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O15085 (ARHGB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho guanine nucleotide exchange factor 11
Alternative name(s):
PDZ-RhoGEF
Gene names
Name:ARHGEF11
Synonyms:KIAA0380
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15

Subunit structure

Interacts with GNA12 and GNA13 through the RGS domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts with SLC1A6 By similarity. Interacts (via DH domain) with GCSAM (via C-terminus). Ref.5 Ref.6 Ref.7 Ref.8 Ref.13

Subcellular location

Cytoplasm. Membrane. Note: Translocated to the membrane upon stimulation. Ref.9

Tissue specificity

Ubiquitously expressed. Ref.6

Domain

The poly-Pro region is essential for plasma membrane localization upon stimulation.

Post-translational modification

Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14). Ref.15

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. Ref.15

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 PDZ (DHR) domain.

Contains 1 PH domain.

Contains 1 RGSL (RGS-like) domain.

Sequence caution

The sequence BAA20834.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionGTPase activation
Guanine-nucleotide releasing factor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.6. Source: UniProtKB

Rho protein signal transduction

Inferred from direct assay Ref.6. Source: UniProtKB

actin cytoskeleton organization

Non-traceable author statement Ref.6. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cellular component movement

Non-traceable author statement Ref.6. Source: UniProtKB

cytokinesis

Non-traceable author statement Ref.6. Source: UniProtKB

establishment of cell polarity

Non-traceable author statement Ref.6. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of Rho GTPase activity

Traceable author statement Ref.6. Source: GOC

regulation of cell growth

Non-traceable author statement Ref.6. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

striated muscle contraction

Non-traceable author statement Ref.6. Source: UniProtKB

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15755723. Source: MGI

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred by curator Ref.6. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled receptor binding

Inferred from direct assay PubMed 15755723. Source: MGI

GTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity

Traceable author statement Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22632972. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRKP461082EBI-311099,EBI-886
Daam1Q8BPM03EBI-6169263,EBI-772938From a different organism.
NCK1P163333EBI-311099,EBI-389883
RHOAP615866EBI-311099,EBI-446668
Z5115Q7DB744EBI-311099,EBI-7864788From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15085-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O15085-2)

The sequence of this isoform differs from the canonical sequence as follows:
     194-194: Q → QRICEVYSRNPASLLEEQIEGARRRVTQLQLKIQQETGGSV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15221522Rho guanine nucleotide exchange factor 11
PRO_0000080928

Regions

Domain47 – 12680PDZ
Domain306 – 486181RGSL
Domain734 – 923190DH
Domain965 – 1079115PH
Coiled coil444 – 47027 Potential
Compositional bias1094 – 10996Poly-Pro

Amino acid modifications

Modified residue2451Phosphoserine Ref.11 Ref.14
Modified residue2511Phosphoserine Ref.11 Ref.16
Modified residue2541Phosphothreonine Ref.11
Modified residue6631Phosphoserine Ref.10
Modified residue6681Phosphothreonine Ref.10 Ref.11 Ref.12
Modified residue6721Phosphothreonine Ref.11
Modified residue11551Phosphoserine Ref.11
Modified residue13001Phosphoserine Ref.11
Modified residue14571Phosphoserine Ref.11
Modified residue14581Phosphoserine Ref.11
Modified residue14751Phosphothreonine Ref.11
Modified residue14801Phosphoserine Ref.11

Natural variations

Alternative sequence1941Q → QRICEVYSRNPASLLEEQIE GARRRVTQLQLKIQQETGGS V in isoform 2.
VSP_042003
Natural variant14161S → G.
Corresponds to variant rs868188 [ dbSNP | Ensembl ].
VAR_061795
Natural variant14271H → R. Ref.3
Corresponds to variant rs945508 [ dbSNP | Ensembl ].
VAR_024285

Secondary structure

................................................................................................. 1522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: CA16E125B9F8A4AA

FASTA1,522167,704
        10         20         30         40         50         60 
MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQPSDASET TGLVQRCVII QKDQHGFGFT 

        70         80         90        100        110        120 
VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS SHLEVVKLIK SGAYVALTLL 

       130        140        150        160        170        180 
GSSPSSMGIS GLQQDPSPAG APRITSVIPS PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ 

       190        200        210        220        230        240 
ILRNMLRQEE KELQDILPLY GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR 

       250        260        270        280        290        300 
NSVLSDPGLD SPRTSPVIMA RVAQHHRRQG SDAAVPSTGD QGVDQSPKPL IIGPEEDYDP 

       310        320        330        340        350        360 
GYFNNESDII FQDLEKLKSR PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ QASPKDSRSL 

       370        380        390        400        410        420 
GKDIWNIFLE KNAPLRVKIP EMLQAEIDSR LRNSEDARGV LCEAQEAAMP EIQEQIHDYR 

       430        440        450        460        470        480 
TKRTLGLGSL YGENDLLDLD GDPLRERQVA EKQLAALGDI LSKYEEDRSA PMDFALNTYM 

       490        500        510        520        530        540 
SHAGIRLREA RPSNTAEKAQ SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI 

       550        560        570        580        590        600 
GKPKSSSQST FHIPLSPVEV KPGNVRNIIQ HFENNQQYDA PEPGTQRLST GSFPEDLLES 

       610        620        630        640        650        660 
DSSRSEIRLG RSESLKGREE MKRSRKAENV PRSRSDVDMD AAAEATRLHQ SASSSTSSLS 

       670        680        690        700        710        720 
TRSLENPTPP FTPKMGRRSI ESPSLGFCTD TLLPHLLEDD LGQLSDLEPE PDAQNWQHTV 

       730        740        750        760        770        780 
GKDVVAGLTQ REIDRQEVIN ELFVTEASHL RTLRVLDLIF YQRMKKENLM PREELARLFP 

       790        800        810        820        830        840 
NLPELIEIHN SWCEAMKKLR EEGPIIKEIS DLMLARFDGP AREELQQVAA QFCSYQSIAL 

       850        860        870        880        890        900 
ELIKTKQRKE SRFQLFMQEA ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SIIKHTEGGT 

       910        920        930        940        950        960 
SEHEKLCRAR DQCREILKYV NEAVKQTENR HRLEGYQKRL DATALERASN PLAAEFKSLD 

       970        980        990       1000       1010       1020 
LTTRKMIHEG PLTWRISKDK TLDLHVLLLE DLLVLLQKQD EKLLLKCHSK TAVGSSDSKQ 

      1030       1040       1050       1060       1070       1080 
TFSPVLKLNA VLIRSVATDK RAFFIICTSK LGPPQIYELV ALTSSDKNTW MELLEEAVRN 

      1090       1100       1110       1120       1130       1140 
ATRHPGAAPM PVHPPPPGPR EPAQQGPTPS RVELDDSDVF HGEPEPEELP GGTGSQQRVQ 

      1150       1160       1170       1180       1190       1200 
GKHQVLLEDP EQEGSAEEEE LGVLPCPSTS LDGENRGIRT RNPIHLAFPG PLFMEGLADS 

      1210       1220       1230       1240       1250       1260 
ALEDVENLRH LILWSLLPGH TMETQAAQEP EDDLTPTPSV ISVTSHPWDP GSPGQAPPGG 

      1270       1280       1290       1300       1310       1320 
EGDNTQLAGL EGERPEQEDM GLCSLEHLPP RTRNSGIWES PELDRNLAED ASSTEAAGGY 

      1330       1340       1350       1360       1370       1380 
KVVRKAEVAG SKVVPALPES GQSEPGPPEV EGGTKATGNC FYVSMPSGPP DSSTDHSEAP 

      1390       1400       1410       1420       1430       1440 
MSPPQPDSLP AGQTEPQPQL QGGNDDPRRP SRSPPSLALR DVGMIFHTIE QLTLKLNRLK 

      1450       1460       1470       1480       1490       1500 
DMELAHRELL KSLGGESSGG TTPVGSFHTE AARWTDGSLS PPAKEPLASD SRNSHELGPC 

      1510       1520 
PEDGSDAPLE DSTADAAASP GP 

« Hide

Isoform 2 [UniParc].

Checksum: B12857A4FE2BA0AC
Show »

FASTA1,562172,244

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-1427.
[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] (ISOFORM 2).
Tissue: Skin.
[5]"Rho-specific binding and guanine nucleotide exchange catalysis by KIAA0380, a dbl family member."
Ruemenapp U., Blomquist A., Schwoerer G., Schablowski H., Psoma A., Jakobs K.H.
FEBS Lett. 459:313-318(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHOA.
[6]"A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho."
Fukuhara S., Murga C., Zohar M., Igishi T., Gutkind J.S.
J. Biol. Chem. 274:5868-5879(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNA12 AND GNA13, TISSUE SPECIFICITY.
Tissue: Brain.
[7]"B plexins activate Rho through PDZ-RhoGEF."
Driessens M.H.E., Olivo C., Nagata K., Inagaki M., Collard J.G.
FEBS Lett. 529:168-172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
[8]"Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF."
Perrot V., Vazquez-Prado J., Gutkind J.S.
J. Biol. Chem. 277:43115-43120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
[9]"Functions of a rho-specific guanine nucleotide exchange factor in neurite retraction. Possible role of a proline-rich motif of KIAA0380 in localization."
Togashi H., Nagata K., Takagishi M., Saitoh N., Inagaki M.
J. Biol. Chem. 275:29570-29578(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"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-663 AND THR-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-245; SER-251; THR-254; THR-668; THR-672; SER-1155; SER-1300; SER-1457; SER-1458; THR-1475 AND SER-1480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"HGAL, a germinal center specific protein, decreases lymphoma cell motility by modulation of the RhoA signaling pathway."
Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A., Sanchez-Garcia I., Helfman D.M., Lossos I.S.
Blood 116:5217-5227(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCSAM.
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced neurite outgrowth."
Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.
J. Cell Biol. 193:985-994(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, PHOSPHORYLATION.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases."
Longenecker K.L., Lewis M.E., Chikumi H., Gutkind J.S., Derewenda Z.S.
Structure 9:559-569(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 281-490.
[18]"Solution structure of the PDZ domain of human Rho guanine nucleotide exchange factor 11."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 44-123.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002378 mRNA. Translation: BAA20834.2. Different initiation.
AL356104, AL157713 Genomic DNA. Translation: CAH72940.1.
AL157713, AL356104 Genomic DNA. Translation: CAH70127.1.
AL157713, AL356104 Genomic DNA. Translation: CAH70128.1.
AL356104, AL157713 Genomic DNA. Translation: CAH72939.1.
CH471121 Genomic DNA. Translation: EAW52893.1.
CH471121 Genomic DNA. Translation: EAW52894.1.
BC057394 mRNA. Translation: AAH57394.1.
CCDSCCDS1162.1. [O15085-1]
CCDS1163.1. [O15085-2]
RefSeqNP_055599.1. NM_014784.3. [O15085-1]
NP_937879.1. NM_198236.2. [O15085-2]
UniGeneHs.516954.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HTJX-ray2.20F281-490[»]
1XCGX-ray2.50A/E714-1081[»]
2DLSNMR-A44-123[»]
3KZ1X-ray2.70A/B710-1085[»]
3T06X-ray2.84A/E672-1081[»]
ProteinModelPortalO15085.
SMRO15085. Positions 37-120, 306-487, 714-1081.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115164. 12 interactions.
DIPDIP-31622N.
IntActO15085. 21 interactions.
MINTMINT-1897198.
STRING9606.ENSP00000357177.

PTM databases

PhosphoSiteO15085.

Proteomic databases

MaxQBO15085.
PaxDbO15085.
PRIDEO15085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361409; ENSP00000354644; ENSG00000132694. [O15085-1]
ENST00000368194; ENSP00000357177; ENSG00000132694. [O15085-2]
GeneID9826.
KEGGhsa:9826.
UCSCuc001fqn.3. human. [O15085-2]
uc001fqo.3. human. [O15085-1]

Organism-specific databases

CTD9826.
GeneCardsGC01M156904.
HGNCHGNC:14580. ARHGEF11.
HPAHPA011026.
HPA012037.
HPA014658.
MIM605708. gene.
neXtProtNX_O15085.
PharmGKBPA24968.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOGENOMHOG000034045.
HOVERGENHBG101340.
KOK12331.
OMATGNCFYV.
OrthoDBEOG7GJ6CF.
PhylomeDBO15085.
TreeFamTF106495.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO15085.
BgeeO15085.
CleanExHS_ARHGEF11.
GenevestigatorO15085.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000219. DH-domain.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERPTHR22825. PTHR22825. 1 hit.
PfamPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGEF11. human.
EvolutionaryTraceO15085.
GeneWikiARHGEF11.
GenomeRNAi9826.
NextBio37012.
PROO15085.
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Entry information

Entry nameARHGB_HUMAN
AccessionPrimary (citable) accession number: O15085
Secondary accession number(s): D3DVD0, Q5VY40, Q6PFW2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 137 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 1

Human chromosome 1: entries, gene names and cross-references to MIM