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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform

Gene

PPP3CB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99IronBy similarity1
Metal bindingi101IronBy similarity1
Metal bindingi127IronBy similarity1
Metal bindingi127ZincBy similarity1
Metal bindingi159ZincBy similarity1
Active sitei160Proton donorBy similarity1
Metal bindingi208ZincBy similarity1
Metal bindingi290ZincBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  • axon extension Source: UniProtKB
  • calcineurin-NFAT signaling cascade Source: BHF-UCL
  • calcium ion regulated exocytosis Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • dephosphorylation Source: UniProtKB
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • heart development Source: Ensembl
  • learning Source: UniProtKB
  • locomotion involved in locomotory behavior Source: Ensembl
  • lymphangiogenesis Source: Ensembl
  • memory Source: UniProtKB
  • negative regulation of T cell mediated cytotoxicity Source: Ensembl
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • positive regulation of NFAT protein import into nucleus Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein dephosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of synaptic plasticity Source: UniProtKB
  • response to cytokine Source: Ensembl
  • signal transduction Source: UniProtKB
  • social behavior Source: UniProtKB
  • T cell activation Source: UniProtKB
  • T cell differentiation Source: Ensembl
  • T cell homeostasis Source: Ensembl
  • T cell proliferation Source: UniProtKB
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS03023-MONOMER.
ReactomeiR-HSA-180024. DARPP-32 events.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
SIGNORiP16298.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC:3.1.3.16)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Gene namesi
Name:PPP3CB
Synonyms:CALNA2, CALNB, CNA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9315. PPP3CB.

Subcellular locationi

GO - Cellular componenti

  • calcineurin complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • plasma membrane Source: UniProtKB
  • T-tubule Source: Ensembl
  • Z disc Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5532.
OpenTargetsiENSG00000107758.
PharmGKBiPA33679.

Chemistry databases

ChEMBLiCHEMBL5278.

Polymorphism and mutation databases

BioMutaiPPP3CB.
DMDMi60659599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000588252 – 524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformAdd BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei478PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16298.
MaxQBiP16298.
PaxDbiP16298.
PeptideAtlasiP16298.
PRIDEiP16298.

PTM databases

DEPODiP16298.
iPTMnetiP16298.
PhosphoSitePlusiP16298.
SwissPalmiP16298.

Expressioni

Gene expression databases

BgeeiENSG00000107758.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevisibleiP16298. HS.

Organism-specific databases

HPAiHPA008233.
HPA008823.

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q99J342EBI-1759540,EBI-6117042From a different organism.
IRF2P143162EBI-1759540,EBI-2866589

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111524. 34 interactors.
DIPiDIP-52337N.
IntActiP16298. 13 interactors.
STRINGi9606.ENSP00000378306.

Chemistry databases

BindingDBiP16298.

Structurei

Secondary structure

1524
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 23Combined sources3
Helixi40 – 43Combined sources4
Helixi52 – 60Combined sources9
Helixi67 – 82Combined sources16
Beta strandi86 – 90Combined sources5
Beta strandi92 – 97Combined sources6
Helixi104 – 114Combined sources11
Turni117 – 119Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi129 – 132Combined sources4
Helixi135 – 148Combined sources14
Turni150 – 152Combined sources3
Beta strandi153 – 155Combined sources3
Helixi163 – 168Combined sources6
Helixi171 – 178Combined sources8
Helixi181 – 192Combined sources12
Beta strandi196 – 200Combined sources5
Turni201 – 203Combined sources3
Beta strandi204 – 209Combined sources6
Helixi218 – 222Combined sources5
Beta strandi232 – 234Combined sources3
Helixi235 – 241Combined sources7
Turni246 – 249Combined sources4
Beta strandi256 – 259Combined sources4
Turni261 – 263Combined sources3
Beta strandi264 – 269Combined sources6
Helixi271 – 281Combined sources11
Beta strandi284 – 288Combined sources5
Beta strandi296 – 299Combined sources4
Turni304 – 306Combined sources3
Beta strandi308 – 315Combined sources8
Helixi320 – 322Combined sources3
Beta strandi328 – 334Combined sources7
Beta strandi337 – 343Combined sources7
Helixi353 – 355Combined sources3
Helixi358 – 378Combined sources21
Beta strandi381 – 383Combined sources3
Turni384 – 386Combined sources3
Helixi479 – 485Combined sources7
Helixi488 – 490Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OR9X-ray2.23A1-524[»]
4ORAX-ray2.75A1-524[»]
4ORCX-ray2.70A1-524[»]
ProteinModelPortaliP16298.
SMRiP16298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 310CatalyticAdd BLAST309
Regioni256 – 262Calcineurin B binding-site 1Sequence analysis7
Regioni305 – 310Calcineurin B binding-site 2Sequence analysis6
Regioni401 – 423Calmodulin-bindingSequence analysisAdd BLAST23
Regioni474 – 496Inhibitory domainAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 21Poly-ProAdd BLAST11

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

eggNOGiKOG0375. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG091G094R.
TreeFamiTF105557.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Calcineurin A beta isoform consists of at least two isoenzymes that may result from alternative splicing events.
Isoform 1 (identifier: P16298-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP
60 70 80 90 100
RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
110 120 130 140 150
HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
160 170 180 190 200
STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
210 220 230 240 250
NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
260 270 280 290 300
EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
310 320 330 340 350
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
360 370 380 390 400
WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA
410 420 430 440 450
RKEIIRNKIR AIGKMARVFS VLREESESVL TLKGLTPTGM LPSGVLAGGR
460 470 480 490 500
QTLQSATVEA IEAEKAIRGF SPPHRICSFE EAKGLDRINE RMPPRKDAVQ
510 520
QDGFNSLNTA HATENHGTGN HTAQ
Length:524
Mass (Da):59,024
Last modified:February 1, 2005 - v2
Checksum:i7661183F3C2362C8
GO
Isoform 2 (identifier: P16298-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-137: E → EHVLGTEDISINPHNNINE
     456-524: ATVEAIEAEK...NHGTGNHTAQ → GNDVMQLAVP...LLFFSSCLSS

Show »
Length:514
Mass (Da):58,013
Checksum:i1B0BFA63FB98E06D
GO
Isoform 3 (identifier: P16298-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV
     456-465: Missing.

Show »
Length:515
Mass (Da):58,081
Checksum:iA6762D9468A09B51
GO
Isoform 4 (identifier: P16298-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV

Note: No experimental confirmation available.
Show »
Length:525
Mass (Da):59,123
Checksum:iADB0ECB75371B574
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005096137E → EHVLGTEDISINPHNNINE in isoform 2. 1 Publication1
Alternative sequenceiVSP_043803395D → DV in isoform 3 and isoform 4. 2 Publications1
Alternative sequenceiVSP_005097456 – 524ATVEA…NHTAQ → GNDVMQLAVPQMDWGTPHSF ANNSHNACREFLLFFSSCLS S in isoform 2. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_012617456 – 465Missing in isoform 3. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29551 mRNA. Translation: AAA35706.1.
M29550 mRNA. Translation: AAA35705.1.
AJ488506 mRNA. Translation: CAD32694.1.
AL353731, AL359074 Genomic DNA. Translation: CAI52487.1.
AL359074, AL353731 Genomic DNA. Translation: CAI52473.1.
CH471083 Genomic DNA. Translation: EAW54497.1.
CH471083 Genomic DNA. Translation: EAW54498.1.
BC028049 mRNA. Translation: AAH28049.1.
CCDSiCCDS44436.1. [P16298-3]
CCDS44437.1. [P16298-4]
CCDS7328.1. [P16298-1]
PIRiA36222.
B36222.
RefSeqiNP_001135825.1. NM_001142353.2. [P16298-4]
NP_001135826.1. NM_001142354.2. [P16298-3]
NP_001276897.1. NM_001289968.1. [P16298-2]
NP_001276898.1. NM_001289969.1.
NP_066955.1. NM_021132.3. [P16298-1]
UniGeneiHs.500067.

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.4. human. [P16298-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29551 mRNA. Translation: AAA35706.1.
M29550 mRNA. Translation: AAA35705.1.
AJ488506 mRNA. Translation: CAD32694.1.
AL353731, AL359074 Genomic DNA. Translation: CAI52487.1.
AL359074, AL353731 Genomic DNA. Translation: CAI52473.1.
CH471083 Genomic DNA. Translation: EAW54497.1.
CH471083 Genomic DNA. Translation: EAW54498.1.
BC028049 mRNA. Translation: AAH28049.1.
CCDSiCCDS44436.1. [P16298-3]
CCDS44437.1. [P16298-4]
CCDS7328.1. [P16298-1]
PIRiA36222.
B36222.
RefSeqiNP_001135825.1. NM_001142353.2. [P16298-4]
NP_001135826.1. NM_001142354.2. [P16298-3]
NP_001276897.1. NM_001289968.1. [P16298-2]
NP_001276898.1. NM_001289969.1.
NP_066955.1. NM_021132.3. [P16298-1]
UniGeneiHs.500067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OR9X-ray2.23A1-524[»]
4ORAX-ray2.75A1-524[»]
4ORCX-ray2.70A1-524[»]
ProteinModelPortaliP16298.
SMRiP16298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111524. 34 interactors.
DIPiDIP-52337N.
IntActiP16298. 13 interactors.
STRINGi9606.ENSP00000378306.

Chemistry databases

BindingDBiP16298.
ChEMBLiCHEMBL5278.

PTM databases

DEPODiP16298.
iPTMnetiP16298.
PhosphoSitePlusiP16298.
SwissPalmiP16298.

Polymorphism and mutation databases

BioMutaiPPP3CB.
DMDMi60659599.

Proteomic databases

EPDiP16298.
MaxQBiP16298.
PaxDbiP16298.
PeptideAtlasiP16298.
PRIDEiP16298.

Protocols and materials databases

DNASUi5532.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.4. human. [P16298-1]

Organism-specific databases

CTDi5532.
DisGeNETi5532.
GeneCardsiPPP3CB.
HGNCiHGNC:9315. PPP3CB.
HPAiHPA008233.
HPA008823.
MIMi114106. gene.
neXtProtiNX_P16298.
OpenTargetsiENSG00000107758.
PharmGKBiPA33679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0375. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG091G094R.
TreeFamiTF105557.

Enzyme and pathway databases

BioCyciZFISH:HS03023-MONOMER.
ReactomeiR-HSA-180024. DARPP-32 events.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
SIGNORiP16298.

Miscellaneous databases

ChiTaRSiPPP3CB. human.
GeneWikiiPPP3CB.
GenomeRNAii5532.
PROiP16298.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107758.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevisibleiP16298. HS.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP2BB_HUMAN
AccessioniPrimary (citable) accession number: P16298
Secondary accession number(s): P16299
, Q5F2F9, Q8N1F0, Q8N3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: November 30, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.