P31323 (KAP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit

Gene names

Name:

PRKAR2B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.8
Subcellular location	Cytoplasm. Cell membrane. Note: Co-localizes with PJA2 in the cytoplasm and at the cell membrane. Ref.8
Tissue specificity	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.
Post-translational modification	Phosphorylated by the activated catalytic chain.
Sequence similarities	Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome activation of phospholipase C activity Traceable author statement. Source: Reactome activation of protein kinase A activity Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cellular response to glucagon stimulus Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fatty acid metabolic process Inferred from electronic annotation. Source: Compara fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome intracellular signal transduction Traceable author statement Ref.1. Source: ProtInc learning Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome response to antipsychotic drug Inferred from electronic annotation. Source: Compara response to clozapine Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Traceable author statement Ref.1. Source: ProtInc ubiquitin protein ligase binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 418	417	cAMP-dependent protein kinase type II-beta regulatory subunit		PRO_0000205390
Regions
	Nucleotide binding	154 – 275	122	cAMP 1
	Nucleotide binding	276 – 418	143	cAMP 2
	Region	2 – 153	152	Dimerization and phosphorylation
Sites
	Binding site	223	1	cAMP 1
	Binding site	232	1	cAMP 1
	Binding site	352	1	cAMP 2
	Binding site	361	1	cAMP 2
Amino acid modifications
	Modified residue	2	1	N-acetylserine Probable
	Modified residue	83	1	Phosphoserine Ref.9
	Modified residue	85	1	Phosphoserine Ref.9
	Modified residue	114	1	Phosphoserine Ref.5 Ref.6 Ref.9
Natural variations
	Natural variant	335	1	E → D. Corresponds to variant rs3729881 [ dbSNP | Ensembl ].		VAR_046549
Experimental info
	Sequence conflict	341 – 342	2	IA → MP in AAA60099. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31323 [UniParc]. Last modified September 23, 2008. Version 3. Checksum: 83F402CCFFEFD186	FASTA	418	46,302
	10 20 30 40 50 60 MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGTAR FGHEGRTWGD 70 80 90 100 110 120 LGAAAGGGTP SKGVNFAEEP MQSDSEDGEE EEAAPADAGA FNAPVINRFT RRASVCAEAY 130 140 150 160 170 180 NPDEEEDDAE SRIIHPKTDD QRNRLQEACK DILLFKNLDP EQMSQVLDAM FEKLVKDGEH 190 200 210 220 230 240 VIDQGDDGDN FYVIDRGTFD IYVKCDGVGR CVGNYDNRGS FGELALMYNT PRAATITATS 250 260 270 280 290 300 PGALWGLDRV TFRRIIVKNN AKKRKMYESF IESLPFLKSL EFSERLKVVD VIGTKVYNDG 310 320 330 340 350 360 EQIIAQGDSA DSFFIVESGE VKITMKRKGK SEVEENGAVE IARCSRGQYF GELALVTNKP 370 380 390 400 410 RAASAHAIGT VKCLAMDVQA FERLLGPCME IMKRNIATYE EQLVALFGTN MDIVEPTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, complementary deoxyribonucleic acid structure and predicted full-length amino acid sequence of the hormone-inducible regulatory subunit of 3'-5'-cyclic adenosine monophosphate-dependent protein kinase from human testis." Levy F.O., Oeyen O., Sandberg M., Tasken K., Eskild W., Hansson V., Jahnsen T. Mol. Endocrinol. 2:1364-1373(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Control of PKA stability and signalling by the RING ligase praja2." Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A. Nat. Cell Biol. 13:412-422(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-114, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31158 mRNA. Translation: AAA60099.1. AK291441 mRNA. Translation: BAF84130.1. CH236947 Genomic DNA. Translation: EAL24395.1. CH471070 Genomic DNA. Translation: EAW83390.1.
IPI	IPI00554752.
PIR	OKHUR2. A40915.
RefSeq	NP_002727.2. NM_002736.2.
UniGene	Hs.433068.
3D structure databases
ProteinModelPortal	P31323.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-554N.
IntAct	P31323. 5 interactions.
MINT	MINT-2782562.
STRING	9606.ENSP00000265717.
PTM databases
PhosphoSite	P31323.
Polymorphism databases
DMDM	206729918.
2D gel databases
OGP	P31323.
Proteomic databases
PaxDb	P31323.
PRIDE	P31323.
Protocols and materials databases
DNASU	5577.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265717; ENSP00000265717; ENSG00000005249. ENST00000543645; ENSP00000440531; ENSG00000005249.
GeneID	5577.
KEGG	hsa:5577.
UCSC	uc003vdx.3. human.
Organism-specific databases
CTD	5577.
GeneCards	GC07P106685.
H-InvDB	HIX0025309.
HGNC	HGNC:9392. PRKAR2B.
HPA	HPA008421.
MIM	176912. gene.
neXtProt	NX_P31323.
PharmGKB	PA33758.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0664.
HOGENOM	HOG000196668.
HOVERGEN	HBG002025.
InParanoid	P31323.
KO	K04739.
OMA	MYENFIE.
OrthoDB	EOG4RV2RN.
PhylomeDB	P31323.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_115566. Cell Cycle. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P31323.
Bgee	P31323.
CleanEx	HS_PRKAR2B.
Genevestigator	P31323.
GermOnline	ENSG00000005249. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
InterPro	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]
Pfam	PF00027. cNMP_binding. 2 hits. PF02197. RIIa. 1 hit. [Graphical view]
PIRSF	PIRSF000548. PK_regulatory. 1 hit.
PRINTS	PR00103. CAMPKINASE.
SMART	SM00100. cNMP. 2 hits. SM00394. RIIa. 1 hit. [Graphical view]
SUPFAM	SSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit. SSF51206. cNMP_binding. 2 hits.
PROSITE	PS00888. CNMP_BINDING_1. 2 hits. PS00889. CNMP_BINDING_2. 2 hits. PS50042. CNMP_BINDING_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P31323.
ChEMBL	CHEMBL2270.
GenomeRNAi	5577.
NextBio	21624.
SOURCE	Search...

Entry information

Entry name

KAP3_HUMAN

Accession

Primary (citable) accession number: P31323
Secondary accession number(s): A4D0R9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.