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P46940

- IQGA1_HUMAN

UniProt

P46940 - IQGA1_HUMAN

Protein

Ras GTPase-activating-like protein IQGAP1

Gene

IQGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. calmodulin binding Source: BHF-UCL
    3. GTPase activator activity Source: ProtInc
    4. GTPase inhibitor activity Source: ProtInc
    5. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: BHF-UCL
    8. protein phosphatase binding Source: UniProtKB
    9. protein serine/threonine kinase activator activity Source: BHF-UCL
    10. Ras GTPase activator activity Source: InterPro

    GO - Biological processi

    1. cellular response to calcium ion Source: BHF-UCL
    2. cellular response to epidermal growth factor stimulus Source: BHF-UCL
    3. energy reserve metabolic process Source: Reactome
    4. epidermal growth factor receptor signaling pathway Source: BHF-UCL
    5. glomerular visceral epithelial cell development Source: UniProtKB
    6. negative regulation of catalytic activity Source: GOC
    7. negative regulation of dephosphorylation Source: Ensembl
    8. positive regulation of GTPase activity Source: GOC
    9. positive regulation of protein kinase activity Source: BHF-UCL
    10. positive regulation of protein serine/threonine kinase activity Source: GOC
    11. regulation of cytokine production Source: Ensembl
    12. regulation of insulin secretion Source: Reactome
    13. signal transduction Source: ProtInc
    14. small GTPase mediated signal transduction Source: InterPro
    15. small molecule metabolic process Source: Reactome

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_23832. Nephrin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras GTPase-activating-like protein IQGAP1
    Alternative name(s):
    p195
    Gene namesi
    Name:IQGAP1
    Synonyms:KIAA0051
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6110. IQGAP1.

    Subcellular locationi

    Cell membrane 1 Publication

    GO - Cellular componenti

    1. actin filament Source: ProtInc
    2. cell junction Source: HPA
    3. cell leading edge Source: Ensembl
    4. cytoplasm Source: HPA
    5. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    8. lateral plasma membrane Source: Ensembl
    9. microtubule Source: UniProtKB
    10. midbody Source: UniProtKB
    11. neuron projection Source: Ensembl
    12. nucleus Source: HPA
    13. plasma membrane Source: HPA
    14. slit diaphragm Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1441 – 14411S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1443. 1 Publication
    Mutagenesisi1441 – 14411S → E: Strongly enhances neurite outgrowth promoting activity; when associated with A-1443. 1 Publication
    Mutagenesisi1443 – 14431S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1441. 1 Publication
    Mutagenesisi1443 – 14431S → D: Strongly enhances neurite outgrowth promoting activity; when associated with A-1441. 1 Publication

    Organism-specific databases

    PharmGKBiPA29910.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 16571656Ras GTPase-activating-like protein IQGAP1PRO_0000056648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei2 – 21Phosphoserine2 Publications
    Modified residuei172 – 1721PhosphotyrosineBy similarity
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei1441 – 14411Phosphoserine; by PKC1 Publication
    Modified residuei1443 – 14431Phosphoserine; by PKC/PRKCE4 Publications

    Post-translational modificationi

    Phosphorylation of Ser-1443 by PKC/PRKCE prevents interaction between C1 and C2, allowing binding of nucleotide-free CDC42. Ser-1443 phosphorylation enhances the ability to promote neurite outgrowth.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46940.
    PaxDbiP46940.
    PeptideAtlasiP46940.
    PRIDEiP46940.

    PTM databases

    PhosphoSiteiP46940.

    Miscellaneous databases

    PMAP-CutDBP46940.

    Expressioni

    Tissue specificityi

    Expressed in the placenta, lung, and kidney. A lower level expression is seen in the heart, liver, skeletal muscle and pancreas.

    Gene expression databases

    ArrayExpressiP46940.
    BgeeiP46940.
    CleanExiHS_IQGAP1.
    GenevestigatoriP46940.

    Organism-specific databases

    HPAiCAB013302.
    HPA014055.

    Interactioni

    Subunit structurei

    Interacts with CDC42; the interaction is demonstrated with IQGAP1 in GTP-bound and in nucleotide-free state. Interacts with RAC1. Does not interact with RHOA. Interacts with TSG101. Interacts with PAK6.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN4O437073EBI-297509,EBI-351526
    CD2APQ9Y5K64EBI-297509,EBI-298152
    CDC42P609532EBI-297509,EBI-81752
    CTNNB1P352223EBI-297509,EBI-491549
    Diaph1O088088EBI-297509,EBI-1026445From a different organism.
    EGFRP005334EBI-297509,EBI-297353
    ERBB2P046265EBI-297509,EBI-641062
    MAGI1Q96QZ74EBI-297509,EBI-924464
    NPHS1O605005EBI-297509,EBI-996920
    NPHS2Q9NP854EBI-297509,EBI-6897706
    PIP5K1CO60331-46EBI-297509,EBI-8838062
    PODXLO005924EBI-297509,EBI-6897823
    RNASELQ058232EBI-297509,EBI-8390477
    TSG101Q998165EBI-297509,EBI-346882

    Protein-protein interaction databases

    BioGridi114353. 89 interactions.
    DIPiDIP-32597N.
    IntActiP46940. 47 interactions.
    MINTiMINT-4999354.
    STRINGi9606.ENSP00000268182.

    Structurei

    Secondary structure

    1
    1657
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 5828
    Helixi65 – 673
    Helixi68 – 725
    Helixi76 – 8510
    Turni87 – 893
    Helixi92 – 943
    Turni96 – 994
    Helixi101 – 1055
    Helixi110 – 1123
    Helixi113 – 12614
    Helixi130 – 1323
    Helixi136 – 1405
    Helixi145 – 16117
    Turni172 – 1743
    Helixi179 – 18810
    Helixi199 – 2013
    Turni206 – 2083
    Helixi962 – 98120
    Helixi984 – 9918
    Helixi1000 – 100910
    Turni1010 – 10134
    Helixi1016 – 103722
    Beta strandi1039 – 10424
    Helixi1043 – 10464
    Helixi1050 – 10589
    Helixi1062 – 108120
    Helixi1091 – 110616
    Helixi1118 – 11214
    Helixi1125 – 115026
    Helixi1151 – 11555
    Helixi1158 – 117417
    Helixi1180 – 119112
    Helixi1192 – 11965
    Helixi1197 – 12015
    Turni1203 – 12075
    Helixi1219 – 123618
    Helixi1246 – 12483
    Helixi1249 – 127022
    Helixi1275 – 12784
    Beta strandi1282 – 12843
    Turni1285 – 12873
    Beta strandi1290 – 12923
    Helixi1299 – 131113
    Helixi1313 – 13164
    Helixi1323 – 13319
    Beta strandi1561 – 15644
    Helixi1565 – 15717
    Beta strandi1572 – 15776
    Helixi1583 – 15875
    Beta strandi1589 – 15935
    Beta strandi1596 – 15994
    Beta strandi1601 – 16088
    Beta strandi1615 – 16173
    Helixi1619 – 162810
    Beta strandi1632 – 16354
    Turni1636 – 16383
    Beta strandi1639 – 16424
    Helixi1643 – 165210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X0HNMR-A1559-1657[»]
    2RR8NMR-A26-210[»]
    3FAYX-ray2.20A962-1345[»]
    3I6XX-ray2.50A/B/C/D1-191[»]
    ProteinModelPortaliP46940.
    SMRiP46940. Positions 26-210, 962-1339, 1561-1657.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46940.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 159116CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini679 – 71234WWPROSITE-ProRule annotationAdd
    BLAST
    Domaini745 – 77430IQ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini775 – 80430IQ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini805 – 83430IQ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini835 – 86430IQ 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1004 – 1237234Ras-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni956 – 1274319C1Add
    BLAST
    Regioni1276 – 1657382C2Add
    BLAST

    Domaini

    Regions C1 and C2 can either interact with nucleotide-free CDC42, or interact together, depending on the phosphorylation state of Ser-1443. When Ser-1443 is not phosphorylated, C1 and C2 interact, which prevents binding of nucleotide-free CDC42 and promotes binding of GTP-bound CDC42. Phosphorylation of Ser-1443 prevents interaction between C1 and C2, which opens the structure of the C-terminus and allows binding and sequestration of nucleotide-free CDC42 on both C1 and C2.1 Publication

    Sequence similaritiesi

    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 4 IQ domains.PROSITE-ProRule annotation
    Contains 1 Ras-GAP domain.PROSITE-ProRule annotation
    Contains 1 WW domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5261.
    HOGENOMiHOG000004842.
    HOVERGENiHBG052143.
    InParanoidiP46940.
    KOiK16848.
    OMAiQDILYQA.
    OrthoDBiEOG7FNC6M.
    PhylomeDBiP46940.
    TreeFamiTF313078.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    1.10.506.10. 2 hits.
    4.10.270.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR027401. Myosin-like_IQ_dom.
    IPR027417. P-loop_NTPase.
    IPR001936. RasGAP.
    IPR000593. RasGAP_C.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00307. CH. 1 hit.
    PF00612. IQ. 4 hits.
    PF00616. RasGAP. 1 hit.
    PF03836. RasGAP_C. 1 hit.
    [Graphical view]
    SMARTiSM00033. CH. 1 hit.
    SM00015. IQ. 4 hits.
    SM00323. RasGAP. 1 hit.
    SM00456. WW. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF48350. SSF48350. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50021. CH. 1 hit.
    PS50096. IQ. 4 hits.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P46940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAADEVDGL GVARPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA     50
    KRWMEACLGE DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ 100
    TRYKATGLHF RHTDNVIQWL NAMDEIGLPK IFYPETTDIY DRKNMPRCIY 150
    CIHALSLYLF KLGLAPQIQD LYGKVDFTEE EINNMKTELE KYGIQMPAFS 200
    KIGGILANEL SVDEAALHAA VIAINEAIDR RIPADTFAAL KNPNAMLVNL 250
    EEPLASTYQD ILYQAKQDKM TNAKNRTENS ERERDVYEEL LTQAEIQGNI 300
    NKVNTFSALA NIDLALEQGD ALALFRALQS PALGLRGLQQ QNSDWYLKQL 350
    LSDKQQKRQS GQTDPLQKEE LQSGVDAANS AAQQYQRRLA AVALINAAIQ 400
    KGVAEKTVLE LMNPEAQLPQ VYPFAADLYQ KELATLQRQS PEHNLTHPEL 450
    SVAVEMLSSV ALINRALESG DVNTVWKQLS SSVTGLTNIE EENCQRYLDE 500
    LMKLKAQAHA ENNEFITWND IQACVDHVNL VVQEEHERIL AIGLINEALD 550
    EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQEIQDESAV 600
    LWLDEIQGGI WQSNKDTQEA QKFALGIFAI NEAVESGDVG KTLSALRSPD 650
    VGLYGVIPEC GETYHSDLAE AKKKKLAVGD NNSKWVKHWV KGGYYYYHNL 700
    ETQEGGWDEP PNFVQNSMQL SREEIQSSIS GVTAAYNREQ LWLANEGLIT 750
    RLQARCRGYL VRQEFRSRMN FLKKQIPAIT CIQSQWRGYK QKKAYQDRLA 800
    YLRSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII KIQAFIRANK 850
    ARDDYKTLIN AEDPPMVVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI 900
    RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM 950
    INKQKGGLKA LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK 1000
    FMDSVIFTLY NYASNQREEY LLLRLFKTAL QEEIKSKVDQ IQEIVTGNPT 1050
    VIKMVVSFNR GARGQNALRQ ILAPVVKEIM DDKSLNIKTD PVDIYKSWVN 1100
    QMESQTGEAS KLPYDVTPEQ ALAHEEVKTR LDSSIRNMRA VTDKFLSAIV 1150
    SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI 1200
    VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI 1250
    INEYLSQSYQ KFRRFFQTAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG 1300
    EIINTHTLLL DHQDAIAPEH NDPIHELLDD LGEVPTIESL IGESSGNLND 1350
    PNKEALAKTE VSLTLTNKFD VPGDENAEMD ARTILLNTKR LIVDVIRFQP 1400
    GETLTEILET PATSEQEAEH QRAMQRRAIR DAKTPDKMKK SKSVKEDSNL 1450
    TLQEKKEKIQ TGLKKLTELG TVDPKNKYQE LINDIARDIR NQRRYRQRRK 1500
    AELVKLQQTY AALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE 1550
    MKGKKSKKIS LKYTAARLHE KGVLLEIEDL QVNQFKNVIF EISPTEEVGD 1600
    FEVKAKFMGV QMETFMLHYQ DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL 1650
    NKKFYGK 1657
    Length:1,657
    Mass (Da):189,252
    Last modified:November 1, 1995 - v1
    Checksum:iA52EC629596EAC33
    GO

    Sequence cautioni

    The sequence BAA06123.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti256 – 2561S → A.
    Corresponds to variant rs12324924 [ dbSNP | Ensembl ].
    VAR_049134

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33075 mRNA. Translation: AAA59187.1.
    D29640 mRNA. Translation: BAA06123.2. Different initiation.
    CH471101 Genomic DNA. Translation: EAX02102.1.
    BC151834 mRNA. Translation: AAI51835.1.
    CCDSiCCDS10362.1.
    PIRiA54854.
    RefSeqiNP_003861.1. NM_003870.3.
    UniGeneiHs.430551.

    Genome annotation databases

    EnsembliENST00000268182; ENSP00000268182; ENSG00000140575.
    GeneIDi8826.
    KEGGihsa:8826.
    UCSCiuc002bpl.1. human.

    Polymorphism databases

    DMDMi1170586.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33075 mRNA. Translation: AAA59187.1 .
    D29640 mRNA. Translation: BAA06123.2 . Different initiation.
    CH471101 Genomic DNA. Translation: EAX02102.1 .
    BC151834 mRNA. Translation: AAI51835.1 .
    CCDSi CCDS10362.1.
    PIRi A54854.
    RefSeqi NP_003861.1. NM_003870.3.
    UniGenei Hs.430551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X0H NMR - A 1559-1657 [» ]
    2RR8 NMR - A 26-210 [» ]
    3FAY X-ray 2.20 A 962-1345 [» ]
    3I6X X-ray 2.50 A/B/C/D 1-191 [» ]
    ProteinModelPortali P46940.
    SMRi P46940. Positions 26-210, 962-1339, 1561-1657.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114353. 89 interactions.
    DIPi DIP-32597N.
    IntActi P46940. 47 interactions.
    MINTi MINT-4999354.
    STRINGi 9606.ENSP00000268182.

    PTM databases

    PhosphoSitei P46940.

    Polymorphism databases

    DMDMi 1170586.

    Proteomic databases

    MaxQBi P46940.
    PaxDbi P46940.
    PeptideAtlasi P46940.
    PRIDEi P46940.

    Protocols and materials databases

    DNASUi 8826.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268182 ; ENSP00000268182 ; ENSG00000140575 .
    GeneIDi 8826.
    KEGGi hsa:8826.
    UCSCi uc002bpl.1. human.

    Organism-specific databases

    CTDi 8826.
    GeneCardsi GC15P090931.
    H-InvDB HIX0172824.
    HGNCi HGNC:6110. IQGAP1.
    HPAi CAB013302.
    HPA014055.
    MIMi 603379. gene.
    neXtProti NX_P46940.
    PharmGKBi PA29910.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5261.
    HOGENOMi HOG000004842.
    HOVERGENi HBG052143.
    InParanoidi P46940.
    KOi K16848.
    OMAi QDILYQA.
    OrthoDBi EOG7FNC6M.
    PhylomeDBi P46940.
    TreeFami TF313078.

    Enzyme and pathway databases

    Reactomei REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_23832. Nephrin interactions.

    Miscellaneous databases

    ChiTaRSi IQGAP1. human.
    EvolutionaryTracei P46940.
    GeneWikii IQGAP1.
    GenomeRNAii 8826.
    NextBioi 33114.
    PMAP-CutDB P46940.
    PROi P46940.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46940.
    Bgeei P46940.
    CleanExi HS_IQGAP1.
    Genevestigatori P46940.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    1.10.506.10. 2 hits.
    4.10.270.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR027401. Myosin-like_IQ_dom.
    IPR027417. P-loop_NTPase.
    IPR001936. RasGAP.
    IPR000593. RasGAP_C.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00307. CH. 1 hit.
    PF00612. IQ. 4 hits.
    PF00616. RasGAP. 1 hit.
    PF03836. RasGAP_C. 1 hit.
    [Graphical view ]
    SMARTi SM00033. CH. 1 hit.
    SM00015. IQ. 4 hits.
    SM00323. RasGAP. 1 hit.
    SM00456. WW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF48350. SSF48350. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50021. CH. 1 hit.
    PS50096. IQ. 4 hits.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human rasGAP-related protein containing calmodulin-binding motifs."
      Weissbach L., Settleman J., Kalady M.F., Snijders A.J., Murthy A.E., Yan Y.-X., Bernards A.
      J. Biol. Chem. 269:20517-20521(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver and Placenta.
    2. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. Bienvenut W.V., Lilla S., Zebisch A., Kolch W.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-25; 81-88; 112-143; 192-230; 466-477; 557-585; 923-935; 989-997; 1391-1397; 1466-1475 AND 1506-1516, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    6. "Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator."
      Grohmanova K., Schlaepfer D., Hess D., Gutierrez P., Beck M., Kroschewski R.
      J. Biol. Chem. 279:48495-48504(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1441-1455, PHOSPHORYLATION AT SER-1443, INTERACTION WITH CDC42 AND RAC1, DOMAIN, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "IQGAP1 promotes neurite outgrowth in a phosphorylation-dependent manner."
      Li Z., McNulty D.E., Marler K.J.M., Lim L., Hall C., Annan R.S., Sacks D.B.
      J. Biol. Chem. 280:13871-13878(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1441-1455, PHOSPHORYLATION AT SER-1441 AND SER-1443, MUTAGENESIS OF SER-1441 AND SER-1443, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs."
      Hart M.J., Callow M.G., Souza B., Polakis P.
      EMBO J. 15:2997-3005(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TSG101.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins."
      Kaur R., Yuan X., Lu M.L., Balk S.P.
      Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAK6.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-330 AND SER-1443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Solution structure of the carboxyl-terminal RGC domain in human IQGAP1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1559-1657.

    Entry informationi

    Entry nameiIQGA1_HUMAN
    AccessioniPrimary (citable) accession number: P46940
    Secondary accession number(s): A7MBM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 155 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 15
      Human chromosome 15: 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

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