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Q9UL26

- RB22A_HUMAN

UniProt

Q9UL26 - RB22A_HUMAN

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Protein
Ras-related protein Rab-22A
Gene
RAB22A, RAB22
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 209GTP By similarity
Nucleotide bindingi60 – 645GTP By similarity
Nucleotide bindingi118 – 1214GTP By similarity
Nucleotide bindingi148 – 1503GTP By similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. GTPase activity Source: UniProtKB
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. endocytosis Source: UniProtKB
  2. endosome organization Source: UniProtKB
  3. protein transport Source: UniProtKB-KW
  4. small GTPase mediated signal transduction Source: InterPro
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-22A
Short name:
Rab-22
Gene namesi
Name:RAB22A
Synonyms:RAB22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9764. RAB22A.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. early endosome Source: UniProtKB
  3. endosome membrane Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. phagocytic vesicle Source: UniProtKB
  6. phagocytic vesicle membrane Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB
  8. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191S → L: Loss of GTPase activity. 1 Publication
Mutagenesisi64 – 641Q → L: Constitutive GTPase activity. Impairs normal protein trafficking through early endosomes. 2 Publications

Organism-specific databases

PharmGKBiPA34112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Ras-related protein Rab-22A
PRO_0000121209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi193 – 1931S-geranylgeranyl cysteine By similarity
Lipidationi194 – 1941S-geranylgeranyl cysteine By similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9UL26.
PaxDbiQ9UL26.
PRIDEiQ9UL26.

PTM databases

PhosphoSiteiQ9UL26.

Expressioni

Gene expression databases

ArrayExpressiQ9UL26.
BgeeiQ9UL26.
CleanExiHS_RAB22A.
GenevestigatoriQ9UL26.

Organism-specific databases

HPAiHPA048921.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEA1Q150753EBI-399456,EBI-298113

Protein-protein interaction databases

BioGridi121505. 10 interactions.
IntActiQ9UL26. 4 interactions.
MINTiMINT-5003659.
STRINGi9606.ENSP00000244040.

Structurei

3D structure databases

ProteinModelPortaliQ9UL26.
SMRiQ9UL26. Positions 2-167.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9UL26.
KOiK07891.
OMAiVTKRSCC.
OrthoDBiEOG77DJ7M.
PhylomeDBiQ9UL26.
TreeFamiTF331262.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UL26-1 [UniParc]FASTAAdd to Basket

« Hide

MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ    50
NELHKFLIWD TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV 100
KELRQHGPPN IVVAIAGNKC DLIDVREVME RDAKDYADSI HAIFVETSAK 150
NAININELFI EISRRIPSTD ANLPSGGKGF KLRRQPSEPK RSCC 194
Length:194
Mass (Da):21,855
Last modified:March 1, 2001 - v2
Checksum:iEBC84711DA3F839B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841R → K in CAC10538. 1 Publication
Sequence conflicti192 – 1932SC → TA in AAL75941. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33497.1.
RefSeqiNP_065724.1. NM_020673.2.
UniGeneiHs.529044.

Genome annotation databases

EnsembliENST00000244040; ENSP00000244040; ENSG00000124209.
GeneIDi57403.
KEGGihsa:57403.
UCSCiuc002xyz.3. human.

Polymorphism databases

DMDMi13633614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33497.1.
RefSeqi NP_065724.1. NM_020673.2.
UniGenei Hs.529044.

3D structure databases

ProteinModelPortali Q9UL26.
SMRi Q9UL26. Positions 2-167.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121505. 10 interactions.
IntActi Q9UL26. 4 interactions.
MINTi MINT-5003659.
STRINGi 9606.ENSP00000244040.

PTM databases

PhosphoSitei Q9UL26.

Polymorphism databases

DMDMi 13633614.

Proteomic databases

MaxQBi Q9UL26.
PaxDbi Q9UL26.
PRIDEi Q9UL26.

Protocols and materials databases

DNASUi 57403.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244040 ; ENSP00000244040 ; ENSG00000124209 .
GeneIDi 57403.
KEGGi hsa:57403.
UCSCi uc002xyz.3. human.

Organism-specific databases

CTDi 57403.
GeneCardsi GC20P056884.
HGNCi HGNC:9764. RAB22A.
HPAi HPA048921.
MIMi 612966. gene.
neXtProti NX_Q9UL26.
PharmGKBi PA34112.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi Q9UL26.
KOi K07891.
OMAi VTKRSCC.
OrthoDBi EOG77DJ7M.
PhylomeDBi Q9UL26.
TreeFami TF331262.

Miscellaneous databases

GeneWikii RAB22A.
GenomeRNAii 57403.
NextBioi 63508.
PROi Q9UL26.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UL26.
Bgeei Q9UL26.
CleanExi HS_RAB22A.
Genevestigatori Q9UL26.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiRB22A_HUMAN
AccessioniPrimary (citable) accession number: Q9UL26
Secondary accession number(s): B3KR86
, E1P605, Q8TF12, Q9H4E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 127 of the entry and version 2 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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