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P62834

- RAP1A_HUMAN

UniProt

P62834 - RAP1A_HUMAN

Protein

Ras-related protein Rap-1A

Gene

RAP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.2 Publications

    Enzyme regulationi

    Activated by guanine nucleotide-exchange factors (GEF) EPAC and EPAC2 in a cAMP-dependent manner, and GFR.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178GTPBy similarity
    Nucleotide bindingi57 – 615GTPBy similarity
    Nucleotide bindingi116 – 1194GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: ProtInc
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein complex binding Source: UniProtKB
    5. protein transporter activity Source: UniProtKB
    6. Rap guanyl-nucleotide exchange factor activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: Reactome
    2. blood coagulation Source: Reactome
    3. cellular response to cAMP Source: UniProtKB
    4. cellular response to nerve growth factor stimulus Source: UniProtKB
    5. energy reserve metabolic process Source: Reactome
    6. establishment of endothelial barrier Source: UniProtKB
    7. nerve growth factor signaling pathway Source: UniProtKB
    8. neurotrophin TRK receptor signaling pathway Source: Reactome
    9. platelet activation Source: Reactome
    10. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    11. positive regulation of neuron projection development Source: UniProtKB
    12. positive regulation of protein kinase activity Source: UniProtKB
    13. positive regulation of Rap GTPase activity Source: UniProtKB
    14. positive regulation of vasculogenesis Source: UniProtKB
    15. protein transport Source: UniProtKB
    16. Rap protein signal transduction Source: UniProtKB
    17. regulation of cell junction assembly Source: UniProtKB
    18. regulation of insulin secretion Source: Reactome
    19. signal transduction Source: ProtInc
    20. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Neurogenesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_23898. Rap1 signalling.
    SignaLinkiP62834.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rap-1A
    Alternative name(s):
    C21KG
    G-22K
    GTP-binding protein smg p21A
    Ras-related protein Krev-1
    Gene namesi
    Name:RAP1A
    Synonyms:KREV1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9855. RAP1A.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasm 1 Publication. Cytoplasmperinuclear region 1 Publication. Cell junction By similarity. Early endosome By similarity
    Note: Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions By similarity. Colocalized with RAPGEF2 in the perinuclear region.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. early endosome Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. guanyl-nucleotide exchange factor complex Source: Ensembl
    7. late endosome Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34217.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 181181Ras-related protein Rap-1APRO_0000030199Add
    BLAST
    Propeptidei182 – 1843Removed in mature formPRO_0000030200

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811Cysteine methyl ester1 Publication
    Lipidationi181 – 1811S-geranylgeranyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP62834.
    PaxDbiP62834.
    PRIDEiP62834.

    2D gel databases

    OGPiP62834.

    PTM databases

    PhosphoSiteiP62834.

    Expressioni

    Gene expression databases

    ArrayExpressiP62834.
    BgeeiP62834.
    CleanExiHS_RAP1A.
    GenevestigatoriP62834.

    Organism-specific databases

    HPAiCAB018335.

    Interactioni

    Subunit structurei

    Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (active GTP-bound form preferentially) with KRIT1 (via C-terminus FERM domain); the interaction does not induce the opening conformation of KRIT1. In its GTP-bound form interacts with PLCE1 and RADIL. Interacts with SGSM1, SGSM2 and SGSM3. Interacts (via GTP-bound active form) with RAPGEF2 (via Ras-associating domain).7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAF1P040492EBI-491414,EBI-365996
    RASSF5Q8WWW0-23EBI-491414,EBI-960502
    Rassf5Q5EBH12EBI-491414,EBI-960530From a different organism.

    Protein-protein interaction databases

    BioGridi111841. 43 interactions.
    DIPiDIP-29106N.
    IntActiP62834. 11 interactions.
    MINTiMINT-1509313.
    STRINGi9606.ENSP00000348786.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Helixi16 – 2510
    Beta strandi36 – 4611
    Beta strandi49 – 5810
    Helixi66 – 749
    Beta strandi76 – 838
    Helixi87 – 915
    Helixi93 – 10412
    Beta strandi111 – 1166
    Helixi121 – 1233
    Helixi128 – 13710
    Turni138 – 1403
    Beta strandi142 – 1454
    Turni148 – 1503
    Helixi154 – 16613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C1YX-ray1.90A1-167[»]
    1GUAX-ray2.00A1-167[»]
    3KUCX-ray1.92A1-167[»]
    4KVGX-ray1.65A/C1-167[»]
    ProteinModelPortaliP62834.
    SMRiP62834. Positions 1-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62834.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 409Effector regionCurated

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Ras family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233973.
    HOVERGENiHBG009351.
    InParanoidiP62834.
    KOiK04353.
    OMAiKPKKSLC.
    OrthoDBiEOG7QVM41.
    PhylomeDBiP62834.
    TreeFamiTF313014.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view]
    PANTHERiPTHR24070. PTHR24070. 1 hit.
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00173. RAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51421. RAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62834-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDCQQ    50
    CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI 100
    LRVKDTEDVP MILVGNKCDL EDERVVGKEQ GQNLARQWCN CAFLESSAKS 150
    KINVNEIFYD LVRQINRKTP VEKKKPKKKS CLLL 184
    Length:184
    Mass (Da):20,987
    Last modified:August 16, 2004 - v1
    Checksum:i42C39290C98E0A92
    GO

    Sequence cautioni

    The sequence CAB55685.2 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12533 mRNA. Translation: CAA31051.1.
    M22995 mRNA. Translation: AAA36150.1.
    AF493912 mRNA. Translation: AAM12626.1.
    AL049557 Genomic DNA. Translation: CAB55685.2. Sequence problems.
    BC014086 mRNA. Translation: AAH14086.1.
    CCDSiCCDS840.1.
    PIRiA32342.
    RefSeqiNP_001010935.1. NM_001010935.2.
    NP_001278825.1. NM_001291896.1.
    NP_002875.1. NM_002884.3.
    UniGeneiHs.190334.

    Genome annotation databases

    EnsembliENST00000356415; ENSP00000348786; ENSG00000116473.
    ENST00000369709; ENSP00000358723; ENSG00000116473.
    GeneIDi5906.
    KEGGihsa:5906.
    UCSCiuc001ebi.3. human.

    Polymorphism databases

    DMDMi51338607.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12533 mRNA. Translation: CAA31051.1 .
    M22995 mRNA. Translation: AAA36150.1 .
    AF493912 mRNA. Translation: AAM12626.1 .
    AL049557 Genomic DNA. Translation: CAB55685.2 . Sequence problems.
    BC014086 mRNA. Translation: AAH14086.1 .
    CCDSi CCDS840.1.
    PIRi A32342.
    RefSeqi NP_001010935.1. NM_001010935.2.
    NP_001278825.1. NM_001291896.1.
    NP_002875.1. NM_002884.3.
    UniGenei Hs.190334.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C1Y X-ray 1.90 A 1-167 [» ]
    1GUA X-ray 2.00 A 1-167 [» ]
    3KUC X-ray 1.92 A 1-167 [» ]
    4KVG X-ray 1.65 A/C 1-167 [» ]
    ProteinModelPortali P62834.
    SMRi P62834. Positions 1-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111841. 43 interactions.
    DIPi DIP-29106N.
    IntActi P62834. 11 interactions.
    MINTi MINT-1509313.
    STRINGi 9606.ENSP00000348786.

    Chemistry

    BindingDBi P62834.
    ChEMBLi CHEMBL1255139.

    PTM databases

    PhosphoSitei P62834.

    Polymorphism databases

    DMDMi 51338607.

    2D gel databases

    OGPi P62834.

    Proteomic databases

    MaxQBi P62834.
    PaxDbi P62834.
    PRIDEi P62834.

    Protocols and materials databases

    DNASUi 5906.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356415 ; ENSP00000348786 ; ENSG00000116473 .
    ENST00000369709 ; ENSP00000358723 ; ENSG00000116473 .
    GeneIDi 5906.
    KEGGi hsa:5906.
    UCSCi uc001ebi.3. human.

    Organism-specific databases

    CTDi 5906.
    GeneCardsi GC01P112084.
    HGNCi HGNC:9855. RAP1A.
    HPAi CAB018335.
    MIMi 179520. gene.
    neXtProti NX_P62834.
    PharmGKBi PA34217.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233973.
    HOVERGENi HBG009351.
    InParanoidi P62834.
    KOi K04353.
    OMAi KPKKSLC.
    OrthoDBi EOG7QVM41.
    PhylomeDBi P62834.
    TreeFami TF313014.

    Enzyme and pathway databases

    Reactomei REACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_23898. Rap1 signalling.
    SignaLinki P62834.

    Miscellaneous databases

    ChiTaRSi RAP1A. human.
    EvolutionaryTracei P62834.
    GeneWikii RAP1A.
    GenomeRNAii 5906.
    NextBioi 22972.
    PROi P62834.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62834.
    Bgeei P62834.
    CleanExi HS_RAP1A.
    Genevestigatori P62834.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region."
      Pizon V., Chardin P., Lerosey I., Olofsson B., Tavitian A.
      Oncogene 3:201-204(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Pizon V.
      Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 3.
    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 (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "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].
    5. "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.
    6. "Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein."
      Nagata K., Itoh H., Katada T., Takenaka K., Ui M., Kaziro Y., Nozawa Y.
      J. Biol. Chem. 264:17000-17005(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Platelet.
    7. "Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K."
      Bokoch G.M., Parkos C.A., Mumby S.M.
      J. Biol. Chem. 263:16744-16749(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-35.
    8. "Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene products."
      Ohmori T., Kikuchi A., Yamamoto K., Kawata M., Kondo J., Takai Y.
      Biochem. Biophys. Res. Commun. 157:670-676(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5; 17-24; 32-42 AND 152-168.
    9. "The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein."
      Buss J.E., Quilliam L.A., Kato K., Casey P.J., Solski P.A., Wong G., Clark R., McCormick F., Bokoch G.M., Der C.J.
      Mol. Cell. Biol. 11:1523-1530(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-181, METHYLATION AT CYS-181.
    10. "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans."
      Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T., Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.
      J. Biol. Chem. 274:37815-37820(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAPGEF2.
    11. "Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
      Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
      J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLCE1.
    12. "RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rap1*GTP and enhances Rap1-dependent B-Raf activation."
      Liao Y., Satoh T., Gao X., Jin T.G., Hu C.D., Kataoka T.
      J. Biol. Chem. 276:28478-28483(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAPGEF2, SUBCELLULAR LOCATION.
    13. "Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon."
      Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.
      Oncogene 21:8105-8113(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLCE1.
    14. "Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."
      Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.
      FEBS J. 274:5518-5532(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGB1BP1 AND KRIT1, INTERACTION WITH KRIT1.
    15. Cited for: INTERACTION WITH RADIL.
    16. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
      Yang H., Sasaki T., Minoshima S., Shimizu N.
      Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: FUNCTION.
    19. "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue."
      Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A.
      Nature 375:554-560(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167.
    20. "Ras/Rap effector specificity determined by charge reversal."
      Nassar N., Horn G., Herrmann C., Block C., Janknecht R., Wittinghofer A.
      Nat. Struct. Biol. 3:723-729(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.

    Entry informationi

    Entry nameiRAP1A_HUMAN
    AccessioniPrimary (citable) accession number: P62834
    Secondary accession number(s): P10113
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 124 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, Direct protein sequencing, 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