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O15085

- ARHGB_HUMAN

UniProt

O15085 - ARHGB_HUMAN

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
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. 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

    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-SubCell

    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 – 2451Phosphoserine3 Publications
    Modified residuei251 – 2511Phosphoserine3 Publications
    Modified residuei254 – 2541Phosphothreonine2 Publications
    Modified residuei663 – 6631Phosphoserine2 Publications
    Modified residuei668 – 6681Phosphothreonine4 Publications
    Modified residuei672 – 6721Phosphothreonine2 Publications
    Modified residuei1155 – 11551Phosphoserine2 Publications
    Modified residuei1300 – 13001Phosphoserine2 Publications
    Modified residuei1457 – 14571Phosphoserine2 Publications
    Modified residuei1458 – 14581Phosphoserine2 Publications
    Modified residuei1475 – 14751Phosphothreonine2 Publications
    Modified residuei1480 – 14801Phosphoserine2 Publications

    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

    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).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. 12 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 – 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.
    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.
    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. 1 PublicationVSP_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

    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 1, 2014
    This is version 139 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