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Q52LW3 (RHG29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1261 AA.
Sequence statusComplete.
Protein existenceEvidence 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. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. Ref.1 Ref.7

Subunit structure

Interacts with PTPN13/PTPL1. Interacts with RAP2A via its coiled coil domain. Interacts with RASIP1 By similarity. 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12611261Rho GTPase-activating protein 29
PRO_0000317582

Regions

Domain671 – 886216Rho-GAP
Zinc finger612 – 65746Phorbol-ester/DAG-type
Region1258 – 12614Interaction with PTPN13/PTPL1
Coiled coil296 – 418123 Potential

Amino acid modifications

Modified residue1711Phosphoserine By similarity
Modified residue1761Phosphoserine Ref.10
Modified residue1791Phosphoserine Ref.10
Modified residue1901Phosphoserine Ref.11
Modified residue9491Phosphoserine Ref.10
Modified residue10191Phosphoserine Ref.8
Modified residue11461Phosphoserine Ref.10

Natural variations

Alternative sequence383 – 39311EEANELYKVCV → TIFFFFICKLN in isoform 2.
VSP_031058
Alternative sequence394 – 1261868Missing in isoform 2.
VSP_031059
Natural variant5521S → C in a breast cancer sample; somatic mutation. Ref.12
VAR_038552
Natural variant11921P → L.
Corresponds to variant rs11165091 [ dbSNP | Ensembl ].
VAR_049145
Natural variant12551G → D. Ref.1 Ref.5
Corresponds to variant rs1999272 [ dbSNP | Ensembl ].
VAR_038553

Experimental info

Sequence conflict581M → I in AAB81012. Ref.1
Sequence conflict1601L → F in AAB81012. Ref.1
Sequence conflict1661S → Y in AAH67839. Ref.4
Sequence conflict2121A → V in BAD92110. Ref.5
Sequence conflict3861N → D in AAB81012. Ref.1
Sequence conflict4031L → V in AAB81012. Ref.1
Sequence conflict4461S → R in AAB81012. Ref.1
Sequence conflict4521D → G in AAB81012. Ref.1
Sequence conflict6751Q → L in AAB81012. Ref.1
Sequence conflict7201Q → L in AAB81012. Ref.1
Sequence conflict8561T → Q in AAB81012. Ref.1
Sequence conflict9911T → A in AAB81012. Ref.1
Sequence conflict11901V → C in AAB81012. Ref.1

Sequences

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

Last modified February 5, 2008. Version 2.
Checksum: 3E46445EA5DA76C8

FASTA1,261142,064
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 6FF8EDA79AB7061C
Show »

FASTA39345,194

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-179; SER-949 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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. expand/collapse author list , 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] [Europe PMC] [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.
CCDSCCDS748.1. [Q52LW3-1]
PIRE59430.
RefSeqNP_004806.3. NM_004815.3. [Q52LW3-1]
UniGeneHs.483238.

3D structure databases

ProteinModelPortalQ52LW3.
SMRQ52LW3. Positions 193-469, 612-886.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114806. 8 interactions.
IntActQ52LW3. 7 interactions.
MINTMINT-1465191.
STRING9606.ENSP00000260526.

PTM databases

PhosphoSiteQ52LW3.

Polymorphism databases

DMDM166977701.

Proteomic databases

MaxQBQ52LW3.
PaxDbQ52LW3.
PRIDEQ52LW3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260526; ENSP00000260526; ENSG00000137962. [Q52LW3-1]
ENST00000370217; ENSP00000359237; ENSG00000137962. [Q52LW3-2]
GeneID9411.
KEGGhsa:9411.
UCSCuc001dqj.4. human. [Q52LW3-1]
uc001dql.3. human. [Q52LW3-2]

Organism-specific databases

CTD9411.
GeneCardsGC01M094634.
H-InvDBHIX0021585.
HGNCHGNC:30207. ARHGAP29.
HPAHPA026534.
MIM610496. gene.
neXtProtNX_Q52LW3.
PharmGKBPA128394548.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310169.
HOGENOMHOG000043077.
HOVERGENHBG108406.
InParanoidQ52LW3.
OMAEYSNQAR.
PhylomeDBQ52LW3.
TreeFamTF351450.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ52LW3.
BgeeQ52LW3.
CleanExHS_ARHGAP29.
GenevestigatorQ52LW3.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
InterProIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 2 hits.
PROSITEPS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9411.
NextBio35256.
PROQ52LW3.
SOURCESearch...

Entry information

Entry nameRHG29_HUMAN
AccessionPrimary (citable) accession number: Q52LW3
Secondary accession number(s): O15463 expand/collapse secondary AC list , Q59H86, Q5VYZ0, Q6NVX2, Q8TBI6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 86 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM