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P63098 (CANB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPP3R1
Synonyms:CNA2, CNB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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).

Subcellular location

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

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calcineurin regulatory subunit family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

dephosphorylation

Non-traceable author statement Ref.1. Source: GOC

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcalcineurin complex

Non-traceable author statement Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium-dependent protein serine/threonine phosphatase activity

Non-traceable author statement Ref.1. Source: UniProtKB

calmodulin binding

Non-traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16648474PubMed 19896943Ref.8. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 20639889. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAP3K5Q996832EBI-915984,EBI-476263
PPP3CAQ082092EBI-915984,EBI-352922

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 170169Calcineurin subunit B type 1
PRO_0000073484

Regions

Domain18 – 5134EF-hand 1
Domain50 – 8536EF-hand 2
Domain87 – 12236EF-hand 3
Domain128 – 16336EF-hand 4
Calcium binding31 – 42121
Calcium binding63 – 74122
Calcium binding100 – 111123
Calcium binding141 – 152124

Amino acid modifications

Modified residue1061Phosphotyrosine By similarity
Lipidation21N-myristoyl glycine By similarity

Secondary structure

................................. 170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63098 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C904715DC0386056

FASTA17019,300
        10         20         30         40         50         60 
MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ QNPLVQRVID 

        70         80         90        100        110        120 
IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD MDKDGYISNG ELFQVLKMMV 

       130        140        150        160        170 
GNNLKDTQLQ QIVDKTIINA DKDGDGRISF EEFCAVVGGL DIHKKMVVDV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence of a cDNA clone for human calcineurin B, the Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein phosphatase."
Guerini D., Krinks M.H., Sikela J.M., Hahn W.E., Klee C.B.
DNA 8:675-682(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[7]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-85; 98-117; 126-135 AND 148-164, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[8]"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex."
Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A., Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W., Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E., Bacquet R., Villafranca J.E.
Nature 378:641-644(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes."
Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.
Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPIA.
[10]"Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin."
Jin L., Harrison S.C.
Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH PPIA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30773 mRNA. Translation: AAB08721.1.
CR456938 mRNA. Translation: CAG33219.1.
AK314893 mRNA. Translation: BAG37407.1.
AC017083 Genomic DNA. Translation: AAY14715.1.
CH471053 Genomic DNA. Translation: EAW99878.1.
BC027913 mRNA. Translation: AAH27913.1.
CCDSCCDS46310.1.
PIRA33391.
RefSeqNP_000936.1. NM_000945.3.
UniGeneHs.280604.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUIX-ray2.10B2-170[»]
1M63X-ray2.80B/F2-170[»]
1MF8X-ray3.10B1-170[»]
2P6BX-ray2.30B/D16-170[»]
3LL8X-ray2.00B/D16-170[»]
4F0ZX-ray1.70B1-170[»]
DisProtDP00565.
ProteinModelPortalP63098.
SMRP63098. Positions 7-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111526. 12 interactions.
DIPDIP-6096N.
IntActP63098. 5 interactions.
MINTMINT-1339650.
STRING9606.ENSP00000234310.

Chemistry

BindingDBP63098.
DrugBankDB00337. Pimecrolimus.

PTM databases

PhosphoSiteP63098.

Polymorphism databases

DMDM52000904.

2D gel databases

OGPP63098.

Proteomic databases

MaxQBP63098.
PaxDbP63098.
PRIDEP63098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234310; ENSP00000234310; ENSG00000221823.
GeneID5534.
KEGGhsa:5534.
UCSCuc002sei.1. human.

Organism-specific databases

CTD5534.
GeneCardsGC02M068358.
HGNCHGNC:9317. PPP3R1.
HPACAB005610.
MIM601302. gene.
neXtProtNX_P63098.
PharmGKBPA33681.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOVERGENHBG105307.
KOK06268.
PhylomeDBP63098.
TreeFamTF105558.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118664. Calcineurin dephosphorylates NFATC1,2,3.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP63098.
BgeeP63098.
CleanExHS_PPP3R1.
GenevestigatorP63098.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF00036. EF-hand_1. 2 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP3R1. human.
EvolutionaryTraceP63098.
GeneWikiPPP3R1.
GenomeRNAi5534.
NextBio21438.
PROP63098.
SOURCESearch...

Entry information

Entry nameCANB1_HUMAN
AccessionPrimary (citable) accession number: P63098
Secondary accession number(s): B2RC10 expand/collapse secondary AC list , B5MDU4, P06705, P15117, Q08044, Q53SL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM