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Protein

Rho guanine nucleotide exchange factor 11

Gene

Arhgef11

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

GTPase 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
Name:Arhgef11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619705. Arhgef11.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity

  • Note: Translocated to the membrane upon stimulation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15271527Rho guanine nucleotide exchange factor 11PRO_0000080929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301PhosphoserineCombined sources
Modified residuei51 – 511PhosphoserineCombined sources
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei268 – 2681PhosphoserineCombined sources
Modified residuei271 – 2711PhosphothreonineBy similarity
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei671 – 6711PhosphoserineBy similarity
Modified residuei676 – 6761PhosphothreonineCombined sources
Modified residuei680 – 6801PhosphothreonineCombined sources
Modified residuei1304 – 13041PhosphoserineBy similarity
Modified residuei1462 – 14621PhosphoserineCombined sources
Modified residuei1463 – 14631PhosphoserineCombined sources
Modified residuei1480 – 14801PhosphothreonineBy similarity
Modified residuei1485 – 14851PhosphoserineCombined sources

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.
PRIDEiQ9ES67.

PTM databases

PhosphoSiteiQ9ES67.
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

Protein-protein interaction databases

DIPiDIP-46242N.
MINTiMINT-270678.
STRINGi10116.ENSRNOP00000020717.

Structurei

Secondary structure

1
1527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi323 – 3297Combined sources
Helixi331 – 3355Combined sources
Helixi338 – 35114Combined sources
Helixi355 – 36713Combined sources
Turni371 – 3733Combined sources
Helixi375 – 38511Combined sources
Helixi398 – 40912Combined sources
Helixi415 – 44127Combined sources
Helixi445 – 4484Combined sources
Helixi450 – 4534Combined sources
Helixi460 – 47314Combined sources
Helixi475 – 4784Combined sources
Helixi483 – 50018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CX6X-ray2.50B307-508[»]
3CX7X-ray2.25B307-508[»]
3CX8X-ray2.00B307-508[»]
ProteinModelPortaliQ9ES67.
SMRiQ9ES67. Positions 61-137, 323-504, 722-1089.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ES67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 14380PDZPROSITE-ProRule annotationAdd
BLAST
Domaini323 – 503181RGSLPROSITE-ProRule annotationAdd
BLAST
Domaini742 – 931190DHPROSITE-ProRule annotationAdd
BLAST
Domaini973 – 1087115PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili461 – 48727Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 RGSL (RGS-like) domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3520. Eukaryota.
COG5422. LUCA.
HOGENOMiHOG000034045.
HOVERGENiHBG101340.
InParanoidiQ9ES67.
KOiK12331.
PhylomeDBiQ9ES67.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR032919. PDZ-RhoGEF.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR016137. RGS.
IPR015212. RGS-like_dom.
[Graphical view]
PANTHERiPTHR12673:SF111. PTHR12673:SF111. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CX6X-ray2.50B307-508[»]
3CX7X-ray2.25B307-508[»]
3CX8X-ray2.00B307-508[»]
ProteinModelPortaliQ9ES67.
SMRiQ9ES67. Positions 61-137, 323-504, 722-1089.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46242N.
MINTiMINT-270678.
STRINGi10116.ENSRNOP00000020717.

PTM databases

PhosphoSiteiQ9ES67.
SwissPalmiQ9ES67.

Proteomic databases

PaxDbiQ9ES67.
PRIDEiQ9ES67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi78966.
KEGGirno:78966.
UCSCiRGD:619705. rat.

Organism-specific databases

CTDi9826.
RGDi619705. Arhgef11.

Phylogenomic databases

eggNOGiKOG3520. Eukaryota.
COG5422. LUCA.
HOGENOMiHOG000034045.
HOVERGENiHBG101340.
InParanoidiQ9ES67.
KOiK12331.
PhylomeDBiQ9ES67.

Miscellaneous databases

EvolutionaryTraceiQ9ES67.
NextBioi614408.
PROiQ9ES67.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR032919. PDZ-RhoGEF.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR016137. RGS.
IPR015212. RGS-like_dom.
[Graphical view]
PANTHERiPTHR12673:SF111. PTHR12673:SF111. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Modulation of the neuronal glutamate transporter EAAT4 by two interacting proteins."
    Jackson M., Song W., Liu M.-Y., Jin L., Dykes-Hoberg M., Lin C.-L.G., Bowers W.J., Federoff H.J., Sternweis P.C., Rothstein J.D.
    Nature 410:89-93(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA; GNA13 AND SLC1A6.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-51; SER-268; SER-272; SER-288; THR-676; THR-680; SER-1462; SER-1463 AND SER-1485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARHGB_RAT
AccessioniPrimary (citable) accession number: Q9ES67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [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
  2. 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.