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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

Prkar1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 1Add
BLAST
Nucleotide bindingi255 – 381127cAMP 2Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: MGI
  3. cAMP-dependent protein kinase regulator activity Source: MGI
  4. protein kinase A catalytic subunit binding Source: MGI
  5. ubiquitin protein ligase binding Source: MGI

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: MGI
  7. negative regulation of meiotic nuclear division 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_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_295338. PKA activation in glucagon signalling.
REACT_310977. PKA activation.
REACT_325290. DARPP-32 events.

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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:104878. Prkar1a.

Subcellular locationi

Cell membrane By similarity

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: MGI
  2. cAMP-dependent protein kinase complex Source: InterPro
  3. cytoplasm Source: MGI
  4. membrane Source: MGI
  5. neuromuscular junction Source: MGI
  6. plasma membrane Source: UniProtKB-SubCell
  7. protein complex Source: MGI
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 subunitPRO_0000205378Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedPRO_0000421786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylalanineCurated
Disulfide bondi18 – 18Interchain (with C-39)By similarity
Disulfide bondi39 – 39Interchain (with C-18)By similarity
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei77 – 771PhosphoserineBy 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

BgeeiQ9DBC7.
ExpressionAtlasiQ9DBC7. baseline and differential.
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).By similarity

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Motif

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

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

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.
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]
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

        10         20         30         40         50
MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL
60 70 80 90 100
REYFERLEKE EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI
110 120 130 140 150
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF
160 170 180 190 200
DAMFPVSFIA GETVIQQGDE GDNFYVIDQG EMDVYVNNEW ATSVGEGGSF
210 220 230 240 250
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL
260 270 280 290 300
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
310 320 330 340 350
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL
360 370 380
DRPRFERVLG PCSDILKRNI QQYNSFVSLS V
Length:381
Mass (Da):43,185
Last modified:January 23, 2007 - v3
Checksum:i08F164BB4528C63B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9DBC7.
SMRiQ9DBC7. Positions 14-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBC7. 13 interactions.
MINTiMINT-1741651.

2D gel databases

REPRODUCTION-2DPAGEIPI00762049.
Q9DBC7.

Proteomic databases

MaxQBiQ9DBC7.
PaxDbiQ9DBC7.
PRIDEiQ9DBC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5573.
MGIiMGI:104878. Prkar1a.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_295338. PKA activation in glucagon signalling.
REACT_310977. PKA activation.
REACT_325290. DARPP-32 events.

Miscellaneous databases

ChiTaRSiPrkar1a. mouse.
NextBioi295622.
PROiQ9DBC7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBC7.
ExpressionAtlasiQ9DBC7. baseline and differential.
GenevestigatoriQ9DBC7.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. cAMP/cGMP_kin.
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]
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]
ProtoNetiSearch...

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(2004) [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(2003) [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(1999) [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(1997) [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(2007) [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(2008) [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(2009) [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: April 1, 2015
This is version 118 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

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.