CANB1_HUMAN
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 03-AUG-2022, entry version 182.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 Ca2+-
RT binding subunit of the Ca2+/calmodulin-stimulated protein 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 IDENTIFICATION
RP 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 INTERACTION WITH RCAN1.
RX PubMed=12809556; DOI=10.1042/bj20030267;
RA Genesca L., Aubareda A., Fuentes J.J., Estivill X., De La Luna S.,
RA Perez-Riba M.;
RT "Phosphorylation of calcipressin 1 increases its ability to inhibit
RT calcineurin and decreases calcipressin half-life.";
RL Biochem. J. 374:567-575(2003).
RN [9]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [10]
RP INTERACTION WITH SPATA33.
RX PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT motility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-170 IN COMPLEX WITH PPP3CA AND
RP CALCIUM.
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., Bacquet R.,
RA Villafranca J.E.;
RT "Crystal structures of human calcineurin and the human FKBP12-FK506-
RT calcineurin complex.";
RL Nature 378:641-644(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-170 IN COMPLEX WITH PPIA; PPP3CA
RP AND CALCIUM.
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 but
RT distinct recognition of immunophilin-drug complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-170 IN COMPLEX WITH PPIA; PPP3CA
RP AND CALCIUM.
RX PubMed=12357034; DOI=10.1073/pnas.212504399;
RA Jin L., Harrison S.C.;
RT "Crystal structure of human calcineurin complexed with cyclosporin A and
RT human cyclophilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 15-170 IN COMPLEX WITH PPP3CA AND
RP CALCIUM.
RX PubMed=17498738; DOI=10.1016/j.jmb.2007.04.032;
RA Li H., Zhang L., Rao A., Harrison S.C., Hogan P.G.;
RT "Structure of calcineurin in complex with PVIVIT peptide: portrait of a
RT low-affinity signalling interaction.";
RL J. Mol. Biol. 369:1296-1306(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 16-170 IN COMPLEX WITH PPP3CA AND
RP CALCIUM.
RX PubMed=22343722; DOI=10.1038/nsmb.2238;
RA Li H., Pink M.D., Murphy J.G., Stein A., Dell'Acqua M.L., Hogan P.G.;
RT "Balanced interactions of calcineurin with AKAP79 regulate Ca2+-
RT calcineurin-NFAT signaling.";
RL Nat. Struct. Mol. Biol. 19:337-345(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH PPP3CA; AFRICAN
RP SWINE FEVER VIRUS MAL-047/A238L AND CALCIUM.
RX PubMed=23468591; DOI=10.1371/journal.pbio.1001492;
RA Grigoriu S., Bond R., Cossio P., Chen J.A., Ly N., Hummer G., Page R.,
RA Cyert M.S., Peti W.;
RT "The molecular mechanism of substrate engagement and immunosuppressant
RT inhibition of calcineurin.";
RL PLoS Biol. 11:E1001492-E1001492(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH PPP3CB AND CALCIUM,
RP AND FUNCTION.
RX PubMed=26794871; DOI=10.1038/cr.2016.14;
RA Li S.J., Wang J., Ma L., Lu C., Wang J., Wu J.W., Wang Z.X.;
RT "Cooperative autoinhibition and multi-level activation mechanisms of
RT calcineurin.";
RL Cell Res. 26:336-349(2016).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PPP3CA AND CALCIUM.
RX PubMed=27974827; DOI=10.1038/srep38920;
RA Sheftic S.R., Page R., Peti W.;
RT "Investigating the human Calcineurin Interaction Network using the piLxVP
RT SLiM.";
RL Sci. Rep. 6:38920-38920(2016).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000269|PubMed:26794871}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding
CC subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175,
CC PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591,
CC PubMed:26794871, PubMed:27974827). There are three catalytic subunits,
CC each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two
CC regulatory subunits which are also encoded by separate genes (PPP3R1
CC and PPP3R2). Interacts with catalytic subunit PPP3CA/calcineurin A
CC (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738,
CC PubMed:22343722, PubMed:23468591, PubMed:27974827). Interacts with
CC catalytic subunit PPP3CB/calcineurin A (PubMed:26794871). Interacts
CC with CIB1 (via C-terminal region); the interaction increases upon
CC cardiomyocyte hypertrophy (By similarity). Interacts with RCAN1
CC (PubMed:12809556). Interacts with SPATA33 (via PQIIIT motif)
CC (PubMed:34446558). {ECO:0000250|UniProtKB:Q63810,
CC ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
CC ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:17498738,
CC ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591,
CC ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827,
CC ECO:0000269|PubMed:34446558, ECO:0000269|PubMed:8524402}.
CC -!- INTERACTION:
CC P63098; Q99683: MAP3K5; NbExp=2; IntAct=EBI-915984, EBI-476263;
CC P63098; Q08209: PPP3CA; NbExp=6; IntAct=EBI-915984, EBI-352922;
CC P63098; Q08209-1: PPP3CA; NbExp=7; IntAct=EBI-915984, EBI-15637215;
CC P63098; Q08209-2: PPP3CA; NbExp=13; IntAct=EBI-915984, EBI-11959013;
CC P63098; P48454: PPP3CC; NbExp=4; IntAct=EBI-915984, EBI-2827192;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane
CC {ECO:0000269|PubMed:25255805}; Lipid-anchor
CC {ECO:0000269|PubMed:25255805}. Note=Translocates from the cytosol to
CC the sarcolemma in a CIB1-dependent manner during cardiomyocyte
CC hypertrophy. {ECO:0000250|UniProtKB:Q63810}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites
CC (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738,
CC PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827).
CC Although African swine fever virus infects pigs and not humans, human
CC PPP3R1 and PPP3CA have been used for the crystallization. PPP3CA and
CC PPP3R1 interact with African swine fever virus Mal-047/A238L (via
CC PKIIIT and FLCVK motifs); the interaction does not block catalytic
CC activity per se but inhibits PPP3CA function by blocking the access to
CC the two substrate recognition (PubMed:23468591).
CC {ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
CC ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
CC ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
CC ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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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 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 PDB; 4OR9; X-ray; 2.23 A; B=1-170.
DR PDB; 4ORA; X-ray; 2.75 A; B=1-170.
DR PDB; 4ORC; X-ray; 2.70 A; B=1-170.
DR PDB; 5SVE; X-ray; 2.60 A; B=1-170.
DR PDB; 6NUC; X-ray; 1.90 A; B=16-170.
DR PDB; 6NUF; X-ray; 1.90 A; B=16-170.
DR PDB; 6NUU; X-ray; 2.30 A; B=16-170.
DR PDBsum; 1AUI; -.
DR PDBsum; 1M63; -.
DR PDBsum; 1MF8; -.
DR PDBsum; 2P6B; -.
DR PDBsum; 3LL8; -.
DR PDBsum; 4F0Z; -.
DR PDBsum; 4OR9; -.
DR PDBsum; 4ORA; -.
DR PDBsum; 4ORC; -.
DR PDBsum; 5SVE; -.
DR PDBsum; 6NUC; -.
DR PDBsum; 6NUF; -.
DR PDBsum; 6NUU; -.
DR AlphaFoldDB; P63098; -.
DR SMR; P63098; -.
DR BioGRID; 111526; 67.
DR ComplexPortal; CPX-1001; Calcineurin-Calmodulin complex, gamma-R1 variant.
DR ComplexPortal; CPX-1003; Calcineurin-Calmodulin complex, alpha-R1 variant.
DR ComplexPortal; CPX-1009; Calcineurin-Calmodulin complex, beta-R1 variant.
DR ComplexPortal; CPX-1112; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DR ComplexPortal; CPX-998; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
DR CORUM; P63098; -.
DR DIP; DIP-6096N; -.
DR ELM; P63098; -.
DR IntAct; P63098; 33.
DR MINT; P63098; -.
DR STRING; 9606.ENSP00000234310; -.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB11693; Voclosporin.
DR iPTMnet; P63098; -.
DR PhosphoSitePlus; P63098; -.
DR SwissPalm; P63098; -.
DR BioMuta; PPP3R1; -.
DR DMDM; 52000904; -.
DR OGP; P63098; -.
DR EPD; P63098; -.
DR jPOST; P63098; -.
DR MassIVE; P63098; -.
DR MaxQB; P63098; -.
DR PaxDb; P63098; -.
DR PeptideAtlas; P63098; -.
DR PRIDE; P63098; -.
DR ProteomicsDB; 57476; -.
DR TopDownProteomics; P63098; -.
DR Antibodypedia; 34930; 237 antibodies from 33 providers.
DR DNASU; 5534; -.
DR Ensembl; ENST00000234310.8; ENSP00000234310.3; ENSG00000221823.11.
DR GeneID; 5534; -.
DR KEGG; hsa:5534; -.
DR MANE-Select; ENST00000234310.8; ENSP00000234310.3; NM_000945.4; NP_000936.1.
DR UCSC; uc002sei.2; human.
DR CTD; 5534; -.
DR DisGeNET; 5534; -.
DR GeneCards; PPP3R1; -.
DR HGNC; HGNC:9317; PPP3R1.
DR HPA; ENSG00000221823; Tissue enhanced (retina).
DR MIM; 601302; gene.
DR neXtProt; NX_P63098; -.
DR OpenTargets; ENSG00000221823; -.
DR PharmGKB; PA33681; -.
DR VEuPathDB; HostDB:ENSG00000221823; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000156530; -.
DR InParanoid; P63098; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; P63098; -.
DR TreeFam; TF105558; -.
DR PathwayCommons; P63098; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR Reactome; R-HSA-2025928; Calcineurin activates NFAT.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR SignaLink; P63098; -.
DR SIGNOR; P63098; -.
DR BioGRID-ORCS; 5534; 43 hits in 1068 CRISPR screens.
DR ChiTaRS; PPP3R1; human.
DR EvolutionaryTrace; P63098; -.
DR GeneWiki; PPP3R1; -.
DR GenomeRNAi; 5534; -.
DR Pharos; P63098; Tbio.
DR PRO; PR:P63098; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P63098; protein.
DR Bgee; ENSG00000221823; Expressed in cortical plate and 185 other tissues.
DR ExpressionAtlas; P63098; baseline and differential.
DR Genevisible; P63098; HS.
DR GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; 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:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; NAS:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IC:ComplexPortal.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP00565; -.
DR IDEAL; IID00060; -.
DR InterPro; IPR015757; Calcineur_B.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45942; PTHR45942; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
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; Cytoplasm; Direct protein sequencing;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..170
FT /note="Calcineurin subunit B type 1"
FT /id="PRO_0000073484"
FT DOMAIN 18..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 87..122
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..163
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 131..136
FT /note="Calcineurin A binding"
FT /evidence="ECO:0000269|PubMed:12218175,
FT ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738,
FT ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591,
FT ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827,
FT ECO:0000269|PubMed:8524402"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
FT ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
FT ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871,
FT ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402,
FT ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63,
FT ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B,
FT ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z,
FT ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA,
FT ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE"
FT SITE 118
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000269|PubMed:23468591"
FT SITE 122
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000269|PubMed:23468591"
FT MOD_RES 106
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63810"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1M63"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:4F0Z"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4F0Z"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6NUC"
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
