CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004441
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform 
Protein Synonyms/Alias
 CAM-PRP catalytic subunit; Calmodulin-dependent calcineurin A subunit beta isoform 
Gene Name
 PPP3CB 
Gene Synonyms/Alias
 CALNA2; CALNB; CNA2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56IPRVDVLKNHLVKEGubiquitination[1]
451SESVLTLKGLTPTGMubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. 
Sequence Annotation
 REGION 2 310 Catalytic.
 REGION 256 262 Calcineurin B binding-site 1 (Potential).
 REGION 305 310 Calcineurin B binding-site 2 (Potential).
 REGION 401 423 Calmodulin-binding (Potential).
 REGION 474 496 Inhibitory domain.
 ACT_SITE 160 160 Proton donor (By similarity).
 METAL 99 99 Iron (By similarity).
 METAL 101 101 Iron (By similarity).
 METAL 127 127 Iron (By similarity).
 METAL 127 127 Zinc (By similarity).
 METAL 159 159 Zinc (By similarity).
 METAL 208 208 Zinc (By similarity).
 METAL 290 290 Zinc (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; Calmodulin-binding; Complete proteome; Hydrolase; Iron; Metal-binding; Protein phosphatase; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP RVDVLKNHLV 60
KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT 120
RYLFLGDYVD RGYFSIEHVL GTEDISINPH NNINECVLYL WVLKILYPST LFLLRGNHEC 180
RHLTEYFTFK QECKIKYSER VYEACMEAFD SLPLAALLNQ QFLCVHGGLS PEIHTLDDIR 240
RLDRFKEPPA FGPMCDLLWS DPSEDFGNEK SQEHFSHNTV RGCSYFYNYP AVCEFLQNNN 300
LLSIIRAHEA QDAGYRMYRK SQTTGFPSLI TIFSAPNYLD VYNNKAAVLK YENNVMNIRQ 360
FNCSPHPYWL PNFMDVFTWS LPFVGEKVTE MLVNVLSICS DDELMTEGED QFDGSAAARK 420
EIIRNKIRAI GKMARVFSVL REESESVLTL KGLTPTGMLP SGVLAGGRQT LQSGNDVMQL 480
AVPQMDWGTP HSFANNSHNA CREFLLFFSS CLSS 514 
Gene Ontology
 GO:0005955; C:calcineurin complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0005516; F:calmodulin binding; IDA:UniProtKB.
 GO:0033192; F:calmodulin-dependent protein phosphatase activity; ISS:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB.
 GO:0048675; P:axon extension; TAS:UniProtKB.
 GO:0017156; P:calcium ion-dependent exocytosis; ISS:UniProtKB.
 GO:0035690; P:cellular response to drug; IDA:UniProtKB.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0007612; P:learning; TAS:UniProtKB.
 GO:0007613; P:memory; TAS:UniProtKB.
 GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IEA:Compara.
 GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
 GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
 GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
 GO:0034097; P:response to cytokine stimulus; IEA:Compara.
 GO:0007165; P:signal transduction; NAS:UniProtKB.
 GO:0035176; P:social behavior; IEP:UniProtKB.
 GO:0030217; P:T cell differentiation; IEA:Compara.
 GO:0043029; P:T cell homeostasis; IEA:Compara.
 GO:0042098; P:T cell proliferation; NAS:UniProtKB. 
Interpro
 IPR004843; Metallo_PEstase_dom.
 IPR006186; Ser/Thr-sp_prot-phosphatase. 
Pfam
 PF00149; Metallophos 
SMART
 SM00156; PP2Ac 
PROSITE
 PS00125; SER_THR_PHOSPHATASE 
PRINTS
 PR00114; STPHPHTASE.