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Protein

Rho GTPase-activating protein 24

Gene

Arhgap24

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

GO - Molecular functioni

  • GTPase activator activity Source: MGI

GO - Biological processi

  • activation of GTPase activity Source: MGI
  • angiogenesis Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • negative regulation of Rac protein signal transduction Source: MGI
  • negative regulation of ruffle assembly Source: MGI
  • signal transduction Source: InterPro
  • wound healing, spreading of epidermal cells Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 24
Alternative name(s):
Rho-type GTPase-activating protein 24
Gene namesi
Name:Arhgap24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1922647. Arhgap24.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • focal adhesion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Rho GTPase-activating protein 24PRO_0000280474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei390 – 3901PhosphoserineCombined sources
Modified residuei395 – 3951PhosphoserineCombined sources
Modified residuei397 – 3971PhosphoserineCombined sources
Modified residuei401 – 4011PhosphoserineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei436 – 4361PhosphoserineBy similarity
Modified residuei451 – 4511PhosphothreonineBy similarity
Modified residuei494 – 4941PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by ROCK, leading to activate the RacGAP activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8C4V1.
PaxDbiQ8C4V1.
PRIDEiQ8C4V1.

PTM databases

iPTMnetiQ8C4V1.
PhosphoSiteiQ8C4V1.

Expressioni

Gene expression databases

BgeeiQ8C4V1.
CleanExiMM_ARHGAP24.
ExpressionAtlasiQ8C4V1. baseline and differential.
GenevisibleiQ8C4V1. MM.

Interactioni

Subunit structurei

Interacts with FLNA.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092138.

Structurei

3D structure databases

ProteinModelPortaliQ8C4V1.
SMRiQ8C4V1. Positions 20-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 123107PHPROSITE-ProRule annotationAdd
BLAST
Domaini133 – 327195Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili648 – 72881Sequence analysisAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000232151.
HOVERGENiHBG058875.
InParanoidiQ8C4V1.
PhylomeDBiQ8C4V1.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C4V1-1) [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

        10         20         30         40         50
MEERCESTES PQGQGRKNTK CGWLRKQGGF VKTWHTRWFV LKGDQLYYFK
60 70 80 90 100
DEDETKPLGT IFLHGNKVIE HPCNEENPGK FLFDVVPGGE RDRMTANHES
110 120 130 140 150
YLLMASTQND MEDWVKSIRR VIWGPFGGGI FGQKLEDTVR YEKRYGNRLA
160 170 180 190 200
PMLVEQCVDF IRQRGLKEEG LFRLPGQANL VKELQDAFDC GEKPSFDSNT
210 220 230 240 250
DVHTVASLLK LYLRELPEPV VPYAKYEDFL SCATLLSKEE EAGVKELMKQ
260 270 280 290 300
VKSLPVVNYN LLKYICRFLD EVQSYSGVNK MSAQNLATVF GPNILRPKVE
310 320 330 340 350
DPLTIMEGTV VVQQLMSVMI SKHDRLFPKD TEPQSKPQDG PNSNNNDGHK
360 370 380 390 400
KATMGQLQNK ENNNTKESPV RRCSWDKPES PQRSSVDNGS PTALSGSKTN
410 420 430 440 450
SPRNSIHKLD ISRSPPLMVK KNPAFNKGSG IVTNGSFSSS NAEGVEKPQT
460 470 480 490 500
TPNGSLQARR TSSLKSSGTK MGTHSVQNGT VRMGILNTDT LGNSLNGRSM
510 520 530 540 550
SWLPNGYVTL RDNKQKEPAG ESGQHNRLST YDNVHQQFSS MSLDDKHSVD
560 570 580 590 600
SATWSTSSCE ISLPENSNSC RSSTTTCPEQ DFYVGNFEDP VLDGPPQDDL
610 620 630 640 650
SHPGDYENKS DRRSVGGRSS RATSSSDNSE TFVGNTSSNH SALHSLVSSL
660 670 680 690 700
KQEMTKQKIE YESRIKSLEQ RNLTLETEML SLHDELDQER KKFTMIEIKM
710 720 730 740
RNAERAKEDA EKRNDMLQKE MEQFFSTFGD LTVEPRRSER GNTIWIQ
Length:747
Mass (Da):84,100
Last modified:March 20, 2007 - v2
Checksum:i769982BA6B90D425
GO
Isoform 2 (identifier: Q8C4V1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.
     92-128: DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG → MPEDRNSGGRPSGALASTPFIPKTTYRRIKRCFSFRK

Show »
Length:656
Mass (Da):73,447
Checksum:i1DD35121A4007443
GO
Isoform 3 (identifier: Q8C4V1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Show »
Length:654
Mass (Da):73,259
Checksum:i7AA6C305CA3D7952
GO

Sequence cautioni

The sequence BAC30402.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831E → K in BAC38105 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9393Missing in isoform 3. 1 PublicationVSP_023719Add
BLAST
Alternative sequencei1 – 9191Missing in isoform 2. 1 PublicationVSP_023720Add
BLAST
Alternative sequencei92 – 12837DRMTA…GPFGG → MPEDRNSGGRPSGALASTPF IPKTTYRRIKRCFSFRK in isoform 2. 1 PublicationVSP_023721Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039617 mRNA. Translation: BAC30402.1. Different initiation.
AK080986 mRNA. Translation: BAC38105.1.
BC023344 mRNA. Translation: AAH23344.1.
BC025502 mRNA. Translation: AAH25502.1.
BC027070 mRNA. Translation: AAH27070.1.
CCDSiCCDS19474.1. [Q8C4V1-1]
CCDS19475.1. [Q8C4V1-3]
RefSeqiNP_001273397.1. NM_001286468.1. [Q8C4V1-3]
NP_083546.2. NM_029270.2.
NP_666273.1. NM_146161.3. [Q8C4V1-3]
XP_006534954.1. XM_006534891.2. [Q8C4V1-3]
XP_011247736.1. XM_011249434.1. [Q8C4V1-3]
UniGeneiMm.440191.

Genome annotation databases

EnsembliENSMUST00000073302; ENSMUSP00000073028; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112852; ENSMUSP00000108473; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112853; ENSMUSP00000108474; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112854; ENSMUSP00000108475; ENSMUSG00000057315. [Q8C4V1-3]
GeneIDi231532.
KEGGimmu:231532.
UCSCiuc008yix.2. mouse. [Q8C4V1-1]
uc008yiz.1. mouse. [Q8C4V1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039617 mRNA. Translation: BAC30402.1. Different initiation.
AK080986 mRNA. Translation: BAC38105.1.
BC023344 mRNA. Translation: AAH23344.1.
BC025502 mRNA. Translation: AAH25502.1.
BC027070 mRNA. Translation: AAH27070.1.
CCDSiCCDS19474.1. [Q8C4V1-1]
CCDS19475.1. [Q8C4V1-3]
RefSeqiNP_001273397.1. NM_001286468.1. [Q8C4V1-3]
NP_083546.2. NM_029270.2.
NP_666273.1. NM_146161.3. [Q8C4V1-3]
XP_006534954.1. XM_006534891.2. [Q8C4V1-3]
XP_011247736.1. XM_011249434.1. [Q8C4V1-3]
UniGeneiMm.440191.

3D structure databases

ProteinModelPortaliQ8C4V1.
SMRiQ8C4V1. Positions 20-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092138.

PTM databases

iPTMnetiQ8C4V1.
PhosphoSiteiQ8C4V1.

Proteomic databases

MaxQBiQ8C4V1.
PaxDbiQ8C4V1.
PRIDEiQ8C4V1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073302; ENSMUSP00000073028; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112852; ENSMUSP00000108473; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112853; ENSMUSP00000108474; ENSMUSG00000057315. [Q8C4V1-3]
ENSMUST00000112854; ENSMUSP00000108475; ENSMUSG00000057315. [Q8C4V1-3]
GeneIDi231532.
KEGGimmu:231532.
UCSCiuc008yix.2. mouse. [Q8C4V1-1]
uc008yiz.1. mouse. [Q8C4V1-2]

Organism-specific databases

CTDi83478.
MGIiMGI:1922647. Arhgap24.

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000232151.
HOVERGENiHBG058875.
InParanoidiQ8C4V1.
PhylomeDBiQ8C4V1.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiArhgap24. mouse.
NextBioi380596.
PROiQ8C4V1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C4V1.
CleanExiMM_ARHGAP24.
ExpressionAtlasiQ8C4V1. baseline and differential.
GenevisibleiQ8C4V1. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-358 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Medulla oblongata and Spinal cord.
  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] (ISOFORM 3).
    Strain: FVB/N.
    Tissue: Eye, Kidney and Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-395; SER-397 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung and Pancreas.

Entry informationi

Entry nameiRHG24_MOUSE
AccessioniPrimary (citable) accession number: Q8C4V1
Secondary accession number(s): Q8CA50, Q8QZZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: January 20, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.