Q52LW3 (RHG29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GTPase-activating protein 29

Alternative name(s):
PTPL1-associated RhoGAP protein 1
Rho-type GTPase-activating protein 29

Gene names

Name:	ARHGAP29
Synonyms:	PARG1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. Ref.1 Ref.7
Subunit structure	Interacts with PTPN13/PTPL1. Interacts with RAP2A via its coiled coil domain. Ref.1 Ref.7
Tissue specificity	Widely expressed. Highly expressed in skeletal muscle and heart. Expressed at intermediate level in placenta, liver and pancreas. Weakly expressed in brain, lung and kidney. Ref.1
Induction	Strongly down-regulated in mantle-cell lymphomas. Up-regulated in migrating glioma cells. Ref.6 Ref.9
Sequence similarities	Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Rho-GAP domain.
Sequence caution	The sequence AAH67839.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	Rho GTPase activator activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q52LW3-1)

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: Q52LW3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     383-393: EEANELYKVCV → TIFFFFICKLN
     394-1261: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1261	1261	Rho GTPase-activating protein 29		PRO_0000317582
Regions
	Domain	671 – 886	216	Rho-GAP
	Zinc finger	612 – 657	46	Phorbol-ester/DAG-type
	Region	1258 – 1261	4	Interaction with PTPN13/PTPL1
	Coiled coil	296 – 418	123	Potential
Amino acid modifications
	Modified residue	171	1	Phosphoserine Ref.10
	Modified residue	176	1	Phosphoserine Ref.10
	Modified residue	179	1	Phosphoserine Ref.10
	Modified residue	190	1	Phosphoserine Ref.10
	Modified residue	913	1	Phosphoserine Ref.8
	Modified residue	930	1	Phosphoserine Ref.11
	Modified residue	949	1	Phosphoserine Ref.10
	Modified residue	1019	1	Phosphoserine Ref.8
	Modified residue	1029	1	Phosphoserine Ref.10
	Modified residue	1146	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	383 – 393	11	EEANELYKVCV → TIFFFFICKLN in isoform 2.		VSP_031058
	Alternative sequence	394 – 1261	868	Missing in isoform 2.		VSP_031059
	Natural variant	552	1	S → C in a breast cancer sample; somatic mutation. Ref.12		VAR_038552
	Natural variant	1192	1	P → L. Corresponds to variant rs11165091 [ dbSNP | Ensembl ].		VAR_049145
	Natural variant	1255	1	G → D. Ref.1 Ref.5 Corresponds to variant rs1999272 [ dbSNP | Ensembl ].		VAR_038553
Experimental info
	Sequence conflict	58	1	M → I in AAB81012. Ref.1
	Sequence conflict	160	1	L → F in AAB81012. Ref.1
	Sequence conflict	166	1	S → Y in AAH67839. Ref.4
	Sequence conflict	212	1	A → V in BAD92110. Ref.5
	Sequence conflict	386	1	N → D in AAB81012. Ref.1
	Sequence conflict	403	1	L → V in AAB81012. Ref.1
	Sequence conflict	446	1	S → R in AAB81012. Ref.1
	Sequence conflict	452	1	D → G in AAB81012. Ref.1
	Sequence conflict	675	1	Q → L in AAB81012. Ref.1
	Sequence conflict	720	1	Q → L in AAB81012. Ref.1
	Sequence conflict	856	1	T → Q in AAB81012. Ref.1
	Sequence conflict	991	1	T → A in AAB81012. Ref.1
	Sequence conflict	1190	1	V → C in AAB81012. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 3E46445EA5DA76C8	FASTA	1,261	142,064
	10 20 30 40 50 60 MIAHKQKKTK KKRAWASGQL STDITTSEMG LKSLSSNSIF DPDYIKELVN DIRKFSHMLL 70 80 90 100 110 120 YLKEAIFSDC FKEVIHIRLE ELLRVLKSIM NKHQNLNSVD LQNAAEMLTA KVKAVNFTEV 130 140 150 160 170 180 NEENKNDLFQ EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSRETK SFENVSVESV 190 200 210 220 230 240 DSSSEKGNFS PLELDNVLLK NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNM 250 260 270 280 290 300 VKLAEATRTN IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM 310 320 330 340 350 360 EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLSSSGGL 370 380 390 400 410 420 AKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR NDLENTKREI LAQLRTLVFQ 430 440 450 460 470 480 CDLTLKAVTV NLFHMQHLQA ASLADSLQSL CDSAKLYDPG QEYSEFVKAT NSTEEEKVDG 490 500 510 520 530 540 NVNKHLNSSQ PSGFGPANSL EDVVRLPDSS NKIEEDRCSN SADITGPSFI RSWTFGMFSD 550 560 570 580 590 600 SESTGGSSES RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SETGPNSLGT 610 620 630 640 650 660 FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFQGVECEE CLLVCHRKCL ENLVIICGHQ 670 680 690 700 710 720 KLPGKIHLFG AEFTQVAKKE PDGIPFILKI CASEIENRAL CLQGIYRVCG NKIKTEKLCQ 730 740 750 760 770 780 ALENGMHLVD ISEFSSHDIC DVLKLYLRQL PEPFILFRLY KEFIDLAKEI QHVNEEQETK 790 800 810 820 830 840 KNSLEDKKWP NMCIEINRIL LKSKDLLRQL PASNFNSLHF LIVHLKRVVD HAEENKMNSK 850 860 870 880 890 900 NLGVIFGPSL IRPRPTTAPI TISSLAEYSN QARLVEFLIT YSQKIFDGSL QPQDVMCSIG 910 920 930 940 950 960 VVDQGCFPKP LLSPEERDIE RSMKSLFFSS KEDIHTSESE SKIFERATSF EESERKQNAL 970 980 990 1000 1010 1020 GKCDACLSDK AQLLLDQEAE SASQKIEDGK TPKPLSLKSD RSTNNVERHT PRTKIRPVSL 1030 1040 1050 1060 1070 1080 PVDRLLLASP PNERNGRNMG NVNLDKFCKN PAFEGVNRKD AATTVCSKFN GFDQQTLQKI 1090 1100 1110 1120 1130 1140 QDKQYEQNSL TAKTTMIMPS ALQEKGVTTS LQISGDHSIN ATQPSKPYAE PVRSVREASE 1150 1160 1170 1180 1190 1200 RRSSDSYPLA PVRAPRTLQP QHWTTFYKPH APIISIRGNE EKPASPSAAV PPGTDHDPHG 1210 1220 1230 1240 1250 1260 LVVKSMPDPD KASACPGQAT GQPKEDSEEL GLPDVNPMCQ RPRLKRMQQF EDLEGEIPQF V
	Isoform 2 [UniParc]. Checksum: 6FF8EDA79AB7061C	FASTA	393	45,194
	10 20 30 40 50 60 MIAHKQKKTK KKRAWASGQL STDITTSEMG LKSLSSNSIF DPDYIKELVN DIRKFSHMLL 70 80 90 100 110 120 YLKEAIFSDC FKEVIHIRLE ELLRVLKSIM NKHQNLNSVD LQNAAEMLTA KVKAVNFTEV 130 140 150 160 170 180 NEENKNDLFQ EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSRETK SFENVSVESV 190 200 210 220 230 240 DSSSEKGNFS PLELDNVLLK NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNM 250 260 270 280 290 300 VKLAEATRTN IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM 310 320 330 340 350 360 EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLSSSGGL 370 380 390 AKNLNKQLEK KRRLEEEALQ KVTIFFFFIC KLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1." Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H. J. Biol. Chem. 272:24333-24338(1997) [PubMed: 9305890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 64-72; 221-228; 349-357; 456-468; 666-678; 943-946; 971-985; 1015-1024; 1069-1079 AND 1212-1224, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PTPN13, VARIANT ASP-1255. Tissue: Skeletal muscle.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Colon.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1261 (ISOFORM 1), VARIANT ASP-1255. Tissue: Brain.
[6]	"Glioma cell motility is associated with reduced transcription of proapoptotic and proliferation genes: a cDNA microarray analysis." Mariani L., Beaudry C., McDonough W.S., Hoelzinger D.B., Demuth T., Ross K.R., Berens T., Coons S.W., Watts G., Trent J.M., Wei J.S., Giese A., Berens M.E. J. Neurooncol. 53:161-176(2001) [PubMed: 11716068] [Abstract] Cited for: INDUCTION.
[7]	"PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector." Myagmar B.-E., Umikawa M., Asato T., Taira K., Oshiro M., Hino A., Takei K., Uezato H., Kariya K. Biochem. Biophys. Res. Commun. 329:1046-1052(2005) [PubMed: 15752761] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAP2A.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-913 AND SER-1019, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle-cell lymphomas." Ripperger T., von Neuhoff N., Kamphues K., Emura M., Lehmann U., Tauscher M., Schraders M., Groenen P., Skawran B., Rudolph C., Callet-Bauchu E., van Krieken J.H., Schlegelberger B., Steinemann D. Haematologica 92:460-468(2007) [PubMed: 17488656] [Abstract] Cited for: INDUCTION.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-176; SER-179; SER-190; SER-949; SER-1029 AND SER-1146, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-552.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U90920 mRNA. Translation: AAB81012.1. AL162735 Genomic DNA. Translation: CAH71750.1. AL162735 Genomic DNA. Translation: CAH71751.1. CH471097 Genomic DNA. Translation: EAW73052.1. CH471097 Genomic DNA. Translation: EAW73051.1. BC022483 mRNA. Translation: AAH22483.1. BC067839 mRNA. Translation: AAH67839.1. Sequence problems. BC093741 mRNA. Translation: AAH93741.1. BC093767 mRNA. Translation: AAH93767.1. AB208873 mRNA. Translation: BAD92110.1.
IPI	IPI00152011. IPI00646444.
PIR	E59430.
RefSeq	NP_004806.3. NM_004815.3.
UniGene	Hs.483238.
3D structure databases
HSSP	HSSP built from PDB template 1Y8F based on UniProtKB Q62768.
ProteinModelPortal	Q52LW3.
SMR	Q52LW3. Positions 191-470, 611-886.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q52LW3. 6 interactions.
MINT	MINT-1465191.
STRING	Q52LW3.
PTM databases
PhosphoSite	Q52LW3.
Polymorphism databases
DMDM	166977701.
Proteomic databases
PRIDE	Q52LW3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260526; ENSP00000260526; ENSG00000137962.
GeneID	9411.
KEGG	hsa:9411.
UCSC	uc001dqj.2. human. uc001dql.2. human.
Organism-specific databases
CTD	9411.
GeneCards	GC01M094634.
H-InvDB	HIX0021585.
HGNC	HGNC:30207. ARHGAP29.
HPA	HPA026534.
MIM	610496. gene.
neXtProt	NX_Q52LW3.
PharmGKB	PA128394548.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13601.
GeneTree	ENSGT00600000084287.
HOGENOM	HBG505975.
HOVERGEN	HBG108406.
InParanoid	Q52LW3.
OMA	ENGMHLV.
OrthoDB	EOG42JNQM.
PhylomeDB	Q52LW3.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q52LW3.
Bgee	Q52LW3.
CleanEx	HS_ARHGAP29.
Genevestigator	Q52LW3.
Family and domain databases
InterPro	IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Gene3D	G3DSA:1.10.555.10. RhoGAP. 1 hit.
Pfam	PF00130. C1_1. 1 hit. PF00620. RhoGAP. 1 hit. [Graphical view]
SMART	SM00109. C1. 1 hit. SM00324. RhoGAP. 1 hit. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit.
PROSITE	PS50238. RHOGAP. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35256.
SOURCE	Search...

Entry information

Entry name

RHG29_HUMAN

Accession

Primary (citable) accession number: Q52LW3
Secondary accession number(s): O15463 , Q59H86, Q5VYZ0, Q6NVX2, Q8TBI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 63 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.