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P12368

- KAP2_RAT

UniProt

P12368 - KAP2_RAT

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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene
Prkar2a
Organism
Rattus norvegicus (Rat)
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. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei205 – 2051cAMP 1 By similarity
Binding sitei214 – 2141cAMP 1 By similarity
Binding sitei335 – 3351cAMP 2 By similarity
Binding sitei344 – 3441cAMP 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 257122cAMP 1 By similarityAdd
BLAST
Nucleotide bindingi258 – 401144cAMP 2 By similarityAdd
BLAST

GO - Molecular functioni

  1. cAMP binding Source: RGD
  2. cAMP-dependent protein kinase regulator activity Source: RGD
  3. protein binding Source: RGD
  4. protein domain specific binding Source: RGD
  5. protein homodimerization activity Source: RGD
  6. protein kinase A catalytic subunit binding Source: RGD
  7. small molecule binding Source: RGD

GO - Biological processi

  1. protein heterooligomerization Source: RGD
  2. regulation of protein kinase activity Source: RGD
  3. response to clozapine Source: RGD
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene namesi
Name:Prkar2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3393. Prkar2a.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity
Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane By similarity.

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: RGD
  2. cytoplasm Source: RGD
  3. perinuclear region of cytoplasm Source: RGD
  4. protein complex Source: RGD
  5. T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 401400cAMP-dependent protein kinase type II-alpha regulatory subunitPRO_0000205388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei48 – 481Phosphoserine By similarity
Modified residuei75 – 751Phosphoserine By similarity
Modified residuei77 – 771Phosphoserine By similarity
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei212 – 2121Phosphothreonine; by PDPK1 By similarity

Post-translational modificationi

Phosphorylated by the activated catalytic chain.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP12368.
PRIDEiP12368.

PTM databases

PhosphoSiteiP12368.

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

GenevestigatoriP12368.

Interactioni

Subunit structurei

The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4 and CBFA2T3 By similarity. Interacts with the phosphorylated form of PJA2 By similarity. Interacts with MYRIP; his interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release.1 Publication

Protein-protein interaction databases

DIPiDIP-555N.
IntActiP12368. 4 interactions.
MINTiMINT-4564663.
STRINGi10116.ENSRNOP00000027552.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2415
Helixi29 – 4315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-A/B1-45[»]
2H9RNMR-A/B1-45[»]
2HWNX-ray1.60A/B/C/D1-45[»]
3TMHX-ray3.80B/C/F/G1-45[»]
ProteinModelPortaliP12368.
SMRiP12368. Positions 1-45, 93-393.

Miscellaneous databases

EvolutionaryTraceiP12368.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 135134Dimerization and phosphorylationAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP12368.
KOiK04739.
PhylomeDBiP12368.

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.

P12368-1 [UniParc]FASTAAdd to Basket

« Hide

MSHIQIPPGL TELLQGYTVE VLRQQPPDLV DFAVEYFTRL REARRQESDS    50
FIAPPTTFHA QESSGVPVIE EDGESESDSD DEDLEVPIPS KFTRRVSVCA 100
ETFNPDEEED NDPRVVHPKT DEQRYRLQEA CKDILLFKNL DQEQLSQVLD 150
AMFEKIVKTD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNR 200
GSFGELALMY NTPRAATIVA TSDGSLWGLD RVTFRRIIVK NNAKKRKMFE 250
SFIESVPLFK SLEMSERMKI VDVIGEKIYK DGERIITQGE KADSFYIIES 300
GEVSILIRSK TKTNKNGGNQ EVEIAHCHKG QYFGELALVT NKPRAASAYA 350
VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSNLDLLDPG 400
Q 401
Length:401
Mass (Da):45,540
Last modified:January 23, 2007 - v3
Checksum:i026FEBFCFACA9C7D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741E → Q in AAA41856. 1 Publication
Sequence conflicti90 – 901S → A in AAA41856. 1 Publication
Sequence conflicti125 – 1251Y → C in AAA41856. 1 Publication
Sequence conflicti154 – 1552EK → KR in AAA41856. 1 Publication
Sequence conflicti198 – 1981D → A in AAA41856. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF533978 mRNA. Translation: AAM97689.1.
J02934 mRNA. Translation: AAA41856.1.
PIRiA28325. OKRT2R.
RefSeqiNP_062137.1. NM_019264.2.
UniGeneiRn.9742.

Genome annotation databases

GeneIDi29699.
KEGGirno:29699.
UCSCiRGD:3393. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF533978 mRNA. Translation: AAM97689.1 .
J02934 mRNA. Translation: AAA41856.1 .
PIRi A28325. OKRT2R.
RefSeqi NP_062137.1. NM_019264.2.
UniGenei Rn.9742.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DRN NMR - A/B 1-45 [» ]
2H9R NMR - A/B 1-45 [» ]
2HWN X-ray 1.60 A/B/C/D 1-45 [» ]
3TMH X-ray 3.80 B/C/F/G 1-45 [» ]
ProteinModelPortali P12368.
SMRi P12368. Positions 1-45, 93-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-555N.
IntActi P12368. 4 interactions.
MINTi MINT-4564663.
STRINGi 10116.ENSRNOP00000027552.

PTM databases

PhosphoSitei P12368.

Proteomic databases

PaxDbi P12368.
PRIDEi P12368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29699.
KEGGi rno:29699.
UCSCi RGD:3393. rat.

Organism-specific databases

CTDi 5576.
RGDi 3393. Prkar2a.

Phylogenomic databases

eggNOGi COG0664.
HOGENOMi HOG000196668.
HOVERGENi HBG002025.
InParanoidi P12368.
KOi K04739.
PhylomeDBi P12368.

Miscellaneous databases

EvolutionaryTracei P12368.
NextBioi 610099.
PROi P12368.

Gene expression databases

Genevestigatori P12368.

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. "cDNA sequence and complete coding region of cAMP-dependent protein kinase type II regulatory subunit from a rat testicular germ cell cDNA library."
    Ziemba A.J., Collard M.W.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain."
    Scott J.D., Glaccum M.B., Zoller M.J., Uhler M.D., Helfman D.M., McKnight G.S., Krebs E.G.
    Proc. Natl. Acad. Sci. U.S.A. 84:5192-5196(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-401.
    Tissue: Skeletal muscle.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: INTERACTION WITH MYRIP.

Entry informationi

Entry nameiKAP2_RAT
AccessioniPrimary (citable) accession number: P12368
Secondary accession number(s): Q8K1M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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