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O15085

- ARHGB_HUMAN

UniProt

O15085 - ARHGB_HUMAN

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Protein
Rho guanine nucleotide exchange factor 11
Gene
ARHGEF11, KIAA0380
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

GO - Molecular functioni

  1. G-protein coupled receptor binding Source: MGI
  2. GTPase activator activity Source: UniProtKB-KW
  3. Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: UniProtKB
  2. Rho protein signal transduction Source: UniProtKB
  3. actin cytoskeleton organization Source: UniProtKB
  4. apoptotic signaling pathway Source: Reactome
  5. axon guidance Source: Reactome
  6. cellular component movement Source: UniProtKB
  7. cytokinesis Source: UniProtKB
  8. establishment of cell polarity Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. positive regulation of apoptotic process Source: Reactome
  11. positive regulation of transcription, DNA-templated Source: UniProtKB
  12. regulation of Rho GTPase activity Source: GOC
  13. regulation of cell growth Source: UniProtKB
  14. regulation of small GTPase mediated signal transduction Source: Reactome
  15. small GTPase mediated signal transduction Source: Reactome
  16. striated muscle contraction Source: UniProtKB
  17. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 11
Alternative name(s):
PDZ-RhoGEF
Gene namesi
Synonyms:KIAA0380
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14580. ARHGEF11.

Subcellular locationi

Cytoplasm. Membrane
Note: Translocated to the membrane upon stimulation.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. intracellular Source: UniProtKB
  4. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15221522Rho guanine nucleotide exchange factor 11
PRO_0000080928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451Phosphoserine2 Publications
Modified residuei251 – 2511Phosphoserine2 Publications
Modified residuei254 – 2541Phosphothreonine1 Publication
Modified residuei663 – 6631Phosphoserine1 Publication
Modified residuei668 – 6681Phosphothreonine3 Publications
Modified residuei672 – 6721Phosphothreonine1 Publication
Modified residuei1155 – 11551Phosphoserine1 Publication
Modified residuei1300 – 13001Phosphoserine1 Publication
Modified residuei1457 – 14571Phosphoserine1 Publication
Modified residuei1458 – 14581Phosphoserine1 Publication
Modified residuei1475 – 14751Phosphothreonine1 Publication
Modified residuei1480 – 14801Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14).1 Publication
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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15085.
PaxDbiO15085.
PRIDEiO15085.

PTM databases

PhosphoSiteiO15085.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ArrayExpressiO15085.
BgeeiO15085.
CleanExiHS_ARHGEF11.
GenevestigatoriO15085.

Organism-specific databases

HPAiHPA011026.
HPA012037.
HPA014658.

Interactioni

Subunit structurei

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi115164. 12 interactions.
DIPiDIP-31622N.
IntActiO15085. 21 interactions.
MINTiMINT-1897198.
STRINGi9606.ENSP00000357177.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 517
Beta strandi53 – 564
Beta strandi59 – 624
Beta strandi64 – 663
Beta strandi68 – 725
Beta strandi74 – 763
Turni77 – 826
Beta strandi88 – 925
Beta strandi98 – 1003
Helixi102 – 1098
Beta strandi111 – 12010
Helixi307 – 3126
Helixi314 – 3196
Helixi321 – 33414
Helixi338 – 34912
Helixi356 – 36813
Helixi381 – 39212
Helixi398 – 42427
Helixi428 – 4314
Turni432 – 4343
Helixi435 – 4384
Helixi443 – 46220
Helixi466 – 48217
Turni716 – 7183
Beta strandi719 – 7246
Helixi725 – 7273
Helixi730 – 75930
Helixi761 – 7666
Helixi772 – 7787
Beta strandi779 – 7813
Helixi782 – 80120
Helixi810 – 8178
Helixi819 – 83315
Helixi836 – 84914
Helixi851 – 86111
Helixi864 – 8663
Helixi871 – 8744
Helixi877 – 89418
Helixi901 – 93939
Turni943 – 9453
Turni951 – 9533
Helixi954 – 9585
Helixi961 – 9633
Beta strandi966 – 9749
Beta strandi977 – 9793
Beta strandi983 – 99816
Beta strandi1024 – 10274
Helixi1028 – 10303
Beta strandi1031 – 10355
Beta strandi1040 – 10478
Beta strandi1050 – 10523
Beta strandi1056 – 10605
Helixi1064 – 108017

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO15085.
SMRiO15085. Positions 37-120, 306-487, 714-1081.

Miscellaneous databases

EvolutionaryTraceiO15085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 12680PDZ
Add
BLAST
Domaini306 – 486181RGSL
Add
BLAST
Domaini734 – 923190DH
Add
BLAST
Domaini965 – 1079115PH
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili444 – 47027 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1094 – 10996Poly-Pro

Domaini

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

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.
Contains 1 PH domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5422.
HOGENOMiHOG000034045.
HOVERGENiHBG101340.
KOiK12331.
OMAiTGNCFYV.
OrthoDBiEOG7GJ6CF.
PhylomeDBiO15085.
TreeFamiTF106495.

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.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
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.
PROSITEiPS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15085-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQPSDASET TGLVQRCVII     50
QKDQHGFGFT VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS 100
SHLEVVKLIK SGAYVALTLL GSSPSSMGIS GLQQDPSPAG APRITSVIPS 150
PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ ILRNMLRQEE KELQDILPLY 200
GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR NSVLSDPGLD 250
SPRTSPVIMA RVAQHHRRQG SDAAVPSTGD QGVDQSPKPL IIGPEEDYDP 300
GYFNNESDII FQDLEKLKSR PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ 350
QASPKDSRSL GKDIWNIFLE KNAPLRVKIP EMLQAEIDSR LRNSEDARGV 400
LCEAQEAAMP EIQEQIHDYR TKRTLGLGSL YGENDLLDLD GDPLRERQVA 450
EKQLAALGDI LSKYEEDRSA PMDFALNTYM SHAGIRLREA RPSNTAEKAQ 500
SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI GKPKSSSQST 550
FHIPLSPVEV KPGNVRNIIQ HFENNQQYDA PEPGTQRLST GSFPEDLLES 600
DSSRSEIRLG RSESLKGREE MKRSRKAENV PRSRSDVDMD AAAEATRLHQ 650
SASSSTSSLS TRSLENPTPP FTPKMGRRSI ESPSLGFCTD TLLPHLLEDD 700
LGQLSDLEPE PDAQNWQHTV GKDVVAGLTQ REIDRQEVIN ELFVTEASHL 750
RTLRVLDLIF YQRMKKENLM PREELARLFP NLPELIEIHN SWCEAMKKLR 800
EEGPIIKEIS DLMLARFDGP AREELQQVAA QFCSYQSIAL ELIKTKQRKE 850
SRFQLFMQEA ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SIIKHTEGGT 900
SEHEKLCRAR DQCREILKYV NEAVKQTENR HRLEGYQKRL DATALERASN 950
PLAAEFKSLD LTTRKMIHEG PLTWRISKDK TLDLHVLLLE DLLVLLQKQD 1000
EKLLLKCHSK TAVGSSDSKQ TFSPVLKLNA VLIRSVATDK RAFFIICTSK 1050
LGPPQIYELV ALTSSDKNTW MELLEEAVRN ATRHPGAAPM PVHPPPPGPR 1100
EPAQQGPTPS RVELDDSDVF HGEPEPEELP GGTGSQQRVQ GKHQVLLEDP 1150
EQEGSAEEEE LGVLPCPSTS LDGENRGIRT RNPIHLAFPG PLFMEGLADS 1200
ALEDVENLRH LILWSLLPGH TMETQAAQEP EDDLTPTPSV ISVTSHPWDP 1250
GSPGQAPPGG EGDNTQLAGL EGERPEQEDM GLCSLEHLPP RTRNSGIWES 1300
PELDRNLAED ASSTEAAGGY KVVRKAEVAG SKVVPALPES GQSEPGPPEV 1350
EGGTKATGNC FYVSMPSGPP DSSTDHSEAP MSPPQPDSLP AGQTEPQPQL 1400
QGGNDDPRRP SRSPPSLALR DVGMIFHTIE QLTLKLNRLK DMELAHRELL 1450
KSLGGESSGG TTPVGSFHTE AARWTDGSLS PPAKEPLASD SRNSHELGPC 1500
PEDGSDAPLE DSTADAAASP GP 1522
Length:1,522
Mass (Da):167,704
Last modified:January 1, 1998 - v1
Checksum:iCA16E125B9F8A4AA
GO
Isoform 2 (identifier: O15085-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-194: Q → QRICEVYSRNPASLLEEQIEGARRRVTQLQLKIQQETGGSV

Note: No experimental confirmation available.

Show »
Length:1,562
Mass (Da):172,244
Checksum:iB12857A4FE2BA0AC
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1416 – 14161S → G.
Corresponds to variant rs868188 [ dbSNP | Ensembl ].
VAR_061795
Natural varianti1427 – 14271H → R.1 Publication
Corresponds to variant rs945508 [ dbSNP | Ensembl ].
VAR_024285

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei194 – 1941Q → QRICEVYSRNPASLLEEQIE GARRRVTQLQLKIQQETGGS V in isoform 2.
VSP_042003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1162.1. [O15085-1]
CCDS1163.1. [O15085-2]
RefSeqiNP_055599.1. NM_014784.3. [O15085-1]
NP_937879.1. NM_198236.2. [O15085-2]
UniGeneiHs.516954.

Genome annotation databases

EnsembliENST00000361409; ENSP00000354644; ENSG00000132694. [O15085-1]
ENST00000368194; ENSP00000357177; ENSG00000132694. [O15085-2]
GeneIDi9826.
KEGGihsa:9826.
UCSCiuc001fqn.3. human. [O15085-2]
uc001fqo.3. human. [O15085-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1162.1. [O15085-1 ]
CCDS1163.1. [O15085-2 ]
RefSeqi NP_055599.1. NM_014784.3. [O15085-1 ]
NP_937879.1. NM_198236.2. [O15085-2 ]
UniGenei Hs.516954.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HTJ X-ray 2.20 F 281-490 [» ]
1XCG X-ray 2.50 A/E 714-1081 [» ]
2DLS NMR - A 44-123 [» ]
3KZ1 X-ray 2.70 A/B 710-1085 [» ]
3T06 X-ray 2.84 A/E 672-1081 [» ]
ProteinModelPortali O15085.
SMRi O15085. Positions 37-120, 306-487, 714-1081.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115164. 12 interactions.
DIPi DIP-31622N.
IntActi O15085. 21 interactions.
MINTi MINT-1897198.
STRINGi 9606.ENSP00000357177.

PTM databases

PhosphoSitei O15085.

Proteomic databases

MaxQBi O15085.
PaxDbi O15085.
PRIDEi O15085.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361409 ; ENSP00000354644 ; ENSG00000132694 . [O15085-1 ]
ENST00000368194 ; ENSP00000357177 ; ENSG00000132694 . [O15085-2 ]
GeneIDi 9826.
KEGGi hsa:9826.
UCSCi uc001fqn.3. human. [O15085-2 ]
uc001fqo.3. human. [O15085-1 ]

Organism-specific databases

CTDi 9826.
GeneCardsi GC01M156904.
HGNCi HGNC:14580. ARHGEF11.
HPAi HPA011026.
HPA012037.
HPA014658.
MIMi 605708. gene.
neXtProti NX_O15085.
PharmGKBi PA24968.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5422.
HOGENOMi HOG000034045.
HOVERGENi HBG101340.
KOi K12331.
OMAi TGNCFYV.
OrthoDBi EOG7GJ6CF.
PhylomeDBi O15085.
TreeFami TF106495.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSi ARHGEF11. human.
EvolutionaryTracei O15085.
GeneWikii ARHGEF11.
GenomeRNAii 9826.
NextBioi 37012.
PROi O15085.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15085.
Bgeei O15085.
CleanExi HS_ARHGEF11.
Genevestigatori O15085.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR000219. DH-domain.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view ]
PANTHERi PTHR22825. PTHR22825. 1 hit.
Pfami PF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiARHGB_HUMAN
AccessioniPrimary (citable) accession number: O15085
Secondary accession number(s): D3DVD0, Q5VY40, Q6PFW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 138 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3

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