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P51151

- RAB9A_HUMAN

UniProt

P51151 - RAB9A_HUMAN

Protein

Ras-related protein Rab-9A

Gene

RAB9A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in the transport of proteins between the endosomes and the trans Golgi network.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 229GTP
    Nucleotide bindingi62 – 665GTPBy similarity
    Nucleotide bindingi124 – 1274GTP
    Nucleotide bindingi154 – 1563GTP

    GO - Molecular functioni

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

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. positive regulation of exocytosis 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-9A
    Gene namesi
    Name:RAB9A
    Synonyms:RAB9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9792. RAB9A.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Endoplasmic reticulum membrane Curated. Golgi apparatus membrane Curated. Late endosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cytoplasmic vesiclephagosome
    Note: Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi membrane Source: UniProtKB-SubCell
    4. late endosome Source: MGI
    5. lysosome Source: MGI
    6. phagocytic vesicle Source: UniProtKB
    7. phagocytic vesicle membrane Source: UniProtKB-SubCell
    8. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34152.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 201200Ras-related protein Rab-9APRO_0000121139Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei179 – 1791Phosphoserine1 Publication
    Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
    Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP51151.
    PaxDbiP51151.
    PeptideAtlasiP51151.
    PRIDEiP51151.

    PTM databases

    PhosphoSiteiP51151.

    Expressioni

    Gene expression databases

    BgeeiP51151.
    CleanExiHS_RAB9A.
    GenevestigatoriP51151.

    Organism-specific databases

    HPAiCAB016411.
    HPA003094.

    Interactioni

    Subunit structurei

    Interacts (preferentially in its GTP-bound form) with GCC2 (via its GRIP domain).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NISCHQ9Y2I15EBI-4401353,EBI-2688731

    Protein-protein interaction databases

    BioGridi114768. 10 interactions.
    DIPiDIP-46409N.
    IntActiP51151. 2 interactions.
    STRINGi9606.ENSP00000420127.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Helixi20 – 2910
    Beta strandi41 – 5111
    Beta strandi54 – 629
    Helixi67 – 693
    Helixi70 – 734
    Helixi74 – 774
    Beta strandi81 – 888
    Helixi92 – 965
    Helixi98 – 10912
    Turni114 – 1163
    Beta strandi119 – 1246
    Helixi135 – 14410
    Beta strandi150 – 1523
    Turni155 – 1573
    Helixi161 – 17313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WMSX-ray1.25A/B1-177[»]
    ProteinModelPortaliP51151.
    SMRiP51151. Positions 1-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51151.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi36 – 449Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP51151.
    KOiK07899.
    OMAiAHLFHTI.
    OrthoDBiEOG7G4QG8.
    PhylomeDBiP51151.
    TreeFamiTF326442.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P51151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE    50
    VDGHFVTMQI WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN 100
    WKKEFIYYAD VKEPESFPFV ILGNKIDISE RQVSTEEAQA WCRDNGDYPY 150
    FETSAKDATN VAAAFEEAVR RVLATEDRSD HLIQTDTVNL HRKPKPSSSC 200
    C 201
    Length:201
    Mass (Da):22,838
    Last modified:October 1, 1996 - v1
    Checksum:i65B502C21E97DB72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44103 mRNA. Translation: AAC51200.1.
    AF498944 mRNA. Translation: AAM21092.1.
    CR450362 mRNA. Translation: CAG29358.1.
    AK290505 mRNA. Translation: BAF83194.1.
    CH471074 Genomic DNA. Translation: EAW98826.1.
    BC017265 mRNA. Translation: AAH17265.1.
    CCDSiCCDS14156.1.
    PIRiG02361.
    RefSeqiNP_001182257.1. NM_001195328.1.
    NP_004242.1. NM_004251.4.
    UniGeneiHs.495704.

    Genome annotation databases

    EnsembliENST00000464506; ENSP00000420127; ENSG00000123595.
    GeneIDi9367.
    KEGGihsa:9367.
    UCSCiuc004cvm.3. human.

    Polymorphism databases

    DMDMi1710003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44103 mRNA. Translation: AAC51200.1 .
    AF498944 mRNA. Translation: AAM21092.1 .
    CR450362 mRNA. Translation: CAG29358.1 .
    AK290505 mRNA. Translation: BAF83194.1 .
    CH471074 Genomic DNA. Translation: EAW98826.1 .
    BC017265 mRNA. Translation: AAH17265.1 .
    CCDSi CCDS14156.1.
    PIRi G02361.
    RefSeqi NP_001182257.1. NM_001195328.1.
    NP_004242.1. NM_004251.4.
    UniGenei Hs.495704.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WMS X-ray 1.25 A/B 1-177 [» ]
    ProteinModelPortali P51151.
    SMRi P51151. Positions 1-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114768. 10 interactions.
    DIPi DIP-46409N.
    IntActi P51151. 2 interactions.
    STRINGi 9606.ENSP00000420127.

    Chemistry

    ChEMBLi CHEMBL1293294.

    PTM databases

    PhosphoSitei P51151.

    Polymorphism databases

    DMDMi 1710003.

    Proteomic databases

    MaxQBi P51151.
    PaxDbi P51151.
    PeptideAtlasi P51151.
    PRIDEi P51151.

    Protocols and materials databases

    DNASUi 9367.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000464506 ; ENSP00000420127 ; ENSG00000123595 .
    GeneIDi 9367.
    KEGGi hsa:9367.
    UCSCi uc004cvm.3. human.

    Organism-specific databases

    CTDi 9367.
    GeneCardsi GC0XP013707.
    HGNCi HGNC:9792. RAB9A.
    HPAi CAB016411.
    HPA003094.
    MIMi 300284. gene.
    neXtProti NX_P51151.
    PharmGKBi PA34152.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P51151.
    KOi K07899.
    OMAi AHLFHTI.
    OrthoDBi EOG7G4QG8.
    PhylomeDBi P51151.
    TreeFami TF326442.

    Miscellaneous databases

    EvolutionaryTracei P51151.
    GeneWikii RAB9A.
    GenomeRNAii 9367.
    NextBioi 35080.
    PROi P51151.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51151.
    CleanExi HS_RAB9A.
    Genevestigatori P51151.

    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 and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene."
      Davies J.P., Cotter P.D., Ioannou Y.A.
      Genomics 41:131-134(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Muscle.
    7. "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
      Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
      Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling."
      Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M., Pfeffer S.R.
      Mol. Biol. Cell 17:4353-4363(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCC2.
    10. "Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185."
      Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.
      Cell 132:286-298(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCC2.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target."
      Chen L., DiGiammarino E., Zhou X.E., Wang Y., Toh D., Hodge T.W., Meehan E.J.
      J. Biol. Chem. 279:40204-40208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP.

    Entry informationi

    Entry nameiRAB9A_HUMAN
    AccessioniPrimary (citable) accession number: P51151
    Secondary accession number(s): A8K390, Q6ICN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 151 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3