Full text data of GAS2L1
GAS2L1
(GAR22)
[Confidence: low (only semi-automatic identification from reviews)]
GAS2-like protein 1 (GAS2-related protein on chromosome 22; Growth arrest-specific protein 2-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
GAS2-like protein 1 (GAS2-related protein on chromosome 22; Growth arrest-specific protein 2-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99501
ID GA2L1_HUMAN Reviewed; 681 AA.
AC Q99501; Q53EN7; Q92640; Q9BUY9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=GAS2-like protein 1;
DE AltName: Full=GAS2-related protein on chromosome 22;
DE AltName: Full=Growth arrest-specific protein 2-like 1;
GN Name=GAS2L1; Synonyms=GAR22;
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 [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
RX PubMed=8975699; DOI=10.1006/geno.1996.0625;
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Identification of new members of the Gas2 and Ras families in the
RT 22q12 chromosome region.";
RL Genomics 38:247-254(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [4]
RP FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=12584248; DOI=10.1242/jcs.00272;
RA Goriounov D., Leung C.L., Liem R.K.;
RT "Protein products of human Gas2-related genes on chromosomes 17 and 22
RT (hGAR17 and hGAR22) associate with both microfilaments and
RT microtubules.";
RL J. Cell Sci. 116:1045-1058(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193; SER-306; THR-391;
RP SER-394; SER-492 AND THR-498, AND MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, 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).
CC -!- FUNCTION: Seems to be involved in the cross-linking of
CC microtubules and microfilaments.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Beta;
CC IsoId=Q99501-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q99501-2; Sequence=VSP_015493;
CC Name=3;
CC IsoId=Q99501-3; Sequence=VSP_015494, VSP_015495;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the GAS2 family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 GAR domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y07848; CAA69176.1; -; Genomic_DNA.
DR EMBL; Y07846; CAA69174.1; -; mRNA.
DR EMBL; AK223602; BAD97322.1; -; mRNA.
DR EMBL; BC001782; AAH01782.1; -; mRNA.
DR EMBL; BC007624; AAH07624.1; -; mRNA.
DR EMBL; BC011047; AAH11047.1; -; mRNA.
DR RefSeq; NP_006469.2; NM_006478.4.
DR RefSeq; NP_689422.1; NM_152236.2.
DR UniGene; Hs.322852; -.
DR ProteinModelPortal; Q99501; -.
DR SMR; Q99501; 219-275.
DR STRING; 9606.ENSP00000344012; -.
DR PhosphoSite; Q99501; -.
DR DMDM; 73915341; -.
DR PaxDb; Q99501; -.
DR PRIDE; Q99501; -.
DR Ensembl; ENST00000341313; ENSP00000344012; ENSG00000185340.
DR Ensembl; ENST00000360113; ENSP00000353229; ENSG00000185340.
DR GeneID; 10634; -.
DR KEGG; hsa:10634; -.
DR CTD; 10634; -.
DR GeneCards; GC22P029702; -.
DR HGNC; HGNC:16955; GAS2L1.
DR MIM; 602128; gene.
DR neXtProt; NX_Q99501; -.
DR PharmGKB; PA38195; -.
DR eggNOG; NOG322939; -.
DR HOGENOM; HOG000007404; -.
DR HOVERGEN; HBG079404; -.
DR InParanoid; Q99501; -.
DR OrthoDB; EOG7VTDR1; -.
DR GeneWiki; GAS2L1; -.
DR GenomeRNAi; 10634; -.
DR NextBio; 40413; -.
DR PRO; PR:Q99501; -.
DR ArrayExpress; Q99501; -.
DR Bgee; Q99501; -.
DR CleanEx; HS_GAS2L1; -.
DR Genevestigator; Q99501; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0008093; F:cytoskeletal adaptor activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR003108; GAS2_dom.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51460; GAR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 681 GAS2-like protein 1.
FT /FTId=PRO_0000190442.
FT DOMAIN 27 147 CH.
FT DOMAIN 203 275 GAR.
FT MOD_RES 193 193 Phosphothreonine.
FT MOD_RES 306 306 Phosphoserine.
FT MOD_RES 352 352 Phosphoserine.
FT MOD_RES 391 391 Phosphothreonine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 492 492 Phosphoserine.
FT MOD_RES 498 498 Phosphothreonine.
FT VAR_SEQ 280 329 AHRPPQPRVCTFSPQRVSPTTSPRPASPVPGSERRGSRPEM
FT TPVSLRSTK -> GPGISCPPIPAPAATPGTVTPQPPPPRA
FT APLVPAVMTQALAPGGSDPAGG (in isoform 3).
FT /FTId=VSP_015494.
FT VAR_SEQ 330 681 Missing (in isoform 3).
FT /FTId=VSP_015495.
FT VAR_SEQ 338 681 Missing (in isoform 2).
FT /FTId=VSP_015493.
FT VARIANT 490 490 S -> G (in dbSNP:rs34124440).
FT /FTId=VAR_059974.
FT CONFLICT 544 544 V -> A (in Ref. 2; BAD97322 and 3;
FT AAH11047).
FT CONFLICT 593 593 P -> S (in Ref. 2; BAD97322).
FT CONFLICT 666 666 H -> R (in Ref. 2; BAD97322).
SQ SEQUENCE 681 AA; 72717 MW; A23A10748535D900 CRC64;
MADPVAGIAG SAAKSVRPFR SSEAYVEAMK EDLAEWLNAL YGLGLPGGGD GFLTGLATGT
TLCQHANAVT EAARALAAAR PARGVAFQAH SVVPGSFMAR DNVATFIGWC RVELGVPEVL
MFETEDLVLR KNEKSVVLCL LEVARRGARL GLLAPRLVQF EQEIERELRA APPAPNAPAA
GEDTTETAPA PGTPARGPRM TPSDLRNLDE LVREILGRCT CPDQFPMIKV SEGKYRVGDS
SLLIFVRVLR SHVMVRVGGG WDTLEHYLDK HDPCRCSSTA HRPPQPRVCT FSPQRVSPTT
SPRPASPVPG SERRGSRPEM TPVSLRSTKE GPETPPRPRD QLPPHPRSRR YSGDSDSSAS
SAQSGPLGTR SDDTGTGPRR ERPSRRLTTG TPASPRRPPA LRSQSRDRLD RGRPRGAPGG
RGAQLSVPSP ARRARSQSRE EQAVLLVRRD RDGQHSWVPR GRGSGGSGRS TPQTPRARSP
AAPRLSRVSS PSPELGTTPA SIFRTPLQLD PQQEQQLFRR LEEEFLANAR ALEAVASVTP
TGPVPDPARA PDPPAPDSAY CSSSSSSSSL SVLGGKCGQP GDSGRTANGL PGPRSQALSS
SSDEGSPCPG MGGPLDAPGS PLACTEPSRT WARGRMDTQP DRKPSRIPTP RGPRRPSGPA
ELGTWHALHS VTPRAEPDSW M
//
ID GA2L1_HUMAN Reviewed; 681 AA.
AC Q99501; Q53EN7; Q92640; Q9BUY9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=GAS2-like protein 1;
DE AltName: Full=GAS2-related protein on chromosome 22;
DE AltName: Full=Growth arrest-specific protein 2-like 1;
GN Name=GAS2L1; Synonyms=GAR22;
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 [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
RX PubMed=8975699; DOI=10.1006/geno.1996.0625;
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Identification of new members of the Gas2 and Ras families in the
RT 22q12 chromosome region.";
RL Genomics 38:247-254(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [4]
RP FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=12584248; DOI=10.1242/jcs.00272;
RA Goriounov D., Leung C.L., Liem R.K.;
RT "Protein products of human Gas2-related genes on chromosomes 17 and 22
RT (hGAR17 and hGAR22) associate with both microfilaments and
RT microtubules.";
RL J. Cell Sci. 116:1045-1058(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193; SER-306; THR-391;
RP SER-394; SER-492 AND THR-498, AND MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, 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).
CC -!- FUNCTION: Seems to be involved in the cross-linking of
CC microtubules and microfilaments.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Beta;
CC IsoId=Q99501-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q99501-2; Sequence=VSP_015493;
CC Name=3;
CC IsoId=Q99501-3; Sequence=VSP_015494, VSP_015495;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the GAS2 family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 GAR domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y07848; CAA69176.1; -; Genomic_DNA.
DR EMBL; Y07846; CAA69174.1; -; mRNA.
DR EMBL; AK223602; BAD97322.1; -; mRNA.
DR EMBL; BC001782; AAH01782.1; -; mRNA.
DR EMBL; BC007624; AAH07624.1; -; mRNA.
DR EMBL; BC011047; AAH11047.1; -; mRNA.
DR RefSeq; NP_006469.2; NM_006478.4.
DR RefSeq; NP_689422.1; NM_152236.2.
DR UniGene; Hs.322852; -.
DR ProteinModelPortal; Q99501; -.
DR SMR; Q99501; 219-275.
DR STRING; 9606.ENSP00000344012; -.
DR PhosphoSite; Q99501; -.
DR DMDM; 73915341; -.
DR PaxDb; Q99501; -.
DR PRIDE; Q99501; -.
DR Ensembl; ENST00000341313; ENSP00000344012; ENSG00000185340.
DR Ensembl; ENST00000360113; ENSP00000353229; ENSG00000185340.
DR GeneID; 10634; -.
DR KEGG; hsa:10634; -.
DR CTD; 10634; -.
DR GeneCards; GC22P029702; -.
DR HGNC; HGNC:16955; GAS2L1.
DR MIM; 602128; gene.
DR neXtProt; NX_Q99501; -.
DR PharmGKB; PA38195; -.
DR eggNOG; NOG322939; -.
DR HOGENOM; HOG000007404; -.
DR HOVERGEN; HBG079404; -.
DR InParanoid; Q99501; -.
DR OrthoDB; EOG7VTDR1; -.
DR GeneWiki; GAS2L1; -.
DR GenomeRNAi; 10634; -.
DR NextBio; 40413; -.
DR PRO; PR:Q99501; -.
DR ArrayExpress; Q99501; -.
DR Bgee; Q99501; -.
DR CleanEx; HS_GAS2L1; -.
DR Genevestigator; Q99501; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0008093; F:cytoskeletal adaptor activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR003108; GAS2_dom.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51460; GAR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 681 GAS2-like protein 1.
FT /FTId=PRO_0000190442.
FT DOMAIN 27 147 CH.
FT DOMAIN 203 275 GAR.
FT MOD_RES 193 193 Phosphothreonine.
FT MOD_RES 306 306 Phosphoserine.
FT MOD_RES 352 352 Phosphoserine.
FT MOD_RES 391 391 Phosphothreonine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 492 492 Phosphoserine.
FT MOD_RES 498 498 Phosphothreonine.
FT VAR_SEQ 280 329 AHRPPQPRVCTFSPQRVSPTTSPRPASPVPGSERRGSRPEM
FT TPVSLRSTK -> GPGISCPPIPAPAATPGTVTPQPPPPRA
FT APLVPAVMTQALAPGGSDPAGG (in isoform 3).
FT /FTId=VSP_015494.
FT VAR_SEQ 330 681 Missing (in isoform 3).
FT /FTId=VSP_015495.
FT VAR_SEQ 338 681 Missing (in isoform 2).
FT /FTId=VSP_015493.
FT VARIANT 490 490 S -> G (in dbSNP:rs34124440).
FT /FTId=VAR_059974.
FT CONFLICT 544 544 V -> A (in Ref. 2; BAD97322 and 3;
FT AAH11047).
FT CONFLICT 593 593 P -> S (in Ref. 2; BAD97322).
FT CONFLICT 666 666 H -> R (in Ref. 2; BAD97322).
SQ SEQUENCE 681 AA; 72717 MW; A23A10748535D900 CRC64;
MADPVAGIAG SAAKSVRPFR SSEAYVEAMK EDLAEWLNAL YGLGLPGGGD GFLTGLATGT
TLCQHANAVT EAARALAAAR PARGVAFQAH SVVPGSFMAR DNVATFIGWC RVELGVPEVL
MFETEDLVLR KNEKSVVLCL LEVARRGARL GLLAPRLVQF EQEIERELRA APPAPNAPAA
GEDTTETAPA PGTPARGPRM TPSDLRNLDE LVREILGRCT CPDQFPMIKV SEGKYRVGDS
SLLIFVRVLR SHVMVRVGGG WDTLEHYLDK HDPCRCSSTA HRPPQPRVCT FSPQRVSPTT
SPRPASPVPG SERRGSRPEM TPVSLRSTKE GPETPPRPRD QLPPHPRSRR YSGDSDSSAS
SAQSGPLGTR SDDTGTGPRR ERPSRRLTTG TPASPRRPPA LRSQSRDRLD RGRPRGAPGG
RGAQLSVPSP ARRARSQSRE EQAVLLVRRD RDGQHSWVPR GRGSGGSGRS TPQTPRARSP
AAPRLSRVSS PSPELGTTPA SIFRTPLQLD PQQEQQLFRR LEEEFLANAR ALEAVASVTP
TGPVPDPARA PDPPAPDSAY CSSSSSSSSL SVLGGKCGQP GDSGRTANGL PGPRSQALSS
SSDEGSPCPG MGGPLDAPGS PLACTEPSRT WARGRMDTQP DRKPSRIPTP RGPRRPSGPA
ELGTWHALHS VTPRAEPDSW M
//
MIM
602128
*RECORD*
*FIELD* NO
602128
*FIELD* TI
*602128 GROWTH ARREST-SPECIFIC 2-LIKE 1; GAS2L1
;;GAS2-RELATED ON CHROMOSOME 22;;
GAR22
read more*FIELD* TX
CLONING
Zucman-Rossi et al. (1996) sequenced 40 kb of DNA on a chromosome 22
cosmid and identified 2 new genes, GAS2L1, which they called GAR22, and
RRP22 (602220). Northern blot analysis revealed a 2.5-kb mRNA expressed
at low levels in all tissues tested. The authors identified 2
alternatively spliced mRNA species from fetal brain. The deduced amino
acid sequence of GAR22 is 41% identical to mouse Gas2 (602835), an
actin-associated protein expressed at high levels in growth-arrested
cells.
Goriounov et al. (2003) cloned alternatively spliced GAR22-alpha and
-beta isoforms. The alpha isoform contains 337 amino acids and has a
calculated molecular mass of 36.3 kD. The beta isoform contains 681
amino acids with a calculated molecular mass of 72.6 kD. The isoforms
share the first 337 amino acids, which contain a calponin homology (CH)
family actin-binding domain, followed by a GAS2-related (GAR) family
microtubule-binding domain. GAR22-beta shares 56% amino acid similarity
with GAR17-beta (GAS2L2; 611398) over the first 337 amino acids, with
62% identity over the CH domains and 75% identity over the GAR domains.
The GAR22-alpha and beta isoforms share 89% and 87% identity to mouse
Gar22-alpha and beta isoforms, respectively. Northern blot analysis of
human tissues detected 2.6-kb GAR22-beta and 3.1-kb GAR22-alpha
transcripts in all tissues tested with highest expression in brain,
kidney, heart, and liver. Goriounov et al. (2003) stated that expression
of the GAR22-beta transcript was much more abundant than that of
GAR22-alpha. Western blot analysis detected mouse Gar22-beta protein in
testis and brain, but mouse Gar22-alpha protein was not detected in
mouse tissues. Immunostaining of mouse testicular tissues localized
mouse Gar22-beta to the cytoplasm of germ cells and to the head of
spermatozoa. Immunofluorescence studies of GAR22 isoforms and mutant
constructs localized the alpha isoform to actin filaments in NIH3T3
cells. The GAR22 CH domain localized to actin filaments, and GAR domain
colocalized with microtubules in COS-7 cells. The GAR22-beta C-terminal
CT22 region also colocalized with microtubules.
GENE FUNCTION
Using in vitro binding assays, Goriounov et al. (2003) showed that the
GAR22-alpha isoform bound preassembled microfilaments but did not bind
microtubules, while the GAR22-beta isoform bound both microfilaments and
microtubules, confirming that the GAR22 CH domain binds actin and that
the GAR and CT22 domains bind microtubules. They showed that the CT22
domain protected microtubules from nocodazole-induced depolymerization.
Using actively proliferating or arrested cell lines, they demonstrated
that the GAR22-beta protein was induced by growth arrest and that it is
likely to be phosphorylated. GAR22-alpha protein was not detected.
Imunofluorescence and colocalization experiments in COS-7 cells,
demonstrated that both GAR22-beta and GAR17-beta may crosslink
microfilaments and microtubules.
GENE STRUCTURE
Zucman-Rossi et al. (1996) determined that the GAS2L1 gene contains 5
exons. Goriounov et al. (2003) stated that the GAR22 gene undergoes
alternative splicing of exon 5B.
MAPPING
Zucman-Rossi et al. (1996) mapped GAS2L1 and RRP22 (602220) between the
EWS (133450) and BAM22 (600157) loci at chromosome 22q12.
*FIELD* RF
1. Goriounov, D.; Leung, C. L.; Liem, R. K. H.: Protein products
of human Gas2-related genes on chromosomes 17 and 22 (hGAR17 and hGAR22)
associate with both microfilaments and microtubules. J. Cell Sci. 116:
1045-1058, 2003.
2. Zucman-Rossi, J.; Legoix, P.; Thomas, G.: Identification of new
members of the Gas2 and Ras families in the 22q12 chromosome region. Genomics 38:
247-254, 1996.
*FIELD* CN
Dorothy S. Reilly - updated: 8/29/2007
*FIELD* CD
Jennifer P. Macke: 11/17/1997
*FIELD* ED
wwang: 07/28/2008
wwang: 8/31/2007
terry: 8/29/2007
alopez: 7/10/1998
dholmes: 1/16/1998
dholmes: 1/6/1998
*RECORD*
*FIELD* NO
602128
*FIELD* TI
*602128 GROWTH ARREST-SPECIFIC 2-LIKE 1; GAS2L1
;;GAS2-RELATED ON CHROMOSOME 22;;
GAR22
read more*FIELD* TX
CLONING
Zucman-Rossi et al. (1996) sequenced 40 kb of DNA on a chromosome 22
cosmid and identified 2 new genes, GAS2L1, which they called GAR22, and
RRP22 (602220). Northern blot analysis revealed a 2.5-kb mRNA expressed
at low levels in all tissues tested. The authors identified 2
alternatively spliced mRNA species from fetal brain. The deduced amino
acid sequence of GAR22 is 41% identical to mouse Gas2 (602835), an
actin-associated protein expressed at high levels in growth-arrested
cells.
Goriounov et al. (2003) cloned alternatively spliced GAR22-alpha and
-beta isoforms. The alpha isoform contains 337 amino acids and has a
calculated molecular mass of 36.3 kD. The beta isoform contains 681
amino acids with a calculated molecular mass of 72.6 kD. The isoforms
share the first 337 amino acids, which contain a calponin homology (CH)
family actin-binding domain, followed by a GAS2-related (GAR) family
microtubule-binding domain. GAR22-beta shares 56% amino acid similarity
with GAR17-beta (GAS2L2; 611398) over the first 337 amino acids, with
62% identity over the CH domains and 75% identity over the GAR domains.
The GAR22-alpha and beta isoforms share 89% and 87% identity to mouse
Gar22-alpha and beta isoforms, respectively. Northern blot analysis of
human tissues detected 2.6-kb GAR22-beta and 3.1-kb GAR22-alpha
transcripts in all tissues tested with highest expression in brain,
kidney, heart, and liver. Goriounov et al. (2003) stated that expression
of the GAR22-beta transcript was much more abundant than that of
GAR22-alpha. Western blot analysis detected mouse Gar22-beta protein in
testis and brain, but mouse Gar22-alpha protein was not detected in
mouse tissues. Immunostaining of mouse testicular tissues localized
mouse Gar22-beta to the cytoplasm of germ cells and to the head of
spermatozoa. Immunofluorescence studies of GAR22 isoforms and mutant
constructs localized the alpha isoform to actin filaments in NIH3T3
cells. The GAR22 CH domain localized to actin filaments, and GAR domain
colocalized with microtubules in COS-7 cells. The GAR22-beta C-terminal
CT22 region also colocalized with microtubules.
GENE FUNCTION
Using in vitro binding assays, Goriounov et al. (2003) showed that the
GAR22-alpha isoform bound preassembled microfilaments but did not bind
microtubules, while the GAR22-beta isoform bound both microfilaments and
microtubules, confirming that the GAR22 CH domain binds actin and that
the GAR and CT22 domains bind microtubules. They showed that the CT22
domain protected microtubules from nocodazole-induced depolymerization.
Using actively proliferating or arrested cell lines, they demonstrated
that the GAR22-beta protein was induced by growth arrest and that it is
likely to be phosphorylated. GAR22-alpha protein was not detected.
Imunofluorescence and colocalization experiments in COS-7 cells,
demonstrated that both GAR22-beta and GAR17-beta may crosslink
microfilaments and microtubules.
GENE STRUCTURE
Zucman-Rossi et al. (1996) determined that the GAS2L1 gene contains 5
exons. Goriounov et al. (2003) stated that the GAR22 gene undergoes
alternative splicing of exon 5B.
MAPPING
Zucman-Rossi et al. (1996) mapped GAS2L1 and RRP22 (602220) between the
EWS (133450) and BAM22 (600157) loci at chromosome 22q12.
*FIELD* RF
1. Goriounov, D.; Leung, C. L.; Liem, R. K. H.: Protein products
of human Gas2-related genes on chromosomes 17 and 22 (hGAR17 and hGAR22)
associate with both microfilaments and microtubules. J. Cell Sci. 116:
1045-1058, 2003.
2. Zucman-Rossi, J.; Legoix, P.; Thomas, G.: Identification of new
members of the Gas2 and Ras families in the 22q12 chromosome region. Genomics 38:
247-254, 1996.
*FIELD* CN
Dorothy S. Reilly - updated: 8/29/2007
*FIELD* CD
Jennifer P. Macke: 11/17/1997
*FIELD* ED
wwang: 07/28/2008
wwang: 8/31/2007
terry: 8/29/2007
alopez: 7/10/1998
dholmes: 1/16/1998
dholmes: 1/6/1998