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P61224

- RAP1B_HUMAN

UniProt

P61224 - RAP1B_HUMAN

Protein

Ras-related protein Rap-1b

Gene

RAP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (10 May 2004)
      Previous versions | rss
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    Functioni

    GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function.3 Publications

    Enzyme regulationi

    Activated by binding to the GTPase-activating protein RAP1GAP. Activated by guanine nucleotide-exchange factor (GEF) EPAC2 in a cAMP-dependent manner.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189GTP
    Nucleotide bindingi57 – 615GTP
    Nucleotide bindingi116 – 1194GTP
    Nucleotide bindingi147 – 1493GTP

    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 complex binding Source: MGI

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell proliferation Source: Ensembl
    3. cellular response to cAMP Source: UniProtKB
    4. energy reserve metabolic process Source: Reactome
    5. establishment of endothelial barrier Source: UniProtKB
    6. platelet activation Source: Reactome
    7. Rap protein signal transduction Source: UniProtKB
    8. regulation of cell junction assembly Source: UniProtKB
    9. regulation of establishment of cell polarity Source: UniProtKB
    10. regulation of insulin secretion Source: Reactome
    11. small molecule metabolic process Source: Reactome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_23898. Rap1 signalling.
    SignaLinkiP61224.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rap-1b
    Alternative name(s):
    GTP-binding protein smg p21B
    Gene namesi
    Name:RAP1B
    ORF Names:OK/SW-cl.11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9857. RAP1B.

    Subcellular locationi

    Cell membrane. Cytoplasmcytosol. Cell junction
    Note: May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular Source: LIFEdb
    5. lipid particle Source: UniProtKB
    6. membrane Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121G → V: Constitutively activated.
    Mutagenesisi25 – 251Q → A: Impairs interaction with KRIT1.
    Mutagenesisi32 – 321Y → A: 25-fold reduction in RAP1GAP-stimulated GTPase activity. 1 Publication
    Mutagenesisi32 – 321Y → F: 2-fold reduction in RAP1GAP-stimulated GTPase activity. 1 Publication
    Mutagenesisi37 – 371E → A: Strong reduction in nucleotide exchange with EPAC2. 1 Publication
    Mutagenesisi38 – 381D → A: Impairs interaction with KRIT1.
    Mutagenesisi63 – 631Q → E: Abolishes complex formation with RAP1GAP. Loss GTPase activity. 1 Publication
    Mutagenesisi64 – 641F → A: Abolishes complex formation with RAP1GAP. Loss GTPase activity. 1 Publication
    Mutagenesisi179 – 1791S → A: Abolishes phosphorylation by PKA. 1 Publication

    Organism-specific databases

    PharmGKBiPA34219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 181181Ras-related protein Rap-1bPRO_0000030209Add
    BLAST
    Propeptidei182 – 1843Removed in mature formPRO_0000030210

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391ADP-ribosylserine; by botulinum toxin1 Publication
    Modified residuei179 – 1791Phosphoserine; by PKA2 Publications
    Modified residuei181 – 1811Cysteine methyl ester1 Publication
    Lipidationi181 – 1811S-geranylgeranyl cysteine1 Publication

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP61224.
    PaxDbiP61224.
    PRIDEiP61224.

    2D gel databases

    OGPiP09526.

    PTM databases

    PhosphoSiteiP61224.

    Expressioni

    Gene expression databases

    BgeeiP61224.
    CleanExiHS_RAP1B.
    GenevestigatoriP61224.

    Interactioni

    Subunit structurei

    Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1, SGSM2 and SGSM3. Interacts with KRIT1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RALGDSQ129672EBI-358143,EBI-365861
    RAP1GAPP477363EBI-358143,EBI-722307
    UBCP0CG482EBI-358143,EBI-3390054

    Protein-protein interaction databases

    BioGridi111843. 31 interactions.
    DIPiDIP-35407N.
    IntActiP61224. 31 interactions.
    MINTiMINT-1133272.
    STRINGi9606.ENSP00000250559.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Helixi16 – 2510
    Turni27 – 293
    Beta strandi36 – 4611
    Beta strandi49 – 5810
    Beta strandi60 – 623
    Beta strandi63 – 653
    Helixi68 – 747
    Beta strandi76 – 838
    Helixi87 – 915
    Helixi93 – 10412
    Beta strandi105 – 1073
    Beta strandi111 – 1166
    Helixi121 – 1233
    Helixi128 – 13710
    Beta strandi142 – 1454
    Turni148 – 1514
    Helixi154 – 16613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BRWX-ray3.40D1-167[»]
    3CF6X-ray2.20R1-167[»]
    4DXAX-ray1.95A1-167[»]
    4HDOX-ray1.67B1-167[»]
    4HDQX-ray1.95B1-167[»]
    4M8NX-ray3.29E/F/G/H1-166[»]
    ProteinModelPortaliP61224.
    SMRiP61224. Positions 1-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61224.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 6743Interaction with KRIT1Add
    BLAST

    Motif

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

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Ras family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiP61224.
    KOiK07836.
    OMAiRDSTHPR.
    OrthoDBiEOG7QVM41.
    PhylomeDBiP61224.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61224-1) [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

    MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ    50
    CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI 100
    LRVKDTDDVP MILVGNKCDL EDERVVGKEQ GQNLARQWNN CAFLESSAKS 150
    KINVNEIFYD LVRQINRKTP VPGKARKKSS CQLL 184
    Length:184
    Mass (Da):20,825
    Last modified:May 10, 2004 - v1
    Checksum:iCE976895E5965224
    GO
    Isoform 2 (identifier: P61224-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         62-108: Missing.

    Show »
    Length:137
    Mass (Da):15,356
    Checksum:iA142020053FE1BC5
    GO
    Isoform 3 (identifier: P61224-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-61: Missing.

    Show »
    Length:165
    Mass (Da):18,778
    Checksum:i5F70CFF192C43A4A
    GO
    Isoform 4 (identifier: P61224-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-61: Missing.

    Show »
    Length:142
    Mass (Da):16,033
    Checksum:iEA48A041F34E0074
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81V → F in AAH95467. (PubMed:15489334)Curated
    Sequence conflicti16 – 161K → N in AAH78173. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei20 – 6142Missing in isoform 4. 1 PublicationVSP_045303Add
    BLAST
    Alternative sequencei43 – 6119Missing in isoform 3. 1 PublicationVSP_045304Add
    BLAST
    Alternative sequencei62 – 10847Missing in isoform 2. 1 PublicationVSP_045305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08004 mRNA. Translation: CAB46488.1.
    AL080212 mRNA. Translation: CAB45777.1.
    AB062128 mRNA. Translation: BAB93460.1.
    AF493913 mRNA. Translation: AAM12627.1.
    AK298818 mRNA. Translation: BAG60950.1.
    AK301401 mRNA. Translation: BAG62936.1.
    AK301428 mRNA. Translation: BAG62956.1.
    AK312371 mRNA. Translation: BAG35289.1.
    CR407689 mRNA. Translation: CAG28617.1.
    BT020093 mRNA. Translation: AAV38896.1.
    EF581377 Genomic DNA. Translation: ABQ52130.1.
    AC015550 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97189.1.
    BC000176 mRNA. Translation: AAH00176.1.
    BC078173 mRNA. Translation: AAH78173.1.
    BC095467 mRNA. Translation: AAH95467.1.
    CCDSiCCDS58252.1. [P61224-2]
    CCDS58253.1. [P61224-3]
    CCDS58254.1. [P61224-4]
    CCDS8984.1. [P61224-1]
    PIRiS01952. TVHUR1.
    RefSeqiNP_001010942.1. NM_001010942.2. [P61224-1]
    NP_001238846.1. NM_001251917.1. [P61224-4]
    NP_001238847.1. NM_001251918.1. [P61224-4]
    NP_001238850.1. NM_001251921.1. [P61224-3]
    NP_001238851.1. NM_001251922.1. [P61224-2]
    NP_056461.1. NM_015646.5. [P61224-1]
    UniGeneiHs.369920.

    Genome annotation databases

    EnsembliENST00000250559; ENSP00000250559; ENSG00000127314. [P61224-1]
    ENST00000341355; ENSP00000441275; ENSG00000127314. [P61224-1]
    ENST00000393436; ENSP00000377085; ENSG00000127314. [P61224-1]
    ENST00000450214; ENSP00000399986; ENSG00000127314. [P61224-4]
    ENST00000537460; ENSP00000439966; ENSG00000127314. [P61224-1]
    ENST00000539091; ENSP00000444830; ENSG00000127314. [P61224-4]
    ENST00000540209; ENSP00000446318; ENSG00000127314. [P61224-3]
    ENST00000542145; ENSP00000440014; ENSG00000127314. [P61224-2]
    GeneIDi5908.
    KEGGihsa:5908.
    UCSCiuc001sub.3. human. [P61224-1]
    uc010stf.2. human.
    uc010stg.2. human.
    uc010sti.2. human.

    Polymorphism databases

    DMDMi47117723.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08004 mRNA. Translation: CAB46488.1 .
    AL080212 mRNA. Translation: CAB45777.1 .
    AB062128 mRNA. Translation: BAB93460.1 .
    AF493913 mRNA. Translation: AAM12627.1 .
    AK298818 mRNA. Translation: BAG60950.1 .
    AK301401 mRNA. Translation: BAG62936.1 .
    AK301428 mRNA. Translation: BAG62956.1 .
    AK312371 mRNA. Translation: BAG35289.1 .
    CR407689 mRNA. Translation: CAG28617.1 .
    BT020093 mRNA. Translation: AAV38896.1 .
    EF581377 Genomic DNA. Translation: ABQ52130.1 .
    AC015550 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97189.1 .
    BC000176 mRNA. Translation: AAH00176.1 .
    BC078173 mRNA. Translation: AAH78173.1 .
    BC095467 mRNA. Translation: AAH95467.1 .
    CCDSi CCDS58252.1. [P61224-2 ]
    CCDS58253.1. [P61224-3 ]
    CCDS58254.1. [P61224-4 ]
    CCDS8984.1. [P61224-1 ]
    PIRi S01952. TVHUR1.
    RefSeqi NP_001010942.1. NM_001010942.2. [P61224-1 ]
    NP_001238846.1. NM_001251917.1. [P61224-4 ]
    NP_001238847.1. NM_001251918.1. [P61224-4 ]
    NP_001238850.1. NM_001251921.1. [P61224-3 ]
    NP_001238851.1. NM_001251922.1. [P61224-2 ]
    NP_056461.1. NM_015646.5. [P61224-1 ]
    UniGenei Hs.369920.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BRW X-ray 3.40 D 1-167 [» ]
    3CF6 X-ray 2.20 R 1-167 [» ]
    4DXA X-ray 1.95 A 1-167 [» ]
    4HDO X-ray 1.67 B 1-167 [» ]
    4HDQ X-ray 1.95 B 1-167 [» ]
    4M8N X-ray 3.29 E/F/G/H 1-166 [» ]
    ProteinModelPortali P61224.
    SMRi P61224. Positions 1-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111843. 31 interactions.
    DIPi DIP-35407N.
    IntActi P61224. 31 interactions.
    MINTi MINT-1133272.
    STRINGi 9606.ENSP00000250559.

    PTM databases

    PhosphoSitei P61224.

    Polymorphism databases

    DMDMi 47117723.

    2D gel databases

    OGPi P09526.

    Proteomic databases

    MaxQBi P61224.
    PaxDbi P61224.
    PRIDEi P61224.

    Protocols and materials databases

    DNASUi 5908.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250559 ; ENSP00000250559 ; ENSG00000127314 . [P61224-1 ]
    ENST00000341355 ; ENSP00000441275 ; ENSG00000127314 . [P61224-1 ]
    ENST00000393436 ; ENSP00000377085 ; ENSG00000127314 . [P61224-1 ]
    ENST00000450214 ; ENSP00000399986 ; ENSG00000127314 . [P61224-4 ]
    ENST00000537460 ; ENSP00000439966 ; ENSG00000127314 . [P61224-1 ]
    ENST00000539091 ; ENSP00000444830 ; ENSG00000127314 . [P61224-4 ]
    ENST00000540209 ; ENSP00000446318 ; ENSG00000127314 . [P61224-3 ]
    ENST00000542145 ; ENSP00000440014 ; ENSG00000127314 . [P61224-2 ]
    GeneIDi 5908.
    KEGGi hsa:5908.
    UCSCi uc001sub.3. human. [P61224-1 ]
    uc010stf.2. human.
    uc010stg.2. human.
    uc010sti.2. human.

    Organism-specific databases

    CTDi 5908.
    GeneCardsi GC12P069005.
    H-InvDB HIX0032084.
    HGNCi HGNC:9857. RAP1B.
    MIMi 179530. gene.
    neXtProti NX_P61224.
    PharmGKBi PA34219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi P61224.
    KOi K07836.
    OMAi RDSTHPR.
    OrthoDBi EOG7QVM41.
    PhylomeDBi P61224.
    TreeFami TF313014.

    Enzyme and pathway databases

    Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_23898. Rap1 signalling.
    SignaLinki P61224.

    Miscellaneous databases

    ChiTaRSi RAP1B. human.
    EvolutionaryTracei P61224.
    GeneWikii RAP1B.
    GenomeRNAii 5908.
    NextBioi 22980.
    PROi P61224.
    SOURCEi Search...

    Gene expression databases

    Bgeei P61224.
    CleanExi HS_RAP1B.
    Genevestigatori P61224.

    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. "Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B)."
      Pizon V., Lerosey I., Chardin P., Tavitian A.
      Nucleic Acids Res. 16:7719-7719(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    3. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 1; 2; 3 AND 4).
      Tissue: Amygdala.
    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. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. SeattleSNPs variation discovery resource
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    9. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Chondrosarcoma, Placenta and Testis.
    12. "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, SUBCELLULAR LOCATION, ADP-RIBOSYLATION AT SER-39.
    13. "Rap1-B is phosphorylated by protein kinase A in intact human platelets."
      Siess W., Winegar D.A., Lapetina E.G.
      Biochem. Biophys. Res. Commun. 170:944-950(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 146-180, PHOSPHORYLATION.
    14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 168-176.
      Tissue: Platelet.
    15. "Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine."
      Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A., Takai Y.
      Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-181, METHYLATION AT CYS-181.
      Tissue: Platelet.
    16. "Mutational analysis of the cAMP-dependent protein kinase-mediated phosphorylation site of Rap1b."
      Altschuler D., Lapetina E.G.
      J. Biol. Chem. 268:7527-7531(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-179 BY PKA, MUTAGENESIS OF SER-179.
    17. "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.
    18. "CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
      Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
      J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. Cited for: FUNCTION.
    20. "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues."
      Scrima A., Thomas C., Deaconescu D., Wittinghofer A.
      EMBO J. 27:1145-1153(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP ANALOG AND RAP1GAP, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF TYR-32; GLN-63 AND PHE-64.
    21. "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B."
      Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O., Bos J.L.
      Nature 455:124-127(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167 IN COMPLEX WITH EPAC2, FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-37.
    22. "Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1)."
      Li X., Zhang R., Draheim K.M., Liu W., Calderwood D.A., Boggon T.J.
      J. Biol. Chem. 287:22317-22327(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN COMPLEX WITH KRIT1; GTP ANALOG AND MAGNESIUM, INTERACTION WITH KRIT1.

    Entry informationi

    Entry nameiRAP1B_HUMAN
    AccessioniPrimary (citable) accession number: P61224
    Secondary accession number(s): B2R5Z2
    , B4DQI8, B4DW74, B4DW94, P09526, Q502X3, Q5TZR4, Q6DCA1, Q6LES0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 128 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 12
      Human chromosome 12: 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