M., Gress T.M., Goubin G.
    Hum. Pathol. 37:256-263(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
    Seto S., Tsujimura K., Koide Y.
    Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRAB20_HUMAN
AccessioniPrimary (citable) accession number: Q9NX57
Secondary accession number(s): Q5T9X5, Q9NX49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.