Q8N264 (RHG24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ARHGAP24
Synonyms:	FILGAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell junction › focal 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 process	Angiogenesis Differentiation
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Developmental protein GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cell 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 plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FLNA	P21333	6	EBI-988764,EBI-350432

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 748	748	Rho GTPase-activating protein 24		PRO_0000280473
Regions
	Domain	19 – 125	107	PH
	Domain	135 – 329	195	Rho-GAP
	Coiled coil	649 – 729	81	Potential
Amino acid modifications
	Modified residue	391	1	Phosphoserine Ref.8
	Modified residue	402	1	Phosphoserine Ref.8
	Modified residue	413	1	Phosphoserine Ref.8
	Modified residue	415	1	Phosphoserine Ref.8
	Modified residue	437	1	Phosphoserine Ref.8
	Modified residue	452	1	Phosphothreonine Ref.8
Natural variations
	Alternative sequence	1 – 95	95	Missing in isoform 3.		VSP_023711
	Alternative sequence	1 – 93	93	Missing in isoform 2.		VSP_023712
	Alternative sequence	1	1	M → MWLRKKDWQIFNEQFLKKEH AVGFCFSKCVLVEFSLKCFK KIKSSYWNNDALAFLGKKFL REKNKMTKKQTRNRQNKFPP KPALRSSPVHRVQHFPLLWK VKEPHYHLFFFAFSYCWSWE PFPSEQQPCPASVLSSQQGK SISLIM in isoform 5.		VSP_023713
	Alternative sequence	91 – 94	4	GDRD → KIFS in isoform 5.		VSP_023714
	Alternative sequence	94 – 130	37	DRMTA…GPFGG → MPEDRNSGGCPAGALASTPF IPKTTYRRIKRCFSFRK in isoform 2.		VSP_023715
	Alternative sequence	95 – 748	654	Missing in isoform 5.		VSP_023716
	Alternative sequence	245 – 246	2	GV → VS in isoform 4.		VSP_023717
	Alternative sequence	247 – 748	502	Missing in isoform 4.		VSP_023718
Experimental info
	Mutagenesis	175	1	R → A: Loss of function. Ref.6 Ref.7
	Mutagenesis	175	1	R → K: Does not abolish the effect on actin stress fibers but moderates its capability to induce membrane protrusions. Ref.6 Ref.7
	Sequence conflict	140	1	T → A in BAC03606. Ref.2
	Sequence conflict	357	1	Q → L in CAB66581. Ref.1
	Sequence conflict	722	1	M → V in BAC03606. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 87A8E6DCA6869229	FASTA	748	84,258
	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
	Isoform 2 [UniParc]. Checksum: 1497D420E9DD3FE5	FASTA	655	73,409
	10 20 30 40 50 60 MPEDRNSGGC PAGALASTPF IPKTTYRRIK RCFSFRKGIF GQKLEDTVRY EKRYGNRLAP 70 80 90 100 110 120 MLVEQCVDFI RQRGLKEEGL FRLPGQANLV KELQDAFDCG EKPSFDSNTD VHTVASLLKL 130 140 150 160 170 180 YLRELPEPVI PYAKYEDFLS CAKLLSKEEE AGVKELAKQV KSLPVVNYNL LKYICRFLDE 190 200 210 220 230 240 VQSYSGVNKM SVQNLATVFG PNILRPKVED PLTIMEGTVV VQQLMSVMIS KHDCLFPKDA 250 260 270 280 290 300 ELQSKPQDGV SNNNEIQKKA TMGQLQNKEN NNTKDSPSRQ CSWDKSESPQ RSSMNNGSPT 310 320 330 340 350 360 ALSGSKTNSP KNSVHKLDVS RSPPLMVKKN PAFNKGSGIV TNGSFSSSNA EGLEKTQTTP 370 380 390 400 410 420 NGSLQARRSS SLKVSGTKMG THSVQNGTVR MGILNSDTLG NPTNVRNMSW LPNGYVTLRD 430 440 450 460 470 480 NKQKEQAGEL GQHNRLSTYD NVHQQFSMMN LDDKQSIDSA TWSTSSCEIS LPENSNSCRS 490 500 510 520 530 540 STTTCPEQDF FGGNFEDPVL DGPPQDDLSH PRDYESKSDH RSVGGRSSRA TSSSDNSETF 550 560 570 580 590 600 VGNSSSNHSA LHSLVSSLKQ EMTKQKIEYE SRIKSLEQRN LTLETEMMSL HDELDQERKK 610 620 630 640 650 FTMIEIKMRN AERAKEDAEK RNDMLQKEME QFFSTFGELT VEPRRTERGN TIWIQ
	Isoform 3 [UniParc]. Checksum: F6A68FEF1E0A5564	FASTA	653	73,290
	10 20 30 40 50 60 MTANHESYLL MASTQNDMED WVKSIRRVIW GPFGGGIFGQ KLEDTVRYEK RYGNRLAPML 70 80 90 100 110 120 VEQCVDFIRQ RGLKEEGLFR LPGQANLVKE LQDAFDCGEK PSFDSNTDVH TVASLLKLYL 130 140 150 160 170 180 RELPEPVIPY AKYEDFLSCA KLLSKEEEAG VKELAKQVKS LPVVNYNLLK YICRFLDEVQ 190 200 210 220 230 240 SYSGVNKMSV QNLATVFGPN ILRPKVEDPL TIMEGTVVVQ QLMSVMISKH DCLFPKDAEL 250 260 270 280 290 300 QSKPQDGVSN NNEIQKKATM GQLQNKENNN TKDSPSRQCS WDKSESPQRS SMNNGSPTAL 310 320 330 340 350 360 SGSKTNSPKN SVHKLDVSRS PPLMVKKNPA FNKGSGIVTN GSFSSSNAEG LEKTQTTPNG 370 380 390 400 410 420 SLQARRSSSL KVSGTKMGTH SVQNGTVRMG ILNSDTLGNP TNVRNMSWLP NGYVTLRDNK 430 440 450 460 470 480 QKEQAGELGQ HNRLSTYDNV HQQFSMMNLD DKQSIDSATW STSSCEISLP ENSNSCRSST 490 500 510 520 530 540 TTCPEQDFFG GNFEDPVLDG PPQDDLSHPR DYESKSDHRS VGGRSSRATS SSDNSETFVG 550 560 570 580 590 600 NSSSNHSALH SLVSSLKQEM TKQKIEYESR IKSLEQRNLT LETEMMSLHD ELDQERKKFT 610 620 630 640 650 MIEIKMRNAE RAKEDAEKRN DMLQKEMEQF FSTFGELTVE PRRTERGNTI WIQ
	Isoform 4 [UniParc]. Checksum: 9AC9E1CA3D589430	FASTA	246	28,249
	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 EEEAVS
	Isoform 5 [UniParc]. Checksum: 44E3F4574FA33D77	FASTA	239	28,221
	10 20 30 40 50 60 MWLRKKDWQI FNEQFLKKEH AVGFCFSKCV LVEFSLKCFK KIKSSYWNND ALAFLGKKFL 70 80 90 100 110 120 REKNKMTKKQ TRNRQNKFPP KPALRSSPVH RVQHFPLLWK VKEPHYHLFF FAFSYCWSWE 130 140 150 160 170 180 PFPSEQQPCP ASVLSSQQGK SISLIMEENN DSTENPQQGQ GRQNAIKCGW LRKQGGFVKT 190 200 210 220 230 WHTRWFVLKG DQLYYFKDED ETKPLGTIFL PGNKVSEHPC NEENPGKFLF EVVPGKIFS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00010448. IPI00166301. IPI00442526. IPI00783816. IPI00829821.
PIR	A59430.
RefSeq	NP_001020787.2. NM_001025616.2. NP_001036134.1. NM_001042669.1. NP_112595.2. NM_031305.2.
UniGene	Hs.444229.
3D structure databases
HSSP	HSSP built from PDB template 1V89 based on UniProtKB P42331.
ProteinModelPortal	Q8N264.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35520N.
IntAct	Q8N264. 3 interactions.
STRING	9606.ENSP00000315334.
PTM databases
PhosphoSite	Q8N264.
Polymorphism databases
DMDM	134035016.
Proteomic databases
PaxDb	Q8N264.
PRIDE	Q8N264.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264343; ENSP00000264343; ENSG00000138639. ENST00000395183; ENSP00000378610; ENSG00000138639. ENST00000395184; ENSP00000378611; ENSG00000138639. ENST00000503995; ENSP00000423206; ENSG00000138639.
GeneID	83478.
KEGG	hsa:83478.
UCSC	uc003hpj.3. human. uc003hpk.3. human. uc003hpm.3. human. uc010ikf.3. human.
Organism-specific databases
CTD	83478.
GeneCards	GC04P086396.
H-InvDB	HIX0004350.
HGNC	HGNC:25361. ARHGAP24.
HPA	HPA014288.
MIM	610586. gene.
neXtProt	NX_Q8N264.
Orphanet	93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB	PA134934054.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG246008.
HOGENOM	HOG000232151.
HOVERGEN	HBG058875.
InParanoid	Q8N264.
OMA	ISTESHI.
OrthoDB	EOG4D26PH.
PhylomeDB	Q8N264.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q8N264.
Bgee	Q8N264.
CleanEx	HS_ARHGAP24.
Genevestigator	Q8N264.
Family and domain databases
Gene3D	1.10.555.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Pfam	PF00169. PH. 1 hit. PF00620. RhoGAP. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00324. RhoGAP. 1 hit. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit.
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50238. RHOGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ARHGAP24. human.
GenomeRNAi	83478.
NextBio	72411.
SOURCE	Search...

Entry information

Entry name

RHG24_HUMAN

Accession

Primary (citable) accession number: Q8N264
Secondary accession number(s): Q4KMG1 , Q6ZNV3, Q86TI5, Q86WE4, Q9H0T6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.