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Q14155

- ARHG7_HUMAN

UniProt

Q14155 - ARHG7_HUMAN

Protein

Rho guanine nucleotide exchange factor 7

Gene

ARHGEF7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions By similarity. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.By similarity3 Publications

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: BHF-UCL
    4. Rho guanyl-nucleotide exchange factor activity Source: InterPro

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. epidermal growth factor receptor signaling pathway Source: Reactome
    3. lamellipodium assembly Source: UniProtKB
    4. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    5. nervous system development Source: UniProtKB-KW
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. positive regulation of apoptotic process Source: UniProtKB
    8. positive regulation of GTPase activity Source: BHF-UCL
    9. regulation of small GTPase mediated signal transduction Source: Reactome
    10. signal transduction Source: ProtInc
    11. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_12484. EGFR downregulation.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinkiQ14155.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho guanine nucleotide exchange factor 7
    Alternative name(s):
    Beta-Pix
    COOL-1
    PAK-interacting exchange factor beta
    p85
    Gene namesi
    Name:ARHGEF7
    Synonyms:COOL1, KIAA0142, P85SPR, PAK3BP, PIXB
    ORF Names:Nbla10314
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:15607. ARHGEF7.

    Subcellular locationi

    Cell junctionfocal adhesion By similarity. Cell projectionruffle By similarity. Cytoplasmcell cortex By similarity. Cell projectionlamellipodium By similarity
    Note: Detected at cell adhesions. A small proportion is detected at focal adhesions.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. focal adhesion Source: UniProtKB-SubCell
    4. lamellipodium Source: UniProtKB
    5. neuronal cell body Source: BHF-UCL
    6. neuron projection Source: BHF-UCL
    7. protein complex Source: UniProtKB
    8. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24977.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 803803Rho guanine nucleotide exchange factor 7PRO_0000080921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761PhosphoserineBy similarity
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei694 – 6941Phosphoserine; by CaMK13 Publications

    Post-translational modificationi

    Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 By similarity. Phosphorylated on Ser-694 by CaMK1; enhancement of GEF activity and downstream activation of RAC1.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14155.
    PaxDbiQ14155.
    PRIDEiQ14155.

    PTM databases

    PhosphoSiteiQ14155.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14155.
    BgeeiQ14155.
    GenevestigatoriQ14155.

    Organism-specific databases

    HPAiHPA004744.

    Interactioni

    Subunit structurei

    Interacts with PAK kinases through the SH3 domain. Interacts with GIT1 and TGFB1I1. Interacts with PTK2/FAK1 and RAC1. Interacts with ITCH and PARVB By similarity. Interacts with unphosphorylated PAK1. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2. Isoform 1 and isoform 5 interact with SNX27.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBLP226819EBI-717515,EBI-518228
    GIT1Q9Y2X74EBI-717515,EBI-466061
    LRRK2Q5S0076EBI-717515,EBI-5323863
    NAA10P412273EBI-717515,EBI-747693
    PAK1Q131537EBI-717515,EBI-1307
    PAK2Q131774EBI-717515,EBI-1045887
    RAC1P630008EBI-717515,EBI-413628
    SCRIBQ141604EBI-717515,EBI-357345
    SH2D1AO608806EBI-717515,EBI-6983382

    Protein-protein interaction databases

    BioGridi114393. 24 interactions.
    IntActiQ14155. 19 interactions.
    MINTiMINT-92779.

    Structurei

    Secondary structure

    1
    803
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Helixi27 – 359
    Helixi39 – 4810
    Helixi63 – 7917
    Helixi109 – 1135
    Helixi118 – 13518
    Beta strandi188 – 1914
    Beta strandi210 – 2156
    Beta strandi218 – 2269
    Beta strandi229 – 24012
    Helixi271 – 30131
    Turni302 – 3043
    Beta strandi305 – 3106
    Helixi311 – 3133
    Helixi316 – 33823
    Helixi346 – 37833
    Turni379 – 3813
    Helixi382 – 3854
    Turni386 – 3894
    Turni395 – 3973
    Helixi398 – 4025
    Turni406 – 4083
    Helixi409 – 4113
    Helixi413 – 42210
    Beta strandi428 – 4303
    Helixi432 – 45322
    Turni454 – 4563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BY1NMR-A260-467[»]
    1ZSGNMR-A179-243[»]
    2L3GNMR-A1-137[»]
    ProteinModelPortaliQ14155.
    SMRiQ14155. Positions 1-137, 151-578.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14155.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 132132CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 24360SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 451181DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini473 – 578106PHPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG314429.
    HOVERGENiHBG050569.
    InParanoidiQ14155.
    KOiK13710.
    OMAiHHEPARL.
    OrthoDBiEOG708W04.
    PhylomeDBiQ14155.
    TreeFamiTF316105.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR000219. DH-domain.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00033. CH. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50021. CH. 1 hit.
    PS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: Q14155-4) [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

    MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP    50
    GTIEKVYPEP RSESECLSNI REFLRGCGAS LRLELLFPPS QPPQHLVTTI 100
    LLSASTFDAN DLYQGQNFNK VLSSLVTLNK VTADIGLGSD SVCARPSSHR 150
    IKSFDSLGSQ SLHTRTSKLF QGQYRSLDMT DNSNNQLVVR AKFNFQQTNE 200
    DELSFSKGDV IHVTRVEEGG WWEGTLNGRT GWFPSNYVRE VKASEKPVSP 250
    KSGTLKSPPK GFDTTAINKS YYNVVLQNIL ETENEYSKEL QTVLSTYLRP 300
    LQTSEKLSSA NISYLMGNLE EICSFQQMLV QSLEECTKLP EAQQRVGGCF 350
    LNLMPQMKTL YLTYCANHPS AVNVLTEHSE ELGEFMETKG ASSPGILVLT 400
    TGLSKPFMRL DKYPTLLKEL ERHMEDYHTD RQDIQKSMAA FKNLSAQCQE 450
    VRKRKELELQ ILTEAIRNWE GDDIKTLGNV TYMSQVLIQC AGSEEKNERY 500
    LLLFPNVLLM LSASPRMSGF IYQGKLPTTG MTITKLEDSE NHRNAFEISG 550
    SMIERILVSC NNQQDLQEWV EHLQKQTKVT SVGNPTIKPH SVPSHTLPSH 600
    PVTPSSKHAD SKPAPLTPAY HTLPHPSHHG TPHTTINWGP LEPPKTPKPW 650
    SLSCLRPAPP LRPSAALCYK EDLSKSPKTM KKLLPKRKPE RKPSDEEFAS 700
    RKSTAALEED AQILKVIEAY CTSAKTRQTL NSTWQGTDLM HNHVLADDDQ 750
    PSLDSLGRRS SLSRLEPSDL SEDSDYDSIW TAHSYRMGST SRKSCCSYIS 800
    HQN 803
    Length:803
    Mass (Da):90,012
    Last modified:July 19, 2004 - v2
    Checksum:i613EBA839E6FDBFD
    GO
    Isoform 1 (identifier: Q14155-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-178: Missing.
         733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL

    Note: Contains a phosphoserine at position 560. Contains a phosphoserine at position 579.

    Show »
    Length:646
    Mass (Da):73,140
    Checksum:iB5B5A83F0EBC28D2
    GO
    Isoform 2 (identifier: Q14155-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         56-105: Missing.

    Show »
    Length:753
    Mass (Da):84,477
    Checksum:i04178E64ACF43846
    GO
    Isoform 3 (identifier: Q14155-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-105: Missing.

    Show »
    Length:782
    Mass (Da):87,770
    Checksum:i9C602026D90A6D01
    GO
    Isoform 5 (identifier: Q14155-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-177: Missing.
         733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL

    Note: Contains a phosphoserine at position 645. Contains a phosphoserine at position 664.

    Show »
    Length:731
    Mass (Da):82,571
    Checksum:iE82D55E6187DADB2
    GO
    Isoform 6 (identifier: Q14155-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-178: Missing.

    Show »
    Length:625
    Mass (Da):70,450
    Checksum:i25DAD75DD4B0AC2E
    GO

    Sequence cautioni

    The sequence AAH50521.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA09763.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAD38906.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 554TIEK → EEKR in BAD66827. (PubMed:15491607)Curated
    Sequence conflicti343 – 3431Q → K in AAH33905. (PubMed:15489334)Curated
    Sequence conflicti552 – 5521M → V in AAH33905. (PubMed:15489334)Curated
    Sequence conflicti595 – 5951H → D in BAD66827. (PubMed:15491607)Curated
    Sequence conflicti636 – 6361I → T in AAH50521. (PubMed:15489334)Curated
    Sequence conflicti740 – 7401M → L in AAH33905. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti790 – 7901T → A Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
    VAR_064694

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 178178Missing in isoform 1 and isoform 6. 3 PublicationsVSP_011032Add
    BLAST
    Alternative sequencei56 – 10550Missing in isoform 2. 1 PublicationVSP_011033Add
    BLAST
    Alternative sequencei85 – 17793Missing in isoform 5. 1 PublicationVSP_034639Add
    BLAST
    Alternative sequencei85 – 10521Missing in isoform 3. 1 PublicationVSP_011034Add
    BLAST
    Alternative sequencei733 – 80371TWQGT…ISHQN → SSRKESAPQVLLPEEEKIIV EETKSNGQTVIEEKSLVDTV YALKDEVQELRQDNKKMKKS LEEEQRARKDLEKLVRKVLK NMNDPAWDETNL in isoform 1 and isoform 5. 4 PublicationsVSP_011035Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63476 mRNA. Translation: BAA09763.2. Different initiation.
    AL834228 mRNA. Translation: CAD38906.1. Different initiation.
    AL390754, AL139086 Genomic DNA. Translation: CAI12461.1.
    AL139086, AL390754 Genomic DNA. Translation: CAI14671.1.
    AL390754, AL139086 Genomic DNA. Translation: CAM13628.1.
    AL139086, AL390754 Genomic DNA. Translation: CAM20788.1.
    CH471085 Genomic DNA. Translation: EAX09143.1.
    BC033905 mRNA. Translation: AAH33905.1.
    BC050521 mRNA. Translation: AAH50521.1. Different initiation.
    BC060776 mRNA. Translation: AAH60776.1.
    AB177849 mRNA. Translation: BAD66827.1.
    AB075521 mRNA. Translation: BAE45764.1.
    CCDSiCCDS32009.1. [Q14155-3]
    CCDS45068.1. [Q14155-4]
    CCDS45069.1. [Q14155-2]
    CCDS9521.1. [Q14155-1]
    RefSeqiNP_001106983.1. NM_001113511.1. [Q14155-4]
    NP_001106984.1. NM_001113512.1. [Q14155-2]
    NP_001106985.1. NM_001113513.1. [Q14155-1]
    NP_003890.1. NM_003899.3. [Q14155-1]
    NP_663788.1. NM_145735.2. [Q14155-3]
    XP_005254147.1. XM_005254090.1. [Q14155-5]
    XP_005254152.1. XM_005254095.1. [Q14155-1]
    UniGeneiHs.508738.

    Genome annotation databases

    EnsembliENST00000317133; ENSP00000325994; ENSG00000102606. [Q14155-3]
    ENST00000375723; ENSP00000364875; ENSG00000102606. [Q14155-6]
    ENST00000375736; ENSP00000364888; ENSG00000102606. [Q14155-1]
    ENST00000375739; ENSP00000364891; ENSG00000102606. [Q14155-2]
    ENST00000375741; ENSP00000364893; ENSG00000102606. [Q14155-4]
    ENST00000426073; ENSP00000397068; ENSG00000102606. [Q14155-1]
    GeneIDi8874.
    KEGGihsa:8874.
    UCSCiuc001vrr.2. human. [Q14155-3]
    uc001vrs.2. human. [Q14155-4]
    uc001vrt.2. human. [Q14155-2]
    uc001vrv.4. human. [Q14155-1]

    Polymorphism databases

    DMDMi50403776.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63476 mRNA. Translation: BAA09763.2 . Different initiation.
    AL834228 mRNA. Translation: CAD38906.1 . Different initiation.
    AL390754 , AL139086 Genomic DNA. Translation: CAI12461.1 .
    AL139086 , AL390754 Genomic DNA. Translation: CAI14671.1 .
    AL390754 , AL139086 Genomic DNA. Translation: CAM13628.1 .
    AL139086 , AL390754 Genomic DNA. Translation: CAM20788.1 .
    CH471085 Genomic DNA. Translation: EAX09143.1 .
    BC033905 mRNA. Translation: AAH33905.1 .
    BC050521 mRNA. Translation: AAH50521.1 . Different initiation.
    BC060776 mRNA. Translation: AAH60776.1 .
    AB177849 mRNA. Translation: BAD66827.1 .
    AB075521 mRNA. Translation: BAE45764.1 .
    CCDSi CCDS32009.1. [Q14155-3 ]
    CCDS45068.1. [Q14155-4 ]
    CCDS45069.1. [Q14155-2 ]
    CCDS9521.1. [Q14155-1 ]
    RefSeqi NP_001106983.1. NM_001113511.1. [Q14155-4 ]
    NP_001106984.1. NM_001113512.1. [Q14155-2 ]
    NP_001106985.1. NM_001113513.1. [Q14155-1 ]
    NP_003890.1. NM_003899.3. [Q14155-1 ]
    NP_663788.1. NM_145735.2. [Q14155-3 ]
    XP_005254147.1. XM_005254090.1. [Q14155-5 ]
    XP_005254152.1. XM_005254095.1. [Q14155-1 ]
    UniGenei Hs.508738.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BY1 NMR - A 260-467 [» ]
    1ZSG NMR - A 179-243 [» ]
    2L3G NMR - A 1-137 [» ]
    ProteinModelPortali Q14155.
    SMRi Q14155. Positions 1-137, 151-578.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114393. 24 interactions.
    IntActi Q14155. 19 interactions.
    MINTi MINT-92779.

    PTM databases

    PhosphoSitei Q14155.

    Polymorphism databases

    DMDMi 50403776.

    Proteomic databases

    MaxQBi Q14155.
    PaxDbi Q14155.
    PRIDEi Q14155.

    Protocols and materials databases

    DNASUi 8874.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317133 ; ENSP00000325994 ; ENSG00000102606 . [Q14155-3 ]
    ENST00000375723 ; ENSP00000364875 ; ENSG00000102606 . [Q14155-6 ]
    ENST00000375736 ; ENSP00000364888 ; ENSG00000102606 . [Q14155-1 ]
    ENST00000375739 ; ENSP00000364891 ; ENSG00000102606 . [Q14155-2 ]
    ENST00000375741 ; ENSP00000364893 ; ENSG00000102606 . [Q14155-4 ]
    ENST00000426073 ; ENSP00000397068 ; ENSG00000102606 . [Q14155-1 ]
    GeneIDi 8874.
    KEGGi hsa:8874.
    UCSCi uc001vrr.2. human. [Q14155-3 ]
    uc001vrs.2. human. [Q14155-4 ]
    uc001vrt.2. human. [Q14155-2 ]
    uc001vrv.4. human. [Q14155-1 ]

    Organism-specific databases

    CTDi 8874.
    GeneCardsi GC13P111766.
    H-InvDB HIX0037536.
    HGNCi HGNC:15607. ARHGEF7.
    HPAi HPA004744.
    MIMi 605477. gene.
    neXtProti NX_Q14155.
    PharmGKBi PA24977.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314429.
    HOVERGENi HBG050569.
    InParanoidi Q14155.
    KOi K13710.
    OMAi HHEPARL.
    OrthoDBi EOG708W04.
    PhylomeDBi Q14155.
    TreeFami TF316105.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_12484. EGFR downregulation.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinki Q14155.

    Miscellaneous databases

    ChiTaRSi ARHGEF7. human.
    EvolutionaryTracei Q14155.
    GeneWikii ARHGEF7.
    GenomeRNAii 8874.
    NextBioi 33313.
    PROi Q14155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14155.
    Bgeei Q14155.
    Genevestigatori Q14155.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR000219. DH-domain.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00033. CH. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50021. CH. 1 hit.
    PS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Amygdala.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1; 2 AND 4).
      Tissue: Brain and Testis.
    7. "Alternative splice variants encoding unstable protein domains exist in the human brain."
      Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.
      J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-803 (ISOFORM 5).
    8. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
      Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
      Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
      Tissue: Neuroblastoma.
    9. Cited for: INTERACTION WITH SCRIB.
    10. "Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
      Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
      Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCRIB.
    11. Cited for: FUNCTION IN CELL MIGRATION.
    12. "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
      Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
      J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRMPD4.
    13. "Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-kinase I/betaPIX signaling complex."
      Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N., Natsume T., Soderling T.R.
      Neuron 57:94-107(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-694, INTERACTION WITH CAMK1.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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 SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Sorting nexin 27 protein regulates trafficking of a p21-activated kinase (PAK) interacting exchange factor (beta-Pix)-G protein-coupled receptor kinase interacting protein (GIT) complex via a PDZ domain interaction."
      Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P., Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.
      J. Biol. Chem. 286:39403-39416(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX27.
    18. "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-249 AND SER-694, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-579 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-664 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis."
      Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J., Veprintsev D.B., Evans P.R., McMahon H.T.
      PLoS ONE 7:E52401-E52401(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIN2.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: STRUCTURE BY NMR OF 260-467.
    22. "Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)."
      Mott H.R., Nietlispach D., Evetts K.A., Owen D.
      Biochemistry 44:10977-10983(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
    23. "Northeast structural genomics consortium target HR4495E."
      Northeast structural genomics consortium (NESG)
      Submitted (DEC-2010) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-137.
    24. Cited for: VARIANT ALA-790.

    Entry informationi

    Entry nameiARHG7_HUMAN
    AccessioniPrimary (citable) accession number: Q14155
    Secondary accession number(s): B1ALK6
    , B1ALK8, Q3LIA4, Q5W9H0, Q6P9G3, Q6PII2, Q86W63, Q8N3M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 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 13
      Human chromosome 13: 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