Full text data of ACTBL2
ACTBL2
[Confidence: high (present in two of the MS resources)]
Beta-actin-like protein 2 (Kappa-actin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Beta-actin-like protein 2 (Kappa-actin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003269
IPI00003269 similar to RIKEN cDNA 4732495G21 gene HQGVMVGMGQKDCYVGDEAQSK unique similar to RIKEN cDNA 4732495G21 gene HQGVMVGMGQKDCYVGDEAQSK unique membrane n/a n/a n/a n/a n/a n/a n/a n/a 7 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoskeleton HQGVMVGMGQKDCYVGDEAQSK (identified at least 3 times) found at its expected molecular weight found at molecular weight
IPI00003269 similar to RIKEN cDNA 4732495G21 gene HQGVMVGMGQKDCYVGDEAQSK unique similar to RIKEN cDNA 4732495G21 gene HQGVMVGMGQKDCYVGDEAQSK unique membrane n/a n/a n/a n/a n/a n/a n/a n/a 7 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoskeleton HQGVMVGMGQKDCYVGDEAQSK (identified at least 3 times) found at its expected molecular weight found at molecular weight
UniProt
Q562R1
ID ACTBL_HUMAN Reviewed; 376 AA.
AC Q562R1; B2RPJ1; Q562R2; Q562S9; Q562X8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=Beta-actin-like protein 2;
DE AltName: Full=Kappa-actin;
GN Name=ACTBL2;
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].
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-187, AND INTERACTION WITH PFN1
RP AND PFDN1.
RC TISSUE=Hepatoma;
RX PubMed=16824795; DOI=10.1016/j.hepres.2006.05.003;
RA Chang K.-W., Yang P.-Y., Lai H.-Y., Yeh T.-S., Chen T.-C., Yeh C.-T.;
RT "Identification of a novel actin isoform in hepatocellular
RT carcinoma.";
RL Hepatol. Res. 36:33-39(2006).
RN [5]
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: Actins are highly conserved proteins that are involved
CC in various types of cell motility and are ubiquitously expressed
CC in all eukaryotic cells (By similarity).
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix.
CC Each actin can bind to 4 others (By similarity). Interacts with
CC PFN1 and PFDN1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form.
CC The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
CC actin repolymerization (By similarity).
CC -!- PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by
CC ALKBH4 is required for maintaining actomyosin dynamics supporting
CC normal cleavage furrow ingression during cytokinesis and cell
CC migration (By similarity).
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC alpha, beta and gamma have been identified. The alpha actins are
CC found in muscle tissues and are a major constituent of the
CC contractile apparatus. The beta and gamma actins coexist in most
CC cell types as components of the cytoskeleton and as mediators of
CC internal cell motility.
CC -!- SIMILARITY: Belongs to the actin family.
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; BX648504; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471123; EAW54967.1; -; Genomic_DNA.
DR EMBL; BC137470; AAI37471.1; -; mRNA.
DR EMBL; BC137473; AAI37474.1; -; mRNA.
DR EMBL; AY970384; AAX82193.1; -; Genomic_DNA.
DR EMBL; AY970433; AAX82242.1; -; Genomic_DNA.
DR EMBL; AY970451; AAX82259.1; -; Genomic_DNA.
DR EMBL; AY970452; AAX82260.1; -; Genomic_DNA.
DR RefSeq; NP_001017992.1; NM_001017992.3.
DR UniGene; Hs.482167; -.
DR ProteinModelPortal; Q562R1; -.
DR SMR; Q562R1; 7-376.
DR IntAct; Q562R1; 13.
DR STRING; 9606.ENSP00000416706; -.
DR PhosphoSite; Q562R1; -.
DR DMDM; 172046825; -.
DR PaxDb; Q562R1; -.
DR PeptideAtlas; Q562R1; -.
DR PRIDE; Q562R1; -.
DR Ensembl; ENST00000423391; ENSP00000416706; ENSG00000169067.
DR GeneID; 345651; -.
DR KEGG; hsa:345651; -.
DR UCSC; uc003jrm.3; human.
DR CTD; 345651; -.
DR GeneCards; GC05M056813; -.
DR HGNC; HGNC:17780; ACTBL2.
DR HPA; HPA041271; -.
DR MIM; 614835; gene.
DR neXtProt; NX_Q562R1; -.
DR PharmGKB; PA142672651; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233339; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; Q562R1; -.
DR OMA; MIGRPRH; -.
DR OrthoDB; EOG72RMZ1; -.
DR PhylomeDB; Q562R1; -.
DR SignaLink; Q562R1; -.
DR GenomeRNAi; 345651; -.
DR NextBio; 98897; -.
DR PRO; PR:Q562R1; -.
DR CleanEx; HS_ACTBL2; -.
DR Genevestigator; Q562R1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT CHAIN 1 376 Beta-actin-like protein 2.
FT /FTId=PRO_0000318849.
FT MOD_RES 45 45 Methionine (R)-sulfoxide (By similarity).
FT MOD_RES 48 48 Methionine (R)-sulfoxide (By similarity).
FT MOD_RES 85 85 N6-methyllysine (By similarity).
FT CONFLICT 121 121 T -> I (in Ref. 4; AAX82242).
FT CONFLICT 135 135 V -> A (in Ref. 4; AAX82260).
FT CONFLICT 162 162 H -> L (in Ref. 4; AAX82259).
FT CONFLICT 163 163 I -> T (in Ref. 4; AAX82193).
SQ SEQUENCE 376 AA; 42003 MW; 6095D374964D71DA CRC64;
MTDNELSALV VDNGSGMCKA GFGGDDAPRA VFPSMIGRPR HQGVMVGMGQ KDCYVGDEAQ
SKRGVLTLKY PIEHGVVTNW DDMEKIWYHT FYNELRVAPD EHPILLTEAP LNPKINREKM
TQIMFEAFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV THIVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYN FTTTAEREIV RDVKEKLCYV ALDFEQEMVR AAASSSPERS
YELPDGQVIT IGNERFRCPE AIFQPSFLGI ESSGIHETTF NSIMKCDVDI RKDLYANTVL
SGGSTMYPGI ADRMQKEIIT LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDEAGPPI VHRKCF
//
ID ACTBL_HUMAN Reviewed; 376 AA.
AC Q562R1; B2RPJ1; Q562R2; Q562S9; Q562X8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=Beta-actin-like protein 2;
DE AltName: Full=Kappa-actin;
GN Name=ACTBL2;
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].
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-187, AND INTERACTION WITH PFN1
RP AND PFDN1.
RC TISSUE=Hepatoma;
RX PubMed=16824795; DOI=10.1016/j.hepres.2006.05.003;
RA Chang K.-W., Yang P.-Y., Lai H.-Y., Yeh T.-S., Chen T.-C., Yeh C.-T.;
RT "Identification of a novel actin isoform in hepatocellular
RT carcinoma.";
RL Hepatol. Res. 36:33-39(2006).
RN [5]
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: Actins are highly conserved proteins that are involved
CC in various types of cell motility and are ubiquitously expressed
CC in all eukaryotic cells (By similarity).
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix.
CC Each actin can bind to 4 others (By similarity). Interacts with
CC PFN1 and PFDN1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form.
CC The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
CC actin repolymerization (By similarity).
CC -!- PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by
CC ALKBH4 is required for maintaining actomyosin dynamics supporting
CC normal cleavage furrow ingression during cytokinesis and cell
CC migration (By similarity).
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC alpha, beta and gamma have been identified. The alpha actins are
CC found in muscle tissues and are a major constituent of the
CC contractile apparatus. The beta and gamma actins coexist in most
CC cell types as components of the cytoskeleton and as mediators of
CC internal cell motility.
CC -!- SIMILARITY: Belongs to the actin family.
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; BX648504; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471123; EAW54967.1; -; Genomic_DNA.
DR EMBL; BC137470; AAI37471.1; -; mRNA.
DR EMBL; BC137473; AAI37474.1; -; mRNA.
DR EMBL; AY970384; AAX82193.1; -; Genomic_DNA.
DR EMBL; AY970433; AAX82242.1; -; Genomic_DNA.
DR EMBL; AY970451; AAX82259.1; -; Genomic_DNA.
DR EMBL; AY970452; AAX82260.1; -; Genomic_DNA.
DR RefSeq; NP_001017992.1; NM_001017992.3.
DR UniGene; Hs.482167; -.
DR ProteinModelPortal; Q562R1; -.
DR SMR; Q562R1; 7-376.
DR IntAct; Q562R1; 13.
DR STRING; 9606.ENSP00000416706; -.
DR PhosphoSite; Q562R1; -.
DR DMDM; 172046825; -.
DR PaxDb; Q562R1; -.
DR PeptideAtlas; Q562R1; -.
DR PRIDE; Q562R1; -.
DR Ensembl; ENST00000423391; ENSP00000416706; ENSG00000169067.
DR GeneID; 345651; -.
DR KEGG; hsa:345651; -.
DR UCSC; uc003jrm.3; human.
DR CTD; 345651; -.
DR GeneCards; GC05M056813; -.
DR HGNC; HGNC:17780; ACTBL2.
DR HPA; HPA041271; -.
DR MIM; 614835; gene.
DR neXtProt; NX_Q562R1; -.
DR PharmGKB; PA142672651; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233339; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; Q562R1; -.
DR OMA; MIGRPRH; -.
DR OrthoDB; EOG72RMZ1; -.
DR PhylomeDB; Q562R1; -.
DR SignaLink; Q562R1; -.
DR GenomeRNAi; 345651; -.
DR NextBio; 98897; -.
DR PRO; PR:Q562R1; -.
DR CleanEx; HS_ACTBL2; -.
DR Genevestigator; Q562R1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT CHAIN 1 376 Beta-actin-like protein 2.
FT /FTId=PRO_0000318849.
FT MOD_RES 45 45 Methionine (R)-sulfoxide (By similarity).
FT MOD_RES 48 48 Methionine (R)-sulfoxide (By similarity).
FT MOD_RES 85 85 N6-methyllysine (By similarity).
FT CONFLICT 121 121 T -> I (in Ref. 4; AAX82242).
FT CONFLICT 135 135 V -> A (in Ref. 4; AAX82260).
FT CONFLICT 162 162 H -> L (in Ref. 4; AAX82259).
FT CONFLICT 163 163 I -> T (in Ref. 4; AAX82193).
SQ SEQUENCE 376 AA; 42003 MW; 6095D374964D71DA CRC64;
MTDNELSALV VDNGSGMCKA GFGGDDAPRA VFPSMIGRPR HQGVMVGMGQ KDCYVGDEAQ
SKRGVLTLKY PIEHGVVTNW DDMEKIWYHT FYNELRVAPD EHPILLTEAP LNPKINREKM
TQIMFEAFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV THIVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYN FTTTAEREIV RDVKEKLCYV ALDFEQEMVR AAASSSPERS
YELPDGQVIT IGNERFRCPE AIFQPSFLGI ESSGIHETTF NSIMKCDVDI RKDLYANTVL
SGGSTMYPGI ADRMQKEIIT LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDEAGPPI VHRKCF
//
MIM
614835
*RECORD*
*FIELD* NO
614835
*FIELD* TI
*614835 ACTIN, BETA-LIKE, 2; ACTBL2
*FIELD* TX
CLONING
Using RT-PCR to amplify actin-like transcripts from hepatocellular
read morecarcinomas, Chang et al. (2006) obtained a partial cDNA for ACTBL2.
MAPPING
Hartz (2012) mapped the ACTBL2 gene to chromosome 5q11.2 based on an
alignment of the ACTBL2 sequence (GenBank GENBANK AY970384) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Chang, K.-W.; Yang, P.-Y.; Lai, H.-Y.; Yeh, T.-S.; Chen, T.-C.;
Yeh, C.-T.: Identification of a novel actin isoform in hepatocellular
carcinoma. Hepatol. Res. 36: 33-39, 2006.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/21/2012.
*FIELD* CD
Patricia A. Hartz: 9/26/2012
*FIELD* ED
mgross: 09/26/2012
*RECORD*
*FIELD* NO
614835
*FIELD* TI
*614835 ACTIN, BETA-LIKE, 2; ACTBL2
*FIELD* TX
CLONING
Using RT-PCR to amplify actin-like transcripts from hepatocellular
read morecarcinomas, Chang et al. (2006) obtained a partial cDNA for ACTBL2.
MAPPING
Hartz (2012) mapped the ACTBL2 gene to chromosome 5q11.2 based on an
alignment of the ACTBL2 sequence (GenBank GENBANK AY970384) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Chang, K.-W.; Yang, P.-Y.; Lai, H.-Y.; Yeh, T.-S.; Chen, T.-C.;
Yeh, C.-T.: Identification of a novel actin isoform in hepatocellular
carcinoma. Hepatol. Res. 36: 33-39, 2006.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/21/2012.
*FIELD* CD
Patricia A. Hartz: 9/26/2012
*FIELD* ED
mgross: 09/26/2012