Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P61006

- RAB8A_HUMAN

UniProt

P61006 - RAB8A_HUMAN

Protein

Ras-related protein Rab-8A

Gene

RAB8A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (26 Apr 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis.3 Publications

    Enzyme regulationi

    Activated in response to insulin.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi121 – 1244GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. axonogenesis Source: UniProtKB
    2. cellular response to insulin stimulus Source: UniProtKB
    3. cilium assembly Source: UniProtKB
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. Golgi vesicle fusion to target membrane Source: BHF-UCL
    6. GTP catabolic process Source: GOC
    7. membrane organization Source: Reactome
    8. mitotic cell cycle Source: Reactome
    9. protein localization to plasma membrane Source: UniProtKB
    10. protein transport Source: UniProtKB-KW
    11. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    12. regulation of protein transport Source: Ensembl
    13. small GTPase mediated signal transduction Source: InterPro
    14. vesicle docking involved in exocytosis Source: BHF-UCL

    Keywords - Biological processi

    Cilium biogenesis/degradation, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-8A
    Alternative name(s):
    Oncogene c-mel
    Gene namesi
    Name:RAB8A
    Synonyms:MEL, RAB8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:7007. RAB8A.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Golgi apparatus. Recycling endosome membrane. Cell projectioncilium. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
    Note: Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis.

    GO - Cellular componenti

    1. centrosome Source: MGI
    2. cilium Source: MGI
    3. cytoplasmic vesicle membrane Source: Reactome
    4. dendrite Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi membrane Source: Reactome
    7. neuronal cell body Source: Ensembl
    8. nonmotile primary cilium Source: BHF-UCL
    9. phagocytic vesicle Source: UniProtKB
    10. phagocytic vesicle membrane Source: UniProtKB-SubCell
    11. plasma membrane Source: UniProtKB-SubCell
    12. postsynaptic density Source: Ensembl
    13. recycling endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221T → N: Loss of interaction with MICALL1. 1 Publication
    Mutagenesisi67 – 671Q → L: Probable constitutively active mutant locked in the active GTP-bound form. Stimulates interaction with MICALL1. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA30743.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 204204Ras-related protein Rab-8APRO_0000121130Add
    BLAST
    Propeptidei205 – 2073Removed in mature formSequence AnalysisPRO_0000370793

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei185 – 1851Phosphoserine3 Publications
    Modified residuei204 – 2041Cysteine methyl esterSequence Analysis
    Lipidationi204 – 2041S-geranylgeranyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP61006.
    PaxDbiP61006.
    PeptideAtlasiP61006.
    PRIDEiP61006.

    PTM databases

    PhosphoSiteiP61006.

    Expressioni

    Gene expression databases

    ArrayExpressiP61006.
    BgeeiP61006.
    CleanExiHS_RAB8A.
    GenevestigatoriP61006.

    Interactioni

    Subunit structurei

    Interacts (GTP-bound form) with MICALL1; regulates RAB8A association with recycling endosomes. Interacts with MICALL2; competes with RAB13 and is involved in E-cadherin endocytic recycling. Interacts with MICAL1. Interacts with EHD1. Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and SGSM3. Interacts with RABIF, RIMS2, RPH3A and RPH3A. Interacts with OPTN. Interacts with RAB3IP. Interacts with MYO5B. Interacts with PIFO. Interacts with BIRC6/bruce. Interacts with OCRL.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OCRLQ0196811EBI-722293,EBI-6148898
    RABIFP472242EBI-722293,EBI-713992

    Protein-protein interaction databases

    BioGridi110382. 35 interactions.
    DIPiDIP-43703N.
    IntActiP61006. 11 interactions.
    MINTiMINT-1416277.
    STRINGi9606.ENSP00000300935.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 148
    Helixi21 – 3010
    Turni38 – 414
    Beta strandi42 – 5211
    Beta strandi55 – 6410
    Turni69 – 724
    Helixi73 – 786
    Beta strandi82 – 898
    Helixi93 – 975
    Helixi99 – 10911
    Beta strandi115 – 1217
    Turni122 – 1243
    Helixi126 – 1283
    Helixi133 – 14210
    Beta strandi146 – 1494
    Turni152 – 1554
    Helixi158 – 17417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QBTX-ray2.00A/C/E/G6-176[»]
    3TNFX-ray2.50A6-176[»]
    4LHVX-ray1.95A/B/C/D/E6-176[»]
    4LHWX-ray1.55A/B/C/D/E6-176[»]
    4LHXX-ray3.05A/B1-184[»]
    4LHYX-ray3.10A/B1-184[»]
    4LHZX-ray3.20A/B1-184[»]
    4LI0X-ray3.30A/B1-184[»]
    ProteinModelPortaliP61006.
    SMRiP61006. Positions 6-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP61006.
    KOiK07901.
    OMAiIDKAFYS.
    PhylomeDBiP61006.
    TreeFamiTF314097.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61006-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI    50
    ELDGKRIKLQ IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR 100
    NWIRNIEEHA SADVEKMILG NKCDVNDKRQ VSKERGEKLA LDYGIKFMET 150
    SAKANINVEN AFFTLARDIK AKMDKKLEGN SPQGSNQGVK ITPDQQKRSS 200
    FFRCVLL 207
    Length:207
    Mass (Da):23,668
    Last modified:April 26, 2004 - v1
    Checksum:iAA52DBF54A2CD056
    GO
    Isoform 2 (identifier: P61006-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         161-205: AFFTLARDIK...QKRSSFFRCV → RYQSKNGQKI...PMCSSVRNTA

    Note: No experimental confirmation available.

    Show »
    Length:207
    Mass (Da):23,564
    Checksum:i249CB68DDF955162
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1837LEGNSPQ → WKATAP in AAB19681. (PubMed:1886711)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei161 – 20545AFFTL…FFRCV → RYQSKNGQKIGRQQPPGEQP GSQNHTGPAEEEQLFPMCSS VRNTA in isoform 2. 1 PublicationVSP_056399Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56741 mRNA. Translation: CAA40065.1.
    S53268 mRNA. Translation: AAB19681.1.
    AF498943 mRNA. Translation: AAM21091.1.
    BT007184 mRNA. Translation: AAP35848.1.
    AK293676 mRNA. Translation: BAG57118.1.
    CR536583 mRNA. Translation: CAG38820.1.
    AC008894 Genomic DNA. No translation available.
    CR542274 mRNA. Translation: CAG47070.1.
    CH471106 Genomic DNA. Translation: EAW84526.1.
    BC002977 mRNA. Translation: AAH02977.1.
    CCDSiCCDS12339.1.
    PIRiB49647.
    RefSeqiNP_005361.2. NM_005370.4.
    UniGeneiHs.642874.

    Genome annotation databases

    EnsembliENST00000300935; ENSP00000300935; ENSG00000167461.
    ENST00000586682; ENSP00000467501; ENSG00000167461.
    GeneIDi4218.
    KEGGihsa:4218.
    UCSCiuc002ndn.4. human.

    Polymorphism databases

    DMDMi46810392.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56741 mRNA. Translation: CAA40065.1 .
    S53268 mRNA. Translation: AAB19681.1 .
    AF498943 mRNA. Translation: AAM21091.1 .
    BT007184 mRNA. Translation: AAP35848.1 .
    AK293676 mRNA. Translation: BAG57118.1 .
    CR536583 mRNA. Translation: CAG38820.1 .
    AC008894 Genomic DNA. No translation available.
    CR542274 mRNA. Translation: CAG47070.1 .
    CH471106 Genomic DNA. Translation: EAW84526.1 .
    BC002977 mRNA. Translation: AAH02977.1 .
    CCDSi CCDS12339.1.
    PIRi B49647.
    RefSeqi NP_005361.2. NM_005370.4.
    UniGenei Hs.642874.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QBT X-ray 2.00 A/C/E/G 6-176 [» ]
    3TNF X-ray 2.50 A 6-176 [» ]
    4LHV X-ray 1.95 A/B/C/D/E 6-176 [» ]
    4LHW X-ray 1.55 A/B/C/D/E 6-176 [» ]
    4LHX X-ray 3.05 A/B 1-184 [» ]
    4LHY X-ray 3.10 A/B 1-184 [» ]
    4LHZ X-ray 3.20 A/B 1-184 [» ]
    4LI0 X-ray 3.30 A/B 1-184 [» ]
    ProteinModelPortali P61006.
    SMRi P61006. Positions 6-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110382. 35 interactions.
    DIPi DIP-43703N.
    IntActi P61006. 11 interactions.
    MINTi MINT-1416277.
    STRINGi 9606.ENSP00000300935.

    PTM databases

    PhosphoSitei P61006.

    Polymorphism databases

    DMDMi 46810392.

    Proteomic databases

    MaxQBi P61006.
    PaxDbi P61006.
    PeptideAtlasi P61006.
    PRIDEi P61006.

    Protocols and materials databases

    DNASUi 4218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300935 ; ENSP00000300935 ; ENSG00000167461 .
    ENST00000586682 ; ENSP00000467501 ; ENSG00000167461 .
    GeneIDi 4218.
    KEGGi hsa:4218.
    UCSCi uc002ndn.4. human.

    Organism-specific databases

    CTDi 4218.
    GeneCardsi GC19P016222.
    HGNCi HGNC:7007. RAB8A.
    MIMi 165040. gene.
    neXtProti NX_P61006.
    PharmGKBi PA30743.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P61006.
    KOi K07901.
    OMAi IDKAFYS.
    PhylomeDBi P61006.
    TreeFami TF314097.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi RAB8A. human.
    GeneWikii RAB8A.
    GenomeRNAii 4218.
    NextBioi 16637.
    PROi P61006.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61006.
    Bgeei P61006.
    CleanExi HS_RAB8A.
    Genevestigatori P61006.

    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. "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells."
      Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A., Louvard D.
      J. Cell Biol. 124:101-115(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The MEL gene: a new member of the RAB/YPT class of RAS-related genes."
      Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R., Johnson K.J.
      Oncogene 6:1347-1351(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Cerebellum.
    6. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Skin.
    10. "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif."
      Joberty G., Tavitian A., Zahraoui A.
      FEBS Lett. 330:323-328(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-204.
    11. "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
      Hattula K., Furuhjelm J., Arffman A., Peranen J.
      Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION.
      Tissue: Brain.
    12. "Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
      Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
      J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN.
    13. "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-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
      Pohl C., Jentsch S.
      Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC6/BRUCE.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: INTERACTION WITH PIFO.
    18. "A molecular network for de novo generation of the apical surface and lumen."
      Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
      Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
      Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
      Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF THR-22 AND GLN-67.
    20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
      Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
      Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO5B.
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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.
    25. "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."
      Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., Shu X., Pei D.
      Cell Res. 22:333-345(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CILIOGENESIS, SUBCELLULAR LOCATION.
    26. Cited for: INTERACTION WITH OCRL.
    27. "A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1."
      Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S., Erdmann K.S., Itzen A.
      EMBO J. 30:1659-1670(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-176 IN COMPLEX WITH OCRL.

    Entry informationi

    Entry nameiRAB8A_HUMAN
    AccessioniPrimary (citable) accession number: P61006
    Secondary accession number(s): B4DEK7, P24407, Q6FHV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 121 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 19
      Human chromosome 19: 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