Full text data of ACTR1B
ACTR1B
(CTRN2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Beta-centractin (Actin-related protein 1B; ARP1B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Beta-centractin (Actin-related protein 1B; ARP1B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P42025
ID ACTY_HUMAN Reviewed; 376 AA.
AC P42025; D3DVH2; Q53SK5; Q9BRB7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Beta-centractin;
DE AltName: Full=Actin-related protein 1B;
DE Short=ARP1B;
GN Name=ACTR1B; Synonyms=CTRN2;
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].
RC TISSUE=Testis;
RX PubMed=7696711; DOI=10.1091/mbc.5.12.1301;
RA Clark S.W., Staub O., Holzbaur E.L.F., Paschal B.M., Vallee R.B.,
RA Meyer D.I., Clark I.B.;
RT "Beta-centractin: characterization and distribution of a new member of
RT the centractin family of actin-related proteins.";
RL Mol. Biol. Cell 5:1301-1310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-93.
RC TISSUE=Lymph, 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 [5]
RP PROTEIN SEQUENCE OF 239-255, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [7]
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).
CC -!- FUNCTION: Component of a multi-subunit complex involved in
CC microtubule based vesicle motility. It is associated with the
CC centrosome.
CC -!- INTERACTION:
CC Q9QZB7:Actr10 (xeno); NbExp=2; IntAct=EBI-367493, EBI-367600;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily.
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; X82207; CAA57691.1; -; mRNA.
DR EMBL; AC017099; AAY24280.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01924.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01927.1; -; Genomic_DNA.
DR EMBL; BC004374; AAH04374.1; -; mRNA.
DR EMBL; BC006372; AAH06372.1; -; mRNA.
DR EMBL; BC010090; AAH10090.1; -; mRNA.
DR RefSeq; NP_005726.1; NM_005735.3.
DR UniGene; Hs.98791; -.
DR ProteinModelPortal; P42025; -.
DR SMR; P42025; 12-376.
DR IntAct; P42025; 12.
DR MINT; MINT-1374548; -.
DR STRING; 9606.ENSP00000289228; -.
DR PhosphoSite; P42025; -.
DR DMDM; 1168333; -.
DR OGP; P42025; -.
DR REPRODUCTION-2DPAGE; IPI00029469; -.
DR PaxDb; P42025; -.
DR PeptideAtlas; P42025; -.
DR PRIDE; P42025; -.
DR DNASU; 10120; -.
DR Ensembl; ENST00000289228; ENSP00000289228; ENSG00000115073.
DR GeneID; 10120; -.
DR KEGG; hsa:10120; -.
DR UCSC; uc002syb.2; human.
DR CTD; 10120; -.
DR GeneCards; GC02M098272; -.
DR HGNC; HGNC:168; ACTR1B.
DR MIM; 605144; gene.
DR neXtProt; NX_P42025; -.
DR PharmGKB; PA24487; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233340; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P42025; -.
DR KO; K16577; -.
DR OMA; VRYPMEH; -.
DR OrthoDB; EOG72G17C; -.
DR PhylomeDB; P42025; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P42025; -.
DR ChiTaRS; ACTR1B; human.
DR GeneWiki; ACTR1B; -.
DR GenomeRNAi; 10120; -.
DR NextBio; 38279; -.
DR PRO; PR:P42025; -.
DR ArrayExpress; P42025; -.
DR Bgee; P42025; -.
DR CleanEx; HS_ACTR1B; -.
DR Genevestigator; P42025; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nitration; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 376 Beta-centractin.
FT /FTId=PRO_0000089060.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 4 4 Nitrated tyrosine (By similarity).
FT VARIANT 93 93 V -> A (in dbSNP:rs11547231).
FT /FTId=VAR_025315.
FT VARIANT 143 143 A -> V (in dbSNP:rs11692435).
FT /FTId=VAR_048187.
SQ SEQUENCE 376 AA; 42293 MW; 24C24ECEE18B83BD CRC64;
MESYDIIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHMRVMAG ALEGDLFIGP
KAEEHRGLLT IRYPMEHGVV RDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPSKN
REKAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRVDIAGRDV SRYLRLLLRK EGVDFHTSAE FEVVRTIKER ACYLSINPQK DEALETEKVQ
YTLPDGSTLD VGPARFRAPE LLFQPDLVGD ESEGLHEVVA FAIHKSDMDL RRTLFANIVL
SGGSTLFKGF GDRLLSEVKK LAPKDIKIKI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGSRA IHRKTF
//
ID ACTY_HUMAN Reviewed; 376 AA.
AC P42025; D3DVH2; Q53SK5; Q9BRB7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Beta-centractin;
DE AltName: Full=Actin-related protein 1B;
DE Short=ARP1B;
GN Name=ACTR1B; Synonyms=CTRN2;
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].
RC TISSUE=Testis;
RX PubMed=7696711; DOI=10.1091/mbc.5.12.1301;
RA Clark S.W., Staub O., Holzbaur E.L.F., Paschal B.M., Vallee R.B.,
RA Meyer D.I., Clark I.B.;
RT "Beta-centractin: characterization and distribution of a new member of
RT the centractin family of actin-related proteins.";
RL Mol. Biol. Cell 5:1301-1310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-93.
RC TISSUE=Lymph, 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 [5]
RP PROTEIN SEQUENCE OF 239-255, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [7]
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).
CC -!- FUNCTION: Component of a multi-subunit complex involved in
CC microtubule based vesicle motility. It is associated with the
CC centrosome.
CC -!- INTERACTION:
CC Q9QZB7:Actr10 (xeno); NbExp=2; IntAct=EBI-367493, EBI-367600;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily.
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; X82207; CAA57691.1; -; mRNA.
DR EMBL; AC017099; AAY24280.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01924.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01927.1; -; Genomic_DNA.
DR EMBL; BC004374; AAH04374.1; -; mRNA.
DR EMBL; BC006372; AAH06372.1; -; mRNA.
DR EMBL; BC010090; AAH10090.1; -; mRNA.
DR RefSeq; NP_005726.1; NM_005735.3.
DR UniGene; Hs.98791; -.
DR ProteinModelPortal; P42025; -.
DR SMR; P42025; 12-376.
DR IntAct; P42025; 12.
DR MINT; MINT-1374548; -.
DR STRING; 9606.ENSP00000289228; -.
DR PhosphoSite; P42025; -.
DR DMDM; 1168333; -.
DR OGP; P42025; -.
DR REPRODUCTION-2DPAGE; IPI00029469; -.
DR PaxDb; P42025; -.
DR PeptideAtlas; P42025; -.
DR PRIDE; P42025; -.
DR DNASU; 10120; -.
DR Ensembl; ENST00000289228; ENSP00000289228; ENSG00000115073.
DR GeneID; 10120; -.
DR KEGG; hsa:10120; -.
DR UCSC; uc002syb.2; human.
DR CTD; 10120; -.
DR GeneCards; GC02M098272; -.
DR HGNC; HGNC:168; ACTR1B.
DR MIM; 605144; gene.
DR neXtProt; NX_P42025; -.
DR PharmGKB; PA24487; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233340; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P42025; -.
DR KO; K16577; -.
DR OMA; VRYPMEH; -.
DR OrthoDB; EOG72G17C; -.
DR PhylomeDB; P42025; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P42025; -.
DR ChiTaRS; ACTR1B; human.
DR GeneWiki; ACTR1B; -.
DR GenomeRNAi; 10120; -.
DR NextBio; 38279; -.
DR PRO; PR:P42025; -.
DR ArrayExpress; P42025; -.
DR Bgee; P42025; -.
DR CleanEx; HS_ACTR1B; -.
DR Genevestigator; P42025; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nitration; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 376 Beta-centractin.
FT /FTId=PRO_0000089060.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 4 4 Nitrated tyrosine (By similarity).
FT VARIANT 93 93 V -> A (in dbSNP:rs11547231).
FT /FTId=VAR_025315.
FT VARIANT 143 143 A -> V (in dbSNP:rs11692435).
FT /FTId=VAR_048187.
SQ SEQUENCE 376 AA; 42293 MW; 24C24ECEE18B83BD CRC64;
MESYDIIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHMRVMAG ALEGDLFIGP
KAEEHRGLLT IRYPMEHGVV RDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPSKN
REKAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRVDIAGRDV SRYLRLLLRK EGVDFHTSAE FEVVRTIKER ACYLSINPQK DEALETEKVQ
YTLPDGSTLD VGPARFRAPE LLFQPDLVGD ESEGLHEVVA FAIHKSDMDL RRTLFANIVL
SGGSTLFKGF GDRLLSEVKK LAPKDIKIKI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGSRA IHRKTF
//
MIM
605144
*RECORD*
*FIELD* NO
605144
*FIELD* TI
*605144 ACTIN-RELATED PROTEIN 1B; ACTR1B
;;ARP1B;;
CENTRACTIN, BETA;;
CTRN2
*FIELD* TX
read moreIsoforms of actin (e.g., ACTG1; 102560), in association with myosin
motor proteins (e.g., MYO1A; 601478), are required for cellular motile
processes. In addition to conventional actins, there are several
actin-related proteins (e.g., ACTR2; 604221). By searching an EST
database and by screening a testis cDNA library, Clark et al. (1994)
isolated cDNAs encoding ACTR1B, which they called beta-centractin. The
deduced 376-amino acid ACTR1B protein and the ACTR1A protein (605143)
are of equal length, and they share 90% amino acid identity and 96%
amino acid similarity. Northern blot analysis detected a 2.0-kb ACTR1B
transcript at variable levels in all tissues tested. Two-dimensional
immunoblot analysis determined that ACTR1B is expressed in the cytosol
as part of the dynactin complex, an activator of dynein-driven vesicle
movement (see 601143), as a 43-kD protein with a pI of 6.4; levels of
ACTR1B were at least 15-fold lower than those of ACTR1A.
By somatic cell hybrid analysis, Elsea et al. (1999) mapped the ACTR1B
gene to chromosome 2. They localized the ACTR1B gene to 2q11.1-q11.2
using FISH.
*FIELD* RF
1. Clark, S. W.; Staub, O.; Clark, I. B.; Holzbaur, E. L. F.; Paschal,
B. M.; Vallee, R. B.; Meyer, D. I.: Beta-centractin: characterization
and distribution of a new member of the centractin family of actin-related
proteins. Molec. Biol. Cell 5: 1301-1310, 1994.
2. Elsea, S. H.; Clark, I. B.; Juyal, R. C.; Meyer, D. J.; Meyer,
D. I.; Patel, P. I.: Assignment of beta-centractin (CTRN2) to human
chromosome 2 bands q11.1-q11.2 with somatic cell hybrids and in situ
hybridization. Cytogenet. Cell Genet. 84: 48-49, 1999.
*FIELD* CD
Paul J. Converse: 7/13/2000
*FIELD* ED
mgross: 07/13/2000
*RECORD*
*FIELD* NO
605144
*FIELD* TI
*605144 ACTIN-RELATED PROTEIN 1B; ACTR1B
;;ARP1B;;
CENTRACTIN, BETA;;
CTRN2
*FIELD* TX
read moreIsoforms of actin (e.g., ACTG1; 102560), in association with myosin
motor proteins (e.g., MYO1A; 601478), are required for cellular motile
processes. In addition to conventional actins, there are several
actin-related proteins (e.g., ACTR2; 604221). By searching an EST
database and by screening a testis cDNA library, Clark et al. (1994)
isolated cDNAs encoding ACTR1B, which they called beta-centractin. The
deduced 376-amino acid ACTR1B protein and the ACTR1A protein (605143)
are of equal length, and they share 90% amino acid identity and 96%
amino acid similarity. Northern blot analysis detected a 2.0-kb ACTR1B
transcript at variable levels in all tissues tested. Two-dimensional
immunoblot analysis determined that ACTR1B is expressed in the cytosol
as part of the dynactin complex, an activator of dynein-driven vesicle
movement (see 601143), as a 43-kD protein with a pI of 6.4; levels of
ACTR1B were at least 15-fold lower than those of ACTR1A.
By somatic cell hybrid analysis, Elsea et al. (1999) mapped the ACTR1B
gene to chromosome 2. They localized the ACTR1B gene to 2q11.1-q11.2
using FISH.
*FIELD* RF
1. Clark, S. W.; Staub, O.; Clark, I. B.; Holzbaur, E. L. F.; Paschal,
B. M.; Vallee, R. B.; Meyer, D. I.: Beta-centractin: characterization
and distribution of a new member of the centractin family of actin-related
proteins. Molec. Biol. Cell 5: 1301-1310, 1994.
2. Elsea, S. H.; Clark, I. B.; Juyal, R. C.; Meyer, D. J.; Meyer,
D. I.; Patel, P. I.: Assignment of beta-centractin (CTRN2) to human
chromosome 2 bands q11.1-q11.2 with somatic cell hybrids and in situ
hybridization. Cytogenet. Cell Genet. 84: 48-49, 1999.
*FIELD* CD
Paul J. Converse: 7/13/2000
*FIELD* ED
mgross: 07/13/2000