logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0031 : [beta]-Actin

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesactin, cytoplasmic 1 [Homo sapiens]; actin, cytoplasmic 1; beta cytoskeletal actin; PS1TP5-binding protein 1; Actin, cytoplasmic 1; Beta-actin; Actin, cytoplasmic 1, N-terminally processed
Gene NamesACTB; actin, beta
Gene Locus7p22; chromosome 7
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001092 NM_001101 60 P60709 102630 HGNC:132 00032 hsa:60

* Information From OMIM

Function: Interaction of phospholipase D (see PLD1; OMIM:602382) with actin microfilaments regulates cell proliferation, vesicle trafficking, and secretion. Kusner et al. (2002) found that highly purified globular actin (G-actin) inhibited both basal and stimulated PLD1 activity, whereas filamentous actin (F-actin) had the opposite effect. Actin-induced modulation of PLD1 activity was independent of the activating stimulus. The effects of actin on PLD1 were isoform specific: human platelet actin, which exists in a 5:1 ratio of beta- and gamma-actin, was only 45% as potent and 40% as efficacious as rabbit skeletal muscle alpha-actin.

* Structure Information

1. Primary Information

Length: 375 aa

Average Mass: 41.736 kDa

Monoisotopic Mass: 41.710 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Actin 1. 33752.00.0
--- cleavage 37 (inside Actin 3..375) ---

3. Sequence Information

Fasta Sequence: SB0031.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 3BYH (EM; 1200 A; A=2-375), 3D2U (X-ray; 221 A; C/G=170-178), 3LUE (EM; -; A/B/C/D/E/F/G/H/I/J=2-375)

* Cleavage Information

1 [sites] cleaved by Calpain 1 and/or 2

Source Reference: [PubMed ID: 9472000] Villa PG, Henzel WJ, Sensenbrenner M, Henderson CE, Pettmann B, Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis. J Cell Sci. 1998 Mar;111 ( Pt 6):713-22.

Cleavage sites (±10aa)


Arg37 Pro

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24415753] Sobierajska K, Skurzynski S, Stasiak M, Kryczka J, Cierniewski CS, Swiatkowska M, Protein disulfide isomerase directly interacts with beta-actin Cys374 and regulates cytoskeleton reorganization. J Biol Chem. 2014 Feb 28;289(9):5758-73. doi: 10.1074/jbc.M113.479477. Epub 2014

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