IPKB_MOUSE
ID IPKB_MOUSE Reviewed; 92 AA.
AC Q04758;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=cAMP-dependent protein kinase inhibitor beta;
DE AltName: Full=PKI-beta;
DE AltName: Full=cAMP-dependent protein kinase inhibitor, testis isoform;
GN Name=Pkib;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=7684369; DOI=10.1016/s0021-9258(18)82074-9;
RA Scarpetta M.A., Uhler M.D.;
RT "Evidence for two additional isoforms of the endogenous protein kinase
RT inhibitor of cAMP-dependent protein kinase in mouse.";
RL J. Biol. Chem. 268:10927-10931(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-92.
RX PubMed=7905001; DOI=10.1016/s0021-9258(17)42170-3;
RA Baude E.J., Dignam S.S., Olsen S.R., Reimann E.M., Uhler M.D.;
RT "Glutamic acid 203 of the cAMP-dependent protein kinase catalytic subunit
RT participates in the inhibition by two isoforms of the protein kinase
RT inhibitor.";
RL J. Biol. Chem. 269:2316-2323(1994).
CC -!- FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent
CC protein kinase activity, this protein interacts with the catalytic
CC subunit of the enzyme after the cAMP-induced dissociation of its
CC regulatory chains.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q04758-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q04758-2; Sequence=VSP_002754;
CC -!- SIMILARITY: Belongs to the PKI family. {ECO:0000305}.
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DR EMBL; L02241; AAB59678.1; -; mRNA.
DR PIR; B46707; B46707.
DR AlphaFoldDB; Q04758; -.
DR STRING; 10090.ENSMUSP00000093329; -.
DR PhosphoSitePlus; Q04758; -.
DR MaxQB; Q04758; -.
DR PaxDb; Q04758; -.
DR PeptideAtlas; Q04758; -.
DR PRIDE; Q04758; -.
DR ProteomicsDB; 269322; -. [Q04758-1]
DR ProteomicsDB; 269323; -. [Q04758-2]
DR UCSC; uc007fcq.2; mouse. [Q04758-1]
DR MGI; MGI:101937; Pkib.
DR eggNOG; ENOG502S8BW; Eukaryota.
DR InParanoid; Q04758; -.
DR PhylomeDB; Q04758; -.
DR ChiTaRS; Pkib; mouse.
DR PRO; PR:Q04758; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q04758; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:MGI.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR InterPro; IPR004171; cAMP_dep_PKI.
DR PANTHER; PTHR15416; PTHR15416; 1.
DR Pfam; PF02827; PKI; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Phosphoprotein; Protein kinase inhibitor;
KW Reference proteome.
FT CHAIN 1..92
FT /note="cAMP-dependent protein kinase inhibitor beta"
FT /id="PRO_0000154539"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 37
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 40
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 41
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27775"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7684369"
FT /id="VSP_002754"
SQ SEQUENCE 92 AA; 9682 MW; F0D537A4AED29956 CRC64;
MGGGTSPEAQ QDSVMRTDSS EMTDVESVIT SFASSARAGR RNALPDIQSS LATSGSSDLP
LKLEALAVKE DAKTKNEEKD QGQPKTPLNE GK
