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O15085

- ARHGB_HUMAN

UniProt

O15085 - ARHGB_HUMAN

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Protein

Rho guanine nucleotide exchange factor 11

Gene

ARHGEF11

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

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. apoptotic signaling pathway Source: Reactome
  3. axon guidance Source: Reactome
  4. cellular component movement Source: UniProtKB
  5. cytokinesis Source: UniProtKB
  6. establishment of cell polarity Source: UniProtKB
  7. G-protein coupled receptor signaling pathway Source: UniProtKB
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. positive regulation of apoptotic process Source: Reactome
  10. positive regulation of Rho GTPase activity Source: GOC
  11. positive regulation of transcription, DNA-templated Source: UniProtKB
  12. regulation of cell growth Source: UniProtKB
  13. regulation of small GTPase mediated signal transduction Source: Reactome
  14. Rho protein signal transduction Source: UniProtKB
  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
Name:ARHGEF11
Synonyms:KIAA0380
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14580. ARHGEF11.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. intracellular Source: UniProtKB
  4. membrane Source: UniProtKB-KW
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 11PRO_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).
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

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).By similarity5 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. 14 interactions.
DIPiDIP-31622N.
IntActiO15085. 21 interactions.
MINTiMINT-1897198.
STRINGi9606.ENSP00000357177.

Structurei

Secondary structure

1
1522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 517Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 624Combined sources
Beta strandi64 – 663Combined sources
Beta strandi68 – 725Combined sources
Beta strandi74 – 763Combined sources
Turni77 – 826Combined sources
Beta strandi88 – 925Combined sources
Beta strandi98 – 1003Combined sources
Helixi102 – 1098Combined sources
Beta strandi111 – 12010Combined sources
Helixi307 – 3126Combined sources
Helixi314 – 3196Combined sources
Helixi321 – 33414Combined sources
Helixi338 – 34912Combined sources
Helixi356 – 36813Combined sources
Helixi381 – 39212Combined sources
Helixi398 – 42427Combined sources
Helixi428 – 4314Combined sources
Turni432 – 4343Combined sources
Helixi435 – 4384Combined sources
Helixi443 – 46220Combined sources
Helixi466 – 48217Combined sources
Turni716 – 7183Combined sources
Beta strandi719 – 7246Combined sources
Helixi725 – 7273Combined sources
Helixi730 – 75930Combined sources
Helixi761 – 7666Combined sources
Helixi772 – 7787Combined sources
Beta strandi779 – 7813Combined sources
Helixi782 – 80120Combined sources
Helixi810 – 8178Combined sources
Helixi819 – 83315Combined sources
Helixi836 – 84914Combined sources
Helixi851 – 86111Combined sources
Helixi864 – 8663Combined sources
Helixi871 – 8744Combined sources
Helixi877 – 89418Combined sources
Helixi901 – 93939Combined sources
Turni943 – 9453Combined sources
Turni951 – 9533Combined sources
Helixi954 – 9585Combined sources
Helixi961 – 9633Combined sources
Beta strandi966 – 9749Combined sources
Beta strandi977 – 9793Combined sources
Beta strandi983 – 99816Combined sources
Beta strandi1024 – 10274Combined sources
Helixi1028 – 10303Combined sources
Beta strandi1031 – 10355Combined sources
Beta strandi1040 – 10478Combined sources
Beta strandi1050 – 10523Combined sources
Beta strandi1056 – 10605Combined sources
Helixi1064 – 108017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 12680PDZPROSITE-ProRule annotationAdd
BLAST
Domaini306 – 486181RGSLPROSITE-ProRule annotationAdd
BLAST
Domaini734 – 923190DHPROSITE-ProRule annotationAdd
BLAST
Domaini965 – 1079115PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili444 – 47027Sequence AnalysisAdd
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 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

eggNOGiCOG5422.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034045.
HOVERGENiHBG101340.
InParanoidiO15085.
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

        10         20         30         40         50
MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQPSDASET TGLVQRCVII
60 70 80 90 100
QKDQHGFGFT VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS
110 120 130 140 150
SHLEVVKLIK SGAYVALTLL GSSPSSMGIS GLQQDPSPAG APRITSVIPS
160 170 180 190 200
PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ ILRNMLRQEE KELQDILPLY
210 220 230 240 250
GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR NSVLSDPGLD
260 270 280 290 300
SPRTSPVIMA RVAQHHRRQG SDAAVPSTGD QGVDQSPKPL IIGPEEDYDP
310 320 330 340 350
GYFNNESDII FQDLEKLKSR PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ
360 370 380 390 400
QASPKDSRSL GKDIWNIFLE KNAPLRVKIP EMLQAEIDSR LRNSEDARGV
410 420 430 440 450
LCEAQEAAMP EIQEQIHDYR TKRTLGLGSL YGENDLLDLD GDPLRERQVA
460 470 480 490 500
EKQLAALGDI LSKYEEDRSA PMDFALNTYM SHAGIRLREA RPSNTAEKAQ
510 520 530 540 550
SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI GKPKSSSQST
560 570 580 590 600
FHIPLSPVEV KPGNVRNIIQ HFENNQQYDA PEPGTQRLST GSFPEDLLES
610 620 630 640 650
DSSRSEIRLG RSESLKGREE MKRSRKAENV PRSRSDVDMD AAAEATRLHQ
660 670 680 690 700
SASSSTSSLS TRSLENPTPP FTPKMGRRSI ESPSLGFCTD TLLPHLLEDD
710 720 730 740 750
LGQLSDLEPE PDAQNWQHTV GKDVVAGLTQ REIDRQEVIN ELFVTEASHL
760 770 780 790 800
RTLRVLDLIF YQRMKKENLM PREELARLFP NLPELIEIHN SWCEAMKKLR
810 820 830 840 850
EEGPIIKEIS DLMLARFDGP AREELQQVAA QFCSYQSIAL ELIKTKQRKE
860 870 880 890 900
SRFQLFMQEA ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SIIKHTEGGT
910 920 930 940 950
SEHEKLCRAR DQCREILKYV NEAVKQTENR HRLEGYQKRL DATALERASN
960 970 980 990 1000
PLAAEFKSLD LTTRKMIHEG PLTWRISKDK TLDLHVLLLE DLLVLLQKQD
1010 1020 1030 1040 1050
EKLLLKCHSK TAVGSSDSKQ TFSPVLKLNA VLIRSVATDK RAFFIICTSK
1060 1070 1080 1090 1100
LGPPQIYELV ALTSSDKNTW MELLEEAVRN ATRHPGAAPM PVHPPPPGPR
1110 1120 1130 1140 1150
EPAQQGPTPS RVELDDSDVF HGEPEPEELP GGTGSQQRVQ GKHQVLLEDP
1160 1170 1180 1190 1200
EQEGSAEEEE LGVLPCPSTS LDGENRGIRT RNPIHLAFPG PLFMEGLADS
1210 1220 1230 1240 1250
ALEDVENLRH LILWSLLPGH TMETQAAQEP EDDLTPTPSV ISVTSHPWDP
1260 1270 1280 1290 1300
GSPGQAPPGG EGDNTQLAGL EGERPEQEDM GLCSLEHLPP RTRNSGIWES
1310 1320 1330 1340 1350
PELDRNLAED ASSTEAAGGY KVVRKAEVAG SKVVPALPES GQSEPGPPEV
1360 1370 1380 1390 1400
EGGTKATGNC FYVSMPSGPP DSSTDHSEAP MSPPQPDSLP AGQTEPQPQL
1410 1420 1430 1440 1450
QGGNDDPRRP SRSPPSLALR DVGMIFHTIE QLTLKLNRLK DMELAHRELL
1460 1470 1480 1490 1500
KSLGGESSGG TTPVGSFHTE AARWTDGSLS PPAKEPLASD SRNSHELGPC
1510 1520
PEDGSDAPLE DSTADAAASP GP
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. Curated

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. 1 PublicationVSP_042003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 14 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.
GeneTreei ENSGT00760000119193.
HOGENOMi HOG000034045.
HOVERGENi HBG101340.
InParanoidi O15085.
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

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: October 29, 2014
This is version 140 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