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Q9UL26

- RB22A_HUMAN

UniProt

Q9UL26 - RB22A_HUMAN

Protein

Ras-related protein Rab-22A

Gene

RAB22A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Mar 2001)
      Previous versions | rss
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    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 – 209GTPBy similarity
    Nucleotide bindingi60 – 645GTPBy similarity
    Nucleotide bindingi118 – 1214GTPBy similarity
    Nucleotide bindingi148 – 1503GTPBy similarity

    GO - Molecular functioni

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

    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

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

    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

    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-22APRO_0000121209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi193 – 1931S-geranylgeranyl cysteineBy similarity
    Lipidationi194 – 1941S-geranylgeranyl cysteineBy 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.By similarity2 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

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

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    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

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 128 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