IPKA_HUMAN
ID IPKA_HUMAN Reviewed; 76 AA.
AC P61925; P04541; Q6IAV2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=cAMP-dependent protein kinase inhibitor alpha;
DE Short=PKI-alpha;
DE AltName: Full=cAMP-dependent protein kinase inhibitor, muscle/brain isoform;
GN Name=PKIA; Synonyms=PRKACN1;
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=1770951; DOI=10.1210/mend-5-9-1246;
RA Olsen S.R., Uhler M.D.;
RT "Inhibition of protein kinase-A by overexpression of the cloned human
RT protein kinase inhibitor.";
RL Mol. Endocrinol. 5:1246-1256(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Knoell R.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- INTERACTION:
CC P61925; P55212: CASP6; NbExp=3; IntAct=EBI-2682139, EBI-718729;
CC P61925; P63167: DYNLL1; NbExp=3; IntAct=EBI-2682139, EBI-349105;
CC P61925; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-2682139, EBI-742371;
CC P61925; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-2682139, EBI-2857471;
CC P61925; O43663: PRC1; NbExp=3; IntAct=EBI-2682139, EBI-741137;
CC P61925; P22694: PRKACB; NbExp=5; IntAct=EBI-2682139, EBI-2679622;
CC P61925; O14980: XPO1; NbExp=2; IntAct=EBI-2682139, EBI-355867;
CC P61925; P30822: CRM1; Xeno; NbExp=17; IntAct=EBI-2682139, EBI-20589;
CC P61925; Q6P5F9: Xpo1; Xeno; NbExp=4; IntAct=EBI-2682139, EBI-2550236;
CC -!- MISCELLANEOUS: The inhibitory site contains regions very similar to the
CC hinge regions (sites that directly interact with the enzyme active
CC site) and 'pseudosubstrate site' of the regulatory chains; but, unlike
CC these chains, PKI does not contain cAMP-binding sites. The arginine
CC residues within the inhibitory site are essential for inhibition and
CC recognition of the enzyme active site.
CC -!- SIMILARITY: Belongs to the PKI family. {ECO:0000305}.
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DR EMBL; S76965; AAB21141.1; -; mRNA.
DR EMBL; AF234641; AAF40206.1; -; Genomic_DNA.
DR EMBL; CR457052; CAG33333.1; -; mRNA.
DR EMBL; BC022265; AAH22265.1; -; mRNA.
DR CCDS; CCDS6222.1; -.
DR PIR; A40468; A40468.
DR RefSeq; NP_006814.1; NM_006823.3.
DR RefSeq; NP_862822.1; NM_181839.2.
DR RefSeq; XP_016869109.1; XM_017013620.1.
DR RefSeq; XP_016869110.1; XM_017013621.1.
DR RefSeq; XP_016869111.1; XM_017013622.1.
DR PDB; 1CMK; X-ray; 2.90 A; I=6-27.
DR PDB; 1JLU; X-ray; 2.25 A; S=6-25.
DR PDB; 1Q8T; X-ray; 2.00 A; B=6-25.
DR PDB; 1VEB; X-ray; 2.89 A; B=6-25.
DR PDB; 1XH4; X-ray; 2.45 A; B=6-25.
DR PDB; 1XH5; X-ray; 2.05 A; B=6-25.
DR PDB; 1XH6; X-ray; 1.90 A; B=6-25.
DR PDB; 1XH7; X-ray; 2.47 A; B=6-25.
DR PDB; 1XH8; X-ray; 1.60 A; B=6-25.
DR PDB; 1XH9; X-ray; 1.64 A; B=6-25.
DR PDB; 1XHA; X-ray; 2.46 A; B=6-25.
DR PDB; 1YDR; X-ray; 2.20 A; I=6-25.
DR PDB; 2C1A; X-ray; 1.95 A; I=6-25.
DR PDB; 2C1B; X-ray; 2.00 A; I=6-25.
DR PDB; 2F7E; X-ray; 2.00 A; I=6-25.
DR PDB; 2GNI; X-ray; 2.27 A; I=6-25.
DR PDB; 2JDS; X-ray; 2.00 A; I=6-25.
DR PDB; 2JDT; X-ray; 2.15 A; I=6-25.
DR PDB; 2JDV; X-ray; 2.08 A; I=6-25.
DR PDB; 2L1L; NMR; -; A=30-54.
DR PDB; 2UVX; X-ray; 2.00 A; I=6-25.
DR PDB; 2UVY; X-ray; 1.95 A; I=6-25.
DR PDB; 2UVZ; X-ray; 1.94 A; I=6-25.
DR PDB; 2UW0; X-ray; 2.00 A; I=6-25.
DR PDB; 2UW3; X-ray; 2.19 A; I=6-25.
DR PDB; 2UW4; X-ray; 2.00 A; I=6-25.
DR PDB; 2UW5; X-ray; 2.14 A; I=6-25.
DR PDB; 2UW6; X-ray; 2.23 A; I=6-25.
DR PDB; 2UW7; X-ray; 2.10 A; I=6-25.
DR PDB; 2UW8; X-ray; 2.00 A; I=6-25.
DR PDB; 2VNW; X-ray; 2.09 A; I=6-25.
DR PDB; 2VNY; X-ray; 1.96 A; I=6-25.
DR PDB; 2VO0; X-ray; 1.94 A; I=6-25.
DR PDB; 2VO3; X-ray; 1.98 A; I=6-25.
DR PDB; 2VO6; X-ray; 1.97 A; I=6-25.
DR PDB; 2VO7; X-ray; 1.98 A; I=6-25.
DR PDB; 3AMA; X-ray; 1.75 A; B=6-25.
DR PDB; 3AMB; X-ray; 2.25 A; B=6-25.
DR PDB; 3L9L; X-ray; 2.00 A; C/D=6-25.
DR PDB; 3L9M; X-ray; 1.90 A; C/D=6-25.
DR PDB; 3L9N; X-ray; 2.00 A; C=6-25.
DR PDB; 3MVJ; X-ray; 2.49 A; I/J/K=6-25.
DR PDB; 3NX8; X-ray; 2.00 A; B=6-25.
DR PDB; 3OOG; X-ray; 2.00 A; B=6-25.
DR PDB; 3OVV; X-ray; 1.58 A; B=6-25.
DR PDB; 3OWP; X-ray; 1.88 A; B=6-25.
DR PDB; 3OXT; X-ray; 2.20 A; B=6-25.
DR PDB; 3P0M; X-ray; 2.03 A; B=6-25.
DR PDB; 3POO; X-ray; 1.60 A; B=6-25.
DR PDB; 3VQH; X-ray; 1.95 A; B=6-25.
DR PDB; 3WYG; X-ray; 2.15 A; D=1-76.
DR PDB; 3X2U; X-ray; 2.40 A; S=6-25.
DR PDB; 3X2V; X-ray; 1.77 A; S=6-25.
DR PDB; 3X2W; X-ray; 1.70 A; S=6-25.
DR PDB; 4AXA; X-ray; 1.90 A; I=6-25.
DR PDB; 4IAC; X-ray; 2.15 A; S=6-25.
DR PDB; 4IAD; X-ray; 1.90 A; S=6-25.
DR PDB; 4IAF; X-ray; 2.20 A; S=6-25.
DR PDB; 4IAI; X-ray; 1.55 A; S=6-25.
DR PDB; 4IAK; X-ray; 1.60 A; S=6-25.
DR PDB; 4IAY; X-ray; 2.00 A; S=6-25.
DR PDB; 4IAZ; X-ray; 1.85 A; S=6-25.
DR PDB; 4IB0; X-ray; 1.87 A; S=6-25.
DR PDB; 4IB1; X-ray; 1.63 A; S=6-25.
DR PDB; 4IB3; X-ray; 2.20 A; S=6-25.
DR PDB; 4IE9; X-ray; 1.92 A; I=6-25.
DR PDB; 4IJ9; X-ray; 2.55 A; I=6-25.
DR PDB; 4O21; X-ray; 1.95 A; S=6-25.
DR PDB; 4O22; X-ray; 1.70 A; S=6-25.
DR PDB; 4UJ1; X-ray; 1.77 A; B=6-25.
DR PDB; 4UJ2; X-ray; 2.02 A; B=6-25.
DR PDB; 4UJ9; X-ray; 1.87 A; B=6-25.
DR PDB; 4UJA; X-ray; 1.93 A; B=6-25.
DR PDB; 4UJB; X-ray; 1.95 A; B=6-25.
DR PDB; 4WB5; X-ray; 1.64 A; I=6-25.
DR PDB; 4WB6; X-ray; 2.10 A; I/J=6-25.
DR PDB; 4WB7; X-ray; 1.90 A; I/J=6-25.
DR PDB; 4WB8; X-ray; 1.55 A; I=6-25.
DR PDB; 4Z83; X-ray; 1.80 A; I=6-25.
DR PDB; 4Z84; X-ray; 1.55 A; I=6-25.
DR PDB; 5BX6; X-ray; 1.89 A; B=6-25.
DR PDB; 5BX7; X-ray; 1.89 A; B=6-25.
DR PDB; 5DH9; X-ray; 2.55 A; D=36-46.
DR PDB; 5LCP; X-ray; 1.43 A; B=6-25.
DR PDB; 5LCQ; X-ray; 1.42 A; B=6-25.
DR PDB; 5LCR; X-ray; 1.56 A; B=6-25.
DR PDB; 5LCT; X-ray; 1.61 A; B=6-25.
DR PDB; 5LCU; X-ray; 1.58 A; B=6-25.
DR PDB; 5M0B; X-ray; 1.51 A; B=6-25.
DR PDB; 5M0C; X-ray; 1.73 A; B=6-25.
DR PDB; 5M0L; X-ray; 1.47 A; B=6-25.
DR PDB; 5M0U; X-ray; 1.67 A; B=6-25.
DR PDB; 5M6V; X-ray; 1.42 A; B=6-25.
DR PDB; 5M6Y; X-ray; 1.37 A; B=6-25.
DR PDB; 5M71; X-ray; 1.49 A; B=6-25.
DR PDB; 5M75; X-ray; 1.54 A; B=6-25.
DR PDB; 5N23; X-ray; 2.09 A; B=6-25.
DR PDB; 5XOJ; X-ray; 2.20 A; D=1-76.
DR PDB; 6E21; Other; 2.00 A; B=6-25.
DR PDB; 6E99; X-ray; 1.88 A; B=6-23.
DR PDB; 6E9L; X-ray; 2.80 A; B=6-23.
DR PDB; 6FRX; X-ray; 1.88 A; B=6-25.
DR PDB; 6QJ7; X-ray; 1.69 A; B=6-25.
DR PDB; 6X2U; X-ray; 2.20 A; D=34-49.
DR PDB; 6X2V; X-ray; 2.82 A; D=34-49.
DR PDB; 6X2W; X-ray; 3.00 A; D=35-49.
DR PDBsum; 1CMK; -.
DR PDBsum; 1JLU; -.
DR PDBsum; 1Q8T; -.
DR PDBsum; 1VEB; -.
DR PDBsum; 1XH4; -.
DR PDBsum; 1XH5; -.
DR PDBsum; 1XH6; -.
DR PDBsum; 1XH7; -.
DR PDBsum; 1XH8; -.
DR PDBsum; 1XH9; -.
DR PDBsum; 1XHA; -.
DR PDBsum; 1YDR; -.
DR PDBsum; 2C1A; -.
DR PDBsum; 2C1B; -.
DR PDBsum; 2F7E; -.
DR PDBsum; 2GNI; -.
DR PDBsum; 2JDS; -.
DR PDBsum; 2JDT; -.
DR PDBsum; 2JDV; -.
DR PDBsum; 2L1L; -.
DR PDBsum; 2UVX; -.
DR PDBsum; 2UVY; -.
DR PDBsum; 2UVZ; -.
DR PDBsum; 2UW0; -.
DR PDBsum; 2UW3; -.
DR PDBsum; 2UW4; -.
DR PDBsum; 2UW5; -.
DR PDBsum; 2UW6; -.
DR PDBsum; 2UW7; -.
DR PDBsum; 2UW8; -.
DR PDBsum; 2VNW; -.
DR PDBsum; 2VNY; -.
DR PDBsum; 2VO0; -.
DR PDBsum; 2VO3; -.
DR PDBsum; 2VO6; -.
DR PDBsum; 2VO7; -.
DR PDBsum; 3AMA; -.
DR PDBsum; 3AMB; -.
DR PDBsum; 3L9L; -.
DR PDBsum; 3L9M; -.
DR PDBsum; 3L9N; -.
DR PDBsum; 3MVJ; -.
DR PDBsum; 3NX8; -.
DR PDBsum; 3OOG; -.
DR PDBsum; 3OVV; -.
DR PDBsum; 3OWP; -.
DR PDBsum; 3OXT; -.
DR PDBsum; 3P0M; -.
DR PDBsum; 3POO; -.
DR PDBsum; 3VQH; -.
DR PDBsum; 3WYG; -.
DR PDBsum; 3X2U; -.
DR PDBsum; 3X2V; -.
DR PDBsum; 3X2W; -.
DR PDBsum; 4AXA; -.
DR PDBsum; 4IAC; -.
DR PDBsum; 4IAD; -.
DR PDBsum; 4IAF; -.
DR PDBsum; 4IAI; -.
DR PDBsum; 4IAK; -.
DR PDBsum; 4IAY; -.
DR PDBsum; 4IAZ; -.
DR PDBsum; 4IB0; -.
DR PDBsum; 4IB1; -.
DR PDBsum; 4IB3; -.
DR PDBsum; 4IE9; -.
DR PDBsum; 4IJ9; -.
DR PDBsum; 4O21; -.
DR PDBsum; 4O22; -.
DR PDBsum; 4UJ1; -.
DR PDBsum; 4UJ2; -.
DR PDBsum; 4UJ9; -.
DR PDBsum; 4UJA; -.
DR PDBsum; 4UJB; -.
DR PDBsum; 4WB5; -.
DR PDBsum; 4WB6; -.
DR PDBsum; 4WB7; -.
DR PDBsum; 4WB8; -.
DR PDBsum; 4Z83; -.
DR PDBsum; 4Z84; -.
DR PDBsum; 5BX6; -.
DR PDBsum; 5BX7; -.
DR PDBsum; 5DH9; -.
DR PDBsum; 5LCP; -.
DR PDBsum; 5LCQ; -.
DR PDBsum; 5LCR; -.
DR PDBsum; 5LCT; -.
DR PDBsum; 5LCU; -.
DR PDBsum; 5M0B; -.
DR PDBsum; 5M0C; -.
DR PDBsum; 5M0L; -.
DR PDBsum; 5M0U; -.
DR PDBsum; 5M6V; -.
DR PDBsum; 5M6Y; -.
DR PDBsum; 5M71; -.
DR PDBsum; 5M75; -.
DR PDBsum; 5N23; -.
DR PDBsum; 5XOJ; -.
DR PDBsum; 6E21; -.
DR PDBsum; 6E99; -.
DR PDBsum; 6E9L; -.
DR PDBsum; 6FRX; -.
DR PDBsum; 6QJ7; -.
DR PDBsum; 6X2U; -.
DR PDBsum; 6X2V; -.
DR PDBsum; 6X2W; -.
DR AlphaFoldDB; P61925; -.
DR BMRB; P61925; -.
DR SMR; P61925; -.
DR BioGRID; 111556; 12.
DR DIP; DIP-56176N; -.
DR ELM; P61925; -.
DR IntAct; P61925; 13.
DR MINT; P61925; -.
DR STRING; 9606.ENSP00000379696; -.
DR DrugBank; DB07204; (1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINE.
DR DrugBank; DB07107; (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE.
DR DrugBank; DB07857; (2R)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine.
DR DrugBank; DB07860; (2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINE.
DR DrugBank; DB08073; (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE.
DR DrugBank; DB06959; (2S)-1-(3H-Indol-3-yl)-3-{[5-(6-isoquinolinyl)-3-pyridinyl]oxy}-2-propanamine.
DR DrugBank; DB07858; (2S)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine.
DR DrugBank; DB07583; (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE.
DR DrugBank; DB07855; (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE.
DR DrugBank; DB07876; (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE.
DR DrugBank; DB08149; 1-[4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine.
DR DrugBank; DB08148; 1-[4-(4-chlorophenyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine.
DR DrugBank; DB08070; 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE.
DR DrugBank; DB03374; 3,5-Diiodotyrosine.
DR DrugBank; DB08113; 3-pyridin-4-yl-1H-indazole.
DR DrugBank; DB08569; 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.] PYRAZOLE.
DR DrugBank; DB08150; 4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium.
DR DrugBank; DB07859; 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE.
DR DrugBank; DB07996; 5-(2-methylpiperazine-1-sulfonyl)isoquinoline.
DR DrugBank; DB08114; 5-benzyl-1,3-thiazol-2-amine.
DR DrugBank; DB07856; 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE.
DR DrugBank; DB08568; A-674563.
DR DrugBank; DB08162; Fasudil.
DR DrugBank; DB07995; H-89.
DR DrugBank; DB04707; Hydroxyfasudil.
DR DrugBank; DB07947; ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB07997; N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE.
DR DrugBank; DB07854; N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE.
DR DrugBank; DB08756; Y-27632.
DR iPTMnet; P61925; -.
DR PhosphoSitePlus; P61925; -.
DR BioMuta; PKIA; -.
DR DMDM; 48428970; -.
DR EPD; P61925; -.
DR MassIVE; P61925; -.
DR MaxQB; P61925; -.
DR PaxDb; P61925; -.
DR PeptideAtlas; P61925; -.
DR PRIDE; P61925; -.
DR ProteomicsDB; 57339; -.
DR Antibodypedia; 52148; 63 antibodies from 17 providers.
DR DNASU; 5569; -.
DR Ensembl; ENST00000352966.9; ENSP00000336552.5; ENSG00000171033.13.
DR Ensembl; ENST00000396418.7; ENSP00000379696.2; ENSG00000171033.13.
DR Ensembl; ENST00000518467.1; ENSP00000430887.1; ENSG00000171033.13.
DR GeneID; 5569; -.
DR KEGG; hsa:5569; -.
DR MANE-Select; ENST00000396418.7; ENSP00000379696.2; NM_006823.4; NP_006814.1.
DR UCSC; uc003yba.4; human.
DR CTD; 5569; -.
DR GeneCards; PKIA; -.
DR HGNC; HGNC:9017; PKIA.
DR HPA; ENSG00000171033; Group enriched (skeletal muscle, tongue).
DR MIM; 606059; gene.
DR neXtProt; NX_P61925; -.
DR OpenTargets; ENSG00000171033; -.
DR PharmGKB; PA33349; -.
DR VEuPathDB; HostDB:ENSG00000171033; -.
DR eggNOG; ENOG502S6JP; Eukaryota.
DR GeneTree; ENSGT00530000064276; -.
DR HOGENOM; CLU_163471_2_0_1; -.
DR InParanoid; P61925; -.
DR OMA; HYKNHFS; -.
DR OrthoDB; 1648219at2759; -.
DR PhylomeDB; P61925; -.
DR TreeFam; TF330809; -.
DR BRENDA; 2.7.11.11; 2681.
DR PathwayCommons; P61925; -.
DR SignaLink; P61925; -.
DR SIGNOR; P61925; -.
DR BioGRID-ORCS; 5569; 12 hits in 1063 CRISPR screens.
DR ChiTaRS; PKIA; human.
DR EvolutionaryTrace; P61925; -.
DR GeneWiki; PKIA; -.
DR GenomeRNAi; 5569; -.
DR Pharos; P61925; Tbio.
DR PRO; PR:P61925; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P61925; protein.
DR Bgee; ENSG00000171033; Expressed in biceps brachii and 203 other tissues.
DR ExpressionAtlas; P61925; baseline and differential.
DR Genevisible; P61925; HS.
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:BHF-UCL.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:BHF-UCL.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR DisProt; DP00934; -.
DR IDEAL; IID00349; -.
DR InterPro; IPR004171; cAMP_dep_PKI.
DR PANTHER; PTHR15416; PTHR15416; 1.
DR Pfam; PF02827; PKI; 1.
DR PIRSF; PIRSF001667; PKI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Protein kinase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..76
FT /note="cAMP-dependent protein kinase inhibitor alpha"
FT /id="PRO_0000154532"
FT REGION 49..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 16
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 19
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT SITE 20
FT /note="Important for inhibition"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:5M6Y"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1CMK"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5M0U"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:3WYG"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2L1L"
SQ SEQUENCE 76 AA; 7989 MW; BDCE072810435951 CRC64;
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRSS
TEQSGEAQGE AAKSES
