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)

Q8N264

- RHG24_HUMAN

UniProt

Q8N264 - RHG24_HUMAN

Protein

Rho GTPase-activating protein 24

Gene

ARHGAP24

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 104 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis.3 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. Rac GTPase activator activity Source: Ensembl

    GO - Biological processi

    1. activation of Rac GTPase activity Source: Ensembl
    2. angiogenesis Source: UniProtKB-KW
    3. cell differentiation Source: UniProtKB-KW
    4. negative regulation of Rac protein signal transduction Source: Ensembl
    5. negative regulation of ruffle assembly Source: Ensembl
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. small GTPase mediated signal transduction Source: Reactome
    8. wound healing, spreading of epidermal cells Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, GTPase activation

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GTPase-activating protein 24
    Alternative name(s):
    Filamin-A-associated RhoGAP
    Short name:
    FilGAP
    RAC1- and CDC42-specific GTPase-activating protein of 72 kDa
    Short name:
    RC-GAP72
    Rho-type GTPase-activating protein 24
    RhoGAP of 73 kDa
    Sarcoma antigen NY-SAR-88
    p73RhoGAP
    Gene namesi
    Name:ARHGAP24
    Synonyms:FILGAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:25361. ARHGAP24.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell junctionfocal adhesion. Cell projection
    Note: Localizes to actin stress fibers. In migrating cells, localizes to membrane lamellae and protusions.

    GO - Cellular componenti

    1. cell projection Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. focal adhesion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi175 – 1751R → A: Loss of function. 2 Publications
    Mutagenesisi175 – 1751R → K: Does not abolish the effect on actin stress fibers but moderates its capability to induce membrane protrusions. 2 Publications

    Organism-specific databases

    Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    PharmGKBiPA134934054.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 748748Rho GTPase-activating protein 24PRO_0000280473Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei391 – 3911Phosphoserine1 Publication
    Modified residuei402 – 4021Phosphoserine1 Publication
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei415 – 4151Phosphoserine1 Publication
    Modified residuei437 – 4371Phosphoserine1 Publication
    Modified residuei452 – 4521Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated by ROCK, leading to activate the RacGAP activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8N264.
    PaxDbiQ8N264.
    PRIDEiQ8N264.

    PTM databases

    PhosphoSiteiQ8N264.

    Expressioni

    Tissue specificityi

    Isoform 1 is widely expressed with a higher level in kidney. Isoform 2 is mainly expressed in endothelial cells.3 Publications

    Inductioni

    Isoform 2 is up-regulated during capillary tube formation in umbilical vein endothelial cells.1 Publication

    Gene expression databases

    ArrayExpressiQ8N264.
    BgeeiQ8N264.
    CleanExiHS_ARHGAP24.
    GenevestigatoriQ8N264.

    Organism-specific databases

    HPAiHPA014288.

    Interactioni

    Subunit structurei

    Interacts with FLNA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLNAP213336EBI-988764,EBI-350432
    HTTP428583EBI-988764,EBI-466029

    Protein-protein interaction databases

    BioGridi123663. 1 interaction.
    DIPiDIP-35520N.
    IntActiQ8N264. 4 interactions.
    MINTiMINT-4725530.
    STRINGi9606.ENSP00000315334.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N264.
    SMRiQ8N264. Positions 16-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 125107PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 329195Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili649 – 72981Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domain mediates the interaction with FLNA leading to its recruitment to lamellae.

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG246008.
    HOGENOMiHOG000232151.
    HOVERGENiHBG058875.
    InParanoidiQ8N264.
    OMAiRYEKRYG.
    OrthoDBiEOG79W94M.
    PhylomeDBiQ8N264.
    TreeFamiTF323577.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N264-1) [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

    MEENNDSTEN PQQGQGRQNA IKCGWLRKQG GFVKTWHTRW FVLKGDQLYY    50
    FKDEDETKPL GTIFLPGNKV SEHPCNEENP GKFLFEVVPG GDRDRMTANH 100
    ESYLLMASTQ NDMEDWVKSI RRVIWGPFGG GIFGQKLEDT VRYEKRYGNR 150
    LAPMLVEQCV DFIRQRGLKE EGLFRLPGQA NLVKELQDAF DCGEKPSFDS 200
    NTDVHTVASL LKLYLRELPE PVIPYAKYED FLSCAKLLSK EEEAGVKELA 250
    KQVKSLPVVN YNLLKYICRF LDEVQSYSGV NKMSVQNLAT VFGPNILRPK 300
    VEDPLTIMEG TVVVQQLMSV MISKHDCLFP KDAELQSKPQ DGVSNNNEIQ 350
    KKATMGQLQN KENNNTKDSP SRQCSWDKSE SPQRSSMNNG SPTALSGSKT 400
    NSPKNSVHKL DVSRSPPLMV KKNPAFNKGS GIVTNGSFSS SNAEGLEKTQ 450
    TTPNGSLQAR RSSSLKVSGT KMGTHSVQNG TVRMGILNSD TLGNPTNVRN 500
    MSWLPNGYVT LRDNKQKEQA GELGQHNRLS TYDNVHQQFS MMNLDDKQSI 550
    DSATWSTSSC EISLPENSNS CRSSTTTCPE QDFFGGNFED PVLDGPPQDD 600
    LSHPRDYESK SDHRSVGGRS SRATSSSDNS ETFVGNSSSN HSALHSLVSS 650
    LKQEMTKQKI EYESRIKSLE QRNLTLETEM MSLHDELDQE RKKFTMIEIK 700
    MRNAERAKED AEKRNDMLQK EMEQFFSTFG ELTVEPRRTE RGNTIWIQ 748
    Length:748
    Mass (Da):84,258
    Last modified:March 20, 2007 - v2
    Checksum:i87A8E6DCA6869229
    GO
    Isoform 2 (identifier: Q8N264-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-93: Missing.
         94-130: DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG → MPEDRNSGGCPAGALASTPFIPKTTYRRIKRCFSFRK

    Show »
    Length:655
    Mass (Da):73,409
    Checksum:i1497D420E9DD3FE5
    GO
    Isoform 3 (identifier: Q8N264-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Show »
    Length:653
    Mass (Da):73,290
    Checksum:iF6A68FEF1E0A5564
    GO
    Isoform 4 (identifier: Q8N264-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         245-246: GV → VS
         247-748: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:246
    Mass (Da):28,249
    Checksum:i9AC9E1CA3D589430
    GO
    Isoform 5 (identifier: Q8N264-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MWLRKKDWQI...QQGKSISLIM
         91-94: GDRD → KIFS
         95-748: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:239
    Mass (Da):28,221
    Checksum:i44E3F4574FA33D77
    GO

    Sequence cautioni

    The sequence AAO65178.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401T → A in BAC03606. (PubMed:14702039)Curated
    Sequence conflicti357 – 3571Q → L in CAB66581. (PubMed:11230166)Curated
    Sequence conflicti722 – 7221M → V in BAC03606. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9595Missing in isoform 3. 1 PublicationVSP_023711Add
    BLAST
    Alternative sequencei1 – 9393Missing in isoform 2. 1 PublicationVSP_023712Add
    BLAST
    Alternative sequencei1 – 11M → MWLRKKDWQIFNEQFLKKEH AVGFCFSKCVLVEFSLKCFK KIKSSYWNNDALAFLGKKFL REKNKMTKKQTRNRQNKFPP KPALRSSPVHRVQHFPLLWK VKEPHYHLFFFAFSYCWSWE PFPSEQQPCPASVLSSQQGK SISLIM in isoform 5. 1 PublicationVSP_023713
    Alternative sequencei91 – 944GDRD → KIFS in isoform 5. 1 PublicationVSP_023714
    Alternative sequencei94 – 13037DRMTA…GPFGG → MPEDRNSGGCPAGALASTPF IPKTTYRRIKRCFSFRK in isoform 2. 1 PublicationVSP_023715Add
    BLAST
    Alternative sequencei95 – 748654Missing in isoform 5. 1 PublicationVSP_023716Add
    BLAST
    Alternative sequencei245 – 2462GV → VS in isoform 4. 1 PublicationVSP_023717
    Alternative sequencei247 – 748502Missing in isoform 4. 1 PublicationVSP_023718Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136646 mRNA. Translation: CAB66581.1.
    AK091196 mRNA. Translation: BAC03606.1.
    AK130576 mRNA. Translation: BAC85384.1.
    BC047918 mRNA. Translation: AAH47918.1.
    BC098580 mRNA. Translation: AAH98580.1.
    AY211925 mRNA. Translation: AAO65178.1. Frameshift.
    CCDSiCCDS34025.1. [Q8N264-1]
    CCDS3611.1. [Q8N264-2]
    CCDS43246.1. [Q8N264-3]
    PIRiA59430.
    RefSeqiNP_001020787.2. NM_001025616.2. [Q8N264-1]
    NP_001036134.1. NM_001042669.1. [Q8N264-3]
    NP_112595.2. NM_031305.2. [Q8N264-2]
    XP_005263320.1. XM_005263263.2. [Q8N264-1]
    UniGeneiHs.444229.

    Genome annotation databases

    EnsembliENST00000264343; ENSP00000264343; ENSG00000138639. [Q8N264-2]
    ENST00000395183; ENSP00000378610; ENSG00000138639. [Q8N264-3]
    ENST00000395184; ENSP00000378611; ENSG00000138639. [Q8N264-1]
    ENST00000503995; ENSP00000423206; ENSG00000138639. [Q8N264-4]
    GeneIDi83478.
    KEGGihsa:83478.
    UCSCiuc003hpj.3. human. [Q8N264-4]
    uc003hpk.3. human. [Q8N264-1]
    uc003hpm.3. human. [Q8N264-2]
    uc010ikf.3. human. [Q8N264-3]

    Polymorphism databases

    DMDMi134035016.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136646 mRNA. Translation: CAB66581.1 .
    AK091196 mRNA. Translation: BAC03606.1 .
    AK130576 mRNA. Translation: BAC85384.1 .
    BC047918 mRNA. Translation: AAH47918.1 .
    BC098580 mRNA. Translation: AAH98580.1 .
    AY211925 mRNA. Translation: AAO65178.1 . Frameshift.
    CCDSi CCDS34025.1. [Q8N264-1 ]
    CCDS3611.1. [Q8N264-2 ]
    CCDS43246.1. [Q8N264-3 ]
    PIRi A59430.
    RefSeqi NP_001020787.2. NM_001025616.2. [Q8N264-1 ]
    NP_001036134.1. NM_001042669.1. [Q8N264-3 ]
    NP_112595.2. NM_031305.2. [Q8N264-2 ]
    XP_005263320.1. XM_005263263.2. [Q8N264-1 ]
    UniGenei Hs.444229.

    3D structure databases

    ProteinModelPortali Q8N264.
    SMRi Q8N264. Positions 16-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123663. 1 interaction.
    DIPi DIP-35520N.
    IntActi Q8N264. 4 interactions.
    MINTi MINT-4725530.
    STRINGi 9606.ENSP00000315334.

    PTM databases

    PhosphoSitei Q8N264.

    Polymorphism databases

    DMDMi 134035016.

    Proteomic databases

    MaxQBi Q8N264.
    PaxDbi Q8N264.
    PRIDEi Q8N264.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264343 ; ENSP00000264343 ; ENSG00000138639 . [Q8N264-2 ]
    ENST00000395183 ; ENSP00000378610 ; ENSG00000138639 . [Q8N264-3 ]
    ENST00000395184 ; ENSP00000378611 ; ENSG00000138639 . [Q8N264-1 ]
    ENST00000503995 ; ENSP00000423206 ; ENSG00000138639 . [Q8N264-4 ]
    GeneIDi 83478.
    KEGGi hsa:83478.
    UCSCi uc003hpj.3. human. [Q8N264-4 ]
    uc003hpk.3. human. [Q8N264-1 ]
    uc003hpm.3. human. [Q8N264-2 ]
    uc010ikf.3. human. [Q8N264-3 ]

    Organism-specific databases

    CTDi 83478.
    GeneCardsi GC04P086396.
    H-InvDB HIX0004350.
    HGNCi HGNC:25361. ARHGAP24.
    HPAi HPA014288.
    MIMi 610586. gene.
    neXtProti NX_Q8N264.
    Orphaneti 93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    PharmGKBi PA134934054.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246008.
    HOGENOMi HOG000232151.
    HOVERGENi HBG058875.
    InParanoidi Q8N264.
    OMAi RYEKRYG.
    OrthoDBi EOG79W94M.
    PhylomeDBi Q8N264.
    TreeFami TF323577.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi ARHGAP24. human.
    GeneWikii ARHGAP24.
    GenomeRNAii 83478.
    NextBioi 72411.
    PROi Q8N264.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N264.
    Bgeei Q8N264.
    CleanExi HS_ARHGAP24.
    Genevestigatori Q8N264.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
      Tissue: Spleen and Tongue.
    3. "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 3 AND 4).
      Tissue: Chondrosarcoma.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 233-510.
    5. "Identification and characterization of ARHGAP24 and ARHGAP25 genes in silico."
      Katoh M., Katoh M.
      Int. J. Mol. Med. 14:333-338(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF ARG-175.
    7. "Characterization of a novel GTPase-activating protein associated with focal adhesions and the actin cytoskeleton."
      Lavelin I., Geiger B.
      J. Biol. Chem. 280:7178-7185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-175.
    8. "FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling."
      Ohta Y., Hartwig J.H., Stossel T.P.
      Nat. Cell Biol. 8:803-814(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FLNA, PHOSPHORYLATION AT SER-391; SER-402; SER-413; SER-415; SER-437 AND THR-452.

    Entry informationi

    Entry nameiRHG24_HUMAN
    AccessioniPrimary (citable) accession number: Q8N264
    Secondary accession number(s): Q4KMG1
    , Q6ZNV3, Q86TI5, Q86WE4, Q9H0T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 104 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3