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Protein

Rho GTPase-activating protein 21

Gene

ARHGAP21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a GTPase-activating protein (GAP) for RHOA and CDC42. Downstream partner of ARF1 which may control Golgi apparatus structure and function. Also required for CTNNA1 recruitment to adherens junctions.2 Publications

GO - Molecular functioni

GO - Biological processi

  • establishment of Golgi localization Source: BHF-UCL
  • Golgi organization Source: BHF-UCL
  • maintenance of Golgi location Source: BHF-UCL
  • organelle transport along microtubule Source: BHF-UCL
  • positive regulation of GTPase activity Source: GOC
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 21
Alternative name(s):
Rho GTPase-activating protein 10
Rho-type GTPase-activating protein 21
Gene namesi
Name:ARHGAP21
Synonyms:ARHGAP10, KIAA1424
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23725. ARHGAP21.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • Golgi apparatus Source: BHF-UCL
  • Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi999 – 9991Y → A: Altered interaction with ARF1 and loss of association to membranes. 1 Publication
Mutagenesisi1053 – 10531I → A: Altered interaction with ARF1 and loss of association to membranes. 1 Publication
Mutagenesisi1183 – 11831R → A: Loss of GTPase activity and loss of function. 2 Publications

Organism-specific databases

PharmGKBiPA134973559.

Polymorphism and mutation databases

BioMutaiARHGAP21.
DMDMi74745129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19571957Rho GTPase-activating protein 21PRO_0000305245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei458 – 4581PhosphoserineCombined sources
Modified residuei716 – 7161PhosphoserineCombined sources
Modified residuei856 – 8561PhosphoserineCombined sources
Modified residuei861 – 8611PhosphoserineBy similarity
Modified residuei881 – 8811PhosphotyrosineCombined sources
Modified residuei923 – 9231PhosphoserineCombined sources
Modified residuei925 – 9251PhosphoserineBy similarity
Modified residuei1098 – 10981PhosphoserineBy similarity
Modified residuei1431 – 14311PhosphoserineCombined sources
Modified residuei1432 – 14321PhosphoserineCombined sources
Cross-linki1443 – 1443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei1515 – 15151PhosphothreonineCombined sources
Modified residuei1526 – 15261PhosphoserineCombined sources
Modified residuei1668 – 16681PhosphoserineCombined sources
Modified residuei1681 – 16811PhosphothreonineBy similarity
Modified residuei1916 – 19161PhosphoserineBy similarity

Post-translational modificationi

Sumoylated with SUMO2 and SUMO3 in proliferating lymphocytes.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5T5U3.
MaxQBiQ5T5U3.
PaxDbiQ5T5U3.
PRIDEiQ5T5U3.

PTM databases

iPTMnetiQ5T5U3.
PhosphoSiteiQ5T5U3.

Expressioni

Tissue specificityi

Widely expressed with higher expression in brain, heart, skeletal muscle and placenta.1 Publication

Inductioni

Up-regulated upon cell differentiation.1 Publication

Gene expression databases

BgeeiQ5T5U3.
CleanExiHS_ARHGAP10.
HS_ARHGAP21.
ExpressionAtlasiQ5T5U3. baseline and differential.
GenevisibleiQ5T5U3. HS.

Organism-specific databases

HPAiHPA036610.

Interactioni

Subunit structurei

Interacts with GTP-bound ARF1 and ARF6. Interacts with CTNNA1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arf1P840783EBI-1642518,EBI-2308190From a different organism.
EEF1DP296922EBI-1642518,EBI-358607

Protein-protein interaction databases

BioGridi121636. 41 interactions.
IntActiQ5T5U3. 43 interactions.
MINTiMINT-2811611.
STRINGi9606.ENSP00000379709.

Structurei

Secondary structure

1
1957
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 534Combined sources
Beta strandi56 – 583Combined sources
Beta strandi79 – 813Combined sources
Beta strandi108 – 1103Combined sources
Helixi111 – 1155Combined sources
Helixi136 – 1449Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi933 – 94311Combined sources
Beta strandi958 – 9658Combined sources
Beta strandi968 – 9736Combined sources
Beta strandi978 – 9803Combined sources
Beta strandi983 – 9853Combined sources
Beta strandi994 – 9974Combined sources
Beta strandi999 – 10013Combined sources
Beta strandi1005 – 10117Combined sources
Beta strandi1016 – 10205Combined sources
Helixi1024 – 103714Combined sources
Helixi1042 – 106221Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DHJNMR-A930-1041[»]
2J59X-ray2.10M/N/O/P/Q/R929-1096[»]
2YUYNMR-A46-158[»]
ProteinModelPortaliQ5T5U3.
SMRiQ5T5U3. Positions 47-158, 924-1041.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5T5U3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 158110PDZPROSITE-ProRule annotationAdd
BLAST
Domaini930 – 1039110PHPROSITE-ProRule annotationAdd
BLAST
Domaini1146 – 1338193Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni929 – 1096168Interaction with ARF1 and ARF6Add
BLAST
Regioni1591 – 1860270Interaction with CTNNA1Add
BLAST

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410KD1S. Eukaryota.
ENOG410YY7B. LUCA.
HOVERGENiHBG106694.
InParanoidiQ5T5U3.
OMAiHVTKPSF.
OrthoDBiEOG7CK361.
PhylomeDBiQ5T5U3.
TreeFamiTF329345.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5T5U3-1) [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
MATRRTGLSE GDGDKLKACE VSKNKDGKEQ SETVSLSEDE TFSWPGPKTV
60 70 80 90 100
TLKRTSQGFG FTLRHFIVYP PESAIQFSYK DEENGNRGGK QRNRLEPMDT
110 120 130 140 150
IFVKQVKEGG PAFEAGLCTG DRIIKVNGES VIGKTYSQVI ALIQNSDTTL
160 170 180 190 200
ELSVMPKDED ILQVLQFTKD VTALAYSQDA YLKGNEAYSG NARNIPEPPP
210 220 230 240 250
ICYPWLPSAP SAMAQPVEIS PPDSSLSKQQ TSTPVLTQPG RAYRMEIQVP
260 270 280 290 300
PSPTDVAKSN TAVCVCNESV RTVIVPSEKV VDLLSNRNNH TGPSHRTEEV
310 320 330 340 350
RYGVSEQTSL KTVSRTTSPP LSIPTTHLIH QPAGSRSLEP SGILLKSGNY
360 370 380 390 400
SGHSDGISSS RSQAVEAPSV SVNHYSPNSH QHIDWKNYKT YKEYIDNRRL
410 420 430 440 450
HIGCRTIQER LDSLRAASQS TTDYNQVVPN RTTLQGRRRS TSHDRVPQSV
460 470 480 490 500
QIRQRSVSQE RLEDSVLMKY CPRSASQGAL TSPSVSFSNH RTRSWDYIEG
510 520 530 540 550
QDETLENVNS GTPIPDSNGE KKQTYKWSGF TEQDDRRGIC ERPRQQEIHK
560 570 580 590 600
SFRGSNFTVA PSVVNSDNRR MSGRGVGSVS QFKKIPPDLK TLQSNRNFQT
610 620 630 640 650
TCGMSLPRGI SQDRSPLVKV RSNSLKAPST HVTKPSFSQK SFVSIKDQRP
660 670 680 690 700
VNHLHQNSLL NQQTWVRTDS APDQQVETGK SPSLSGASAK PAPQSSENAG
710 720 730 740 750
TSDLELPVSQ RNQDLSLQEA ETEQSDTLDN KEAVILREKP PSGRQTPQPL
760 770 780 790 800
RHQSYILAVN DQETGSDTTC WLPNDARREV HIKRMEERKA SSTSPPGDSL
810 820 830 840 850
ASIPFIDEPT SPSIDHDIAH IPASAVISAS TSQVPSIATV PPCLTTSAPL
860 870 880 890 900
IRRQLSHDHE SVGPPSLDAQ PNSKTERSKS YDEGLDDYRE DAKLSFKHVS
910 920 930 940 950
SLKGIKIADS QKSSEDSGSR KDSSSEVFSD AAKEGWLHFR PLVTDKGKRV
960 970 980 990 1000
GGSIRPWKQM YVVLRGHSLY LYKDKREQTT PSEEEQPISV NACLIDISYS
1010 1020 1030 1040 1050
ETKRKNVFRL TTSDCECLFQ AEDRDDMLAW IKTIQESSNL NEEDTGVTNR
1060 1070 1080 1090 1100
DLISRRIKEY NNLMSKAEQL PKTPRQSLSI RQTLLGAKSE PKTQSPHSPK
1110 1120 1130 1140 1150
EESERKLLSK DDTSPPKDKG TWRKGIPSIM RKTFEKKPTA TGTFGVRLDD
1160 1170 1180 1190 1200
CPPAHTNRYI PLIVDICCKL VEERGLEYTG IYRVPGNNAA ISSMQEELNK
1210 1220 1230 1240 1250
GMADIDIQDD KWRDLNVISS LLKSFFRKLP EPLFTNDKYA DFIEANRKED
1260 1270 1280 1290 1300
PLDRLKTLKR LIHDLPEHHY ETLKFLSAHL KTVAENSEKN KMEPRNLAIV
1310 1320 1330 1340 1350
FGPTLVRTSE DNMTHMVTHM PDQYKIVETL IQHHDWFFTE EGAEEPLTTV
1360 1370 1380 1390 1400
QEESTVDSQP VPNIDHLLTN IGRTGVSPGD VSDSATSDST KSKGSWGSGK
1410 1420 1430 1440 1450
DQYSRELLVS SIFAAASRKR KKPKEKAQPS SSEDELDNVF FKKENVEQCH
1460 1470 1480 1490 1500
NDTKEESKKE SETLGRKQKI IIAKENSTRK DPSTTKDEKI SLGKESTPSE
1510 1520 1530 1540 1550
EPSPPHNSKH NKSPTLSCRF AILKESPRSL LAQKSSHLEE TGSDSGTLLS
1560 1570 1580 1590 1600
TSSQASLARF SMKKSTSPET KHSEFLANVS TITSDYSTTS SATYLTSLDS
1610 1620 1630 1640 1650
SRLSPEVQSV AESKGDEADD ERSELISEGR PVETDSESEF PVFPTALTSE
1660 1670 1680 1690 1700
RLFRGKLQEV TKSSRRNSEG SELSCTEGSL TSSLDSRRQL FSSHKLIECD
1710 1720 1730 1740 1750
TLSRKKSARF KSDSGSLGDA KNEKEAPSLT KVFDVMKKGK STGSLLTPTR
1760 1770 1780 1790 1800
GESEKQEPTW KTKIADRLKL RPRAPADDMF GVGNHKVNAE TAKRKSIRRR
1810 1820 1830 1840 1850
HTLGGHRDAT EISVLNFWKV HEQSGERESE LSAVNRLKPK CSAQDLSISD
1860 1870 1880 1890 1900
WLARERLRTS TSDLSRGEIG DPQTENPSTR EIATTDTPLS LHCNTGSSSS
1910 1920 1930 1940 1950
TLASTNRPLL SIPPQSPDQI NGESFQNVSK NASSAANAQP HKLSETPGSK

AEFHPCL
Length:1,957
Mass (Da):217,331
Last modified:December 21, 2004 - v1
Checksum:iEEE781DED0166E69
GO
Isoform 3 (identifier: Q5T5U3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-174: Missing.
     1159-1174: YIPLIVDICCKLVEER → VGDTSPPDFLKSLIQF
     1175-1957: Missing.

Note: No experimental confirmation available.
Show »
Length:1,164
Mass (Da):129,244
Checksum:i80CF3F8A87B81B90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051S → N in AAM22955 (PubMed:12056806).Curated
Sequence conflicti900 – 9001S → P in AAM22955 (PubMed:12056806).Curated
Sequence conflicti1782 – 17821V → A in AAM22955 (PubMed:12056806).Curated
Sequence conflicti1949 – 19491S → T in AAM22955 (PubMed:12056806).Curated
Sequence conflicti1949 – 19491S → T in CAD39153 (PubMed:17974005).Curated
Sequence conflicti1949 – 19491S → T in AAH22931 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti712 – 7121N → S.2 Publications
Corresponds to variant rs3748222 [ dbSNP | Ensembl ].
VAR_035187
Natural varianti1593 – 15931T → A.
Corresponds to variant rs1133897 [ dbSNP | Ensembl ].
VAR_035188
Natural varianti1610 – 16101V → A.
Corresponds to variant rs1143051 [ dbSNP | Ensembl ].
VAR_035189
Natural varianti1628 – 16281E → K.
Corresponds to variant rs1143057 [ dbSNP | Ensembl ].
VAR_035190
Natural varianti1726 – 17261A → T.
Corresponds to variant rs1143075 [ dbSNP | Ensembl ].
VAR_035191
Natural varianti1949 – 19491S → N.
Corresponds to variant rs1127893 [ dbSNP | Ensembl ].
VAR_035192

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 17410Missing in isoform 3. 1 PublicationVSP_028298
Alternative sequencei1159 – 117416YIPLI…LVEER → VGDTSPPDFLKSLIQF in isoform 3. 1 PublicationVSP_028300Add
BLAST
Alternative sequencei1175 – 1957783Missing in isoform 3. 1 PublicationVSP_028301Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480466 mRNA. Translation: AAM22955.1.
AL355979, AL392104 Genomic DNA. Translation: CAI14323.1.
AL392104, AL355979 Genomic DNA. Translation: CAI40176.1.
AB037845 mRNA. Translation: BAA92662.2.
BX537570 mRNA. Translation: CAD97787.1.
AL834495 mRNA. Translation: CAD39153.1.
BC022931 mRNA. Translation: AAH22931.1.
PIRiA59438.
RefSeqiNP_065875.3. NM_020824.3.
XP_005252599.1. XM_005252542.2.
UniGeneiHs.524195.

Genome annotation databases

EnsembliENST00000320481; ENSP00000365604; ENSG00000107863.
ENST00000396432; ENSP00000379709; ENSG00000107863.
GeneIDi57584.
KEGGihsa:57584.
UCSCiuc001isb.2. human. [Q5T5U3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480466 mRNA. Translation: AAM22955.1.
AL355979, AL392104 Genomic DNA. Translation: CAI14323.1.
AL392104, AL355979 Genomic DNA. Translation: CAI40176.1.
AB037845 mRNA. Translation: BAA92662.2.
BX537570 mRNA. Translation: CAD97787.1.
AL834495 mRNA. Translation: CAD39153.1.
BC022931 mRNA. Translation: AAH22931.1.
PIRiA59438.
RefSeqiNP_065875.3. NM_020824.3.
XP_005252599.1. XM_005252542.2.
UniGeneiHs.524195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DHJNMR-A930-1041[»]
2J59X-ray2.10M/N/O/P/Q/R929-1096[»]
2YUYNMR-A46-158[»]
ProteinModelPortaliQ5T5U3.
SMRiQ5T5U3. Positions 47-158, 924-1041.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121636. 41 interactions.
IntActiQ5T5U3. 43 interactions.
MINTiMINT-2811611.
STRINGi9606.ENSP00000379709.

PTM databases

iPTMnetiQ5T5U3.
PhosphoSiteiQ5T5U3.

Polymorphism and mutation databases

BioMutaiARHGAP21.
DMDMi74745129.

Proteomic databases

EPDiQ5T5U3.
MaxQBiQ5T5U3.
PaxDbiQ5T5U3.
PRIDEiQ5T5U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320481; ENSP00000365604; ENSG00000107863.
ENST00000396432; ENSP00000379709; ENSG00000107863.
GeneIDi57584.
KEGGihsa:57584.
UCSCiuc001isb.2. human. [Q5T5U3-1]

Organism-specific databases

CTDi57584.
GeneCardsiARHGAP21.
HGNCiHGNC:23725. ARHGAP21.
HPAiHPA036610.
MIMi609870. gene.
neXtProtiNX_Q5T5U3.
PharmGKBiPA134973559.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KD1S. Eukaryota.
ENOG410YY7B. LUCA.
HOVERGENiHBG106694.
InParanoidiQ5T5U3.
OMAiHVTKPSF.
OrthoDBiEOG7CK361.
PhylomeDBiQ5T5U3.
TreeFamiTF329345.

Miscellaneous databases

ChiTaRSiARHGAP21. human.
EvolutionaryTraceiQ5T5U3.
GenomeRNAii57584.
NextBioi64150.
PROiQ5T5U3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T5U3.
CleanExiHS_ARHGAP10.
HS_ARHGAP21.
ExpressionAtlasiQ5T5U3. baseline and differential.
GenevisibleiQ5T5U3. HS.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ARHGAP10, a novel human gene coding for a potentially cytoskeletal Rho-GTPase activating protein."
    Basseres D.S., Tizzei E.V., Duarte A.A.S., Costa F.F., Saad S.T.O.
    Biochem. Biophys. Res. Commun. 294:579-585(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, VARIANT SER-712.
    Tissue: Brain.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-1957 (ISOFORM 1).
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1957 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-1957 (ISOFORM 1), VARIANT SER-712.
    Tissue: Amygdala and Cervix.
  6. "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] OF 1522-1957 (ISOFORM 1).
    Tissue: Urinary bladder.
  7. "Characterization of human ARHGAP10 gene in silico."
    Katoh M., Katoh M.
    Int. J. Oncol. 25:1201-1206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics."
    Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B., De Matteis M.A., Franco M., Chavrier P.
    Nat. Cell Biol. 7:353-364(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARF1 AND ARF6, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-1183.
  9. "ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion."
    Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.
    Nat. Cell Biol. 7:954-960(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTNNA1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-1183.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Role of the Arf6 GDP/GTP cycle and Arf6 GTPase-activating proteins in actin remodeling and intracellular transport."
    Klein S., Franco M., Chardin P., Luton F.
    J. Biol. Chem. 281:12352-12361(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF6.
  12. "Head and neck squamous cell carcinoma transcriptome analysis by comprehensive validated differential display."
    Carles A., Millon R., Cromer A., Ganguli G., Lemaire F., Young J., Wasylyk C., Muller D., Schultz I., Rabouel Y., Dembele D., Zhao C., Marchal P., Ducray C., Bracco L., Abecassis J., Poch O., Wasylyk B.
    Oncogene 25:1821-1831(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458; SER-923 AND SER-1668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-56; SER-716; SER-856; SER-1431; SER-1432 AND SER-1526, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Post-translational modification of the RhoGTPase activating protein 21, ARHGAP21, by SUMO2/3."
    Bigarella C.L., Vieira Ferro K.P., Barcellos K.S., Martins-de-Souza D., Traina F., Novello J.C., Olalla Saad S.T., Archangelo L.F.
    FEBS Lett. 586:3522-3528(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-1443.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-881 AND THR-1515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes."
    Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N., El Khadali F., Franco M., Chavrier P., Houdusse A.
    EMBO J. 26:1953-1962(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 929-1096 IN COMPLEX WITH ARF1, MUTAGENESIS OF TYR-999 AND ILE-1053, SUBCELLULAR LOCATION.
  21. "Solution structure of the PH domain of Rho GTPase-activating protein 21 from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 930-1041.

Entry informationi

Entry nameiRHG21_HUMAN
AccessioniPrimary (citable) accession number: Q5T5U3
Secondary accession number(s): Q0VF98
, Q7Z3P7, Q8N3A2, Q8NI19, Q8TBV5, Q9P2C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Depletion of ARHGAP21 induces cell spreading and accumulation of F-actin stress fibers.
Required for In1A-dependent entry of Listeria monocytogenes into cells.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.