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P63248 (IPKA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase inhibitor alpha

Short name=PKI-alpha
Alternative name(s):
cAMP-dependent protein kinase inhibitor, muscle/brain isoform
Gene names
Name:Pkia
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length76 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Tissue specificity

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

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.

Sequence similarities

Belongs to the PKI family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7675cAMP-dependent protein kinase inhibitor alpha
PRO_0000154533

Sites

Site161Important for inhibition By similarity
Site191Important for inhibition By similarity
Site201Important for inhibition By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity

Secondary structure

... 76
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63248 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FCCE07281498788A

FASTA767,960
        10         20         30         40         50         60 
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEDDGQRSS 

        70 
TEQSGEAQGE AAKSES 

« Hide

References

« Hide 'large scale' references
[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(1991) [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. expand/collapse author list , 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(2005) [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 (SEP-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(2004) [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(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-25 IN COMPLEX WITH PRKACA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS38383.1.
PIRA40536.
RefSeqNP_032888.1. NM_008862.3.
UniGeneMm.3193.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP63248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202207. 1 interaction.
DIPDIP-6087N.
IntActP63248. 2 interactions.
MINTMINT-4098688.
STRING10090.ENSMUSP00000028999.

PTM databases

PhosphoSiteP63248.

Proteomic databases

MaxQBP63248.
PaxDbP63248.
PRIDEP63248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028999; ENSMUSP00000028999; ENSMUSG00000027499.
GeneID18767.
KEGGmmu:18767.
UCSCuc008oof.1. mouse.

Organism-specific databases

CTD5569.
MGIMGI:104747. Pkia.

Phylogenomic databases

eggNOGNOG45574.
GeneTreeENSGT00530000064276.
HOGENOMHOG000059641.
HOVERGENHBG101093.
InParanoidP63248.
KOK15985.
OMATTNTTDV.
OrthoDBEOG7JHM8S.
PhylomeDBP63248.
TreeFamTF330809.

Gene expression databases

BgeeP63248.
CleanExMM_PKIA.
GenevestigatorP63248.

Family and domain databases

InterProIPR004171. cAMP_dep_PKI.
[Graphical view]
PfamPF02827. PKI. 1 hit.
[Graphical view]
PIRSFPIRSF001667. PKI. 1 hit.
ProDomPD010366. cAMP_dep_PKI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP63248.
NextBio294971.
PROP63248.
SOURCESearch...

Entry information

Entry nameIPKA_MOUSE
AccessionPrimary (citable) accession number: P63248
Secondary accession number(s): P27776, Q3UTL0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot