ACTBL_HUMAN
ID ACTBL_HUMAN Reviewed; 376 AA.
AC Q562R1; B2RPJ1; Q562R2; Q562S9; Q562X8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 AND
RP 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 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., Buerckstuemmer T.,
RA 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells. {ECO:0000250}.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. Each
CC actin can bind to 4 others (By similarity). Interacts with PFN1 and
CC PFDN1. {ECO:0000250, ECO:0000269|PubMed:16824795}.
CC -!- INTERACTION:
CC Q562R1; Q8IW35: CEP97; NbExp=2; IntAct=EBI-1773495, EBI-1566210;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin
CC repolymerization (By similarity). {ECO:0000250}.
CC -!- PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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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 CCDS; CCDS34163.1; -.
DR RefSeq; NP_001017992.1; NM_001017992.3.
DR AlphaFoldDB; Q562R1; -.
DR SMR; Q562R1; -.
DR BioGRID; 131362; 292.
DR IntAct; Q562R1; 181.
DR MINT; Q562R1; -.
DR STRING; 9606.ENSP00000416706; -.
DR GlyGen; Q562R1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q562R1; -.
DR MetOSite; Q562R1; -.
DR PhosphoSitePlus; Q562R1; -.
DR SwissPalm; Q562R1; -.
DR BioMuta; ACTBL2; -.
DR DMDM; 172046825; -.
DR EPD; Q562R1; -.
DR jPOST; Q562R1; -.
DR MassIVE; Q562R1; -.
DR MaxQB; Q562R1; -.
DR PaxDb; Q562R1; -.
DR PeptideAtlas; Q562R1; -.
DR PRIDE; Q562R1; -.
DR ProteomicsDB; 62562; -.
DR Antibodypedia; 56201; 71 antibodies from 18 providers.
DR DNASU; 345651; -.
DR Ensembl; ENST00000423391.3; ENSP00000416706.1; ENSG00000169067.4.
DR GeneID; 345651; -.
DR KEGG; hsa:345651; -.
DR MANE-Select; ENST00000423391.3; ENSP00000416706.1; NM_001017992.4; NP_001017992.1.
DR UCSC; uc003jrm.3; human.
DR CTD; 345651; -.
DR DisGeNET; 345651; -.
DR GeneCards; ACTBL2; -.
DR HGNC; HGNC:17780; ACTBL2.
DR HPA; ENSG00000169067; Not detected.
DR MIM; 614835; gene.
DR neXtProt; NX_Q562R1; -.
DR OpenTargets; ENSG00000169067; -.
DR PharmGKB; PA142672651; -.
DR VEuPathDB; HostDB:ENSG00000169067; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000162627; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q562R1; -.
DR OMA; SNMKIKI; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q562R1; -.
DR TreeFam; TF354237; -.
DR PathwayCommons; Q562R1; -.
DR SignaLink; Q562R1; -.
DR BioGRID-ORCS; 345651; 15 hits in 1072 CRISPR screens.
DR GenomeRNAi; 345651; -.
DR Pharos; Q562R1; Tbio.
DR PRO; PR:Q562R1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q562R1; protein.
DR Bgee; ENSG00000169067; Expressed in cortical plate and 17 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
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; Cytoplasm; Cytoskeleton; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Beta-actin-like protein 2"
FT /id="PRO_0000318849"
FT MOD_RES 45
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 121
FT /note="T -> I (in Ref. 4; AAX82242)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="V -> A (in Ref. 4; AAX82260)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="H -> L (in Ref. 4; AAX82259)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> T (in Ref. 4; AAX82193)"
FT /evidence="ECO:0000305"
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
