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Q9Y3P9

- RBGP1_HUMAN

UniProt

Q9Y3P9 - RBGP1_HUMAN

Protein

Rab GTPase-activating protein 1

Gene

RABGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (21 Aug 2007)
      Previous versions | rss
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    Functioni

    May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei608 – 6081Arginine fingerBy similarity
    Sitei649 – 6491Glutamine fingerBy similarity

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. GTPase activator activity Source: ProtInc
    3. protein binding Source: IntAct
    4. Rab GTPase activator activity Source: InterPro
    5. tubulin binding Source: ProtInc

    GO - Biological processi

    1. cell cycle Source: ProtInc
    2. positive regulation of GTPase activity Source: GOC

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab GTPase-activating protein 1
    Alternative name(s):
    GAP and centrosome-associated protein
    Rab6 GTPase-activating protein GAPCenA
    Gene namesi
    Name:RABGAP1
    ORF Names:HSPC094
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17155. RABGAP1.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Predominantly cytosolic but also associated with the centrosome.1 Publication

    GO - Cellular componenti

    1. centrosome Source: ProtInc
    2. cytosol Source: ProtInc
    3. microtubule associated complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134977298.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10691069Rab GTPase-activating protein 1PRO_0000298779Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei996 – 9961Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y3P9.
    PaxDbiQ9Y3P9.
    PRIDEiQ9Y3P9.

    PTM databases

    PhosphoSiteiQ9Y3P9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3P9.
    BgeeiQ9Y3P9.
    CleanExiHS_RABGAP1.
    GenevestigatoriQ9Y3P9.

    Interactioni

    Subunit structurei

    Interacts with RAB6A and tubulin gamma.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPL1Q9H0R82EBI-1057545,EBI-746969

    Protein-protein interaction databases

    BioGridi117166. 15 interactions.
    IntActiQ9Y3P9. 13 interactions.
    MINTiMINT-258769.
    STRINGi9606.ENSP00000362751.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y3P9.
    SMRiQ9Y3P9. Positions 538-825.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini142 – 298157PIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini566 – 752187Rab-GAP TBCPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili798 – 1047250Sequence AnalysisAdd
    BLAST

    Domaini

    The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.By similarity

    Sequence similaritiesi

    Contains 1 PID domain.PROSITE-ProRule annotation
    Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5210.
    HOGENOMiHOG000007923.
    HOVERGENiHBG063892.
    InParanoidiQ9Y3P9.
    OMAiMIPSPPE.
    OrthoDBiEOG751NDS.
    PhylomeDBiQ9Y3P9.
    TreeFamiTF317184.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    IPR022164. Kinesin-like.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    IPR000195. Rab-GTPase-TBC_dom.
    [Graphical view]
    PfamiPF12473. DUF3694. 1 hit.
    PF00640. PID. 1 hit.
    PF00566. RabGAP-TBC. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 1 hit.
    SM00164. TBC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47923. SSF47923. 2 hits.
    PROSITEiPS01179. PID. 1 hit.
    PS50086. TBC_RABGAP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9Y3P9-1) [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

    MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK     50
    IVGNGSEQQL QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL 100
    SASSTINPVP LVGLQKPEMS LPVKPGQGDS EASSPFTPVA DEDSVVFSKL 150
    TYLGCASVNA PRSEVEALRM MSILRSQCQI SLDVTLSVPN VSEGIVRLLD 200
    PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA ELFRIHVFRC 250
    EIQEAVSRIL YSFATAFRRS AKQTPLSATA APQTPDSDIF TFSVSLEIKE 300
    DDGKGYFSAV PKDKDRQCFK LRQGIDKKIV IYVQQTTNKE LAIERCFGLL 350
    LSPGKDVRNS DMHLLDLESM GKSSDGKSYV ITGSWNPKSP HFQVVNEETP 400
    KDKVLFMTTA VDLVITEVQE PVRFLLETKV RVCSPNERLF WPFSKRSTTE 450
    NFFLKLKQIK QRERKNNTDT LYEVVCLESE SERERRKTTA SPSVRLPQSG 500
    SQSSVIPSPP EDDEEEDNDE PLLSGSGDVS KECAEKILET WGELLSKWHL 550
    NLNVRPKQLS SLVRNGVPEA LRGEVWQLLA GCHNNDHLVE KYRILITKES 600
    PQDSAITRDI NRTFPAHDYF KDTGGDGQDS LYKICKAYSV YDEEIGYCQG 650
    QSFLAAVLLL HMPEEQAFSV LVKIMFDYGL RELFKQNFED LHCKFYQLER 700
    LMQEYIPDLY NHFLDISLEA HMYASQWFLT LFTAKFPLYM VFHIIDLLLC 750
    EGISVIFNVA LGLLKTSKDD LLLTDFEGAL KFFRVQLPKR YRSEENAKKL 800
    MELACNMKIS QKKLKKYEKE YHTMREQQAQ QEDPIERFER ENRRLQEANM 850
    RLEQENDDLA HELVTSKIAL RKDLDNAEEK ADALNKELLM TKQKLIDAEE 900
    EKRRLEEESA QLKEMCRREL DKAESEIKKN SSIIGDYKQI CSQLSERLEK 950
    QQTANKVEIE KIRQKVDDCE RCREFFNKEG RVKGISSTKE VLDEDTDEEK 1000
    ETLKNQLREM ELELAQTKLQ LVEAECKIQD LEHHLGLALN EVQAAKKTWF 1050
    NRTLSSIKTA TGVQGKETC 1069
    Length:1,069
    Mass (Da):121,737
    Last modified:August 21, 2007 - v3
    Checksum:iF3B09BD3CF993F3A
    GO
    Isoform 21 Publication (identifier: Q9Y3P9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: Missing.
         637-667: AYSVYDEEIGYCQGQSFLAAVLLLHMPEEQA → VFHVKKKKDSILSGGSTLKLHKKQLQSVICI
         668-1069: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:599
    Mass (Da):67,098
    Checksum:i549686265A37B8BB
    GO
    Isoform 3 (identifier: Q9Y3P9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         480-1069: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:479
    Mass (Da):53,195
    Checksum:i56599C32796E7909
    GO
    Isoform 41 Publication (identifier: Q9Y3P9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         258-265: RILYSFAT → PQEKTLCK
         266-1069: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:265
    Mass (Da):28,712
    Checksum:i7BA5E80C1D8A71FF
    GO

    Sequence cautioni

    The sequence AAH20609.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AK022408 differs from that shown. Reason: Intron retention.
    The sequence AAF28917.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAH54492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB40267.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6868Missing in isoform 2. 1 PublicationVSP_052510Add
    BLAST
    Alternative sequencei258 – 2658RILYSFAT → PQEKTLCK in isoform 4. 1 PublicationVSP_052511
    Alternative sequencei266 – 1069804Missing in isoform 4. 1 PublicationVSP_052512Add
    BLAST
    Alternative sequencei480 – 1069590Missing in isoform 3. 1 PublicationVSP_052515Add
    BLAST
    Alternative sequencei637 – 66731AYSVY…PEEQA → VFHVKKKKDSILSGGSTLKL HKKQLQSVICI in isoform 2. 1 PublicationVSP_052513Add
    BLAST
    Alternative sequencei668 – 1069402Missing in isoform 2. 1 PublicationVSP_052514Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011679 mRNA. Translation: CAB40267.2. Different initiation.
    AB449897 mRNA. Translation: BAH16640.1.
    AF161357 mRNA. Translation: AAF28917.1. Frameshift.
    AK022408 mRNA. No translation available.
    AK131449 mRNA. Translation: BAD18594.1.
    AL365338, AC007066 Genomic DNA. Translation: CAH70298.2.
    CH471090 Genomic DNA. Translation: EAW87555.1.
    BC020609 mRNA. Translation: AAH20609.1. Sequence problems.
    BC054492 mRNA. Translation: AAH54492.1. Different initiation.
    AL050195 mRNA. Translation: CAB43313.1.
    CCDSiCCDS6848.2. [Q9Y3P9-1]
    PIRiT13163.
    RefSeqiNP_036329.3. NM_012197.3. [Q9Y3P9-1]
    XP_005251923.1. XM_005251866.1. [Q9Y3P9-1]
    XP_006717094.1. XM_006717031.1. [Q9Y3P9-1]
    UniGeneiHs.271341.

    Genome annotation databases

    EnsembliENST00000373647; ENSP00000362751; ENSG00000011454. [Q9Y3P9-1]
    ENST00000456584; ENSP00000414386; ENSG00000011454. [Q9Y3P9-2]
    GeneIDi23637.
    KEGGihsa:23637.
    UCSCiuc004bnm.1. human. [Q9Y3P9-4]
    uc011lzh.2. human. [Q9Y3P9-1]

    Polymorphism databases

    DMDMi156633605.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011679 mRNA. Translation: CAB40267.2 . Different initiation.
    AB449897 mRNA. Translation: BAH16640.1 .
    AF161357 mRNA. Translation: AAF28917.1 . Frameshift.
    AK022408 mRNA. No translation available.
    AK131449 mRNA. Translation: BAD18594.1 .
    AL365338 , AC007066 Genomic DNA. Translation: CAH70298.2 .
    CH471090 Genomic DNA. Translation: EAW87555.1 .
    BC020609 mRNA. Translation: AAH20609.1 . Sequence problems.
    BC054492 mRNA. Translation: AAH54492.1 . Different initiation.
    AL050195 mRNA. Translation: CAB43313.1 .
    CCDSi CCDS6848.2. [Q9Y3P9-1 ]
    PIRi T13163.
    RefSeqi NP_036329.3. NM_012197.3. [Q9Y3P9-1 ]
    XP_005251923.1. XM_005251866.1. [Q9Y3P9-1 ]
    XP_006717094.1. XM_006717031.1. [Q9Y3P9-1 ]
    UniGenei Hs.271341.

    3D structure databases

    ProteinModelPortali Q9Y3P9.
    SMRi Q9Y3P9. Positions 538-825.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117166. 15 interactions.
    IntActi Q9Y3P9. 13 interactions.
    MINTi MINT-258769.
    STRINGi 9606.ENSP00000362751.

    PTM databases

    PhosphoSitei Q9Y3P9.

    Polymorphism databases

    DMDMi 156633605.

    Proteomic databases

    MaxQBi Q9Y3P9.
    PaxDbi Q9Y3P9.
    PRIDEi Q9Y3P9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373647 ; ENSP00000362751 ; ENSG00000011454 . [Q9Y3P9-1 ]
    ENST00000456584 ; ENSP00000414386 ; ENSG00000011454 . [Q9Y3P9-2 ]
    GeneIDi 23637.
    KEGGi hsa:23637.
    UCSCi uc004bnm.1. human. [Q9Y3P9-4 ]
    uc011lzh.2. human. [Q9Y3P9-1 ]

    Organism-specific databases

    CTDi 23637.
    GeneCardsi GC09P125703.
    H-InvDB HIX0008361.
    HGNCi HGNC:17155. RABGAP1.
    neXtProti NX_Q9Y3P9.
    PharmGKBi PA134977298.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5210.
    HOGENOMi HOG000007923.
    HOVERGENi HBG063892.
    InParanoidi Q9Y3P9.
    OMAi MIPSPPE.
    OrthoDBi EOG751NDS.
    PhylomeDBi Q9Y3P9.
    TreeFami TF317184.

    Miscellaneous databases

    ChiTaRSi RABGAP1. human.
    GeneWikii RABGAP1.
    GenomeRNAii 23637.
    NextBioi 46429.
    PROi Q9Y3P9.

    Gene expression databases

    ArrayExpressi Q9Y3P9.
    Bgeei Q9Y3P9.
    CleanExi HS_RABGAP1.
    Genevestigatori Q9Y3P9.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    IPR022164. Kinesin-like.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    IPR000195. Rab-GTPase-TBC_dom.
    [Graphical view ]
    Pfami PF12473. DUF3694. 1 hit.
    PF00640. PID. 1 hit.
    PF00566. RabGAP-TBC. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    SM00164. TBC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47923. SSF47923. 2 hits.
    PROSITEi PS01179. PID. 1 hit.
    PS50086. TBC_RABGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome."
      Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F., Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M., Goud B.
      EMBO J. 18:1772-1782(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAB6A AND TUBULIN GAMMA, SUBCELLULAR LOCATION.
      Tissue: PlacentaImported.
    2. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
      Ishibashi K., Kanno E., Itoh T., Fukuda M.
      Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Human partial CDS from CD34+ stem cells."
      Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Umbilical cord blood.
    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] (ISOFORMS 2 AND 4).
      Tissue: Mammary gland and TestisImported.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORM 1).
      Tissue: PlacentaImported and UterusImported.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 824-1069 (ISOFORM 1).
      Tissue: Uterus.
    9. "A role for the Rab6A' GTPase in the inactivation of the Mad2-spindle checkpoint."
      Miserey-Lenkei S., Couedel-Courteille A., Del Nery E., Bardin S., Piel M., Racine V., Sibarita J.-B., Perez F., Bornens M., Goud B.
      EMBO J. 25:278-289(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRBGP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3P9
    Secondary accession number(s): B9A6L2
    , Q05CW2, Q6ZMY1, Q9HA28, Q9P0E2, Q9UG67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 117 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3