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 25-JAN-2012, entry version 75. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92123220; PubMed=1770951; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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 -!- MISCELLANEOUS: The inhibitory site contains regions very similar CC to the hinge regions (sites that directly interact with the enzyme CC active site) and "pseudosubstrate site" of the regulatory chains; CC but, unlike these chains, PKI does not contain cAMP-binding sites. CC The arginine residues within the inhibitory site are essential for CC inhibition and recognition of the enzyme active site. CC -!- SIMILARITY: Belongs to the PKI family. 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; S76965; AAB21141.1; -; mRNA. DR EMBL; AF234641; AAF40206.1; -; Genomic_DNA. DR EMBL; CR457052; CAG33333.1; -; mRNA. DR EMBL; BC022265; AAH22265.1; -; mRNA. DR IPI; IPI00220907; -. DR PIR; A40468; A40468. DR RefSeq; NP_006814.1; NM_006823.3. DR RefSeq; NP_862822.1; NM_181839.2. DR UniGene; Hs.433700; -. DR UniGene; Hs.655384; -. DR PDB; 1CMK; X-ray; 2.90 A; I=6-26. 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 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 ProteinModelPortal; P61925; -. DR DIP; DIP-56176N; -. DR IntAct; P61925; 1. DR STRING; P61925; -. DR PhosphoSite; P61925; -. DR DMDM; 48428970; -. DR PRIDE; P61925; -. DR Ensembl; ENST00000352966; ENSP00000336552; ENSG00000171033. DR Ensembl; ENST00000396418; ENSP00000379696; ENSG00000171033. DR GeneID; 5569; -. DR KEGG; hsa:5569; -. DR UCSC; uc003yba.1; human. DR CTD; 5569; -. DR GeneCards; GC08P079478; -. DR H-InvDB; HIX0007603; -. DR HGNC; HGNC:9017; PKIA. DR HPA; HPA042791; -. DR MIM; 606059; gene. DR neXtProt; NX_P61925; -. DR PharmGKB; PA33349; -. DR eggNOG; prNOG21162; -. DR GeneTree; ENSGT00530000064276; -. DR HOGENOM; HBG268011; -. DR HOVERGEN; HBG101093; -. DR InParanoid; P61925; -. DR OMA; NKTEGEG; -. DR OrthoDB; EOG4C87V2; -. DR NextBio; 21582; -. DR ArrayExpress; P61925; -. DR Bgee; P61925; -. DR CleanEx; HS_PKIA; -. DR Genevestigator; P61925; -. DR GermOnline; ENSG00000171033; Homo sapiens. DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; TAS:UniProtKB. DR InterPro; IPR004171; cAMP_dep_PKI. DR Pfam; PF02827; PKI; 1. DR PIRSF; PIRSF001667; PKI; 1. DR ProDom; PD010366; cAMP_dep_PKI; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Protein kinase inhibitor; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 76 cAMP-dependent protein kinase inhibitor FT alpha. FT /FTId=PRO_0000154532. FT SITE 16 16 Important for inhibition (By similarity). FT SITE 19 19 Important for inhibition (By similarity). FT SITE 20 20 Important for inhibition (By similarity). FT MOD_RES 2 2 Blocked amino end (Thr) (By similarity). FT HELIX 7 12 SQ SEQUENCE 76 AA; 7989 MW; BDCE072810435951 CRC64; MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRSS TEQSGEAQGE AAKSES //