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Protein

cAMP-dependent protein kinase type I-beta regulatory subunit

Gene

Prkar1b

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)DescriptionActionsGraphical viewLength
Binding sitei202cAMP 11
Binding sitei211cAMP 11
Binding sitei326cAMP 21
Binding sitei335cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi137 – 254cAMP 1Add BLAST118
Nucleotide bindingi255 – 381cAMP 2Add BLAST127

GO - Molecular functioni

GO - Biological processi

  • animal organ morphogenesis Source: MGI
  • cell proliferation Source: MGI
  • learning or memory Source: MGI
  • negative regulation of cAMP-dependent protein kinase activity Source: MGI
  • protein phosphorylation Source: MGI
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-180024. DARPP-32 events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type I-beta regulatory subunit
Gene namesi
Name:Prkar1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:97759. Prkar1b.

Subcellular locationi

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: InterPro
  • cytoplasm Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002053822 – 381cAMP-dependent protein kinase type I-beta regulatory subunitAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Disulfide bondi18Interchain (with C-39)By similarity
Modified residuei21Nitrated tyrosineBy similarity1
Disulfide bondi39Interchain (with C-18)By similarity
Modified residuei77PhosphoserineCombined sources1
Modified residuei83PhosphoserineCombined sources1
Modified residuei85PhosphothreonineCombined sources1
Modified residuei97Omega-N-methylarginineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Methylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP12849.
PaxDbiP12849.
PeptideAtlasiP12849.
PRIDEiP12849.

PTM databases

iPTMnetiP12849.
PhosphoSitePlusiP12849.

Expressioni

Tissue specificityi

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Gene expression databases

BgeeiENSMUSG00000025855.
ExpressionAtlasiP12849. baseline and differential.
GenevisibleiP12849. MM.

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. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1B to the plasma membrane (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP12849. 5 interactors.
STRINGi10090.ENSMUSP00000026973.

Structurei

3D structure databases

ProteinModelPortaliP12849.
SMRiP12849.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 136Dimerization and phosphorylationAdd BLAST135

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 100Pseudophosphorylation motif5

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP12849.
KOiK04739.
OMAiDQWERAN.
OrthoDBiEOG091G0F1K.
PhylomeDBiP12849.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
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.

P12849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPSCFHSE DEDSLKGCEM YVQKHGIQQV LKECIVHLCV AKPDRPLRFL
60 70 80 90 100
REHFEKLEKE ENRQILARQK SNSQCDSHDE EISPTPPNPV VKARRRRGGV
110 120 130 140 150
SAEVYTEEDA VSYVRKVIPK DYKTMTALAK AISKNVLFSH LDDNERSDIF
160 170 180 190 200
DAMFPVTHIG GETVIQQGNE GDNFYVIDQG EVDVYVNGEW VTNISEGGSF
210 220 230 240 250
GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL RKRKMYEEFL
260 270 280 290 300
SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA
310 320 330 340 350
SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL
360 370 380
DRPRFERVLG PCSEILKRNI QRYNSFISLT V
Length:381
Mass (Da):43,224
Last modified:January 23, 2007 - v2
Checksum:i42287E553FA16023
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20473 mRNA. Translation: AAA39935.1.
CCDSiCCDS19803.1.
PIRiA30205. OKMSR1.
RefSeqiNP_001240819.1. NM_001253890.1.
NP_032949.3. NM_008923.3.
XP_006504723.1. XM_006504660.3.
XP_006504724.1. XM_006504661.3.
XP_006504726.1. XM_006504663.2.
XP_017176208.1. XM_017320719.1.
UniGeneiMm.306163.

Genome annotation databases

EnsembliENSMUST00000026973; ENSMUSP00000026973; ENSMUSG00000025855.
ENSMUST00000110890; ENSMUSP00000106515; ENSMUSG00000025855.
GeneIDi19085.
KEGGimmu:19085.
UCSCiuc009afy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20473 mRNA. Translation: AAA39935.1.
CCDSiCCDS19803.1.
PIRiA30205. OKMSR1.
RefSeqiNP_001240819.1. NM_001253890.1.
NP_032949.3. NM_008923.3.
XP_006504723.1. XM_006504660.3.
XP_006504724.1. XM_006504661.3.
XP_006504726.1. XM_006504663.2.
XP_017176208.1. XM_017320719.1.
UniGeneiMm.306163.

3D structure databases

ProteinModelPortaliP12849.
SMRiP12849.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12849. 5 interactors.
STRINGi10090.ENSMUSP00000026973.

PTM databases

iPTMnetiP12849.
PhosphoSitePlusiP12849.

Proteomic databases

MaxQBiP12849.
PaxDbiP12849.
PeptideAtlasiP12849.
PRIDEiP12849.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026973; ENSMUSP00000026973; ENSMUSG00000025855.
ENSMUST00000110890; ENSMUSP00000106515; ENSMUSG00000025855.
GeneIDi19085.
KEGGimmu:19085.
UCSCiuc009afy.2. mouse.

Organism-specific databases

CTDi5575.
MGIiMGI:97759. Prkar1b.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP12849.
KOiK04739.
OMAiDQWERAN.
OrthoDBiEOG091G0F1K.
PhylomeDBiP12849.
TreeFamiTF314920.

Enzyme and pathway databases

ReactomeiR-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-180024. DARPP-32 events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiPrkar1b. mouse.
PROiP12849.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025855.
ExpressionAtlasiP12849. baseline and differential.
GenevisibleiP12849. MM.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
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...

Entry informationi

Entry nameiKAP1_MOUSE
AccessioniPrimary (citable) accession number: P12849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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 one 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.