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Q8N264 (RHG24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ARHGAP24
Synonyms:FILGAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with FLNA. Ref.8

Subcellular location

Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell junctionfocal adhesion. Cell projection. Note: Localizes to actin stress fibers. In migrating cells, localizes to membrane lamellae and protusions. Ref.7 Ref.8

Tissue specificity

Isoform 1 is widely expressed with a higher level in kidney. Isoform 2 is mainly expressed in endothelial cells. Ref.6 Ref.7 Ref.8

Induction

Isoform 2 is up-regulated during capillary tube formation in umbilical vein endothelial cells. Ref.6

Domain

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

Post-translational modification

Phosphorylated by ROCK, leading to activate the RacGAP activity. Ref.8

Sequence similarities

Contains 1 PH domain.

Contains 1 Rho-GAP domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionDevelopmental protein
GTPase activation
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of ruffle assembly

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRac GTPase activator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.8PubMed 17500595. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N264-1)

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.
Isoform 2 (identifier: Q8N264-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.
     94-130: DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG → MPEDRNSGGCPAGALASTPFIPKTTYRRIKRCFSFRK
Isoform 3 (identifier: Q8N264-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.
Isoform 4 (identifier: Q8N264-4)

The sequence of this isoform differs from the canonical sequence as follows:
     245-246: GV → VS
     247-748: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8N264-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 748748Rho GTPase-activating protein 24
PRO_0000280473

Regions

Domain19 – 125107PH
Domain135 – 329195Rho-GAP
Coiled coil649 – 72981 Potential

Amino acid modifications

Modified residue3911Phosphoserine Ref.8
Modified residue4021Phosphoserine Ref.8
Modified residue4131Phosphoserine Ref.8
Modified residue4151Phosphoserine Ref.8
Modified residue4371Phosphoserine Ref.8
Modified residue4521Phosphothreonine Ref.8

Natural variations

Alternative sequence1 – 9595Missing in isoform 3.
VSP_023711
Alternative sequence1 – 9393Missing in isoform 2.
VSP_023712
Alternative sequence11M → MWLRKKDWQIFNEQFLKKEH AVGFCFSKCVLVEFSLKCFK KIKSSYWNNDALAFLGKKFL REKNKMTKKQTRNRQNKFPP KPALRSSPVHRVQHFPLLWK VKEPHYHLFFFAFSYCWSWE PFPSEQQPCPASVLSSQQGK SISLIM in isoform 5.
VSP_023713
Alternative sequence91 – 944GDRD → KIFS in isoform 5.
VSP_023714
Alternative sequence94 – 13037DRMTA…GPFGG → MPEDRNSGGCPAGALASTPF IPKTTYRRIKRCFSFRK in isoform 2.
VSP_023715
Alternative sequence95 – 748654Missing in isoform 5.
VSP_023716
Alternative sequence245 – 2462GV → VS in isoform 4.
VSP_023717
Alternative sequence247 – 748502Missing in isoform 4.
VSP_023718

Experimental info

Mutagenesis1751R → A: Loss of function. Ref.6 Ref.7
Mutagenesis1751R → K: Does not abolish the effect on actin stress fibers but moderates its capability to induce membrane protrusions. Ref.6 Ref.7
Sequence conflict1401T → A in BAC03606. Ref.2
Sequence conflict3571Q → L in CAB66581. Ref.1
Sequence conflict7221M → V in BAC03606. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 87A8E6DCA6869229

FASTA74884,258
        10         20         30         40         50         60 
MEENNDSTEN PQQGQGRQNA IKCGWLRKQG GFVKTWHTRW FVLKGDQLYY FKDEDETKPL 

        70         80         90        100        110        120 
GTIFLPGNKV SEHPCNEENP GKFLFEVVPG GDRDRMTANH ESYLLMASTQ NDMEDWVKSI 

       130        140        150        160        170        180 
RRVIWGPFGG GIFGQKLEDT VRYEKRYGNR LAPMLVEQCV DFIRQRGLKE EGLFRLPGQA 

       190        200        210        220        230        240 
NLVKELQDAF DCGEKPSFDS NTDVHTVASL LKLYLRELPE PVIPYAKYED FLSCAKLLSK 

       250        260        270        280        290        300 
EEEAGVKELA KQVKSLPVVN YNLLKYICRF LDEVQSYSGV NKMSVQNLAT VFGPNILRPK 

       310        320        330        340        350        360 
VEDPLTIMEG TVVVQQLMSV MISKHDCLFP KDAELQSKPQ DGVSNNNEIQ KKATMGQLQN 

       370        380        390        400        410        420 
KENNNTKDSP SRQCSWDKSE SPQRSSMNNG SPTALSGSKT NSPKNSVHKL DVSRSPPLMV 

       430        440        450        460        470        480 
KKNPAFNKGS GIVTNGSFSS SNAEGLEKTQ TTPNGSLQAR RSSSLKVSGT KMGTHSVQNG 

       490        500        510        520        530        540 
TVRMGILNSD TLGNPTNVRN MSWLPNGYVT LRDNKQKEQA GELGQHNRLS TYDNVHQQFS 

       550        560        570        580        590        600 
MMNLDDKQSI DSATWSTSSC EISLPENSNS CRSSTTTCPE QDFFGGNFED PVLDGPPQDD 

       610        620        630        640        650        660 
LSHPRDYESK SDHRSVGGRS SRATSSSDNS ETFVGNSSSN HSALHSLVSS LKQEMTKQKI 

       670        680        690        700        710        720 
EYESRIKSLE QRNLTLETEM MSLHDELDQE RKKFTMIEIK MRNAERAKED AEKRNDMLQK 

       730        740 
EMEQFFSTFG ELTVEPRRTE RGNTIWIQ 

« Hide

Isoform 2 [UniParc].

Checksum: 1497D420E9DD3FE5
Show »

FASTA65573,409
Isoform 3 [UniParc].

Checksum: F6A68FEF1E0A5564
Show »

FASTA65373,290
Isoform 4 [UniParc].

Checksum: 9AC9E1CA3D589430
Show »

FASTA24628,249
Isoform 5 [UniParc].

Checksum: 44E3F4574FA33D77
Show »

FASTA23928,221

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Immunomic analysis of human sarcoma."
Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.
Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract]
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]"A vascular cell-restricted RhoGAP, p73RhoGAP, is a key regulator of angiogenesis."
Su Z.-J., Hahn C.N., Goodall G.J., Reck N.M., Leske A.F., Davy A., Kremmidiotis G., Vadas M.A., Gamble J.R.
Proc. Natl. Acad. Sci. U.S.A. 101:12212-12217(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34025.1. [Q8N264-1]
CCDS3611.1. [Q8N264-2]
CCDS43246.1. [Q8N264-3]
PIRA59430.
RefSeqNP_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]
UniGeneHs.444229.

3D structure databases

ProteinModelPortalQ8N264.
SMRQ8N264. Positions 16-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123663. 1 interaction.
DIPDIP-35520N.
IntActQ8N264. 4 interactions.
MINTMINT-4725530.
STRING9606.ENSP00000315334.

PTM databases

PhosphoSiteQ8N264.

Polymorphism databases

DMDM134035016.

Proteomic databases

MaxQBQ8N264.
PaxDbQ8N264.
PRIDEQ8N264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264343; ENSP00000264343; ENSG00000138639. [Q8N264-2]
ENST00000395183; ENSP00000378610; ENSG00000138639. [Q8N264-3]
ENST00000395184; ENSP00000378611; ENSG00000138639. [Q8N264-1]
ENST00000503995; ENSP00000423206; ENSG00000138639. [Q8N264-4]
GeneID83478.
KEGGhsa:83478.
UCSCuc003hpj.3. human. [Q8N264-4]
uc003hpk.3. human. [Q8N264-1]
uc003hpm.3. human. [Q8N264-2]
uc010ikf.3. human. [Q8N264-3]

Organism-specific databases

CTD83478.
GeneCardsGC04P086396.
H-InvDBHIX0004350.
HGNCHGNC:25361. ARHGAP24.
HPAHPA014288.
MIM610586. gene.
neXtProtNX_Q8N264.
Orphanet93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBPA134934054.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246008.
HOGENOMHOG000232151.
HOVERGENHBG058875.
InParanoidQ8N264.
OMARYEKRYG.
OrthoDBEOG79W94M.
PhylomeDBQ8N264.
TreeFamTF323577.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ8N264.
BgeeQ8N264.
CleanExHS_ARHGAP24.
GenevestigatorQ8N264.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP24. human.
GeneWikiARHGAP24.
GenomeRNAi83478.
NextBio72411.
PROQ8N264.
SOURCESearch...

Entry information

Entry nameRHG24_HUMAN
AccessionPrimary (citable) accession number: Q8N264
Secondary accession number(s): Q4KMG1 expand/collapse secondary AC list , Q6ZNV3, Q86TI5, Q86WE4, Q9H0T6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM