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Protein

Ras GTPase-activating-like protein IQGAP1

Gene

IQGAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calcium ion binding Source: BHF-UCL
  • calmodulin binding Source: BHF-UCL
  • GTPase activator activity Source: ProtInc
  • GTPase inhibitor activity Source: ProtInc
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: BHF-UCL
  • S100 protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140575-MONOMER.
ReactomeiR-HSA-373753. Nephrin interactions.
R-HSA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNORiP46940.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:6110. IQGAP1.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: ProtInc
  • axon Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • growth cone Source: UniProtKB
  • lateral plasma membrane Source: Ensembl
  • membrane raft Source: Ensembl
  • microtubule Source: UniProtKB
  • midbody Source: UniProtKB
  • neuron projection Source: UniProtKB
  • nucleus Source: Ensembl
  • plasma membrane Source: Reactome
  • protein complex Source: Ensembl
  • ruffle Source: UniProtKB
  • slit diaphragm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1441S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1443. 1 Publication1
Mutagenesisi1441S → E: Strongly enhances neurite outgrowth promoting activity; when associated with A-1443. 1 Publication1
Mutagenesisi1443S → A: Abolishes neurite outgrowth promoting activity; when associated with A-1441. 1 Publication1
Mutagenesisi1443S → D: Strongly enhances neurite outgrowth promoting activity; when associated with A-1441. 1 Publication1

Organism-specific databases

DisGeNETi8826.
OpenTargetsiENSG00000140575.
PharmGKBiPA29910.

Polymorphism and mutation databases

BioMutaiIQGAP1.
DMDMi1170586.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000566482 – 1657Ras GTPase-activating-like protein IQGAP1Add BLAST1656

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei172PhosphotyrosineBy similarity1
Modified residuei330PhosphoserineCombined sources1
Modified residuei1441Phosphoserine; by PKC1 Publication1
Modified residuei1443Phosphoserine; by PKC/PRKCECombined sources2 Publications1

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP46940.
MaxQBiP46940.
PaxDbiP46940.
PeptideAtlasiP46940.
PRIDEiP46940.

PTM databases

iPTMnetiP46940.
PhosphoSitePlusiP46940.
SwissPalmiP46940.

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

BgeeiENSG00000140575.
CleanExiHS_IQGAP1.
ExpressionAtlasiP46940. baseline and differential.
GenevisibleiP46940. HS.

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
ACTN4O437074EBI-297509,EBI-351526
CD2APQ9Y5K64EBI-297509,EBI-298152
CDC42P609534EBI-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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calmodulin binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114353. 261 interactors.
DIPiDIP-32597N.
IntActiP46940. 190 interactors.
MINTiMINT-4999354.
STRINGi9606.ENSP00000268182.

Structurei

Secondary structure

11657
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 58Combined sources28
Helixi65 – 67Combined sources3
Helixi68 – 72Combined sources5
Helixi76 – 85Combined sources10
Turni87 – 89Combined sources3
Helixi92 – 94Combined sources3
Turni96 – 99Combined sources4
Helixi101 – 105Combined sources5
Helixi110 – 112Combined sources3
Helixi113 – 126Combined sources14
Helixi130 – 132Combined sources3
Helixi136 – 140Combined sources5
Helixi145 – 161Combined sources17
Turni172 – 174Combined sources3
Helixi179 – 188Combined sources10
Helixi199 – 201Combined sources3
Turni206 – 208Combined sources3
Helixi962 – 981Combined sources20
Helixi984 – 991Combined sources8
Helixi1000 – 1009Combined sources10
Turni1010 – 1013Combined sources4
Helixi1016 – 1037Combined sources22
Beta strandi1039 – 1042Combined sources4
Helixi1043 – 1046Combined sources4
Helixi1050 – 1058Combined sources9
Helixi1062 – 1081Combined sources20
Helixi1091 – 1106Combined sources16
Helixi1118 – 1121Combined sources4
Helixi1125 – 1150Combined sources26
Helixi1151 – 1155Combined sources5
Helixi1158 – 1174Combined sources17
Helixi1180 – 1191Combined sources12
Helixi1192 – 1196Combined sources5
Helixi1197 – 1201Combined sources5
Turni1203 – 1207Combined sources5
Helixi1219 – 1236Combined sources18
Helixi1246 – 1248Combined sources3
Helixi1249 – 1270Combined sources22
Helixi1275 – 1278Combined sources4
Beta strandi1282 – 1284Combined sources3
Turni1285 – 1287Combined sources3
Beta strandi1290 – 1292Combined sources3
Helixi1299 – 1311Combined sources13
Helixi1313 – 1316Combined sources4
Helixi1323 – 1331Combined sources9
Beta strandi1561 – 1564Combined sources4
Helixi1565 – 1571Combined sources7
Beta strandi1572 – 1577Combined sources6
Helixi1583 – 1587Combined sources5
Beta strandi1589 – 1593Combined sources5
Beta strandi1596 – 1599Combined sources4
Beta strandi1601 – 1608Combined sources8
Beta strandi1615 – 1617Combined sources3
Helixi1619 – 1628Combined sources10
Beta strandi1632 – 1635Combined sources4
Turni1636 – 1638Combined sources3
Beta strandi1639 – 1642Combined sources4
Helixi1643 – 1652Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X0HNMR-A1559-1657[»]
2RR8NMR-A26-210[»]
3FAYX-ray2.20A962-1345[»]
3I6XX-ray2.50A/B/C/D1-191[»]
5L0OX-ray2.36A/B/C/D1-191[»]
ProteinModelPortaliP46940.
SMRiP46940.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46940.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 159CHPROSITE-ProRule annotationAdd BLAST116
Domaini679 – 712WWPROSITE-ProRule annotationAdd BLAST34
Domaini745 – 774IQ 1PROSITE-ProRule annotationAdd BLAST30
Domaini775 – 804IQ 2PROSITE-ProRule annotationAdd BLAST30
Domaini805 – 834IQ 3PROSITE-ProRule annotationAdd BLAST30
Domaini835 – 864IQ 4PROSITE-ProRule annotationAdd BLAST30
Domaini1004 – 1237Ras-GAPPROSITE-ProRule annotationAdd BLAST234

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni956 – 1274C1Add BLAST319
Regioni1276 – 1657C2Add BLAST382

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

eggNOGiKOG2128. Eukaryota.
COG5261. LUCA.
GeneTreeiENSGT00600000084379.
HOGENOMiHOG000004842.
HOVERGENiHBG052143.
InParanoidiP46940.
KOiK16848.
OMAiIPECGET.
OrthoDBiEOG091G00ET.
PhylomeDBiP46940.
TreeFamiTF313078.

Family and domain databases

CDDicd00014. CH. 1 hit.
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.
IPR000593. RasGAP_C.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
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

        10         20         30         40         50
MSAADEVDGL GVARPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA
60 70 80 90 100
KRWMEACLGE DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ
110 120 130 140 150
TRYKATGLHF RHTDNVIQWL NAMDEIGLPK IFYPETTDIY DRKNMPRCIY
160 170 180 190 200
CIHALSLYLF KLGLAPQIQD LYGKVDFTEE EINNMKTELE KYGIQMPAFS
210 220 230 240 250
KIGGILANEL SVDEAALHAA VIAINEAIDR RIPADTFAAL KNPNAMLVNL
260 270 280 290 300
EEPLASTYQD ILYQAKQDKM TNAKNRTENS ERERDVYEEL LTQAEIQGNI
310 320 330 340 350
NKVNTFSALA NIDLALEQGD ALALFRALQS PALGLRGLQQ QNSDWYLKQL
360 370 380 390 400
LSDKQQKRQS GQTDPLQKEE LQSGVDAANS AAQQYQRRLA AVALINAAIQ
410 420 430 440 450
KGVAEKTVLE LMNPEAQLPQ VYPFAADLYQ KELATLQRQS PEHNLTHPEL
460 470 480 490 500
SVAVEMLSSV ALINRALESG DVNTVWKQLS SSVTGLTNIE EENCQRYLDE
510 520 530 540 550
LMKLKAQAHA ENNEFITWND IQACVDHVNL VVQEEHERIL AIGLINEALD
560 570 580 590 600
EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQEIQDESAV
610 620 630 640 650
LWLDEIQGGI WQSNKDTQEA QKFALGIFAI NEAVESGDVG KTLSALRSPD
660 670 680 690 700
VGLYGVIPEC GETYHSDLAE AKKKKLAVGD NNSKWVKHWV KGGYYYYHNL
710 720 730 740 750
ETQEGGWDEP PNFVQNSMQL SREEIQSSIS GVTAAYNREQ LWLANEGLIT
760 770 780 790 800
RLQARCRGYL VRQEFRSRMN FLKKQIPAIT CIQSQWRGYK QKKAYQDRLA
810 820 830 840 850
YLRSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII KIQAFIRANK
860 870 880 890 900
ARDDYKTLIN AEDPPMVVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI
910 920 930 940 950
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM
960 970 980 990 1000
INKQKGGLKA LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK
1010 1020 1030 1040 1050
FMDSVIFTLY NYASNQREEY LLLRLFKTAL QEEIKSKVDQ IQEIVTGNPT
1060 1070 1080 1090 1100
VIKMVVSFNR GARGQNALRQ ILAPVVKEIM DDKSLNIKTD PVDIYKSWVN
1110 1120 1130 1140 1150
QMESQTGEAS KLPYDVTPEQ ALAHEEVKTR LDSSIRNMRA VTDKFLSAIV
1160 1170 1180 1190 1200
SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI
1210 1220 1230 1240 1250
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI
1260 1270 1280 1290 1300
INEYLSQSYQ KFRRFFQTAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG
1310 1320 1330 1340 1350
EIINTHTLLL DHQDAIAPEH NDPIHELLDD LGEVPTIESL IGESSGNLND
1360 1370 1380 1390 1400
PNKEALAKTE VSLTLTNKFD VPGDENAEMD ARTILLNTKR LIVDVIRFQP
1410 1420 1430 1440 1450
GETLTEILET PATSEQEAEH QRAMQRRAIR DAKTPDKMKK SKSVKEDSNL
1460 1470 1480 1490 1500
TLQEKKEKIQ TGLKKLTELG TVDPKNKYQE LINDIARDIR NQRRYRQRRK
1510 1520 1530 1540 1550
AELVKLQQTY AALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE
1560 1570 1580 1590 1600
MKGKKSKKIS LKYTAARLHE KGVLLEIEDL QVNQFKNVIF EISPTEEVGD
1610 1620 1630 1640 1650
FEVKAKFMGV QMETFMLHYQ DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL

NKKFYGK
Length:1,657
Mass (Da):189,252
Last modified:November 1, 1995 - v1
Checksum:iA52EC629596EAC33
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049134256S → A.Corresponds to variant rs12324924dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X0HNMR-A1559-1657[»]
2RR8NMR-A26-210[»]
3FAYX-ray2.20A962-1345[»]
3I6XX-ray2.50A/B/C/D1-191[»]
5L0OX-ray2.36A/B/C/D1-191[»]
ProteinModelPortaliP46940.
SMRiP46940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114353. 261 interactors.
DIPiDIP-32597N.
IntActiP46940. 190 interactors.
MINTiMINT-4999354.
STRINGi9606.ENSP00000268182.

PTM databases

iPTMnetiP46940.
PhosphoSitePlusiP46940.
SwissPalmiP46940.

Polymorphism and mutation databases

BioMutaiIQGAP1.
DMDMi1170586.

Proteomic databases

EPDiP46940.
MaxQBiP46940.
PaxDbiP46940.
PeptideAtlasiP46940.
PRIDEiP46940.

Protocols and materials databases

DNASUi8826.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268182; ENSP00000268182; ENSG00000140575.
GeneIDi8826.
KEGGihsa:8826.
UCSCiuc002bpl.2. human.

Organism-specific databases

CTDi8826.
DisGeNETi8826.
GeneCardsiIQGAP1.
H-InvDBHIX0172824.
HGNCiHGNC:6110. IQGAP1.
HPAiCAB013302.
HPA014055.
MIMi603379. gene.
neXtProtiNX_P46940.
OpenTargetsiENSG00000140575.
PharmGKBiPA29910.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2128. Eukaryota.
COG5261. LUCA.
GeneTreeiENSGT00600000084379.
HOGENOMiHOG000004842.
HOVERGENiHBG052143.
InParanoidiP46940.
KOiK16848.
OMAiIPECGET.
OrthoDBiEOG091G00ET.
PhylomeDBiP46940.
TreeFamiTF313078.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140575-MONOMER.
ReactomeiR-HSA-373753. Nephrin interactions.
R-HSA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNORiP46940.

Miscellaneous databases

ChiTaRSiIQGAP1. human.
EvolutionaryTraceiP46940.
GeneWikiiIQGAP1.
GenomeRNAii8826.
PMAP-CutDBP46940.
PROiP46940.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140575.
CleanExiHS_IQGAP1.
ExpressionAtlasiP46940. baseline and differential.
GenevisibleiP46940. HS.

Family and domain databases

CDDicd00014. CH. 1 hit.
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.
IPR000593. RasGAP_C.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
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 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.