Full text data of ACAP2
ACAP2
(CENTB2, KIAA0041)
[Confidence: low (only semi-automatic identification from reviews)]
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2; Cnt-b2)
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2; Cnt-b2)
UniProt
Q15057
ID ACAP2_HUMAN Reviewed; 778 AA.
AC Q15057; A8K2V4; Q8N5Z8; Q9UQR3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-2003, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-beta-2;
DE Short=Cnt-b2;
GN Name=ACAP2; Synonyms=CENTB2, KIAA0041;
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 [MRNA], FUNCTION, ENZYME REGULATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-442.
RC TISSUE=Leukocyte;
RX PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J.,
RA Hsu V.W., Donaldson J.G., Randazzo P.A.;
RT "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT periphery.";
RL J. Cell Biol. 151:627-638(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC factor 6 (ARF6).
CC -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC direct and probably recruits ACAP2 to membranes. Interacts with
CC MICALL1; the interaction is indirect through RAB35 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane
CC protein (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in lung.
CC -!- SIMILARITY: Contains 3 ANK repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05064.2; Type=Erroneous initiation;
CC Sequence=CAB41450.1; Type=Frameshift; Positions=98, 106, 111;
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DR EMBL; AJ238248; CAB41450.1; ALT_FRAME; mRNA.
DR EMBL; D26069; BAA05064.2; ALT_INIT; mRNA.
DR EMBL; AK290369; BAF83058.1; -; mRNA.
DR EMBL; CH471052; EAW78027.1; -; Genomic_DNA.
DR EMBL; BC031005; AAH31005.1; -; mRNA.
DR EMBL; BC060767; AAH60767.1; -; mRNA.
DR RefSeq; NP_036419.3; NM_012287.5.
DR UniGene; Hs.593373; -.
DR ProteinModelPortal; Q15057; -.
DR SMR; Q15057; 7-360, 378-758.
DR IntAct; Q15057; 1.
DR STRING; 9606.ENSP00000324287; -.
DR PhosphoSite; Q15057; -.
DR DMDM; 39932727; -.
DR PaxDb; Q15057; -.
DR PeptideAtlas; Q15057; -.
DR PRIDE; Q15057; -.
DR Ensembl; ENST00000326793; ENSP00000324287; ENSG00000114331.
DR GeneID; 23527; -.
DR KEGG; hsa:23527; -.
DR UCSC; uc003fun.4; human.
DR CTD; 23527; -.
DR GeneCards; GC03M194995; -.
DR HGNC; HGNC:16469; ACAP2.
DR HPA; HPA034807; -.
DR HPA; HPA034808; -.
DR MIM; 607766; gene.
DR neXtProt; NX_Q15057; -.
DR PharmGKB; PA26407; -.
DR eggNOG; COG5347; -.
DR HOGENOM; HOG000220815; -.
DR HOVERGEN; HBG050889; -.
DR InParanoid; Q15057; -.
DR KO; K12489; -.
DR OMA; VYEAKIE; -.
DR OrthoDB; EOG7PVWNT; -.
DR PhylomeDB; Q15057; -.
DR ChiTaRS; ACAP2; human.
DR GeneWiki; CENTB2; -.
DR GenomeRNAi; 23527; -.
DR NextBio; 45992; -.
DR PRO; PR:Q15057; -.
DR ArrayExpress; Q15057; -.
DR Bgee; Q15057; -.
DR CleanEx; HS_ACAP2; -.
DR Genevestigator; Q15057; -.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001164; ArfGAP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS51021; BAR; FALSE_NEG.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Complete proteome; Endosome;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 778 Arf-GAP with coiled-coil, ANK repeat and
FT PH domain-containing protein 2.
FT /FTId=PRO_0000074210.
FT DOMAIN 1 226 BAR.
FT DOMAIN 266 361 PH.
FT DOMAIN 399 520 Arf-GAP.
FT REPEAT 640 669 ANK 1.
FT REPEAT 673 702 ANK 2.
FT REPEAT 706 735 ANK 3.
FT ZN_FING 414 437 C4-type.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT MOD_RES 742 742 Phosphotyrosine.
FT MUTAGEN 442 442 R->Q: Loss of GAP activity.
FT CONFLICT 5 5 V -> G (in Ref. 1; CAB41450).
FT CONFLICT 42 42 C -> G (in Ref. 1; CAB41450).
FT CONFLICT 229 229 V -> G (in Ref. 1; CAB41450).
FT CONFLICT 252 252 S -> R (in Ref. 1; CAB41450).
FT CONFLICT 258 258 E -> K (in Ref. 1; CAB41450).
FT CONFLICT 296 296 L -> V (in Ref. 1; CAB41450).
FT CONFLICT 564 564 G -> E (in Ref. 6; AAH60767).
SQ SEQUENCE 778 AA; 88029 MW; 64B620957FEE6195 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS
ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD
SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL
LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA
DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF
//
ID ACAP2_HUMAN Reviewed; 778 AA.
AC Q15057; A8K2V4; Q8N5Z8; Q9UQR3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-2003, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-beta-2;
DE Short=Cnt-b2;
GN Name=ACAP2; Synonyms=CENTB2, KIAA0041;
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 [MRNA], FUNCTION, ENZYME REGULATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-442.
RC TISSUE=Leukocyte;
RX PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J.,
RA Hsu V.W., Donaldson J.G., Randazzo P.A.;
RT "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT periphery.";
RL J. Cell Biol. 151:627-638(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC factor 6 (ARF6).
CC -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC direct and probably recruits ACAP2 to membranes. Interacts with
CC MICALL1; the interaction is indirect through RAB35 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane
CC protein (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in lung.
CC -!- SIMILARITY: Contains 3 ANK repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05064.2; Type=Erroneous initiation;
CC Sequence=CAB41450.1; Type=Frameshift; Positions=98, 106, 111;
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DR EMBL; AJ238248; CAB41450.1; ALT_FRAME; mRNA.
DR EMBL; D26069; BAA05064.2; ALT_INIT; mRNA.
DR EMBL; AK290369; BAF83058.1; -; mRNA.
DR EMBL; CH471052; EAW78027.1; -; Genomic_DNA.
DR EMBL; BC031005; AAH31005.1; -; mRNA.
DR EMBL; BC060767; AAH60767.1; -; mRNA.
DR RefSeq; NP_036419.3; NM_012287.5.
DR UniGene; Hs.593373; -.
DR ProteinModelPortal; Q15057; -.
DR SMR; Q15057; 7-360, 378-758.
DR IntAct; Q15057; 1.
DR STRING; 9606.ENSP00000324287; -.
DR PhosphoSite; Q15057; -.
DR DMDM; 39932727; -.
DR PaxDb; Q15057; -.
DR PeptideAtlas; Q15057; -.
DR PRIDE; Q15057; -.
DR Ensembl; ENST00000326793; ENSP00000324287; ENSG00000114331.
DR GeneID; 23527; -.
DR KEGG; hsa:23527; -.
DR UCSC; uc003fun.4; human.
DR CTD; 23527; -.
DR GeneCards; GC03M194995; -.
DR HGNC; HGNC:16469; ACAP2.
DR HPA; HPA034807; -.
DR HPA; HPA034808; -.
DR MIM; 607766; gene.
DR neXtProt; NX_Q15057; -.
DR PharmGKB; PA26407; -.
DR eggNOG; COG5347; -.
DR HOGENOM; HOG000220815; -.
DR HOVERGEN; HBG050889; -.
DR InParanoid; Q15057; -.
DR KO; K12489; -.
DR OMA; VYEAKIE; -.
DR OrthoDB; EOG7PVWNT; -.
DR PhylomeDB; Q15057; -.
DR ChiTaRS; ACAP2; human.
DR GeneWiki; CENTB2; -.
DR GenomeRNAi; 23527; -.
DR NextBio; 45992; -.
DR PRO; PR:Q15057; -.
DR ArrayExpress; Q15057; -.
DR Bgee; Q15057; -.
DR CleanEx; HS_ACAP2; -.
DR Genevestigator; Q15057; -.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001164; ArfGAP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS51021; BAR; FALSE_NEG.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Complete proteome; Endosome;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 778 Arf-GAP with coiled-coil, ANK repeat and
FT PH domain-containing protein 2.
FT /FTId=PRO_0000074210.
FT DOMAIN 1 226 BAR.
FT DOMAIN 266 361 PH.
FT DOMAIN 399 520 Arf-GAP.
FT REPEAT 640 669 ANK 1.
FT REPEAT 673 702 ANK 2.
FT REPEAT 706 735 ANK 3.
FT ZN_FING 414 437 C4-type.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT MOD_RES 742 742 Phosphotyrosine.
FT MUTAGEN 442 442 R->Q: Loss of GAP activity.
FT CONFLICT 5 5 V -> G (in Ref. 1; CAB41450).
FT CONFLICT 42 42 C -> G (in Ref. 1; CAB41450).
FT CONFLICT 229 229 V -> G (in Ref. 1; CAB41450).
FT CONFLICT 252 252 S -> R (in Ref. 1; CAB41450).
FT CONFLICT 258 258 E -> K (in Ref. 1; CAB41450).
FT CONFLICT 296 296 L -> V (in Ref. 1; CAB41450).
FT CONFLICT 564 564 G -> E (in Ref. 6; AAH60767).
SQ SEQUENCE 778 AA; 88029 MW; 64B620957FEE6195 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS
ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD
SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL
LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA
DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF
//
MIM
607766
*RECORD*
*FIELD* NO
607766
*FIELD* TI
*607766 CENTAURIN, BETA-2; CENTB2
;;KIAA0041;;
ARF-GAP WITH COILED-COIL, ANKYRIN REPEAT, AND PLECKSTRIN HOMOLOGY
read moreDOMAINS 2; ACAP2
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated myeloid cell line
cDNA library, Nomura et al. (1994) cloned a partial cDNA encoding
CENTB2, which they designated KIAA0041. The 3-prime untranslated region
of the CENTB2 mRNA contains an Alu repeat. CENTB2 shares 52% sequence
identity with CENTB1 (607763) and about 28% identity with ankyrin (see
106410). Northern blot analysis revealed ubiquitous expression, with
highest levels detected in peripheral blood leukocytes, followed by
placenta, kidney, spleen, and ovary. Lowest levels were detected in
brain.
Using the partial KIAA0041 sequence as probe, Jackson et al. (2000)
obtained a full-length cDNA encoding CENTB2, which they designated
ACAP2, from a lymphocyte cDNA library. The deduced 778-amino acid
protein contains 2 N-terminal coiled-coil regions, a pleckstrin homology
(PH) domain, an ARF-GAP domain (see ARF6; 600464), and C-terminal
ankyrin repeats. ACAP2 shares significant similarity with CENTB1, which
the authors called ACAP1, and 95% identity with mouse Acap2. It also
shares similarity with ASAP1 (605953) and PAP (603817) in the ARF-GAP
domain and in the overall domain structure. Jackson et al. (2000) also
identified homologous sequences in C. elegans, A. thaliana, and D.
melanogaster. By PCR, they detected ACAP2 mRNA expressed at similar
levels in all tissues examined. Western blot analysis detected ACAP2
expression in all cell lines examined.
By Northern blot analysis, Dowler et al. (2000) detected expression of a
4.5-kb Centb2 transcript in all mouse tissues tested.
GENE FUNCTION
Jackson et al. (2000) determined that ACAP1 and ACAP2 were recruited to
platelet-derived growth factor (PDGF; see 173430)-induced dorsal
membrane ruffles in NIH 3T3 mouse fibroblasts, and overexpression
inhibited ruffle formation. In vitro, ACAP1 and ACAP2 preferred ARF6 as
substrate rather than ARF1 (103180) or ARF5 (103188), and the GAP
activity of both ACAPs was dependent upon phosphatidylinositol
4,5-bisphosphate (PtdIns(4,5)P2). Mutation of a highly conserved
arginine in both ACAPs resulted in lack of ARF-GAP activity.
Overexpression in HeLa cells of either ACAP blocked the formation of
ARF6-dependent protrusions. Both ACAPs were also recruited to
peripheral, tubular membranes, where activation of ARF6 occurs and
allows membrane recycling back to the plasma membrane.
Dowler et al. (2000) determined that the isolated PH domain of mouse
Centb2 exhibited moderate affinity for PtdIns(3,5)P2, but it did not
bind any other phosphoinositides tested, including PtdIns(4,5)P2.
MAPPING
By PCR of a human/rodent hybrid panel, Nomura et al. (1994) mapped the
CENTB2 gene to chromosome 3.
*FIELD* RF
1. Dowler, S.; Currie, R. A.; Campbell, D. G.; Deak, M.; Kular, G.;
Downes, C. P.; Alessi, D. R.: Identification of pleckstrin-homology-domain-containing
proteins with novel phosphoinositide-binding specificities. Biochem.
J. 351: 19-31, 2000.
2. Jackson, T. R.; Brown, F. D.; Nie, Z.; Miura, K.; Foroni, L.; Sun,
J.; Hsu, V. W.; Donaldson, J. G.; Randazzo, P. A.: ACAPs are Arf6
GTPase-activating proteins that function in the cell periphery. J.
Cell Biol. 151: 627-638, 2000.
3. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Patricia A. Hartz: 5/8/2003
*FIELD* ED
mgross: 05/09/2003
mgross: 5/8/2003
*RECORD*
*FIELD* NO
607766
*FIELD* TI
*607766 CENTAURIN, BETA-2; CENTB2
;;KIAA0041;;
ARF-GAP WITH COILED-COIL, ANKYRIN REPEAT, AND PLECKSTRIN HOMOLOGY
read moreDOMAINS 2; ACAP2
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated myeloid cell line
cDNA library, Nomura et al. (1994) cloned a partial cDNA encoding
CENTB2, which they designated KIAA0041. The 3-prime untranslated region
of the CENTB2 mRNA contains an Alu repeat. CENTB2 shares 52% sequence
identity with CENTB1 (607763) and about 28% identity with ankyrin (see
106410). Northern blot analysis revealed ubiquitous expression, with
highest levels detected in peripheral blood leukocytes, followed by
placenta, kidney, spleen, and ovary. Lowest levels were detected in
brain.
Using the partial KIAA0041 sequence as probe, Jackson et al. (2000)
obtained a full-length cDNA encoding CENTB2, which they designated
ACAP2, from a lymphocyte cDNA library. The deduced 778-amino acid
protein contains 2 N-terminal coiled-coil regions, a pleckstrin homology
(PH) domain, an ARF-GAP domain (see ARF6; 600464), and C-terminal
ankyrin repeats. ACAP2 shares significant similarity with CENTB1, which
the authors called ACAP1, and 95% identity with mouse Acap2. It also
shares similarity with ASAP1 (605953) and PAP (603817) in the ARF-GAP
domain and in the overall domain structure. Jackson et al. (2000) also
identified homologous sequences in C. elegans, A. thaliana, and D.
melanogaster. By PCR, they detected ACAP2 mRNA expressed at similar
levels in all tissues examined. Western blot analysis detected ACAP2
expression in all cell lines examined.
By Northern blot analysis, Dowler et al. (2000) detected expression of a
4.5-kb Centb2 transcript in all mouse tissues tested.
GENE FUNCTION
Jackson et al. (2000) determined that ACAP1 and ACAP2 were recruited to
platelet-derived growth factor (PDGF; see 173430)-induced dorsal
membrane ruffles in NIH 3T3 mouse fibroblasts, and overexpression
inhibited ruffle formation. In vitro, ACAP1 and ACAP2 preferred ARF6 as
substrate rather than ARF1 (103180) or ARF5 (103188), and the GAP
activity of both ACAPs was dependent upon phosphatidylinositol
4,5-bisphosphate (PtdIns(4,5)P2). Mutation of a highly conserved
arginine in both ACAPs resulted in lack of ARF-GAP activity.
Overexpression in HeLa cells of either ACAP blocked the formation of
ARF6-dependent protrusions. Both ACAPs were also recruited to
peripheral, tubular membranes, where activation of ARF6 occurs and
allows membrane recycling back to the plasma membrane.
Dowler et al. (2000) determined that the isolated PH domain of mouse
Centb2 exhibited moderate affinity for PtdIns(3,5)P2, but it did not
bind any other phosphoinositides tested, including PtdIns(4,5)P2.
MAPPING
By PCR of a human/rodent hybrid panel, Nomura et al. (1994) mapped the
CENTB2 gene to chromosome 3.
*FIELD* RF
1. Dowler, S.; Currie, R. A.; Campbell, D. G.; Deak, M.; Kular, G.;
Downes, C. P.; Alessi, D. R.: Identification of pleckstrin-homology-domain-containing
proteins with novel phosphoinositide-binding specificities. Biochem.
J. 351: 19-31, 2000.
2. Jackson, T. R.; Brown, F. D.; Nie, Z.; Miura, K.; Foroni, L.; Sun,
J.; Hsu, V. W.; Donaldson, J. G.; Randazzo, P. A.: ACAPs are Arf6
GTPase-activating proteins that function in the cell periphery. J.
Cell Biol. 151: 627-638, 2000.
3. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Patricia A. Hartz: 5/8/2003
*FIELD* ED
mgross: 05/09/2003
mgross: 5/8/2003