Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NZN5

- ARHGC_HUMAN

UniProt

Q9NZN5 - ARHGC_HUMAN

Protein

Rho guanine nucleotide exchange factor 12

Gene

ARHGEF12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 GNA13.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei308 – 3092Breakpoint for translocation to form KMT2A/MLL1-ARHGEF12 oncogene

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. axon guidance Source: Reactome
    3. G-protein coupled receptor signaling pathway Source: MGI
    4. neurotrophin TRK receptor signaling pathway Source: Reactome
    5. positive regulation of apoptotic process Source: Reactome
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. small GTPase mediated signal transduction Source: Reactome
    8. 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 12
    Alternative name(s):
    Leukemia-associated RhoGEF
    Gene namesi
    Name:ARHGEF12
    Synonyms:KIAA0382, LARG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14193. ARHGEF12.

    Subcellular locationi

    Cytoplasm Curated. Membrane Curated
    Note: Translocated to the membrane upon stimulation.Curated

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving ARHGEF12 may be a cause of acute leukemia. Translocation t(11;11)(q23;23) with KMT2A/MLL1.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA24969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 15441543Rho guanine nucleotide exchange factor 12PRO_0000080930Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei341 – 3411Phosphoserine1 Publication
    Modified residuei637 – 6371Phosphoserine1 Publication
    Modified residuei736 – 7361Phosphothreonine1 Publication
    Modified residuei1327 – 13271PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NZN5.
    PaxDbiQ9NZN5.
    PRIDEiQ9NZN5.

    PTM databases

    PhosphoSiteiQ9NZN5.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 2 is found in jejunum and testis.

    Gene expression databases

    ArrayExpressiQ9NZN5.
    BgeeiQ9NZN5.
    CleanExiHS_ARHGEF12.
    GenevestigatoriQ9NZN5.

    Organism-specific databases

    HPAiCAB025581.
    HPA018911.

    Interactioni

    Subunit structurei

    Interacts with GNA12 and GNA13, probably through the RGS-like domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts through its PDZ domain with IGF1R beta subunit. Interacts with GCSAM.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IGF1RP080697EBI-821440,EBI-475981
    Lpar1P617933EBI-821440,EBI-7512335From a different organism.
    RHOAP615862EBI-821440,EBI-446668

    Protein-protein interaction databases

    BioGridi116945. 13 interactions.
    DIPiDIP-37887N.
    IntActiQ9NZN5. 11 interactions.
    MINTiMINT-1774807.
    STRINGi9606.ENSP00000380942.

    Structurei

    Secondary structure

    1
    1544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi70 – 767
    Beta strandi85 – 873
    Beta strandi89 – 913
    Beta strandi93 – 964
    Helixi102 – 1065
    Beta strandi112 – 1198
    Turni122 – 1243
    Helixi127 – 1359
    Beta strandi137 – 1459
    Helixi769 – 7724
    Helixi775 – 7784
    Helixi783 – 81230
    Helixi814 – 8207
    Helixi825 – 8328
    Helixi835 – 85319
    Beta strandi857 – 8604
    Helixi865 – 8728
    Helixi875 – 88915
    Helixi891 – 90414
    Helixi906 – 91712
    Helixi919 – 9213
    Helixi926 – 9294
    Helixi932 – 94918
    Helixi954 – 99340
    Beta strandi1001 – 10033
    Helixi1005 – 10073
    Helixi1008 – 10114
    Helixi1015 – 10173
    Beta strandi1020 – 103314
    Beta strandi1038 – 105316
    Beta strandi1056 – 10583
    Beta strandi1078 – 10814
    Helixi1082 – 10843
    Beta strandi1085 – 10895
    Beta strandi1091 – 10933
    Beta strandi1096 – 11027
    Beta strandi1107 – 11137
    Helixi1117 – 113721

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TXDX-ray2.13A766-1138[»]
    1X86X-ray3.22A/C/E/G766-1138[»]
    2OMJNMR-A67-151[»]
    2OS6NMR-A67-151[»]
    ProteinModelPortaliQ9NZN5.
    SMRiQ9NZN5. Positions 67-151, 766-1138.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZN5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 15180PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini367 – 558192RGSLAdd
    BLAST
    Domaini787 – 977191DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini1019 – 1132114PHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili194 – 26269Sequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000034046.
    HOVERGENiHBG050571.
    InParanoidiQ9NZN5.
    KOiK07532.
    OMAiMTPEMPT.
    OrthoDBiEOG7GJ6CF.
    PhylomeDBiQ9NZN5.
    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.
    IPR001331. GDS_CDC24_CS.
    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.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 1 hit.
    SSF48097. SSF48097. 1 hit.
    SSF50156. SSF50156. 1 hit.
    PROSITEiPS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZN5-1) [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

    MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS     50
    SKKTKSSSEE SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED 100
    GAAMRAGVQT GDRIIKVNGT LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG 150
    SPQIPLADSE VEPSVIGHMS PIMTSPHSPG ASGNMERITS PVLMGEENNV 200
    VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ EAKKHIPQLQ 250
    EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AETDPGDVLG RTDCSSGDAS 300
    RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI 350
    IGAEDDDFGT EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT 400
    LLCYLYSDLY KHTNSKETRR IFLEFHQFFL DRSAHLKVSV PDEMSADLEK 450
    RRPELIPEDL HRHYIQTMQE RVHPEVQRHL EDFRQKRSMG LTLAESELTK 500
    LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK SSTMQYVILM 550
    YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI 600
    LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPSSVSPEP QDSAKLRQSG 650
    LANEGTDAGY LPANSMSSVA SGASFSQEGG KENDTGSKQV GETSAPGDTL 700
    DGTPRTLNTV FDFPPPPLDQ VQEEECEVER VTEHGTPKPF RKFDSVAFGE 750
    SQSEDEQFEN DLETDPPNWQ QLVSREVLLG LKPCEIKRQE VINELFYTER 800
    AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ LHIGLNEQMK 850
    AVRKRNETSV IDQIGEDLLT WFSGPGEEKL KHAAATFCSN QPFALEMIKS 900
    RQKKDSRFQT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY 950
    TEWPTEREKV KKAADHCRQI LNYVNQAVKE AENKQRLEDY QRRLDTSSLK 1000
    LSEYPNVEEL RNLDLTKRKM IHEGPLVWKV NRDKTIDLYT LLLEDILVLL 1050
    QKQDDRLVLR CHSKILASTA DSKHTFSPVI KLSTVLVRQV ATDNKALFVI 1100
    SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK PIPLPQSTPG 1150
    EGDNDEEDPS KLKEEQHGIS VTGLQSPDRD LGLESTLISS KPQSHSLSTS 1200
    GKSEVRDLFV AERQFAKEQH TDGTLKEVGE DYQIAIPDSH LPVSEERWAL 1250
    DALRNLGLLK QLLVQQLGLT EKSVQEDWQH FPRYRTASQG PQTDSVIQNS 1300
    ENIKAYHSGE GHMPFRTGTG DIATCYSPRT STESFAPRDS VGLAPQDSQA 1350
    SNILVMDHMI MTPEMPTMEP EGGLDDSGEH FFDAREAHSD ENPSEGDGAV 1400
    NKEEKDVNLR ISGNYLILDG YDPVQESSTD EEVASSLTLQ PMTGIPAVES 1450
    THQQQHSPQN THSDGAISPF TPEFLVQQRW GAMEYSCFEI QSPSSCADSQ 1500
    SQIMEYIHKI EADLEHLKKV EESYTILCQR LAGSALTDKH SDKS 1544
    Length:1,544
    Mass (Da):173,232
    Last modified:October 1, 2000 - v1
    Checksum:i0B7E319CF7C7A224
    GO
    Isoform 2 (identifier: Q9NZN5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-66: Missing.

    Note: Contains a phosphoserine at position 41.

    Show »
    Length:1,525
    Mass (Da):171,115
    Checksum:i47FF1323DE2DFF55
    GO

    Sequence cautioni

    The sequence AAH63117.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti973 – 9731Y → F.1 Publication
    Corresponds to variant rs2305013 [ dbSNP | Ensembl ].
    VAR_020191

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei48 – 6619Missing in isoform 2. 2 PublicationsVSP_008131Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180681 mRNA. Translation: AAF36817.1.
    AB002380 mRNA. Translation: BAA20836.2.
    BC063117 mRNA. Translation: AAH63117.1. Sequence problems.
    CCDSiCCDS41727.1. [Q9NZN5-1]
    CCDS55794.1. [Q9NZN5-2]
    RefSeqiNP_001185594.1. NM_001198665.1. [Q9NZN5-2]
    NP_056128.1. NM_015313.2. [Q9NZN5-1]
    UniGeneiHs.24598.

    Genome annotation databases

    EnsembliENST00000356641; ENSP00000349056; ENSG00000196914. [Q9NZN5-2]
    ENST00000397843; ENSP00000380942; ENSG00000196914. [Q9NZN5-1]
    GeneIDi23365.
    KEGGihsa:23365.
    UCSCiuc001pxl.2. human. [Q9NZN5-1]
    uc009zat.3. human. [Q9NZN5-2]

    Polymorphism databases

    DMDMi34395525.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180681 mRNA. Translation: AAF36817.1 .
    AB002380 mRNA. Translation: BAA20836.2 .
    BC063117 mRNA. Translation: AAH63117.1 . Sequence problems.
    CCDSi CCDS41727.1. [Q9NZN5-1 ]
    CCDS55794.1. [Q9NZN5-2 ]
    RefSeqi NP_001185594.1. NM_001198665.1. [Q9NZN5-2 ]
    NP_056128.1. NM_015313.2. [Q9NZN5-1 ]
    UniGenei Hs.24598.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TXD X-ray 2.13 A 766-1138 [» ]
    1X86 X-ray 3.22 A/C/E/G 766-1138 [» ]
    2OMJ NMR - A 67-151 [» ]
    2OS6 NMR - A 67-151 [» ]
    ProteinModelPortali Q9NZN5.
    SMRi Q9NZN5. Positions 67-151, 766-1138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116945. 13 interactions.
    DIPi DIP-37887N.
    IntActi Q9NZN5. 11 interactions.
    MINTi MINT-1774807.
    STRINGi 9606.ENSP00000380942.

    PTM databases

    PhosphoSitei Q9NZN5.

    Polymorphism databases

    DMDMi 34395525.

    Proteomic databases

    MaxQBi Q9NZN5.
    PaxDbi Q9NZN5.
    PRIDEi Q9NZN5.

    Protocols and materials databases

    DNASUi 23365.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356641 ; ENSP00000349056 ; ENSG00000196914 . [Q9NZN5-2 ]
    ENST00000397843 ; ENSP00000380942 ; ENSG00000196914 . [Q9NZN5-1 ]
    GeneIDi 23365.
    KEGGi hsa:23365.
    UCSCi uc001pxl.2. human. [Q9NZN5-1 ]
    uc009zat.3. human. [Q9NZN5-2 ]

    Organism-specific databases

    CTDi 23365.
    GeneCardsi GC11P120207.
    H-InvDB HIX0010202.
    HIX0036240.
    HGNCi HGNC:14193. ARHGEF12.
    HPAi CAB025581.
    HPA018911.
    MIMi 604763. gene.
    neXtProti NX_Q9NZN5.
    PharmGKBi PA24969.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5422.
    HOGENOMi HOG000034046.
    HOVERGENi HBG050571.
    InParanoidi Q9NZN5.
    KOi K07532.
    OMAi MTPEMPT.
    OrthoDBi EOG7GJ6CF.
    PhylomeDBi Q9NZN5.
    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 ARHGEF12. human.
    EvolutionaryTracei Q9NZN5.
    GeneWikii ARHGEF12.
    GenomeRNAii 23365.
    NextBioi 45421.
    PROi Q9NZN5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZN5.
    Bgeei Q9NZN5.
    CleanExi HS_ARHGEF12.
    Genevestigatori Q9NZN5.

    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.
    IPR001331. GDS_CDC24_CS.
    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.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 1 hit.
    SSF48097. SSF48097. 1 hit.
    SSF50156. SSF50156. 1 hit.
    PROSITEi PS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a gene at 11q23 encoding a guanine nucleotide exchange factor: evidence for its fusion with MLL in acute myeloid leukemia."
      Kourlas P.J., Strout M.P., Becknell B., Veronese M.L., Croce C.M., Theil K.S., Krahe R., Ruutu T., Knuutila S., Bloomfield C.D., Caligiuri M.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:2145-2150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHROMOSOMAL TRANSLOCATION.
      Tissue: Prostate.
    2. "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] OF 1-584 (ISOFORM 2).
      Tissue: Thyroid.
    3. "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] OF 102-1544, VARIANT PHE-973.
      Tissue: Brain.
    4. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links heterotrimeric G proteins of the G(12) family to Rho."
      Fukuhara S., Chikumi H., Gutkind J.S.
      FEBS Lett. 485:183-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RHOA; GNA12 AND GNA13.
    6. "Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF."
      Taya S., Inagaki N., Sengiku H., Makino H., Iwamatsu A., Urakawa I., Nagao K., Kataoka S., Kaibuchi K.
      J. Cell Biol. 155:809-820(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF1R.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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.
    16. "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-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor."
      Kristelly R., Gao G., Tesmer J.J.
      J. Biol. Chem. 279:47352-47362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 766-1138 IN COMPLEX WITH RHOA, SUBUNIT.
    19. "Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor."
      Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J., Shi Y.
      Protein Sci. 17:1003-1014(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 67-151 IN COMPLEX WITH PLXNB1, SUBUNIT.

    Entry informationi

    Entry nameiARHGC_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZN5
    Secondary accession number(s): O15086, Q6P526
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 130 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 11
      Human chromosome 11: 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