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P63248

- IPKA_MOUSE

UniProt

P63248 - IPKA_MOUSE

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Protein

cAMP-dependent protein kinase inhibitor alpha

Gene

Pkia

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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: 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

MaxQBiP63248.
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:
PDBe
RCSB PDB
PDBj
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 23, 2007 - v2
Checksum:iFCCE07281498788A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi18767.
KEGGimmu:18767.
UCSCiuc008oof.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS38383.1.
PIRi A40536.
RefSeqi NP_032888.1. NM_008862.3.
UniGenei Mm.3193.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APM X-ray 2.00 I 6-25 [» ]
1ATP X-ray 2.20 I 6-25 [» ]
1PVK model - I 6-25 [» ]
2CPK X-ray 2.70 I 6-25 [» ]
2GNF X-ray 2.28 I 6-25 [» ]
2GNG X-ray 1.87 I 6-25 [» ]
2QUR X-ray 2.50 B 6-25 [» ]
3FJQ X-ray 1.60 I 6-25 [» ]
3OW3 X-ray 1.90 B 6-25 [» ]
3QAL X-ray 1.70 I 6-23 [» ]
3QAM X-ray 1.92 I 6-24 [» ]
4DFX X-ray 1.35 I 6-25 [» ]
4DFZ X-ray 2.00 I 6-25 [» ]
4DG0 X-ray 2.00 I 6-25 [» ]
4DG2 X-ray 2.00 I 6-25 [» ]
4DG3 X-ray 1.80 A 6-25 [» ]
4DH1 X-ray 2.00 I 6-25 [» ]
4DH3 X-ray 2.20 I 6-25 [» ]
4DH5 X-ray 2.20 I 6-25 [» ]
4DH7 X-ray 1.80 I 6-25 [» ]
4DH8 X-ray 2.30 I 6-25 [» ]
4HPT X-ray 2.15 I 6-25 [» ]
4HPU X-ray 1.55 I 6-25 [» ]
ProteinModelPortali P63248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202207. 1 interaction.
DIPi DIP-6087N.
IntActi P63248. 2 interactions.
MINTi MINT-4098688.
STRINGi 10090.ENSMUSP00000028999.

PTM databases

PhosphoSitei P63248.

Proteomic databases

MaxQBi P63248.
PaxDbi P63248.
PRIDEi P63248.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028999 ; ENSMUSP00000028999 ; ENSMUSG00000027499 .
GeneIDi 18767.
KEGGi mmu:18767.
UCSCi uc008oof.1. mouse.

Organism-specific databases

CTDi 5569.
MGIi MGI:104747. Pkia.

Phylogenomic databases

eggNOGi NOG45574.
GeneTreei ENSGT00530000064276.
HOGENOMi HOG000059641.
HOVERGENi HBG101093.
InParanoidi P63248.
KOi K15985.
OMAi TTNTTDV.
OrthoDBi EOG7JHM8S.
PhylomeDBi P63248.
TreeFami TF330809.

Miscellaneous databases

EvolutionaryTracei P63248.
NextBioi 294971.
PROi P63248.
SOURCEi Search...

Gene expression databases

Bgeei P63248.
CleanExi MM_PKIA.
Genevestigatori P63248.

Family and domain databases

InterProi IPR004171. cAMP_dep_PKI.
[Graphical view ]
Pfami PF02827. PKI. 1 hit.
[Graphical view ]
PIRSFi PIRSF001667. PKI. 1 hit.
ProDomi PD010366. cAMP_dep_PKI. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

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(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.
    , 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.

Entry informationi

Entry nameiIPKA_MOUSE
AccessioniPrimary (citable) accession number: P63248
Secondary accession number(s): P27776, Q3UTL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 84 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