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)

P20338

- RAB4A_HUMAN

UniProt

P20338 - RAB4A_HUMAN

Protein

Ras-related protein Rab-4A

Gene

RAB4A

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 160 (01 Oct 2014)
      Sequence version 3 (06 Mar 2013)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protein transport. Probably involved in vesicular traffic By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 289GTP1 Publication
    Nucleotide bindingi68 – 725GTP1 Publication
    Nucleotide bindingi126 – 1294GTP1 Publication
    Nucleotide bindingi156 – 1583GTP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. antigen processing and presentation Source: UniProtKB
    2. GTP catabolic process Source: GOC
    3. membrane organization Source: Reactome
    4. regulation of endocytosis Source: Ensembl
    5. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinkiP20338.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-4A
    Gene namesi
    Name:RAB4A
    Synonyms:RAB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9781. RAB4A.

    Subcellular locationi

    Membrane; Peripheral membrane protein. Cytoplasm
    Note: Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1.

    GO - Cellular componenti

    1. endosome Source: Ensembl
    2. extracellular vesicular exosome Source: UniProtKB
    3. membrane Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: UniProtKB
    5. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511G → A: 10-fold decrease in ZFYVE20 binding affinity. 1 Publication
    Mutagenesisi51 – 511G → L: 10-fold decrease in ZFYVE20 binding affinity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 218218Ras-related protein Rab-4APRO_0000121093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041Phosphoserine; by CDK12 Publications
    Lipidationi216 – 2161S-geranylgeranyl cysteineBy similarity
    Modified residuei218 – 2181Cysteine methyl esterBy similarity
    Lipidationi218 – 2181S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

    Phosphorylated by CDK1 kinase during mitosis.2 Publications

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP20338.
    PaxDbiP20338.
    PRIDEiP20338.

    PTM databases

    PhosphoSiteiP20338.

    Expressioni

    Gene expression databases

    BgeeiP20338.
    CleanExiHS_RAB4A.
    GenevestigatoriP20338.

    Organism-specific databases

    HPAiCAB004990.

    Interactioni

    Subunit structurei

    Interacts with SGSM1, SGSM2 and SGSM3 By similarity. Interacts with RAB11FIP1, RABEP1, ZFYVE20 and RUFY1. Interacts (membrane-bound form) with NDRG1; the interaction involves NDRG1 in vesicular recycling of E-cadherin.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GDI1P311502EBI-722284,EBI-946999
    GDI2P503952EBI-722284,EBI-1049143

    Protein-protein interaction databases

    BioGridi111805. 31 interactions.
    DIPiDIP-372N.
    IntActiP20338. 14 interactions.
    MINTiMINT-1376149.
    STRINGi9606.ENSP00000355651.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 2111
    Helixi26 – 3510
    Beta strandi46 – 5712
    Beta strandi60 – 6910
    Helixi73 – 753
    Helixi76 – 805
    Beta strandi87 – 948
    Helixi98 – 1025
    Helixi104 – 11411
    Beta strandi120 – 1267
    Helixi128 – 1336
    Helixi138 – 14710
    Beta strandi151 – 1544
    Turni157 – 1593
    Helixi163 – 17917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YU9X-ray2.07A7-177[»]
    1Z0KX-ray1.92A/C7-177[»]
    2BMDX-ray1.80A6-189[»]
    2BMEX-ray1.57A/B/C/D6-189[»]
    ProteinModelPortaliP20338.
    SMRiP20338. Positions 7-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20338.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi42 – 509Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiP20338.
    KOiK07879.
    OMAiDESNHTI.
    OrthoDBiEOG7QK0CV.
    PhylomeDBiP20338.
    TreeFamiTF300032.

    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.

    P20338-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTAMSETY DFLFKFLVIG NAGTGKSCLL HQFIEKKFKD DSNHTIGVEF    50
    GSKIINVGGK YVKLQIWDTA GQERFRSVTR SYYRGAAGAL LVYDITSRET 100
    YNALTNWLTD ARMLASQNIV IILCGNKKDL DADREVTFLE ASRFAQENEL 150
    MFLETSALTG ENVEEAFVQC ARKILNKIES GELDPERMGS GIQYGDAALR 200
    QLRSPRRAQA PNAQECGC 218
    Length:218
    Mass (Da):24,390
    Last modified:March 6, 2013 - v3
    Checksum:i983D65E1162741B0
    GO

    Sequence cautioni

    The sequence AAA60244.1 differs from that shown. Reason: Frameshift at position 6.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621N → D in AAA60244. (PubMed:2501306)Curated
    Sequence conflicti208 – 2081A → T in AAA60244. (PubMed:2501306)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28211 mRNA. Translation: AAA60244.1. Frameshift.
    AY585832 mRNA. Translation: AAT91347.1.
    AF498934 mRNA. Translation: AAM21082.1.
    AK313807 mRNA. Translation: BAG36543.1.
    AL162595, AL117350 Genomic DNA. Translation: CAI19037.1.
    AL117350, AL162595 Genomic DNA. Translation: CAI22870.1.
    CH471098 Genomic DNA. Translation: EAW69890.1.
    BC002438 mRNA. Translation: AAH02438.1.
    BC004309 mRNA. Translation: AAH04309.1.
    CCDSiCCDS31050.1.
    PIRiE34323.
    RefSeqiNP_001258927.1. NM_001271998.1.
    NP_004569.2. NM_004578.3.
    UniGeneiHs.296169.

    Genome annotation databases

    EnsembliENST00000366690; ENSP00000355651; ENSG00000168118.
    GeneIDi5867.
    KEGGihsa:5867.
    UCSCiuc001hth.4. human.

    Polymorphism databases

    DMDMi460018296.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28211 mRNA. Translation: AAA60244.1 . Frameshift.
    AY585832 mRNA. Translation: AAT91347.1 .
    AF498934 mRNA. Translation: AAM21082.1 .
    AK313807 mRNA. Translation: BAG36543.1 .
    AL162595 , AL117350 Genomic DNA. Translation: CAI19037.1 .
    AL117350 , AL162595 Genomic DNA. Translation: CAI22870.1 .
    CH471098 Genomic DNA. Translation: EAW69890.1 .
    BC002438 mRNA. Translation: AAH02438.1 .
    BC004309 mRNA. Translation: AAH04309.1 .
    CCDSi CCDS31050.1.
    PIRi E34323.
    RefSeqi NP_001258927.1. NM_001271998.1.
    NP_004569.2. NM_004578.3.
    UniGenei Hs.296169.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YU9 X-ray 2.07 A 7-177 [» ]
    1Z0K X-ray 1.92 A/C 7-177 [» ]
    2BMD X-ray 1.80 A 6-189 [» ]
    2BME X-ray 1.57 A/B/C/D 6-189 [» ]
    ProteinModelPortali P20338.
    SMRi P20338. Positions 7-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111805. 31 interactions.
    DIPi DIP-372N.
    IntActi P20338. 14 interactions.
    MINTi MINT-1376149.
    STRINGi 9606.ENSP00000355651.

    PTM databases

    PhosphoSitei P20338.

    Polymorphism databases

    DMDMi 460018296.

    Proteomic databases

    MaxQBi P20338.
    PaxDbi P20338.
    PRIDEi P20338.

    Protocols and materials databases

    DNASUi 5867.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366690 ; ENSP00000355651 ; ENSG00000168118 .
    GeneIDi 5867.
    KEGGi hsa:5867.
    UCSCi uc001hth.4. human.

    Organism-specific databases

    CTDi 5867.
    GeneCardsi GC01P229406.
    HGNCi HGNC:9781. RAB4A.
    HPAi CAB004990.
    MIMi 179511. gene.
    neXtProti NX_P20338.
    PharmGKBi PA34141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi P20338.
    KOi K07879.
    OMAi DESNHTI.
    OrthoDBi EOG7QK0CV.
    PhylomeDBi P20338.
    TreeFami TF300032.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinki P20338.

    Miscellaneous databases

    EvolutionaryTracei P20338.
    GeneWikii RAB4A.
    GenomeRNAii 5867.
    NextBioi 22786.
    PROi P20338.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20338.
    CleanExi HS_RAB4A.
    Genevestigatori P20338.

    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. "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
      Zahraoui A., Touchot N., Chardin P., Tavitian A.
      J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Regulation of CD4 expression via recycling by HRES-1/RAB4 controls susceptibility to HIV infection."
      Nagy G., Ward J., Mosser D.D., Koncz A., Gergely P. Jr., Stancato C., Qian Y., Fernandez D., Niland B., Grossman C.E., Telarico T., Banki K., Perl A.
      J. Biol. Chem. 281:34574-34591(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Brain.
    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: Caudate nucleus.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin and Uterus.
    8. "Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2."
      Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.
      Nature 350:715-718(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK1.
    9. "Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle."
      van der Sluijs P., Hull M., Huber L.A., Male P., Goud B., Mellman I.
      EMBO J. 11:4379-4389(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-204 BY CDK1.
    10. "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles."
      Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K., van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.
      Biochem. J. 346:593-601(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RABEP1.
    11. Cited for: INTERACTION WITH RAB11FIP1.
      Tissue: Cervix carcinoma.
    12. "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes."
      de Renzis S., Soennichsen B., Zerial M.
      Nat. Cell Biol. 4:124-133(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFYVE20.
    13. "Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
      Lindsay A.J., McCaffrey M.W.
      FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP1.
    14. Cited for: INTERACTION WITH RUFY1.
    15. "The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved in vesicular recycling of E-cadherin."
      Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L., Pili R., Denmeade S.R., DeMarzo A.M., Carducci M.A.
      PLoS ONE 2:E844-E844(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDRG1.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "High resolution crystal structures of human Rab4a in its active and inactive conformations."
      Huber S.K., Scheidig A.J.
      FEBS Lett. 579:2821-2829(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 6-189 IN COMPLEX WITH GTP ANALOG AND GDP.
    18. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
      Eathiraj S., Pan X., Ritacco C., Lambright D.G.
      Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 7-177 IN COMPLEX WITH GTP, INTERACTION WITH ZFYVE20, MUTAGENESIS OF GLY-51.

    Entry informationi

    Entry nameiRAB4A_HUMAN
    AccessioniPrimary (citable) accession number: P20338
    Secondary accession number(s): Q5T7P7, Q9BQ44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 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

    Caution

    It is uncertain whether Met-1 or Met-6 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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