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Q9DBC7

- KAP0_MOUSE

UniProt

Q9DBC7 - KAP0_MOUSE

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Protein
cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene
Prkar1a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021cAMP 1
Binding sitei211 – 2111cAMP 1
Binding sitei326 – 3261cAMP 2
Binding sitei335 – 3351cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 254118cAMP 1
Add
BLAST
Nucleotide bindingi255 – 381127cAMP 2
Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  3. cAMP-dependent protein kinase regulator activity Source: MGI
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cardiac muscle cell proliferation Source: MGI
  2. cell proliferation Source: MGI
  3. female meiotic division Source: Ensembl
  4. heart development Source: MGI
  5. mesoderm formation Source: MGI
  6. negative regulation of cAMP-dependent protein kinase activity Source: Ensembl
  7. negative regulation of meiosis Source: Ensembl
  8. negative regulation of protein kinase activity Source: MGI
  9. organ morphogenesis Source: MGI
  10. protein phosphorylation Source: MGI
  11. sarcomere organization Source: MGI
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit
Cleaved into the following chain:
Gene namesi
Name:Prkar1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104878. Prkar1a.

Subcellular locationi

Cell membrane By similarity

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. cAMP-dependent protein kinase complex Source: Ensembl
  3. cytoplasm Source: MGI
  4. neuromuscular junction Source: MGI
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunit
PRO_0000205378Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
PRO_0000421786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei2 – 21N-acetylalanine Inferred
Disulfide bondi18 – 18Interchain (with C-39) By similarity
Disulfide bondi39 – 39Interchain (with C-18) By similarity
Modified residuei83 – 831Phosphoserine2 Publications
Modified residuei101 – 1011Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9DBC7.
PaxDbiQ9DBC7.
PRIDEiQ9DBC7.

2D gel databases

REPRODUCTION-2DPAGEIPI00762049.
Q9DBC7.

Expressioni

Gene expression databases

ArrayExpressiQ9DBC7.
BgeeiQ9DBC7.
GenevestigatoriQ9DBC7.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bcl2l11O54918-12EBI-645677,EBI-526076

Protein-protein interaction databases

IntActiQ9DBC7. 13 interactions.
MINTiMINT-1741651.

Structurei

3D structure databases

ProteinModelPortaliQ9DBC7.
SMRiQ9DBC7. Positions 14-380.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 136136Dimerization and phosphorylation
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1005Pseudophosphorylation motif

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOVERGENiHBG002025.
InParanoidiQ9DBC7.
KOiK04739.
OMAiFSAEVYT.
OrthoDBiEOG72JWG6.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DBC7-1 [UniParc]FASTAAdd to Basket

« Hide

MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL    50
REYFERLEKE EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI 100
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF 150
DAMFPVSFIA GETVIQQGDE GDNFYVIDQG EMDVYVNNEW ATSVGEGGSF 200
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL 250
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA 300
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL 350
DRPRFERVLG PCSDILKRNI QQYNSFVSLS V 381
Length:381
Mass (Da):43,185
Last modified:January 23, 2007 - v3
Checksum:i08F164BB4528C63B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS25583.1.
RefSeqiNP_068680.1. NM_021880.2.
XP_006532574.1. XM_006532511.1.
UniGeneiMm.30039.

Genome annotation databases

EnsembliENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612.
ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
GeneIDi19084.
KEGGimmu:19084.
UCSCiuc007mcu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS25583.1.
RefSeqi NP_068680.1. NM_021880.2.
XP_006532574.1. XM_006532511.1.
UniGenei Mm.30039.

3D structure databases

ProteinModelPortali Q9DBC7.
SMRi Q9DBC7. Positions 14-380.
ModBasei Search...

Protein-protein interaction databases

IntActi Q9DBC7. 13 interactions.
MINTi MINT-1741651.

2D gel databases

REPRODUCTION-2DPAGE IPI00762049.
Q9DBC7.

Proteomic databases

MaxQBi Q9DBC7.
PaxDbi Q9DBC7.
PRIDEi Q9DBC7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049527 ; ENSMUSP00000056500 ; ENSMUSG00000020612 .
ENSMUST00000106677 ; ENSMUSP00000102288 ; ENSMUSG00000020612 .
GeneIDi 19084.
KEGGi mmu:19084.
UCSCi uc007mcu.1. mouse.

Organism-specific databases

CTDi 5573.
MGIi MGI:104878. Prkar1a.

Phylogenomic databases

eggNOGi COG0664.
GeneTreei ENSGT00530000062947.
HOVERGENi HBG002025.
InParanoidi Q9DBC7.
KOi K04739.
OMAi FSAEVYT.
OrthoDBi EOG72JWG6.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.

Miscellaneous databases

ChiTaRSi PRKAR1A. mouse.
NextBioi 295622.
PROi Q9DBC7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9DBC7.
Bgeei Q9DBC7.
Genevestigatori Q9DBC7.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR002373. 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 ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. 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.

Entry informationi

Entry nameiKAP0_MOUSE
AccessioniPrimary (citable) accession number: Q9DBC7
Secondary accession number(s): Q3UKU7, Q9JHR5, Q9JHR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi