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Protein

Rho guanine nucleotide exchange factor 11

Gene

Arhgef11

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGTPase activation, Guanine-nucleotide releasing factor

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 11
Alternative name(s):
RhoGEF glutamate transport modulator GTRAP48
Gene namesi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619705 Arhgef11

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000809291 – 1527Rho guanine nucleotide exchange factor 11Add BLAST1527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei30PhosphoserineCombined sources1
Modified residuei32PhosphoserineBy similarity1
Modified residuei51PhosphoserineCombined sources1
Modified residuei262PhosphoserineBy similarity1
Modified residuei268PhosphoserineCombined sources1
Modified residuei271PhosphothreonineBy similarity1
Modified residuei272PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei643PhosphoserineBy similarity1
Modified residuei671PhosphoserineBy similarity1
Modified residuei676PhosphothreonineCombined sources1
Modified residuei680PhosphothreonineCombined sources1
Modified residuei1299PhosphoserineBy similarity1
Modified residuei1304PhosphoserineBy similarity1
Modified residuei1462PhosphoserineCombined sources1
Modified residuei1463PhosphoserineCombined sources1
Modified residuei1467PhosphothreonineBy similarity1
Modified residuei1480PhosphothreonineBy similarity1
Modified residuei1485PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14).By similarity
Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex when previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14), leading to its degradation, thereby restricting RhoA activity and facilitating growth cone spreading and neurite outgrowth.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9ES67
PeptideAtlasiQ9ES67
PRIDEiQ9ES67

PTM databases

iPTMnetiQ9ES67
PhosphoSitePlusiQ9ES67
SwissPalmiQ9ES67

Interactioni

Subunit structurei

Interacts with RHOA, GNA13 and SLC1A6. Interacts with GNA12, PLXNB1 and PLXNB2 (By similarity). Interacts (via DH domain) with GCSAM (via C-terminus) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Gna13P276013EBI-15735216,EBI-2255627From Mus musculus.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-46242N
IntActiQ9ES67, 1 interactor
STRINGi10116.ENSRNOP00000020717

Structurei

Secondary structure

11527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi323 – 329Combined sources7
Helixi331 – 335Combined sources5
Helixi338 – 351Combined sources14
Helixi355 – 367Combined sources13
Turni371 – 373Combined sources3
Helixi375 – 385Combined sources11
Helixi398 – 409Combined sources12
Helixi415 – 441Combined sources27
Helixi445 – 448Combined sources4
Helixi450 – 453Combined sources4
Helixi460 – 473Combined sources14
Helixi475 – 478Combined sources4
Helixi483 – 500Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CX6X-ray2.50B307-508[»]
3CX7X-ray2.25B307-508[»]
3CX8X-ray2.00B307-508[»]
ProteinModelPortaliQ9ES67
SMRiQ9ES67
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ES67

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 143PDZPROSITE-ProRule annotationAdd BLAST80
Domaini323 – 503RGSLPROSITE-ProRule annotationAdd BLAST181
Domaini742 – 931DHPROSITE-ProRule annotationAdd BLAST190
Domaini973 – 1087PHPROSITE-ProRule annotationAdd BLAST115

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili461 – 487Sequence analysisAdd BLAST27

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3520 Eukaryota
COG5422 LUCA
HOGENOMiHOG000034045
HOVERGENiHBG101340
InParanoidiQ9ES67
KOiK12331
PhylomeDBiQ9ES67

Family and domain databases

CDDicd13391 PH_PRG, 1 hit
cd08753 RGS_PDZRhoGEF, 1 hit
cd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR001331 GDS_CDC24_CS
IPR001478 PDZ
IPR032919 PDZ-RhoGEF
IPR036034 PDZ_sf
IPR037889 PDZRhoGEF_RGS
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR037803 PRG_PH
IPR016137 RGS
IPR015212 RGS-like_dom
IPR036305 RGS_sf
PANTHERiPTHR12673:SF111 PTHR12673:SF111, 1 hit
PfamiView protein in Pfam
PF00595 PDZ, 1 hit
PF09128 RGS-like, 1 hit
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SM00233 PH, 1 hit
SM00315 RGS, 1 hit
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
SSF48097 SSF48097, 1 hit
SSF50156 SSF50156, 1 hit
PROSITEiView protein in PROSITE
PS00741 DH_1, 1 hit
PS50010 DH_2, 1 hit
PS50106 PDZ, 1 hit
PS50003 PH_DOMAIN, 1 hit
PS50132 RGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q9ES67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIRLPHSID RSASKKQSHL SSPIASWLSS LSSLGDSTPE RTSPSHHRQP
60 70 80 90 100
SDTSETTAGL VQRCVIIQKD QHGFGFTVSG DRIVLVQSVR PGGAAMKAGV
110 120 130 140 150
KEGDRIIKVN GTMVTNSSHL EVVKLIKSGA YAALTLLGSS PPSVGVSGLQ
160 170 180 190 200
QNPSVAGVLR VNPIIPPPPP PPPLPPPQHI TGPKPLQDPE VQKHATQILW
210 220 230 240 250
NMLRQEEEEL QDILPPCGET SQRTCEGRLS VDSQEADSGL DSGTERFPSI
260 270 280 290 300
SESLMNRNSV LSDPGLDSPQ TSPVILARVA QHHRRQGSDA ALLPLNHQGI
310 320 330 340 350
DQSPKPLIIG PEEDYDPGYF NNESDIIFQD LEKLKSHPAY LVVFLRYILS
360 370 380 390 400
QADPGPLLFY LCSEVYQQTN PKDSRSLGKD IWNIFLEKNA PLRVKIPEML
410 420 430 440 450
QAEIDLRLRN NEDPRNVLCE AQEAVMLEIQ EQINDYRSKR TLGLGSLYGE
460 470 480 490 500
NDLLGLDGDP LRERQMAEKQ LAALGDILSK YEEDRSAPMD FAVNTFMSHA
510 520 530 540 550
GIRLRESRSS CTAEKTQSAP DKDKWLPFFP KTKKQSSNSK KEKDALEDKK
560 570 580 590 600
RNPILRYIGK PKSSSQSIKP GNVRNIIQHF ENSHQYDVPE PGTQRLSTGS
610 620 630 640 650
FPEDLLESDS SRSEIRLGRS GSLKGREEMK RSRKAENVPR PRSDVDMDAA
660 670 680 690 700
AEAARLHQSA SSSASSLSTR SLENPTPPFT PKMGRRSIES PNLGFCTDVI
710 720 730 740 750
LPHLLEDDLG QLSDLEPEPE VQNWQHTVGK DVVANLTQRE IDRQEVINEL
760 770 780 790 800
FVTEASHLRT LRVLDLIFYQ RMRKENLMPR EELARLFPNL PELIEIHNSW
810 820 830 840 850
CEAMKKLREE GPIIRDISDP MLARFDGPAR EELQQVAAQF CSYQSVALEL
860 870 880 890 900
IRTKQRKESR FQLFMQEAES HPQCRRLQLR DLIVSEMQRL TKYPLLLENI
910 920 930 940 950
IKHTEGGTSE HEKLCRARDQ CREILKFVNE AVKQTENRHR LEGYQKRLDA
960 970 980 990 1000
TALERASNPL AAEFKSLDLT TRKMIHEGPL TWRISKDKTL DLQVLLLEDL
1010 1020 1030 1040 1050
VVLLQRQEER LLLKCHSKTA VGSSDSKQTF SPVLKLNAVL IRSVATDKRA
1060 1070 1080 1090 1100
FFIICTSELG PPQIYELVAL TSSDKNIWME LLEEAVQNAT KHPGAAPIPI
1110 1120 1130 1140 1150
HPSPPGSQEP AYQGSTSSRV EINDSEVYHT EKEPKKLPEG PGPEQRVQDK
1160 1170 1180 1190 1200
QLIAQGEPVQ EEDEEELRTL PRAPPSLDGE NRGIRTRDPV LLALTGPLLM
1210 1220 1230 1240 1250
EGLADAALED VENLRHLILW SLLPGHTVKT QAAGEPEDDL TPTPSVVSIT
1260 1270 1280 1290 1300
SHPWDPGSPG QAPTISDSTR LARPEGSQPE GEDVAVSSLA HLPPRTRSSG
1310 1320 1330 1340 1350
VWDSPELDRN PAAEAASTEP AASYKVVRKV SLLPGGGVGA AKVAGSNAIP
1360 1370 1380 1390 1400
DSGQSESELS EVEGGAQATG NCFYVSMPAG PLDSSTEPTG TPPSPSQCHS
1410 1420 1430 1440 1450
LPAWPTEPQP YRGVRGGQCS SLVRRDVDVI FHTIEQLTIK LHRLKDMELA
1460 1470 1480 1490 1500
HRELLKSLGG ESSGGTTPVG SFHTEAARWT DYSLSPPAKE ALASDSQNGQ
1510 1520
EQGSCPEEGS DIALEDSATD TAVSPGP
Length:1,527
Mass (Da):168,534
Last modified:March 1, 2001 - v1
Checksum:iABAEA20F541A3A9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225961 mRNA Translation: AAG28597.1
RefSeqiNP_076472.1, NM_023982.1
UniGeneiRn.229365

Genome annotation databases

GeneIDi78966
KEGGirno:78966
UCSCiRGD:619705 rat

Similar proteinsi

Entry informationi

Entry nameiARHGB_RAT
AccessioniPrimary (citable) accession number: Q9ES67
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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