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P20936

- RASA1_HUMAN

UniProt

P20936 - RASA1_HUMAN

Protein

Ras GTPase-activating protein 1

Gene

RASA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1.2 Publications

    GO - Molecular functioni

    1. glycoprotein binding Source: UniProtKB
    2. GTPase binding Source: UniProtKB
    3. potassium channel inhibitor activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. Ras GTPase activator activity Source: RefGenome
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. embryo development Source: UniProtKB
    2. intracellular signal transduction Source: UniProtKB
    3. mitotic cytokinesis Source: UniProtKB
    4. negative regulation of cell adhesion Source: UniProtKB
    5. negative regulation of cell-matrix adhesion Source: UniProtKB
    6. negative regulation of neuron apoptotic process Source: UniProtKB
    7. negative regulation of Ras protein signal transduction Source: RefGenome
    8. positive regulation of Ras GTPase activity Source: RefGenome
    9. regulation of actin filament polymerization Source: UniProtKB
    10. regulation of cell shape Source: UniProtKB
    11. regulation of RNA metabolic process Source: UniProtKB
    12. signal transduction Source: UniProtKB
    13. vasculogenesis Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_17025. Downstream signal transduction.
    SignaLinkiP20936.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras GTPase-activating protein 1
    Short name:
    GAP
    Short name:
    GTPase-activating protein
    Short name:
    RasGAP
    Alternative name(s):
    Ras p21 protein activator
    p120GAP
    Gene namesi
    Name:RASA1
    Synonyms:GAP, RASA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9871. RASA1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. intrinsic component of the cytoplasmic side of the plasma membrane Source: RefGenome
    4. ruffle Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Mutations in the SH2 domain of RASA seem to be oncogenic and cause basal cell carcinomas.
    Capillary malformation-arteriovenous malformation (CMAVM) [MIM:608354]: A disorder characterized by atypical capillary malformations that are multiple, small, round to oval in shape and pinkish red in color. These capillary malformations are associated with either arteriovenous malformation, arteriovenous fistula, or Parkes Weber syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti540 – 5401C → Y in CMAVM. 1 Publication
    VAR_017744
    Parkes Weber syndrome (PKWS) [MIM:608355]: Disorder characterized by a cutaneous flush with underlying multiple micro-arteriovenous fistulas, in association with soft tissue and skeletal hypertrophy of the affected limb.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi608354. phenotype.
    608355. phenotype.
    Orphaneti137667. Capillary malformation - arteriovenous malformation.
    90307. Parkes Weber syndrome.
    PharmGKBiPA34232.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10471047Ras GTPase-activating protein 1PRO_0000056636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei615 – 6151Phosphotyrosine2 Publications

    Post-translational modificationi

    The N-terminus is blocked.
    Phosphorylated by SRC and LCK. The phosphorylation SRC inhibits its ability to stimulate the Ras-GTPase activity, whereas phosphorylation by LCK does not display any effect on stimulation activity.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP20936.
    PaxDbiP20936.
    PRIDEiP20936.

    PTM databases

    PhosphoSiteiP20936.

    Miscellaneous databases

    PMAP-CutDBP20936.

    Expressioni

    Tissue specificityi

    In placental villi, detected only in the trophoblast layer (cytotrophoblast and syncytiotrophoblast). Not detected in stromal, endothelial or Hofbauer cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP20936.
    BgeeiP20936.
    CleanExiHS_RASA1.
    GenevestigatoriP20936.

    Organism-specific databases

    HPAiCAB007789.

    Interactioni

    Subunit structurei

    Interacts with SQSTM1. Interacts with SPSB1; the interaction does not promote degradation. Interacts with CAV2 (tyrosine phosphorylated form). Directly interacts with NCK1. Interacts with PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-1026476,EBI-375446
    ARP1027516EBI-1026476,EBI-608057
    CAPNS1P046323EBI-1026476,EBI-711828
    DLC1Q96QB16EBI-1026476,EBI-2608428
    EGFRP005337EBI-1026476,EBI-297353
    ERBB2P046267EBI-1026476,EBI-641062
    ERBB3P218606EBI-1026476,EBI-720706
    GAB1Q1348025EBI-1026476,EBI-517684
    KITP1072116EBI-1026476,EBI-1379503
    METP0858115EBI-1026476,EBI-1039152
    NCK1P163336EBI-1026476,EBI-389883
    PDGFRBP096193EBI-1026476,EBI-641237

    Protein-protein interaction databases

    BioGridi111856. 54 interactions.
    DIPiDIP-144N.
    IntActiP20936. 36 interactions.
    MINTiMINT-195165.
    STRINGi9606.ENSP00000274376.

    Structurei

    Secondary structure

    1
    1047
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi283 – 2886
    Beta strandi296 – 2983
    Beta strandi306 – 3127
    Beta strandi316 – 3227
    Turni323 – 3253
    Beta strandi328 – 3325
    Helixi333 – 3353
    Beta strandi336 – 3383
    Helixi720 – 7234
    Helixi724 – 7307
    Helixi736 – 7449
    Beta strandi746 – 7483
    Helixi749 – 76214
    Helixi766 – 78015
    Helixi784 – 7863
    Turni787 – 7893
    Helixi793 – 80513
    Helixi807 – 82317
    Helixi832 – 8343
    Helixi841 – 86020
    Helixi861 – 8655
    Helixi868 – 88417
    Helixi891 – 90010
    Turni901 – 9044
    Helixi905 – 9106
    Turni912 – 9165
    Helixi924 – 94118
    Beta strandi946 – 9494
    Helixi951 – 9566
    Helixi957 – 97418
    Helixi992 – 100413
    Helixi1006 – 10138
    Helixi1020 – 103819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WERX-ray1.60A714-1047[»]
    1WQ1X-ray2.50G714-1047[»]
    2GQINMR-A282-339[»]
    2GSBNMR-A341-446[»]
    2J05X-ray1.50A/B281-341[»]
    2J06X-ray1.80A/B281-341[»]
    2M51NMR-A281-341[»]
    4FSSX-ray2.25A/B/C281-341[»]
    ProteinModelPortaliP20936.
    SMRiP20936. Positions 168-446, 475-573, 593-713, 718-1041.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20936.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini181 – 27292SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini279 – 34163SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 44191SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini474 – 577104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini581 – 67696C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini748 – 942195Ras-GAPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 226Poly-Gly
    Compositional biasi135 – 1417Poly-Pro
    Compositional biasi163 – 1686Poly-Glu

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-GAP domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG282054.
    HOGENOMiHOG000007794.
    HOVERGENiHBG057470.
    InParanoidiP20936.
    KOiK04352.
    OMAiQAQDWMK.
    OrthoDBiEOG7HTHG8.
    PhylomeDBiP20936.
    TreeFamiTF105301.

    Family and domain databases

    Gene3Di1.10.506.10. 1 hit.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001936. RasGAP.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00169. PH. 1 hit.
    PF00616. RasGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    SMARTiSM00239. C2. 1 hit.
    SM00233. PH. 1 hit.
    SM00323. RasGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50004. C2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20936-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPVAAAPYP     50
    GLVETGVAGT LGGGAALGSE FLGAGSVAGA LGGAGLTGGG TAAGVAGAAA 100
    GVAGAAVAGP SGDMALTKLP TSLLAETLGP GGGFPPLPPP PYLPPLGAGL 150
    GTVDEGDSLD GPEYEEEEVA IPLTAPPTNQ WYHGKLDRTI AEERLRQAGK 200
    SGSYLIRESD RRPGSFVLSF LSQMNVVNHF RIIAMCGDYY IGGRRFSSLS 250
    DLIGYYSHVS CLLKGEKLLY PVAPPEPVED RRRVRAILPY TKVPDTDEIS 300
    FLKGDMFIVH NELEDGWMWV TNLRTDEQGL IVEDLVEEVG REEDPHEGKI 350
    WFHGKISKQE AYNLLMTVGQ VCSFLVRPSD NTPGDYSLYF RTNENIQRFK 400
    ICPTPNNQFM MGGRYYNSIG DIIDHYRKEQ IVEGYYLKEP VPMQDQEQVL 450
    NDTVDGKEIY NTIRRKTKDA FYKNIVKKGY LLKKGKGKRW KNLYFILEGS 500
    DAQLIYFESE KRATKPKGLI DLSVCSVYVV HDSLFGRPNC FQIVVQHFSE 550
    EHYIFYFAGE TPEQAEDWMK GLQAFCNLRK SSPGTSNKRL RQVSSLVLHI 600
    EEAHKLPVKH FTNPYCNIYL NSVQVAKTHA REGQNPVWSE EFVFDDLPPD 650
    INRFEITLSN KTKKSKDPDI LFMRCQLSRL QKGHATDEWF LLSSHIPLKG 700
    IEPGSLRVRA RYSMEKIMPE EEYSEFKELI LQKELHVVYA LSHVCGQDRT 750
    LLASILLRIF LHEKLESLLL CTLNDREISM EDEATTLFRA TTLASTLMEQ 800
    YMKATATQFV HHALKDSILK IMESKQSCEL SPSKLEKNED VNTNLTHLLN 850
    ILSELVEKIF MASEILPPTL RYIYGCLQKS VQHKWPTNTT MRTRVVSGFV 900
    FLRLICPAIL NPRMFNIISD SPSPIAARTL ILVAKSVQNL ANLVEFGAKE 950
    PYMEGVNPFI KSNKHRMIMF LDELGNVPEL PDTTEHSRTD LSRDLAALHE 1000
    ICVAHSDELR TLSNERGAQQ HVLKKLLAIT ELLQQKQNQY TKTNDVR 1047
    Length:1,047
    Mass (Da):116,403
    Last modified:February 1, 1991 - v1
    Checksum:iC35B6567F5BC5370
    GO
    Isoform 2 (identifier: P20936-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-177: Missing.
         178-180: TNQ → MKG

    Show »
    Length:870
    Mass (Da):100,398
    Checksum:iB328E701911065F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti789 – 7891R → A AA sequence (PubMed:8360177)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti398 – 3981R → L in basal cell carcinomas. 1 Publication
    VAR_002650
    Natural varianti400 – 4001K → E in basal cell carcinomas. 1 Publication
    VAR_002651
    Natural varianti401 – 4011I → V in basal cell carcinomas. 1 Publication
    VAR_002652
    Natural varianti540 – 5401C → Y in CMAVM. 1 Publication
    VAR_017744

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 177177Missing in isoform 2. 2 PublicationsVSP_001625Add
    BLAST
    Alternative sequencei178 – 1803TNQ → MKG in isoform 2. 2 PublicationsVSP_001626

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23379 mRNA. Translation: AAA52517.1.
    M23612 mRNA. Translation: AAA35865.1.
    AK312739 mRNA. Translation: BAG35610.1.
    BC033015 mRNA. Translation: AAH33015.1.
    CCDSiCCDS34200.1. [P20936-1]
    CCDS47243.1. [P20936-2]
    PIRiA40121.
    B40121.
    RefSeqiNP_002881.1. NM_002890.2. [P20936-1]
    NP_072179.1. NM_022650.2. [P20936-2]
    UniGeneiHs.664080.

    Genome annotation databases

    EnsembliENST00000274376; ENSP00000274376; ENSG00000145715. [P20936-1]
    ENST00000456692; ENSP00000411221; ENSG00000145715. [P20936-2]
    GeneIDi5921.
    KEGGihsa:5921.
    UCSCiuc003kiw.3. human. [P20936-1]
    uc003kix.3. human. [P20936-2]

    Polymorphism databases

    DMDMi121743.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23379 mRNA. Translation: AAA52517.1 .
    M23612 mRNA. Translation: AAA35865.1 .
    AK312739 mRNA. Translation: BAG35610.1 .
    BC033015 mRNA. Translation: AAH33015.1 .
    CCDSi CCDS34200.1. [P20936-1 ]
    CCDS47243.1. [P20936-2 ]
    PIRi A40121.
    B40121.
    RefSeqi NP_002881.1. NM_002890.2. [P20936-1 ]
    NP_072179.1. NM_022650.2. [P20936-2 ]
    UniGenei Hs.664080.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WER X-ray 1.60 A 714-1047 [» ]
    1WQ1 X-ray 2.50 G 714-1047 [» ]
    2GQI NMR - A 282-339 [» ]
    2GSB NMR - A 341-446 [» ]
    2J05 X-ray 1.50 A/B 281-341 [» ]
    2J06 X-ray 1.80 A/B 281-341 [» ]
    2M51 NMR - A 281-341 [» ]
    4FSS X-ray 2.25 A/B/C 281-341 [» ]
    ProteinModelPortali P20936.
    SMRi P20936. Positions 168-446, 475-573, 593-713, 718-1041.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111856. 54 interactions.
    DIPi DIP-144N.
    IntActi P20936. 36 interactions.
    MINTi MINT-195165.
    STRINGi 9606.ENSP00000274376.

    PTM databases

    PhosphoSitei P20936.

    Polymorphism databases

    DMDMi 121743.

    Proteomic databases

    MaxQBi P20936.
    PaxDbi P20936.
    PRIDEi P20936.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274376 ; ENSP00000274376 ; ENSG00000145715 . [P20936-1 ]
    ENST00000456692 ; ENSP00000411221 ; ENSG00000145715 . [P20936-2 ]
    GeneIDi 5921.
    KEGGi hsa:5921.
    UCSCi uc003kiw.3. human. [P20936-1 ]
    uc003kix.3. human. [P20936-2 ]

    Organism-specific databases

    CTDi 5921.
    GeneCardsi GC05P086565.
    GeneReviewsi RASA1.
    HGNCi HGNC:9871. RASA1.
    HPAi CAB007789.
    MIMi 139150. gene.
    608354. phenotype.
    608355. phenotype.
    neXtProti NX_P20936.
    Orphaneti 137667. Capillary malformation - arteriovenous malformation.
    90307. Parkes Weber syndrome.
    PharmGKBi PA34232.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282054.
    HOGENOMi HOG000007794.
    HOVERGENi HBG057470.
    InParanoidi P20936.
    KOi K04352.
    OMAi QAQDWMK.
    OrthoDBi EOG7HTHG8.
    PhylomeDBi P20936.
    TreeFami TF105301.

    Enzyme and pathway databases

    Reactomei REACT_17025. Downstream signal transduction.
    SignaLinki P20936.

    Miscellaneous databases

    ChiTaRSi RASA1. human.
    EvolutionaryTracei P20936.
    GeneWikii RAS_p21_protein_activator_1.
    GenomeRNAii 5921.
    NextBioi 23056.
    PMAP-CutDB P20936.
    PROi P20936.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20936.
    Bgeei P20936.
    CleanExi HS_RASA1.
    Genevestigatori P20936.

    Family and domain databases

    Gene3Di 1.10.506.10. 1 hit.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001936. RasGAP.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00169. PH. 1 hit.
    PF00616. RasGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    SMARTi SM00239. C2. 1 hit.
    SM00233. PH. 1 hit.
    SM00323. RasGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50004. C2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of two types of GAP complementary DNA from human placenta."
      Trahey M., Wong G., Halenbeck R., Rubinfeld B., Martin G.A., Ladner M., Long C.M., Crosier W.J., Watt K., Koths K., McCormick F.
      Science 242:1697-1700(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    3. "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: Testis.
    4. "Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein."
      Zhang Y., Zhang G., Mollat P., Carles C., Riva M., Frobert Y., Malassine A., Rostene W., Thang D.C., Beltchev B., Tavitian A., Thane M.N.
      J. Biol. Chem. 268:18875-18881(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 294-303; 326-334; 392-398; 439-457; 458-466; 479-483; 777-790 AND 821-825, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    5. "Purification, characterization, and western blot analysis of human GTPase-activating protein from native and recombinant sources."
      Halenbeck R., Crosier W.J., Clark R., McCormick F., Koths K.
      J. Biol. Chem. 265:21922-21928(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-7 (ISOFORM 2).
    6. "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm."
      Giglione C., Gonfloni S., Parmeggiani A.
      Eur. J. Biochem. 268:3275-3283(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, FUNCTION.
    7. "GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit."
      Kazlauskas A., Kashishian A., Cooper J.A., Valius M.
      Mol. Cell. Biol. 12:2534-2544(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB.
    8. "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
      Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
      Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1.
    9. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
      Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
      J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV2.
    10. "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
      Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
      Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV2.
    11. "The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway."
      Wang D., Li Z., Messing E.M., Wu G.
      J. Biol. Chem. 280:16393-16401(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPSB1.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding."
      Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S., Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T., Brazil D.P., Hemmings B.A., Park J.
      J. Biol. Chem. 283:1480-1491(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDPK1.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity."
      Ger M., Zitkus Z., Valius M.
      Cell. Signal. 23:1651-1658(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCK1.
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence."
      Yang Y.S., Garbay C., Duschesne M., Cornille F., Jullian N., Fromage N., Tocque B., Roques B.P.
      EMBO J. 13:1270-1279(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 275-350.
    19. "Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras."
      Scheffzek K., Lautwein A., Kabsch W., Reza Ahmadian M., Wittinghofer A.
      Nature 384:591-596(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 714-1047.
    20. "The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants."
      Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A.
      Science 277:333-338(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 714-1047 IN COMPLEX WITH RAS.
    21. "Solution structure of the SH3 domain and of the second SH2 domain of human RAS GTPase-activating protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAY-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 282-446.
    22. "Nonsense mutations in the C-terminal SH2 region of the GTPase activating protein (GAP) gene in human tumours."
      Friedman E., Gejman P.V., Martin G.A., McCormick F.
      Nat. Genet. 5:242-247(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-398; GLU-400 AND VAL-401.
    23. "Capillary malformation-arteriovenous malformation, a new clinical and genetic disorder caused by RASA1 mutations."
      Eerola I., Boon L.M., Mulliken J.B., Burrows P.E., Dompmartin A., Watanabe S., Vanwijck R., Vikkula M.
      Am. J. Hum. Genet. 73:1240-1249(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMAVM TYR-540.

    Entry informationi

    Entry nameiRASA1_HUMAN
    AccessioniPrimary (citable) accession number: P20936
    Secondary accession number(s): B2R6W3, Q9UDI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 179 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3