Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene

PRKAR2B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 sitei223 – 2231cAMP 1
Binding sitei232 – 2321cAMP 1
Binding sitei352 – 3521cAMP 2
Binding sitei361 – 3611cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi154 – 275122cAMP 1Add
BLAST
Nucleotide bindingi276 – 418143cAMP 2Add
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene namesi
Name:PRKAR2B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Colocalizes with PJA2 in the cytoplasm and at the cell membrane.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 418417cAMP-dependent protein kinase type II-beta regulatory subunitPRO_0000205389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCurated
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by the activated catalytic chain.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP31322.
PeptideAtlasiP31322.
PRIDEiP31322.

PTM databases

iPTMnetiP31322.

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.

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 the phosphorylated form of PJA2 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-547N.
STRINGi9913.ENSBTAP00000019916.

Structurei

3D structure databases

ProteinModelPortaliP31322.
SMRiP31322. Positions 3-41, 132-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 153152Dimerization and phosphorylationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP31322.
KOiK04739.

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.

P31322-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ EENERKGTAR
60 70 80 90 100
FGHEGRTWGD AGAAGGGGTP SKGVNFAEEP RHSDSENGEE EEEEAADAGA
110 120 130 140 150
FNAPVINRFT RRASVCAEAY NPDEEEDDAE SRIIHPKTDD QRNRLQEACK
160 170 180 190 200
DILLFKNLDP EQMSQVLDAM FEKLVKEGEH VIDQGDDGDN FYVIDRGTFD
210 220 230 240 250
IYVKCDGVGR CVGNYDNRGS FGELALMYNT PRAATITATS PGALWGLDRV
260 270 280 290 300
TFRRIIVKNN AKKRKMYESF IESLPFLKSL EVSERLKVVD VIGTKVYNDG
310 320 330 340 350
EQIIAQGDSA DSFFIVESGE VKITMKRKGK SEVEENGAVE IARCSRGQYF
360 370 380 390 400
GELALVTNKP RAASAHAIGT VKCLAMDVQA FERLLGPCME IMKRNIATYE
410
EQLVALFGTN MDIVEPTA
Length:418
Mass (Da):46,336
Last modified:January 23, 2007 - v2
Checksum:i669CE065D0455D3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05692 mRNA. Translation: AAA30755.1.
PIRiA36528. OKBOR2.
RefSeqiNP_777074.1. NM_174649.2.
UniGeneiBt.462.

Genome annotation databases

GeneIDi282463.
KEGGibta:282463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05692 mRNA. Translation: AAA30755.1.
PIRiA36528. OKBOR2.
RefSeqiNP_777074.1. NM_174649.2.
UniGeneiBt.462.

3D structure databases

ProteinModelPortaliP31322.
SMRiP31322. Positions 3-41, 132-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-547N.
STRINGi9913.ENSBTAP00000019916.

Chemistry

ChEMBLiCHEMBL2111446.

PTM databases

iPTMnetiP31322.

Proteomic databases

PaxDbiP31322.
PeptideAtlasiP31322.
PRIDEiP31322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282463.
KEGGibta:282463.

Organism-specific databases

CTDi5577.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP31322.
KOiK04739.

Miscellaneous databases

PROiP31322.

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...

Publicationsi

  1. "Identification of the MAP2- and P75-binding domain in the regulatory subunit (RII beta) of type II cAMP-dependent protein kinase. Cloning and expression of the cDNA for bovine brain RII beta."
    Luo Z., Shafit-Zagardo B., Erlichman J.
    J. Biol. Chem. 265:21804-21810(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiKAP3_BOVIN
AccessioniPrimary (citable) accession number: P31322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 110 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. 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.