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Protein

cAMP-dependent protein kinase inhibitor alpha

Gene

Pkia

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei16 – 161Important for inhibitionBy similarity
Sitei19 – 191Important for inhibitionBy similarity
Sitei20 – 201Important for inhibitionBy similarity

GO - Molecular functioni

  1. cAMP-dependent protein kinase inhibitor activity Source: MGI
  2. protein kinase A catalytic subunit binding Source: MGI

GO - Biological processi

  1. negative regulation of cAMP-dependent protein kinase activity Source: MGI
  2. negative regulation of catalytic activity Source: MGI
  3. negative regulation of protein import into nucleus Source: MGI
  4. negative regulation of protein kinase activity Source: MGI
  5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  6. regulation of G2/M transition of mitotic cell cycle Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Protein kinase inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase inhibitor alpha
Short name:
PKI-alpha
Alternative name(s):
cAMP-dependent protein kinase inhibitor, muscle/brain isoform
Gene namesi
Name:Pkia
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:104747. Pkia.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7675cAMP-dependent protein kinase inhibitor alphaPRO_0000154533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP63248.
PRIDEiP63248.

PTM databases

PhosphoSiteiP63248.

Expressioni

Tissue specificityi

Present at high levels in skeletal muscle and brain but is present at lower levels in heart, testis and liver.

Gene expression databases

BgeeiP63248.
CleanExiMM_PKIA.
GenevestigatoriP63248.

Interactioni

Protein-protein interaction databases

BioGridi202207. 1 interaction.
DIPiDIP-6087N.
IntActiP63248. 2 interactions.
MINTiMINT-4098688.
STRINGi10090.ENSMUSP00000028999.

Structurei

Secondary structure

1
76
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APMX-ray2.00I6-25[»]
1ATPX-ray2.20I6-25[»]
1PVKmodel-I6-25[»]
2CPKX-ray2.70I6-25[»]
2GNFX-ray2.28I6-25[»]
2GNGX-ray1.87I6-25[»]
2QURX-ray2.50B6-25[»]
3FJQX-ray1.60I6-25[»]
3OW3X-ray1.90B6-25[»]
3QALX-ray1.70I6-23[»]
3QAMX-ray1.92I6-24[»]
4DFXX-ray1.35I6-25[»]
4DFZX-ray2.00I6-25[»]
4DG0X-ray2.00I6-25[»]
4DG2X-ray2.00I6-25[»]
4DG3X-ray1.80A6-25[»]
4DH1X-ray2.00I6-25[»]
4DH3X-ray2.20I6-25[»]
4DH5X-ray2.20I6-25[»]
4DH7X-ray1.80I6-25[»]
4DH8X-ray2.30I6-25[»]
4HPTX-ray2.15I6-25[»]
4HPUX-ray1.55I6-25[»]
ProteinModelPortaliP63248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63248.

Family & Domainsi

Sequence similaritiesi

Belongs to the PKI family.Curated

Phylogenomic databases

eggNOGiNOG45574.
GeneTreeiENSGT00530000064276.
HOGENOMiHOG000059641.
HOVERGENiHBG101093.
InParanoidiP63248.
KOiK15985.
OMAiTTNTTDV.
OrthoDBiEOG7JHM8S.
PhylomeDBiP63248.
TreeFamiTF330809.

Family and domain databases

InterProiIPR004171. cAMP_dep_PKI.
[Graphical view]
PfamiPF02827. PKI. 1 hit.
[Graphical view]
PIRSFiPIRSF001667. PKI. 1 hit.
ProDomiPD010366. cAMP_dep_PKI. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT
60 70
EGEDDGQRSS TEQSGEAQGE AAKSES
Length:76
Mass (Da):7,960
Last modified:January 22, 2007 - v2
Checksum:iFCCE07281498788A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63554 mRNA. Translation: AAA39940.1.
AK139347 mRNA. Translation: BAE23970.1.
CH466577 Genomic DNA. Translation: EDL05208.1.
CH466577 Genomic DNA. Translation: EDL05209.1.
BC048244 mRNA. Translation: AAH48244.1.
CCDSiCCDS38383.1.
PIRiA40536.
RefSeqiNP_032888.1. NM_008862.3.
UniGeneiMm.3193.

Genome annotation databases

EnsembliENSMUST00000028999; ENSMUSP00000028999; ENSMUSG00000027499.
ENSMUST00000193330; ENSMUSP00000141466; ENSMUSG00000027499.
GeneIDi18767.
KEGGimmu:18767.
UCSCiuc008oof.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63554 mRNA. Translation: AAA39940.1.
AK139347 mRNA. Translation: BAE23970.1.
CH466577 Genomic DNA. Translation: EDL05208.1.
CH466577 Genomic DNA. Translation: EDL05209.1.
BC048244 mRNA. Translation: AAH48244.1.
CCDSiCCDS38383.1.
PIRiA40536.
RefSeqiNP_032888.1. NM_008862.3.
UniGeneiMm.3193.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APMX-ray2.00I6-25[»]
1ATPX-ray2.20I6-25[»]
1PVKmodel-I6-25[»]
2CPKX-ray2.70I6-25[»]
2GNFX-ray2.28I6-25[»]
2GNGX-ray1.87I6-25[»]
2QURX-ray2.50B6-25[»]
3FJQX-ray1.60I6-25[»]
3OW3X-ray1.90B6-25[»]
3QALX-ray1.70I6-23[»]
3QAMX-ray1.92I6-24[»]
4DFXX-ray1.35I6-25[»]
4DFZX-ray2.00I6-25[»]
4DG0X-ray2.00I6-25[»]
4DG2X-ray2.00I6-25[»]
4DG3X-ray1.80A6-25[»]
4DH1X-ray2.00I6-25[»]
4DH3X-ray2.20I6-25[»]
4DH5X-ray2.20I6-25[»]
4DH7X-ray1.80I6-25[»]
4DH8X-ray2.30I6-25[»]
4HPTX-ray2.15I6-25[»]
4HPUX-ray1.55I6-25[»]
ProteinModelPortaliP63248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202207. 1 interaction.
DIPiDIP-6087N.
IntActiP63248. 2 interactions.
MINTiMINT-4098688.
STRINGi10090.ENSMUSP00000028999.

PTM databases

PhosphoSiteiP63248.

Proteomic databases

PaxDbiP63248.
PRIDEiP63248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028999; ENSMUSP00000028999; ENSMUSG00000027499.
ENSMUST00000193330; ENSMUSP00000141466; ENSMUSG00000027499.
GeneIDi18767.
KEGGimmu:18767.
UCSCiuc008oof.1. mouse.

Organism-specific databases

CTDi5569.
MGIiMGI:104747. Pkia.

Phylogenomic databases

eggNOGiNOG45574.
GeneTreeiENSGT00530000064276.
HOGENOMiHOG000059641.
HOVERGENiHBG101093.
InParanoidiP63248.
KOiK15985.
OMAiTTNTTDV.
OrthoDBiEOG7JHM8S.
PhylomeDBiP63248.
TreeFamiTF330809.

Miscellaneous databases

EvolutionaryTraceiP63248.
NextBioi294971.
PROiP63248.
SOURCEiSearch...

Gene expression databases

BgeeiP63248.
CleanExiMM_PKIA.
GenevestigatoriP63248.

Family and domain databases

InterProiIPR004171. cAMP_dep_PKI.
[Graphical view]
PfamiPF02827. PKI. 1 hit.
[Graphical view]
PIRSFiPIRSF001667. PKI. 1 hit.
ProDomiPD010366. cAMP_dep_PKI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA clones for an inhibitor protein of cAMP-dependent protein kinase."
    Olsen S.R., Uhler M.D.
    J. Biol. Chem. 266:11158-11162(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.
  5. "Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor."
    Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H., Taylor S.S., Sowadski J.M.
    Biochemistry 32:2154-2161(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-25 IN COMPLEX WITH PRKACA.

Entry informationi

Entry nameiIPKA_MOUSE
AccessioniPrimary (citable) accession number: P63248
Secondary accession number(s): P27776, Q3UTL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2004
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The inhibitory site contains regions very similar to the hinge regions (sites that directly interact with the enzyme active site) and "pseudosubstrate site" of the regulatory chains; but, unlike these chains, PKI does not contain cAMP-binding sites. The arginine residues within the inhibitory site are essential for inhibition and recognition of the enzyme active site (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.