Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01229
Entry Name
UniProt Accession
Theoretical PI
5.29
Molecular Weight
41736.73
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Actin, cytoplasmic 1, N-terminally processed
Protein Synonyms/Alias
Beta-actin;
Gene Name
ACTB
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
245
Canonical
KSYELPDGQVITIGN
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Utsumi T, Sakurai N, Nakano K, Ishisaka R. C-terminal 15 kDa fragment ofcytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediatedcleavage and targeted to mitochondria. FEBS Lett. 2003 Mar 27;539(1-3):37-44.[PMID:12650923]
Functional Description
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Sequence Annotation
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 2 2 N-acetylaspartate; in Actin, cytoplasmic1, N-terminally processed.
Modified residue: 44 44 Methionine (R)-sulfoxide.
Modified residue: 47 47 Methionine (R)-sulfoxide.
Modified residue: 73 73 Tele-methylhistidine.
Modified residue: 84 84 N6-methyllysine.
Protein Length
375 AA.
Protein Sequence
(Canonical)
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS  60
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT  120
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL  180
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY  240
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS  300
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ  360
EYDESGPSIV HRKCF                                                   375
FASTA
(Canonical)
>LipidDB-9606-01229|P60709
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF
Gene Ontology
GO:0030424; C:axon; IEA:Ensembl
GO:0072562; C:blood microparticle; IDA:UniProt
GO:0030863; C:cortical cytoskeleton; IEA:Ensembl
GO:0005737; C:cytoplasm; TAS:UniProtKB
GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL
GO:0005856; C:cytoskeleton; TAS:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0005615; C:extracellular space; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0070688; C:MLL5-L complex; IDA:UniProtKB
GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB
GO:0000790; C:nuclear chromatin; IDA:UniProt
GO:0005654; C:nucleoplasm; TAS:Reactome
GO:0014069; C:postsynaptic density; IEA:Ensembl
GO:0043234; C:protein complex; IDA:UniProt
GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0019894; F:kinesin binding; IPI:UniProtKB
GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL
GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB
GO:0030957; F:Tat protein binding; IPI:BHF-UCL
GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome
GO:0034332; P:adherens junction organization; TAS:Reactome
GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProt
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0034329; P:cell junction assembly; TAS:Reactome
GO:0045216; P:cell-cell junction organization; TAS:Reactome
GO:0006928; P:cellular component movement; TAS:UniProtKB
GO:0044267; P:cellular protein metabolic process; TAS:Reactome
GO:0006325; P:chromatin organization; TAS:Reactome
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0045087; P:innate immune response; TAS:Reactome
GO:0061024; P:membrane organization; TAS:Reactome
GO:0070527; P:platelet aggregation; IMP:UniProtKB
GO:0006457; P:protein folding; TAS:Reactome
GO:0001895; P:retina homeostasis; IEP:UniProt
GO:0021762; P:substantia nigra development; IEP:UniProt
Interpro
InterPro; IPR004000; Actin-related
InterPro; IPR020902; Actin/actin-like_CS
InterPro; IPR004001; Actin_CS
Pfam
Pfam; PF00022; Actin;
SMART
SMART; SM00268; ACTIN;
PROSITE
PROSITE; PS00406; ACTINS_1;
PROSITE; PS00432; ACTINS_2;
PROSITE; PS01132; ACTINS_ACT_LIKE;
PRINTS
PRINTS; PR00190; ACTIN;