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Rho GTPase-activating protein 27 (CIN85-associated multi-domain-containing Rho GTPase-activating protein 1) (Rho-type GTPase-activating protein 27) (SH3 domain-containing protein 20)

 RHG27_HUMAN             Reviewed;         889 AA.
Q6ZUM4; A4FU35; A8K3N5; C9JTF3; Q494U0; Q6NWZ8; Q8WY58;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 3.
22-NOV-2017, entry version 135.
RecName: Full=Rho GTPase-activating protein 27;
AltName: Full=CIN85-associated multi-domain-containing Rho GTPase-activating protein 1;
AltName: Full=Rho-type GTPase-activating protein 27;
AltName: Full=SH3 domain-containing protein 20;
Name=ARHGAP27; Synonyms=CAMGAP1, SH3D20; ORFNames=PP905;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryo, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 270-889 (ISOFORMS 1 AND 3), AND VARIANT
GLN-889.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION, AND TISSUE SPECIFICITY.
PubMed=15492870;
Katoh Y., Katoh M.;
"Identification and characterization of ARHGAP27 gene in silico.";
Int. J. Mol. Med. 14:943-947(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-466, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Rho GTPase-activating protein which may be involved in
clathrin-mediated endocytosis. GTPase activators for the Rho-type
GTPases act by converting them to an inactive GDP-bound state. Has
activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6ZUM4-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZUM4-2; Sequence=VSP_031053;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6ZUM4-3; Sequence=VSP_031056;
Note=No experimental confirmation available.;
Name=4; Synonyms=SH3D20;
IsoId=Q6ZUM4-4; Sequence=VSP_031054, VSP_031055;
-!- TISSUE SPECIFICITY: Expressed in germinal center B-cell, spleen,
chronic lymphocytic leukemia, pancreatic cancer and lung cancer.
{ECO:0000269|PubMed:15492870}.
-!- CAUTION: According to HGNC, ARHGAP27 and SH3D20 are 2 separate
genes, corresponding to isoform 2 and isoform 4, respectively.
However, a rat transcript and paralog proteins with a similar
domain structure suggest the existence of a single gene encoding
for a protein of 889 residues as displayed here. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI01389.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI01390.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI01391.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF258593; AAG23796.1; -; mRNA.
EMBL; AK125535; BAC86196.1; -; mRNA.
EMBL; AK290650; BAF83339.1; -; mRNA.
EMBL; AC003070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC067345; AAH67345.1; -; mRNA.
EMBL; BC101388; AAI01389.1; ALT_INIT; mRNA.
EMBL; BC101389; AAI01390.1; ALT_INIT; mRNA.
EMBL; BC101390; AAI01391.1; ALT_INIT; mRNA.
EMBL; BC101391; AAI01392.3; -; mRNA.
CCDS; CCDS11498.1; -. [Q6ZUM4-2]
CCDS; CCDS32670.1; -. [Q6ZUM4-4]
CCDS; CCDS74082.1; -. [Q6ZUM4-1]
RefSeq; NP_001269219.1; NM_001282290.1. [Q6ZUM4-1]
RefSeq; NP_777579.2; NM_174919.3. [Q6ZUM4-4]
RefSeq; NP_954976.1; NM_199282.2. [Q6ZUM4-2]
RefSeq; XP_006721808.1; XM_006721745.2. [Q6ZUM4-1]
UniGene; Hs.205326; -.
PDB; 3PP2; X-ray; 1.42 A; A/B=491-613.
PDBsum; 3PP2; -.
ProteinModelPortal; Q6ZUM4; -.
SMR; Q6ZUM4; -.
BioGrid; 128369; 3.
IntAct; Q6ZUM4; 1.
MINT; MINT-5006179; -.
STRING; 9606.ENSP00000366121; -.
iPTMnet; Q6ZUM4; -.
PhosphoSitePlus; Q6ZUM4; -.
BioMuta; ARHGAP27; -.
DMDM; 300669680; -.
EPD; Q6ZUM4; -.
MaxQB; Q6ZUM4; -.
PaxDb; Q6ZUM4; -.
PeptideAtlas; Q6ZUM4; -.
PRIDE; Q6ZUM4; -.
Ensembl; ENST00000290470; ENSP00000290470; ENSG00000159314. [Q6ZUM4-4]
Ensembl; ENST00000376922; ENSP00000366121; ENSG00000159314. [Q6ZUM4-2]
Ensembl; ENST00000428638; ENSP00000403323; ENSG00000159314. [Q6ZUM4-1]
Ensembl; ENST00000528273; ENSP00000436137; ENSG00000159314. [Q6ZUM4-4]
Ensembl; ENST00000610792; ENSP00000477741; ENSG00000276907. [Q6ZUM4-1]
Ensembl; ENST00000611188; ENSP00000481302; ENSG00000276907. [Q6ZUM4-4]
Ensembl; ENST00000612916; ENSP00000480582; ENSG00000276836. [Q6ZUM4-2]
Ensembl; ENST00000616021; ENSP00000478738; ENSG00000276907. [Q6ZUM4-2]
Ensembl; ENST00000633003; ENSP00000487991; ENSG00000276907. [Q6ZUM4-4]
GeneID; 201176; -.
KEGG; hsa:201176; -.
UCSC; uc002iix.4; human. [Q6ZUM4-1]
CTD; 201176; -.
DisGeNET; 201176; -.
EuPathDB; HostDB:ENSG00000159314.11; -.
GeneCards; ARHGAP27; -.
HGNC; HGNC:31813; ARHGAP27.
HPA; HPA023919; -.
HPA; HPA053053; -.
MIM; 610591; gene.
neXtProt; NX_Q6ZUM4; -.
OpenTargets; ENSG00000159314; -.
PharmGKB; PA134873327; -.
eggNOG; KOG1450; Eukaryota.
eggNOG; KOG4269; Eukaryota.
eggNOG; ENOG410ZP6T; LUCA.
GeneTree; ENSGT00890000139322; -.
HOVERGEN; HBG005328; -.
InParanoid; Q6ZUM4; -.
KO; K20636; -.
OMA; ETVWEDE; -.
OrthoDB; EOG091G164H; -.
PhylomeDB; Q6ZUM4; -.
TreeFam; TF329345; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
SignaLink; Q6ZUM4; -.
GenomeRNAi; 201176; -.
PRO; PR:Q6ZUM4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000159314; -.
CleanEx; HS_ARHGAP27; -.
ExpressionAtlas; Q6ZUM4; baseline and differential.
Genevisible; Q6ZUM4; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; ISS:HGNC.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005096; F:GTPase activator activity; ISS:HGNC.
GO; GO:0017124; F:SH3 domain binding; ISS:HGNC.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:HGNC.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00201; WW; 3.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00169; PH; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00397; WW; 2.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00456; WW; 3.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF50998; SSF50998; 1.
SUPFAM; SSF51045; SSF51045; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Endocytosis; GTPase activation; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SH3 domain.
CHAIN 1 889 Rho GTPase-activating protein 27.
/FTId=PRO_0000317578.
DOMAIN 6 69 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 246 280 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 299 333 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 411 444 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 496 612 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 697 886 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:Q6TLK4}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 461 461 Phosphothreonine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 341 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_031053.
VAR_SEQ 221 263 DDPPEPVYANIERQPRATSPGAAAAPLPSPVWETHTDAGTG
RP -> PPRALGRGGGWRARDRARTEPGRKETRSAQRRARR
PPLSEDFG (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15498874}.
/FTId=VSP_031054.
VAR_SEQ 264 889 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15498874}.
/FTId=VSP_031055.
VAR_SEQ 416 442 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031056.
VARIANT 889 889 H -> Q (in dbSNP:rs117139057).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038551.
CONFLICT 41 41 S -> N (in Ref. 1; AAG23796).
{ECO:0000305}.
CONFLICT 162 162 C -> R (in Ref. 2; BAF83339).
{ECO:0000305}.
CONFLICT 213 213 P -> R (in Ref. 4; AAH67345).
{ECO:0000305}.
STRAND 499 510 {ECO:0000244|PDB:3PP2}.
STRAND 521 528 {ECO:0000244|PDB:3PP2}.
STRAND 531 536 {ECO:0000244|PDB:3PP2}.
HELIX 549 552 {ECO:0000244|PDB:3PP2}.
STRAND 554 560 {ECO:0000244|PDB:3PP2}.
STRAND 565 568 {ECO:0000244|PDB:3PP2}.
HELIX 571 573 {ECO:0000244|PDB:3PP2}.
STRAND 575 583 {ECO:0000244|PDB:3PP2}.
STRAND 589 593 {ECO:0000244|PDB:3PP2}.
HELIX 597 611 {ECO:0000244|PDB:3PP2}.
SEQUENCE 889 AA; 98396 MW; E341CCC4D012DA4C CRC64;
MAADVVGDVY VLVEHPFEYT GKDGRRVAIR PNERYRLLRR STEHWWHVRR EPGGRPFYLP
AQYVRELPAL GNPAAAAPPG PHPSPAAPEP LAYDYRFVSA AATAGPDGAP EESGGRASSL
CGPAQRGAAT QRSSLAPGLP ACLYLRPAAP VRPAQSLNDL ACAAVSPPAG LLGSSGSFKA
CSVAGSWVCP RPLARSDSEN VYEVIQDLHV PPPEESAEQV DDPPEPVYAN IERQPRATSP
GAAAAPLPSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE AAEGAASPAT SPASVDSHVS
LETEWGQYWD EESRRVFFYN PLTGETAWED EAENEPEEEL EMQPGLSPGS PGDPRPPTPE
TDYPESLTSY PEEDYSPVGS FGEPGPTSPL TTPPGWSCHV SQDKQMLYTN HFTQEQWVRL
EDPHGKPYFY NPEDSSVRWE LPQVPVPAPR SIHKSSQDGD TPAQASPPEE KVPAELDEVG
SWEEVSPATA AVRTKTLDKA GVLHRTKTAD KGKRLRKKHW SASWTVLEGG VLTFFKDSKT
SAAGGLRQPS KFSTPEYTVE LRGATLSWAP KDKSSRKNVL ELRSRDGSEY LIQHDSEAII
STWHKAIAQG IQELSAELPP EESESSRVDF GSSERLGSWQ EKEEDARPNA AAPALGPVGL
ESDLSKVRHK LRKFLQRRPT LQSLREKGYI KDQVFGCALA ALCERERSRV PRFVQQCIRA
VEARGLDIDG LYRISGNLAT IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE
PLFPFSHFRQ FIAAIKLQDQ ARRSRCVRDL VRSLPAPNHD TLRMLFQHLC RVIEHGEQNR
MSVQSVAIVF GPTLLRPEVE ETSMPMTMVF QNQVVELILQ QCADIFPPH


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EIAAB34658 Arhgap6,Mouse,Mus musculus,Rho GTPase-activating protein 6,Rho-type GTPase-activating protein 6,Rho-type GTPase-activating protein RhoGAPX-1
EIAAB34716 ARHGAP32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,GRIT,GTPase regulator interacting with TrkA,Homo sapiens,Human,KIAA0712,p200RhoGAP,p250G
EIAAB34702 ARHGAP26,Chicken,Gallus gallus,GRAF,GTPase regulator associated with focal adhesion kinase,Rho GTPase-activating protein 26,Rho-type GTPase-activating protein 26
EIAAB35871 GARNL4,GTPase-activating Rap_Ran-GAP domain-like protein 4,Homo sapiens,Human,KIAA1039,Rap1 GTPase-activating protein 2,RAP1GA2,Rap1GAP2,RAP1GAP2
EIAAB35872 Garnl4,GTPase-activating Rap_Ran-GAP domain-like protein 4,Kiaa1039,Mouse,Mus musculus,Rap1 GTPase-activating protein 2,Rap1ga2,Rap1GAP2,Rap1gap2
EIAAB39891 Arhgap14,Kiaa0411,Mouse,Mus musculus,Rho GTPase-activating protein 14,SLIT-ROBO Rho GTPase-activating protein 3,srGAP2,Srgap2,srGAP3,Srgap3,WAVE-associated Rac GTPase-activating protein,WRP


 

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