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Protein

Calcineurin subunit B type 1

Gene

PPP3R1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi31 – 42121Add
BLAST
Calcium bindingi63 – 74122Add
BLAST
Calcium bindingi100 – 111123Add
BLAST
Calcium bindingi141 – 152124Add
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-111447. Activation of BAD and translocation to mitochondria.
R-BTA-180024. DARPP-32 events.
R-BTA-2871809. FCERI mediated Ca+2 mobilization.
R-BTA-4086398. Ca2+ pathway.
R-BTA-5607763. CLEC7A (Dectin-1) induces NFAT activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcineurin subunit B type 1
Alternative name(s):
Protein phosphatase 2B regulatory subunit 1
Protein phosphatase 3 regulatory subunit B alpha isoform 1
Gene namesi
Name:PPP3R1
Synonyms:CNA2, CNB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Cell membrane By similarity; Lipid-anchor By similarity
  • Cell membranesarcolemma

  • Note: Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocytes hypertrophy.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 170169Calcineurin subunit B type 1PRO_0000073483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei106 – 1061PhosphotyrosineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP63099.
PRIDEiP63099.

Interactioni

Subunit structurei

Interacts with CIB1 (via C-terminal region); the interaction increases upon cardiomyocytes hypertrophy (By similarity). Composed of a catalytic subunit (A) and a regulatory subunit (B).By similarity1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014038.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 3014Combined sources
Turni31 – 344Combined sources
Helixi40 – 434Combined sources
Beta strandi49 – 513Combined sources
Helixi55 – 628Combined sources
Beta strandi67 – 693Combined sources
Helixi72 – 8211Combined sources
Helixi88 – 9912Combined sources
Beta strandi104 – 1074Combined sources
Helixi109 – 12012Combined sources
Helixi126 – 14015Combined sources
Beta strandi144 – 1496Combined sources
Helixi150 – 1578Combined sources
Helixi162 – 1654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TCOX-ray2.50B2-170[»]
ProteinModelPortaliP63099.
SMRiP63099. Positions 7-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63099.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5134EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini50 – 8536EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini87 – 12236EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 16336EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119179.
HOGENOMiHOG000233019.
HOVERGENiHBG105307.
InParanoidiP63099.
KOiK06268.
OMAiYIGNGEL.
OrthoDBiEOG75QR5D.
TreeFamiTF105558.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ
60 70 80 90 100
QNPLVQRVID IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD
110 120 130 140 150
MDKDGYISNG ELFQVLKMMV GNNLKDTQLQ QIVDKTIINA DKDGDGRISF
160 170
EEFCAVVGGL DIHKKMVVDV
Length:170
Mass (Da):19,300
Last modified:January 23, 2007 - v2
Checksum:iC904715DC0386056
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121C → M AA sequence (PubMed:6321184).Curated
Sequence conflicti154 – 1541C → S AA sequence (PubMed:6321184).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71666 mRNA. Translation: CAA50659.1.
PIRiI45831. S34127.
RefSeqiNP_777008.1. NM_174583.2.
UniGeneiBt.212.

Genome annotation databases

EnsembliENSBTAT00000014038; ENSBTAP00000014038; ENSBTAG00000010619.
GeneIDi282321.
KEGGibta:282321.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71666 mRNA. Translation: CAA50659.1.
PIRiI45831. S34127.
RefSeqiNP_777008.1. NM_174583.2.
UniGeneiBt.212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TCOX-ray2.50B2-170[»]
ProteinModelPortaliP63099.
SMRiP63099. Positions 7-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014038.

Proteomic databases

PaxDbiP63099.
PRIDEiP63099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014038; ENSBTAP00000014038; ENSBTAG00000010619.
GeneIDi282321.
KEGGibta:282321.

Organism-specific databases

CTDi5534.

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119179.
HOGENOMiHOG000233019.
HOVERGENiHBG105307.
InParanoidiP63099.
KOiK06268.
OMAiYIGNGEL.
OrthoDBiEOG75QR5D.
TreeFamiTF105558.

Enzyme and pathway databases

ReactomeiR-BTA-111447. Activation of BAD and translocation to mitochondria.
R-BTA-180024. DARPP-32 events.
R-BTA-2871809. FCERI mediated Ca+2 mobilization.
R-BTA-4086398. Ca2+ pathway.
R-BTA-5607763. CLEC7A (Dectin-1) induces NFAT activation.

Miscellaneous databases

EvolutionaryTraceiP63099.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of a cDNA clone coding for the calcium-binding subunit of calcineurin from bovine brain: an identical amino acid sequence to the human protein."
    Nargang C.E., Bottorff D.A., Adachi K.
    DNA Seq. 4:313-318(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The structure of the B subunit of calcineurin."
    Aitken A., Klee C.B., Cohen P.
    Eur. J. Biochem. 139:663-671(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-169, MYRISTOYLATION AT GLY-2.
    Tissue: Brain.
  3. "Calcineurin: a calcium- and calmodulin-binding protein of the nervous system."
    Klee C.B., Crouch T.H., Krinks M.H.
    Proc. Natl. Acad. Sci. U.S.A. 76:6270-6273(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  4. "X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex."
    Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A.
    Cell 82:507-522(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FKBP1A.

Entry informationi

Entry nameiCANB1_BOVIN
AccessioniPrimary (citable) accession number: P63099
Secondary accession number(s): P06705, P15117, Q08044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.