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Q9UL26 (RB22A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-22A

Short name=Rab-22
Gene names
Name:RAB22A
Synonyms:RAB22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form. Ref.9 Ref.11

Subunit structure

Interacts directly with ZFYVE20 By similarity. Binds EEA1 By similarity. Interacts (in its GTP-bound form) with RABGEF1. Interacts (in its GTP-bound form) with RINL. Ref.10 Ref.11

Subcellular location

Endosome membrane; Lipid-anchor By similarity. Cell membrane; Lipid-anchor By similarity. Early endosome. Cell projectionruffle. Cytoplasmic vesicle. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.9 Ref.10 Ref.12

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasmic vesicle
Endosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from direct assay PubMed 11870209. Source: UniProtKB

endosome organization

Inferred from expression pattern PubMed 11870209. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from direct assay PubMed 11870209. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

phagocytic vesicle

Inferred from direct assay Ref.12. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 11870209. Source: UniProtKB

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement PubMed 11870209. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EEA1Q150753EBI-399456,EBI-298113

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Ras-related protein Rab-22A
PRO_0000121209

Regions

Nucleotide binding12 – 209GTP By similarity
Nucleotide binding60 – 645GTP By similarity
Nucleotide binding118 – 1214GTP By similarity
Nucleotide binding148 – 1503GTP By similarity
Motif34 – 429Effector region By similarity

Amino acid modifications

Lipidation1931S-geranylgeranyl cysteine By similarity
Lipidation1941S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis191S → L: Loss of GTPase activity. Ref.10
Mutagenesis641Q → L: Constitutive GTPase activity. Impairs normal protein trafficking through early endosomes. Ref.9 Ref.10
Sequence conflict1841R → K in CAC10538. Ref.3
Sequence conflict192 – 1932SC → TA in AAL75941. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UL26 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: EBC84711DA3F839B

FASTA19421,855
        10         20         30         40         50         60 
MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD 

        70         80         90        100        110        120 
TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV KELRQHGPPN IVVAIAGNKC 

       130        140        150        160        170        180 
DLIDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANLPSGGKGF 

       190 
KLRRQPSEPK RSCC 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel human cDNA similar to Canis familiaris mRNA for Rab22 protein."
Ding J.B., Yu L., Zhao S.Y.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an apically located GTP-binding protein in polarised intestinal epithelial cells."
Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A., Fransen J.A.M.
Eur. J. Cell Biol. 79:308-316(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon carcinoma.
[3]"Mapping and characterization of the human RAB22A gene."
Kussmann S., Hansmann I., Schlote D.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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. expand/collapse author list , 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].
Tissue: Tongue.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Colon and Uterus.
[9]"Rab22a regulates the sorting of transferrin to recycling endosomes."
Magadan J.G., Barbieri M.A., Mesa R., Stahl P.D., Mayorga L.S.
Mol. Cell. Biol. 26:2595-2614(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-64.
[10]"Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide exchange factor for Rab5a and Rab22."
Woller B., Luiskandl S., Popovic M., Prieler B.E., Ikonge G., Mutzl M., Rehmann H., Herbst R.
Biochim. Biophys. Acta 1813:1198-1210(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RINL, MUTAGENESIS OF SER-19 AND GLN-64, SUBCELLULAR LOCATION.
[11]"Rab22 controls NGF signaling and neurite outgrowth in PC12 cells."
Wang L., Liang Z., Li G.
Mol. Biol. Cell 22:3853-3860(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RABGEF1.
[12]"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: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125104 mRNA. Translation: AAL75941.1.
AF091034 mRNA. Translation: AAF00047.2.
AJ276210 mRNA. Translation: CAC10538.1.
BT007046 mRNA. Translation: AAP35695.1.
AK091180 mRNA. Translation: BAG52298.1.
AL035455 Genomic DNA. Translation: CAC15020.1.
CH471077 Genomic DNA. Translation: EAW75496.1.
CH471077 Genomic DNA. Translation: EAW75497.1.
BC015710 mRNA. Translation: AAH15710.1.
BC063457 mRNA. Translation: AAH63457.1.
RefSeqNP_065724.1. NM_020673.2.
UniGeneHs.529044.

3D structure databases

ProteinModelPortalQ9UL26.
SMRQ9UL26. Positions 2-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121505. 10 interactions.
IntActQ9UL26. 4 interactions.
MINTMINT-5003659.
STRING9606.ENSP00000244040.

PTM databases

PhosphoSiteQ9UL26.

Polymorphism databases

DMDM13633614.

Proteomic databases

PaxDbQ9UL26.
PRIDEQ9UL26.

Protocols and materials databases

DNASU57403.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244040; ENSP00000244040; ENSG00000124209.
GeneID57403.
KEGGhsa:57403.
UCSCuc002xyz.3. human.

Organism-specific databases

CTD57403.
GeneCardsGC20P056884.
HGNCHGNC:9764. RAB22A.
HPAHPA048921.
MIM612966. gene.
neXtProtNX_Q9UL26.
PharmGKBPA34112.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9UL26.
KOK07891.
OMAKCDLSDA.
OrthoDBEOG77DJ7M.
PhylomeDBQ9UL26.
TreeFamTF331262.

Gene expression databases

ArrayExpressQ9UL26.
BgeeQ9UL26.
CleanExHS_RAB22A.
GenevestigatorQ9UL26.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB22A.
GenomeRNAi57403.
NextBio63508.
PROQ9UL26.
SOURCESearch...

Entry information

Entry nameRB22A_HUMAN
AccessionPrimary (citable) accession number: Q9UL26
Secondary accession number(s): B3KR86 expand/collapse secondary AC list , E1P605, Q8TF12, Q9H4E6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM