GenomeNet

Database: UniProt
Entry: Q6ZUM4
LinkDB: Q6ZUM4
Original site: Q6ZUM4 
ID   RHG27_HUMAN             Reviewed;         889 AA.
AC   Q6ZUM4; A4FU35; A8K3N5; C9JTF3; Q494U0; Q6NWZ8; Q8WY58;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 3.
DT   26-NOV-2014, entry version 106.
DE   RecName: Full=Rho GTPase-activating protein 27;
DE   AltName: Full=CIN85-associated multi-domain-containing Rho GTPase-activating protein 1;
DE   AltName: Full=Rho-type GTPase-activating protein 27;
DE   AltName: Full=SH3 domain-containing protein 20;
GN   Name=ARHGAP27; Synonyms=CAMGAP1, SH3D20; ORFNames=PP905;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA   Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA   Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA   Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo, and Prostate;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 270-889 (ISOFORMS 1 AND 3), AND VARIANT
RP   GLN-889.
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=15492870;
RA   Katoh Y., Katoh M.;
RT   "Identification and characterization of ARHGAP27 gene in silico.";
RL   Int. J. Mol. Med. 14:943-947(2004).
CC   -!- FUNCTION: Rho GTPase-activating protein which may be involved in
CC       clathrin-mediated endocytosis. GTPase activators for the Rho-type
CC       GTPases act by converting them to an inactive GDP-bound state. Has
CC       activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZUM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZUM4-2; Sequence=VSP_031053;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q6ZUM4-3; Sequence=VSP_031056;
CC         Note=No experimental confirmation available.;
CC       Name=4; Synonyms=SH3D20;
CC         IsoId=Q6ZUM4-4; Sequence=VSP_031054, VSP_031055;
CC   -!- TISSUE SPECIFICITY: Expressed in germinal center B-cell, spleen,
CC       chronic lymphocytic leukemia, pancreatic cancer and lung cancer.
CC       {ECO:0000269|PubMed:15492870}.
CC   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00145}.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00172}.
CC   -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00192}.
CC   -!- SIMILARITY: Contains 3 WW domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00224}.
CC   -!- CAUTION: According to HGNC, ARHGAP27 and SH3D20 are 2 separate
CC       genes, corresponding to isoform 2 and isoform 4, respectively.
CC       However, a rat transcript and paralog proteins with a similar
CC       domain structure suggest the existence of a single gene encoding
CC       for a protein of 889 residues as displayed here. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI01389.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAI01390.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAI01391.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AF258593; AAG23796.1; -; mRNA.
DR   EMBL; AK125535; BAC86196.1; -; mRNA.
DR   EMBL; AK290650; BAF83339.1; -; mRNA.
DR   EMBL; AC003070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067345; AAH67345.1; -; mRNA.
DR   EMBL; BC101388; AAI01389.1; ALT_INIT; mRNA.
DR   EMBL; BC101389; AAI01390.1; ALT_INIT; mRNA.
DR   EMBL; BC101390; AAI01391.1; ALT_INIT; mRNA.
DR   EMBL; BC101391; AAI01392.3; -; mRNA.
DR   CCDS; CCDS11498.1; -. [Q6ZUM4-2]
DR   CCDS; CCDS32670.1; -. [Q6ZUM4-4]
DR   CCDS; CCDS74082.1; -. [Q6ZUM4-1]
DR   RefSeq; NP_001269219.1; NM_001282290.1. [Q6ZUM4-1]
DR   RefSeq; NP_777579.2; NM_174919.3. [Q6ZUM4-4]
DR   RefSeq; NP_954976.1; NM_199282.2. [Q6ZUM4-2]
DR   RefSeq; XP_006721808.1; XM_006721745.1. [Q6ZUM4-1]
DR   RefSeq; XP_006721809.1; XM_006721746.1. [Q6ZUM4-1]
DR   RefSeq; XP_006725671.1; XM_006725608.1. [Q6ZUM4-1]
DR   RefSeq; XP_006725672.1; XM_006725609.1. [Q6ZUM4-1]
DR   UniGene; Hs.205326; -.
DR   PDB; 3PP2; X-ray; 1.42 A; A/B=491-613.
DR   PDBsum; 3PP2; -.
DR   ProteinModelPortal; Q6ZUM4; -.
DR   SMR; Q6ZUM4; 10-67, 498-612, 678-886.
DR   BioGrid; 128369; 4.
DR   IntAct; Q6ZUM4; 1.
DR   MINT; MINT-5006179; -.
DR   STRING; 9606.ENSP00000366121; -.
DR   PhosphoSite; Q6ZUM4; -.
DR   DMDM; 300669680; -.
DR   MaxQB; Q6ZUM4; -.
DR   PaxDb; Q6ZUM4; -.
DR   PRIDE; Q6ZUM4; -.
DR   Ensembl; ENST00000290470; ENSP00000290470; ENSG00000159314. [Q6ZUM4-4]
DR   Ensembl; ENST00000376922; ENSP00000366121; ENSG00000159314. [Q6ZUM4-2]
DR   Ensembl; ENST00000428638; ENSP00000403323; ENSG00000159314. [Q6ZUM4-1]
DR   Ensembl; ENST00000528273; ENSP00000436137; ENSG00000159314. [Q6ZUM4-4]
DR   Ensembl; ENST00000528384; ENSP00000431591; ENSG00000159314.
DR   Ensembl; ENST00000610792; ENSP00000477741; ENSG00000276907. [Q6ZUM4-1]
DR   Ensembl; ENST00000611188; ENSP00000481302; ENSG00000276907. [Q6ZUM4-4]
DR   Ensembl; ENST00000616021; ENSP00000478738; ENSG00000276907. [Q6ZUM4-2]
DR   GeneID; 201176; -.
DR   KEGG; hsa:201176; -.
DR   UCSC; uc002iix.3; human. [Q6ZUM4-1]
DR   UCSC; uc010dal.3; human. [Q6ZUM4-4]
DR   CTD; 201176; -.
DR   GeneCards; GC17M043538; -.
DR   HGNC; HGNC:31813; ARHGAP27.
DR   HPA; HPA023919; -.
DR   MIM; 610591; gene.
DR   neXtProt; NX_Q6ZUM4; -.
DR   PharmGKB; PA134873327; -.
DR   eggNOG; NOG279563; -.
DR   GeneTree; ENSGT00760000118882; -.
DR   HOVERGEN; HBG005328; -.
DR   InParanoid; Q6ZUM4; -.
DR   OMA; TPEYTVD; -.
DR   PhylomeDB; Q6ZUM4; -.
DR   TreeFam; TF329345; -.
DR   SignaLink; Q6ZUM4; -.
DR   GenomeRNAi; 201176; -.
DR   NextBio; 90073; -.
DR   PRO; PR:Q6ZUM4; -.
DR   Bgee; Q6ZUM4; -.
DR   CleanEx; HS_ARHGAP27; -.
DR   ExpressionAtlas; Q6ZUM4; baseline and differential.
DR   Genevestigator; Q6ZUM4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; ISS:HGNC.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030675; F:Rac GTPase activator activity; ISS:HGNC.
DR   GO; GO:0017124; F:SH3 domain binding; ISS:HGNC.
DR   GO; GO:0043089; P:positive regulation of Cdc42 GTPase activity; ISS:HGNC.
DR   GO; GO:0032855; P:positive regulation of Rac GTPase activity; ISS:GOC.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR011047; Quinonprotein_ADH-like_supfam.
DR   InterPro; IPR015767; Rho_GTPase_act.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001202; WW_dom.
DR   PANTHER; PTHR23181; PTHR23181; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00456; WW; 3.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   SUPFAM; SSF51045; SSF51045; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   Endocytosis; GTPase activation; Membrane; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; SH3 domain.
FT   CHAIN         1    889       Rho GTPase-activating protein 27.
FT                                /FTId=PRO_0000317578.
FT   DOMAIN        8     69       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   DOMAIN      246    280       WW 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      299    333       WW 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      411    444       WW 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      496    612       PH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00145}.
FT   DOMAIN      697    886       Rho-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00172}.
FT   MOD_RES     216    216       Phosphoserine. {ECO:0000250}.
FT   VAR_SEQ       1    341       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_031053.
FT   VAR_SEQ     221    263       DDPPEPVYANIERQPRATSPGAAAAPLPSPVWETHTDAGTG
FT                                RP -> PPRALGRGGGWRARDRARTEPGRKETRSAQRRARR
FT                                PPLSEDFG (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:15498874}.
FT                                /FTId=VSP_031054.
FT   VAR_SEQ     264    889       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:15498874}.
FT                                /FTId=VSP_031055.
FT   VAR_SEQ     416    442       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_031056.
FT   VARIANT     889    889       H -> Q (in dbSNP:rs34793644).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_038551.
FT   CONFLICT     41     41       S -> N (in Ref. 1; AAG23796).
FT                                {ECO:0000305}.
FT   CONFLICT    162    162       C -> R (in Ref. 2; BAF83339).
FT                                {ECO:0000305}.
FT   CONFLICT    213    213       P -> R (in Ref. 4; AAH67345).
FT                                {ECO:0000305}.
FT   STRAND      499    510       {ECO:0000244|PDB:3PP2}.
FT   STRAND      521    528       {ECO:0000244|PDB:3PP2}.
FT   STRAND      531    536       {ECO:0000244|PDB:3PP2}.
FT   HELIX       549    552       {ECO:0000244|PDB:3PP2}.
FT   STRAND      554    560       {ECO:0000244|PDB:3PP2}.
FT   STRAND      565    568       {ECO:0000244|PDB:3PP2}.
FT   HELIX       571    573       {ECO:0000244|PDB:3PP2}.
FT   STRAND      575    583       {ECO:0000244|PDB:3PP2}.
FT   STRAND      589    593       {ECO:0000244|PDB:3PP2}.
FT   HELIX       597    611       {ECO:0000244|PDB:3PP2}.
SQ   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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