GenomeNet

Database: UniProt
Entry: P63098
LinkDB: P63098
Original site: P63098 
ID   CANB1_HUMAN             Reviewed;         170 AA.
AC   P63098; B2RC10; B5MDU4; P06705; P15117; Q08044; Q53SL0;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   26-NOV-2014, entry version 120.
DE   RecName: Full=Calcineurin subunit B type 1;
DE   AltName: Full=Protein phosphatase 2B regulatory subunit 1;
DE   AltName: Full=Protein phosphatase 3 regulatory subunit B alpha isoform 1;
GN   Name=PPP3R1; Synonyms=CNA2, CNB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2558868; DOI=10.1089/dna.1.1989.8.675;
RA   Guerini D., Krinks M.H., Sikela J.M., Hahn W.E., Klee C.B.;
RT   "Isolation and sequence of a cDNA clone for human calcineurin B, the
RT   Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein
RT   phosphatase.";
RL   DNA 8:675-682(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 58-85; 98-117; 126-135 AND 148-164, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=8524402; DOI=10.1038/378641a0;
RA   Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A.,
RA   Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W.,
RA   Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E.,
RA   Bacquet R., Villafranca J.E.;
RT   "Crystal structures of human calcineurin and the human FKBP12-FK506-
RT   calcineurin complex.";
RL   Nature 378:641-644(1995).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPIA.
RX   PubMed=12218175; DOI=10.1073/pnas.192206699;
RA   Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
RT   "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common
RT   but distinct recognition of immunophilin-drug complexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH PPIA.
RX   PubMed=12357034; DOI=10.1073/pnas.212504399;
RA   Jin L., Harrison S.C.;
RT   "Crystal structure of human calcineurin complexed with cyclosporin A
RT   and human cyclophilin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
CC   -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC       calmodulin stimulated protein phosphatase. Confers calcium
CC       sensitivity.
CC   -!- SUBUNIT: Interacts with CIB1 (via C-terminal region); the
CC       interaction increases upon cardiomyocytes hypertrophy (By
CC       similarity). Composed of a catalytic subunit (A) and a regulatory
CC       subunit (B). {ECO:0000250, ECO:0000269|PubMed:12218175,
CC       ECO:0000269|PubMed:12357034}.
CC   -!- INTERACTION:
CC       Q99683:MAP3K5; NbExp=2; IntAct=EBI-915984, EBI-476263;
CC       Q08209:PPP3CA; NbExp=2; IntAct=EBI-915984, EBI-352922;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
CC       membrane {ECO:0000250}. Cell membrane, sarcolemma.
CC       Note=Translocates from the cytosol to the sarcolemma in a CIB1-
CC       dependent manner during cardiomyocytes hypertrophy. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding
CC       sites.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 EF-hand domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00448}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M30773; AAB08721.1; -; mRNA.
DR   EMBL; CR456938; CAG33219.1; -; mRNA.
DR   EMBL; AK314893; BAG37407.1; -; mRNA.
DR   EMBL; AC017083; AAY14715.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99878.1; -; Genomic_DNA.
DR   EMBL; BC027913; AAH27913.1; -; mRNA.
DR   CCDS; CCDS46310.1; -.
DR   PIR; A33391; A33391.
DR   RefSeq; NP_000936.1; NM_000945.3.
DR   UniGene; Hs.280604; -.
DR   PDB; 1AUI; X-ray; 2.10 A; B=2-170.
DR   PDB; 1M63; X-ray; 2.80 A; B/F=2-170.
DR   PDB; 1MF8; X-ray; 3.10 A; B=1-170.
DR   PDB; 2P6B; X-ray; 2.30 A; B/D=16-170.
DR   PDB; 3LL8; X-ray; 2.00 A; B/D=16-170.
DR   PDB; 4F0Z; X-ray; 1.70 A; B=1-170.
DR   PDBsum; 1AUI; -.
DR   PDBsum; 1M63; -.
DR   PDBsum; 1MF8; -.
DR   PDBsum; 2P6B; -.
DR   PDBsum; 3LL8; -.
DR   PDBsum; 4F0Z; -.
DR   DisProt; DP00565; -.
DR   ProteinModelPortal; P63098; -.
DR   SMR; P63098; 7-161.
DR   BioGrid; 111526; 19.
DR   DIP; DIP-6096N; -.
DR   IntAct; P63098; 5.
DR   MINT; MINT-1339650; -.
DR   STRING; 9606.ENSP00000234310; -.
DR   PhosphoSite; P63098; -.
DR   DMDM; 52000904; -.
DR   OGP; P63098; -.
DR   MaxQB; P63098; -.
DR   PaxDb; P63098; -.
DR   PRIDE; P63098; -.
DR   Ensembl; ENST00000234310; ENSP00000234310; ENSG00000221823.
DR   GeneID; 5534; -.
DR   KEGG; hsa:5534; -.
DR   UCSC; uc002sei.1; human.
DR   CTD; 5534; -.
DR   GeneCards; GC02M068405; -.
DR   HGNC; HGNC:9317; PPP3R1.
DR   HPA; CAB005610; -.
DR   MIM; 601302; gene.
DR   neXtProt; NX_P63098; -.
DR   PharmGKB; PA33681; -.
DR   eggNOG; COG5126; -.
DR   GeneTree; ENSGT00760000119179; -.
DR   HOVERGEN; HBG105307; -.
DR   InParanoid; P63098; -.
DR   KO; K06268; -.
DR   PhylomeDB; P63098; -.
DR   TreeFam; TF105558; -.
DR   Reactome; REACT_15334; DARPP-32 events.
DR   Reactome; REACT_163834; FCERI mediated Ca+2 mobilization.
DR   Reactome; REACT_172761; Ca2+ pathway.
DR   ChiTaRS; PPP3R1; human.
DR   EvolutionaryTrace; P63098; -.
DR   GeneWiki; PPP3R1; -.
DR   GenomeRNAi; 5534; -.
DR   NextBio; 21438; -.
DR   PRO; PR:P63098; -.
DR   Bgee; P63098; -.
DR   CleanEx; HS_PPP3R1; -.
DR   ExpressionAtlas; P63098; baseline and differential.
DR   Genevestigator; P63098; -.
DR   GO; GO:0005955; C:calcineurin complex; NAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; NAS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; NAS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR   GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0051531; P:NFAT protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0001569; P:patterning of blood vessels; IEA:Ensembl.
DR   GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR   Gene3D; 1.10.238.10; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF00036; EF-hand_1; 2.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 4.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Lipoprotein; Membrane; Metal-binding;
KW   Myristate; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    170       Calcineurin subunit B type 1.
FT                                /FTId=PRO_0000073484.
FT   DOMAIN       18     51       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN       50     85       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN       87    122       EF-hand 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      128    163       EF-hand 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND      31     42       1.
FT   CA_BIND      63     74       2.
FT   CA_BIND     100    111       3.
FT   CA_BIND     141    152       4.
FT   MOD_RES     106    106       Phosphotyrosine. {ECO:0000250}.
FT   LIPID         2      2       N-myristoyl glycine. {ECO:0000250}.
FT   HELIX         9     11       {ECO:0000244|PDB:4F0Z}.
FT   STRAND       12     14       {ECO:0000244|PDB:4F0Z}.
FT   HELIX        17     30       {ECO:0000244|PDB:4F0Z}.
FT   STRAND       35     38       {ECO:0000244|PDB:4F0Z}.
FT   HELIX        40     44       {ECO:0000244|PDB:4F0Z}.
FT   HELIX        47     49       {ECO:0000244|PDB:4F0Z}.
FT   HELIX        55     62       {ECO:0000244|PDB:4F0Z}.
FT   STRAND       67     71       {ECO:0000244|PDB:4F0Z}.
FT   HELIX        72     80       {ECO:0000244|PDB:4F0Z}.
FT   STRAND       81     85       {ECO:0000244|PDB:1M63}.
FT   HELIX        88     99       {ECO:0000244|PDB:4F0Z}.
FT   STRAND      104    107       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       109    120       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       121    123       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       126    140       {ECO:0000244|PDB:4F0Z}.
FT   STRAND      144    149       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       150    157       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       158    160       {ECO:0000244|PDB:4F0Z}.
FT   HELIX       162    165       {ECO:0000244|PDB:3LL8}.
SQ   SEQUENCE   170 AA;  19300 MW;  C904715DC0386056 CRC64;
     MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ QNPLVQRVID
     IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD MDKDGYISNG ELFQVLKMMV
     GNNLKDTQLQ QIVDKTIINA DKDGDGRISF EEFCAVVGGL DIHKKMVVDV
//
DBGET integrated database retrieval system