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Protein

Rho GTPase-activating protein 5

Gene

Arhgap5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of RASA1/p120GAP.

GO - Molecular functioni

GO - Biological processi

  • positive regulation of cell migration Source: MGI
  • positive regulation of mesenchymal cell proliferation Source: MGI
  • regulation of cell size Source: MGI
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 5
Alternative name(s):
Rho-type GTPase-activating protein 5
p190-B
Gene namesi
Name:Arhgap5
Synonyms:Rhogap5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1332637. Arhgap5.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity

  • Note: Also membrane-associated when found in fibrillar patterns that colocalize with the alpha5-beta1 integrin receptor (ITGA5/ITGB1) for fibronectin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15011501Rho GTPase-activating protein 5PRO_0000056703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei550 – 5501Nitrated tyrosineBy similarity
Modified residuei765 – 7651PhosphoserineBy similarity
Modified residuei951 – 9511PhosphoserineBy similarity
Modified residuei968 – 9681PhosphoserineBy similarity
Modified residuei1115 – 11151PhosphoserineBy similarity
Modified residuei1194 – 11941PhosphoserineCombined sources
Modified residuei1201 – 12011PhosphoserineCombined sources
Modified residuei1217 – 12171PhosphoserineCombined sources

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

EPDiP97393.
MaxQBiP97393.
PaxDbiP97393.
PRIDEiP97393.

PTM databases

iPTMnetiP97393.
PhosphoSiteiP97393.

Expressioni

Tissue specificityi

Expressed in spinal cord, cerebellum, kidney, testis and lung.

Gene expression databases

CleanExiMM_ARHGAP5.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP97393. 1 interaction.
MINTiMINT-1733994.
STRINGi10090.ENSMUSP00000106353.

Structurei

3D structure databases

ProteinModelPortaliP97393.
SMRiP97393. Positions 12-248, 1244-1455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 32559FF 1Add
BLAST
Domaini366 – 42055FF 2Add
BLAST
Domaini427 – 48155FF 3Add
BLAST
Domaini482 – 54867FF 4Add
BLAST
Domaini1261 – 1448188Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1224 – 124421Lys-richAdd
BLAST

Sequence similaritiesi

Contains 4 FF domains.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
HOVERGENiHBG051844.
InParanoidiP97393.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAKNKEPRP PSYTVSVVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY
60 70 80 90 100
PEHTSVLSTI DFGGRVVNND HFLYWGDITQ NGEDGVECKI HVIEQTEFID
110 120 130 140 150
DQTFLPHRST NLQPYIKRAA ASKLQSAEKL MYICTDQLGL EQDFEQKQMP
160 170 180 190 200
EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV NNLFVQLSKS KKPVIIAATK
210 220 230 240 250
CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT ALVQMLDKTR
260 270 280 290 300
GKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
310 320 330 340 350
PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIS TLPRAFNTLL
360 370 380 390 400
PDLEEIEHLN WLEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI
410 420 430 440 450
PFDLLSTLEA EKVYQNHVQH LISEKRRIEM KEKFKKTLEK IQFISPGQPW
460 470 480 490 500
EEVMCFVMED EAFKYITEAD SKEVYGRHQR EIVEKAKEEF QEMLFEHSEL
510 520 530 540 550
FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES LLLKHIGFVY
560 570 580 590 600
HPTKETCLSG QYCTDIKVEN LLATSLLEMD HNRVRLYHDS TNIDKVNLFI
610 620 630 640 650
LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYILSQLWT
660 670 680 690 700
AAFKPHGCFC VFNSIESLSF IGEFIGKIRT EASQIRKDKY MTNLPFTLIL
710 720 730 740 750
ANQRDSISKN LPILRHQGQQ LANKLQCPFV DVPTGTYPRK FNESQIKQAL
760 770 780 790 800
RGVLESVKHN LDVVSPVPIN KDVSEADLRI VMCAMCGDPF SVDLILSPFL
810 820 830 840 850
DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI GVRKDELVHG
860 870 880 890 900
YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
910 920 930 940 950
MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL
960 970 980 990 1000
SDNTRESTHQ SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL
1010 1020 1030 1040 1050
LPTPSDRSRY RLDLEGNEYP VHSTPNCHDH ERNHKVPPPI KPKPVVPKTN
1060 1070 1080 1090 1100
VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA HPEDMDSSDN YVEPLDTIFK
1110 1120 1130 1140 1150
QKGYSDEIYV VPDDSQNRII KIRNSFVNNT QGDEENGFSD PQKVMESVGL
1160 1170 1180 1190 1200
QNININLKLC LVKPSHTTEE HTQMQAMMRL SLLPKKRKGR HRGSEEDPLL
1210 1220 1230 1240 1250
SPVETWKGGI DNPAITSDQE VDDKKIKKKT HKVKEDKKQK KKTKTFNPPT
1260 1270 1280 1290 1300
RRNWESNYFG MPLQDLVTAE KPIPLFVEKC VEFIEDTGLC TEGLYRVSGN
1310 1320 1330 1340 1350
KTDQDNIQKQ FDQDHNINLA SMEVTVNAVA GALKAFFADL PDPLIPYSLH
1360 1370 1380 1390 1400
PELLEAAKIP DKTERFHALK EIVKKFHPVN YDVFRYVITH LNRVSQQNKI
1410 1420 1430 1440 1450
NLMTADNLSI CFWPTLMRPD FENREFLSTT KIHQSVVETF IQQCQFFFYN
1460 1470 1480 1490 1500
GEIVETANTV APPPTSNPGQ LVESMVPLQL PPPLQPQLIQ PQLQTDPLGI

I
Length:1,501
Mass (Da):172,113
Last modified:July 27, 2011 - v2
Checksum:iC2E14661E838548D
GO

Sequence cautioni

The sequence AK041016 differs from that shown. Reason: Frameshift at position 1140. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 722HF → SL in AAD12768 (PubMed:9838117).Curated
Sequence conflicti93 – 931I → N in AAD12768 (PubMed:9838117).Curated
Sequence conflicti118 – 1181R → H in AAD12768 (PubMed:9838117).Curated
Sequence conflicti348 – 3492TL → SV in AAD12768 (PubMed:9838117).Curated
Sequence conflicti416 – 4161N → K in AAD12768 (PubMed:9838117).Curated
Sequence conflicti629 – 6291I → F in AAD12768 (PubMed:9838117).Curated
Sequence conflicti681 – 6811Missing in AAD12768 (PubMed:9838117).Curated
Sequence conflicti787 – 7871G → A in AAD12768 (PubMed:9838117).Curated
Sequence conflicti793 – 7931D → H in AAD12768 (PubMed:9838117).Curated
Sequence conflicti849 – 8491H → T in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1079 – 10813LAH → FG in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1092 – 10921V → A in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1140 – 11401D → DR in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1153 – 11531I → T in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1185 – 11851K → KP in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1413 – 14153WPT → GQP in AAD12768 (PubMed:9838117).Curated
Sequence conflicti1463 – 14631P → Q in AAD12768 (PubMed:9838117).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67160 Genomic DNA. Translation: AAD12768.1.
AC114002 Genomic DNA. No translation available.
AC155819 Genomic DNA. No translation available.
AK041016 mRNA. No translation available.
PIRiT42724.
UniGeneiMm.35059.
Mm.466962.
Mm.474991.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67160 Genomic DNA. Translation: AAD12768.1.
AC114002 Genomic DNA. No translation available.
AC155819 Genomic DNA. No translation available.
AK041016 mRNA. No translation available.
PIRiT42724.
UniGeneiMm.35059.
Mm.466962.
Mm.474991.

3D structure databases

ProteinModelPortaliP97393.
SMRiP97393. Positions 12-248, 1244-1455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97393. 1 interaction.
MINTiMINT-1733994.
STRINGi10090.ENSMUSP00000106353.

PTM databases

iPTMnetiP97393.
PhosphoSiteiP97393.

Proteomic databases

EPDiP97393.
MaxQBiP97393.
PaxDbiP97393.
PRIDEiP97393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1332637. Arhgap5.

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
HOVERGENiHBG051844.
InParanoidiP97393.

Miscellaneous databases

PROiP97393.
SOURCEiSearch...

Gene expression databases

CleanExiMM_ARHGAP5.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, genomic organization and chromosomal assignment of the mouse p190-B gene."
    Burbelo P.D., Finegold A.A., Kozak C.A., Yamada Y., Takami H.
    Biochim. Biophys. Acta 1443:203-210(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 1-1149.
    Strain: C57BL/6J.
    Tissue: Aorta and Vein.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194; SER-1201 AND SER-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas and Testis.

Entry informationi

Entry nameiRHG05_MOUSE
AccessioniPrimary (citable) accession number: P97393
Secondary accession number(s): E9Q0L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 127 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.