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P46940 (IQGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras GTPase-activating-like protein IQGAP1
Alternative name(s):
p195
Gene names
Name:IQGAP1
Synonyms:KIAA0051
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1657 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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. Ref.6 Ref.10 Ref.12

Subcellular location

Cell membrane Ref.6.

Tissue specificity

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

Domain

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. Ref.6

Post-translational modification

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.

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 4 IQ domains.

Contains 1 Ras-GAP domain.

Contains 1 WW domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandCalmodulin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to calcium ion

Inferred from direct assay PubMed 18567582. Source: BHF-UCL

energy reserve metabolic process

Traceable author statement. Source: Reactome

glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of catalytic activity

Traceable author statement Ref.8. Source: GOC

negative regulation of dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of GTPase activity

Traceable author statement Ref.1. Source: GOC

positive regulation of protein kinase activity

Inferred from mutant phenotype PubMed 17563371. Source: BHF-UCL

regulation of cytokine production

Inferred from electronic annotation. Source: Ensembl

regulation of insulin secretion

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentactin filament

Traceable author statement Ref.8. Source: ProtInc

cell junction

Inferred from direct assay. Source: HPA

cell leading edge

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 22493426. Source: UniProtKB

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from electronic annotation. Source: Ensembl

slit diaphragm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTPase activator activity

Traceable author statement Ref.1. Source: ProtInc

GTPase inhibitor activity

Traceable author statement Ref.8. Source: ProtInc

Ras GTPase activator activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Traceable author statement PubMed 18567582. Source: BHF-UCL

calmodulin binding

Inferred from physical interaction PubMed 18567582. Source: BHF-UCL

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay PubMed 22493426. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10793131. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 17563371. Source: BHF-UCL

protein phosphatase binding

Inferred from physical interaction PubMed 16380380. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 16571656Ras GTPase-activating-like protein IQGAP1
PRO_0000056648

Regions

Domain44 – 159116CH
Domain679 – 71234WW
Domain745 – 77430IQ 1
Domain775 – 80430IQ 2
Domain805 – 83430IQ 3
Domain835 – 86430IQ 4
Domain1004 – 1237234Ras-GAP
Region956 – 1274319C1
Region1276 – 1657382C2

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.13 Ref.15 Ref.16
Modified residue21Phosphoserine Ref.9 Ref.13
Modified residue1721Phosphotyrosine By similarity
Modified residue3301Phosphoserine Ref.13
Modified residue14411Phosphoserine; by PKC Probable
Modified residue14431Phosphoserine; by PKC/PRKCE Ref.6 Ref.7 Ref.11 Ref.13

Natural variations

Natural variant2561S → A.
Corresponds to variant rs12324924 [ dbSNP | Ensembl ].
VAR_049134

Experimental info

Mutagenesis14411S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1443. Ref.7
Mutagenesis14411S → E: Strongly enhances neurite outgrowth promoting activity; when associated with A-1443. Ref.7
Mutagenesis14431S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1441. Ref.7
Mutagenesis14431S → D: Strongly enhances neurite outgrowth promoting activity; when associated with A-1441. Ref.7

Secondary structure

....................................................................................................... 1657
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46940 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A52EC629596EAC33

FASTA1,657189,252
        10         20         30         40         50         60 
MSAADEVDGL GVARPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA KRWMEACLGE 

        70         80         90        100        110        120 
DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ TRYKATGLHF RHTDNVIQWL 

       130        140        150        160        170        180 
NAMDEIGLPK IFYPETTDIY DRKNMPRCIY CIHALSLYLF KLGLAPQIQD LYGKVDFTEE 

       190        200        210        220        230        240 
EINNMKTELE KYGIQMPAFS KIGGILANEL SVDEAALHAA VIAINEAIDR RIPADTFAAL 

       250        260        270        280        290        300 
KNPNAMLVNL EEPLASTYQD ILYQAKQDKM TNAKNRTENS ERERDVYEEL LTQAEIQGNI 

       310        320        330        340        350        360 
NKVNTFSALA NIDLALEQGD ALALFRALQS PALGLRGLQQ QNSDWYLKQL LSDKQQKRQS 

       370        380        390        400        410        420 
GQTDPLQKEE LQSGVDAANS AAQQYQRRLA AVALINAAIQ KGVAEKTVLE LMNPEAQLPQ 

       430        440        450        460        470        480 
VYPFAADLYQ KELATLQRQS PEHNLTHPEL SVAVEMLSSV ALINRALESG DVNTVWKQLS 

       490        500        510        520        530        540 
SSVTGLTNIE EENCQRYLDE LMKLKAQAHA ENNEFITWND IQACVDHVNL VVQEEHERIL 

       550        560        570        580        590        600 
AIGLINEALD EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQEIQDESAV 

       610        620        630        640        650        660 
LWLDEIQGGI WQSNKDTQEA QKFALGIFAI NEAVESGDVG KTLSALRSPD VGLYGVIPEC 

       670        680        690        700        710        720 
GETYHSDLAE AKKKKLAVGD NNSKWVKHWV KGGYYYYHNL ETQEGGWDEP PNFVQNSMQL 

       730        740        750        760        770        780 
SREEIQSSIS GVTAAYNREQ LWLANEGLIT RLQARCRGYL VRQEFRSRMN FLKKQIPAIT 

       790        800        810        820        830        840 
CIQSQWRGYK QKKAYQDRLA YLRSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII 

       850        860        870        880        890        900 
KIQAFIRANK ARDDYKTLIN AEDPPMVVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI 

       910        920        930        940        950        960 
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM INKQKGGLKA 

       970        980        990       1000       1010       1020 
LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK FMDSVIFTLY NYASNQREEY 

      1030       1040       1050       1060       1070       1080 
LLLRLFKTAL QEEIKSKVDQ IQEIVTGNPT VIKMVVSFNR GARGQNALRQ ILAPVVKEIM 

      1090       1100       1110       1120       1130       1140 
DDKSLNIKTD PVDIYKSWVN QMESQTGEAS KLPYDVTPEQ ALAHEEVKTR LDSSIRNMRA 

      1150       1160       1170       1180       1190       1200 
VTDKFLSAIV SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI 

      1210       1220       1230       1240       1250       1260 
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI INEYLSQSYQ 

      1270       1280       1290       1300       1310       1320 
KFRRFFQTAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG EIINTHTLLL DHQDAIAPEH 

      1330       1340       1350       1360       1370       1380 
NDPIHELLDD LGEVPTIESL IGESSGNLND PNKEALAKTE VSLTLTNKFD VPGDENAEMD 

      1390       1400       1410       1420       1430       1440 
ARTILLNTKR LIVDVIRFQP GETLTEILET PATSEQEAEH QRAMQRRAIR DAKTPDKMKK 

      1450       1460       1470       1480       1490       1500 
SKSVKEDSNL TLQEKKEKIQ TGLKKLTELG TVDPKNKYQE LINDIARDIR NQRRYRQRRK 

      1510       1520       1530       1540       1550       1560 
AELVKLQQTY AALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE MKGKKSKKIS 

      1570       1580       1590       1600       1610       1620 
LKYTAARLHE KGVLLEIEDL QVNQFKNVIF EISPTEEVGD FEVKAKFMGV QMETFMLHYQ 

      1630       1640       1650 
DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL NKKFYGK 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33075 mRNA. Translation: AAA59187.1.
D29640 mRNA. Translation: BAA06123.2. Different initiation.
CH471101 Genomic DNA. Translation: EAX02102.1.
BC151834 mRNA. Translation: AAI51835.1.
CCDSCCDS10362.1.
PIRA54854.
RefSeqNP_003861.1. NM_003870.3.
UniGeneHs.430551.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0HNMR-A1559-1657[»]
2RR8NMR-A26-210[»]
3FAYX-ray2.20A962-1345[»]
3I6XX-ray2.50A/B/C/D1-191[»]
ProteinModelPortalP46940.
SMRP46940. Positions 26-210, 962-1339, 1561-1657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114353. 80 interactions.
IntActP46940. 48 interactions.
MINTMINT-4999354.
STRING9606.ENSP00000268182.

PTM databases

PhosphoSiteP46940.

Polymorphism databases

DMDM1170586.

Proteomic databases

MaxQBP46940.
PaxDbP46940.
PeptideAtlasP46940.
PRIDEP46940.

Protocols and materials databases

DNASU8826.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268182; ENSP00000268182; ENSG00000140575.
GeneID8826.
KEGGhsa:8826.
UCSCuc002bpl.1. human.

Organism-specific databases

CTD8826.
GeneCardsGC15P090931.
H-InvDBHIX0172824.
HGNCHGNC:6110. IQGAP1.
HPACAB013302.
HPA014055.
MIM603379. gene.
neXtProtNX_P46940.
PharmGKBPA29910.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5261.
HOGENOMHOG000004842.
HOVERGENHBG052143.
InParanoidP46940.
KOK16848.
OMAQDILYQA.
OrthoDBEOG7FNC6M.
PhylomeDBP46940.
TreeFamTF313078.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpressP46940.
BgeeP46940.
CleanExHS_IQGAP1.
GenevestigatorP46940.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.10.506.10. 2 hits.
4.10.270.10. 1 hit.
InterProIPR001715. 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]
PfamPF00307. CH. 1 hit.
PF00612. IQ. 4 hits.
PF00616. RasGAP. 1 hit.
PF03836. RasGAP_C. 1 hit.
[Graphical view]
SMARTSM00033. CH. 1 hit.
SM00015. IQ. 4 hits.
SM00323. RasGAP. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF48350. SSF48350. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50021. 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]
ProtoNetSearch...

Other

ChiTaRSIQGAP1. human.
EvolutionaryTraceP46940.
GeneWikiIQGAP1.
GenomeRNAi8826.
NextBio33114.
PMAP-CutDBP46940.
PROP46940.
SOURCESearch...

Entry information

Entry nameIQGA1_HUMAN
AccessionPrimary (citable) accession number: P46940
Secondary accession number(s): A7MBM3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM