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Q9DBC7 (KAP0_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene names
Name:Prkar1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells By similarity.

Subunit structure

The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with PRKX; regulates this cAMP-dependent protein kinase By similarity. Interacts with CBFA2T3. Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA By similarity. Ref.4 Ref.9

Subcellular location

Cell membrane By similarity.

Post-translational modification

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity By similarity.

Miscellaneous

Two types of regulatory chains are found: type I, which predominates in skeletal muscle, and type II, which predominates in cardiac muscle By similarity.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 18316483. Source: MGI

cell proliferation

Traceable author statement PubMed 7775586. Source: MGI

female meiotic division

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from mutant phenotype PubMed 18316483. Source: MGI

mesoderm formation

Inferred from mutant phenotype PubMed 12004056. Source: MGI

negative regulation of cAMP-dependent protein kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from mutant phenotype PubMed 18316483. Source: MGI

organ morphogenesis

Traceable author statement PubMed 7775586. Source: MGI

protein phosphorylation

Traceable author statement PubMed 7775586. Source: MGI

sarcomere organization

Inferred from mutant phenotype PubMed 18316483. Source: MGI

   Cellular_componentAMP-activated protein kinase complex

Inferred from electronic annotation. Source: Ensembl

cAMP-dependent protein kinase complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 1448119. Source: MGI

neuromuscular junction

Inferred from direct assay PubMed 8794865. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

cAMP-dependent protein kinase regulator activity

Inferred from direct assay PubMed 7775586. Source: MGI

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bcl2l11O54918-12EBI-645677,EBI-526076

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunit
PRO_0000205378
Initiator methionine11Removed; alternate By similarity
Chain2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
PRO_0000421786

Regions

Nucleotide binding137 – 254118cAMP 1
Nucleotide binding255 – 381127cAMP 2
Region1 – 136136Dimerization and phosphorylation
Motif96 – 1005Pseudophosphorylation motif

Sites

Binding site2021cAMP 1
Binding site2111cAMP 1
Binding site3261cAMP 2
Binding site3351cAMP 2

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylalanine Probable
Modified residue831Phosphoserine Ref.6 Ref.8
Modified residue1011Phosphoserine Ref.5
Disulfide bond18Interchain (with C-39) By similarity
Disulfide bond39Interchain (with C-18) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBC7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 08F164BB4528C63B

FASTA38143,185
        10         20         30         40         50         60 
MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL REYFERLEKE 

        70         80         90        100        110        120 
EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK 

       130        140        150        160        170        180 
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG 

       190        200        210        220        230        240 
EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL 

       250        260        270        280        290        300 
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA 

       310        320        330        340        350        360 
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG 

       370        380 
PCSDILKRNI QQYNSFVSLS V 

« Hide

References

« Hide 'large scale' references
[1]"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: Bone marrow, Kidney, Liver and Placenta.
[2]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"Alternative 5'-exons of the mouse cAMP-dependent protein kinase subunit RIalpha gene are conserved and expressed in both a ubiquitous and tissue-restricted fashion."
Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M.
FEBS Lett. 476:272-276(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
[4]"Identification of tethering domains for protein kinase A type Ialpha regulatory subunits on sperm fibrous sheath protein FSC1."
Miki K., Eddy E.M.
J. Biol. Chem. 273:34384-34390(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKAP4.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a phospho-regulated manner."
Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.
FEBS Lett. 584:873-877(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBFA2T3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005039 mRNA. Translation: BAB23766.1.
AK027916 mRNA. Translation: BAC25664.1.
AK051068 mRNA. Translation: BAC34516.1.
AK145797 mRNA. Translation: BAE26655.1.
AK145860 mRNA. Translation: BAE26704.1.
AK147188 mRNA. Translation: BAE27748.1.
AK150427 mRNA. Translation: BAE29550.1.
AK151124 mRNA. Translation: BAE30132.1.
AK153227 mRNA. Translation: BAE31820.1.
BC003461 mRNA. Translation: AAH03461.1.
BC005697 mRNA. Translation: AAH05697.1.
AJ278427 Genomic DNA. Translation: CAB94778.1.
AJ278429 Genomic DNA. Translation: CAB94718.1.
CCDSCCDS25583.1.
RefSeqNP_068680.1. NM_021880.2.
XP_006532574.1. XM_006532511.1.
UniGeneMm.30039.

3D structure databases

ProteinModelPortalQ9DBC7.
SMRQ9DBC7. Positions 14-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DBC7. 13 interactions.
MINTMINT-1741651.

2D gel databases

REPRODUCTION-2DPAGEIPI00762049.
Q9DBC7.

Proteomic databases

MaxQBQ9DBC7.
PaxDbQ9DBC7.
PRIDEQ9DBC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612.
ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
GeneID19084.
KEGGmmu:19084.
UCSCuc007mcu.1. mouse.

Organism-specific databases

CTD5573.
MGIMGI:104878. Prkar1a.

Phylogenomic databases

eggNOGCOG0664.
GeneTreeENSGT00530000062947.
HOVERGENHBG002025.
InParanoidQ9DBC7.
KOK04739.
OMAFSAEVYT.
OrthoDBEOG72JWG6.
TreeFamTF314920.

Gene expression databases

ArrayExpressQ9DBC7.
BgeeQ9DBC7.
GenevestigatorQ9DBC7.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR002373. cAMP/cGMP_kin.
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAR1A. mouse.
NextBio295622.
PROQ9DBC7.
SOURCESearch...

Entry information

Entry nameKAP0_MOUSE
AccessionPrimary (citable) accession number: Q9DBC7
Secondary accession number(s): Q3UKU7, Q9JHR5, Q9JHR6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 3 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

MGD cross-references

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