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Reviewed, UniProtKB/Swiss-Prot P13861 (KAP2_HUMAN)

Last modified February 9, 2010. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene names
Name: PRKAR2A
Synonyms: PKR2, PRKAR2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 AKAP4 and CBFA2T3. Ref.3

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 404403cAMP-dependent protein kinase type II-alpha regulatory subunit
PRO_0000205385

Regions

Nucleotide binding139 – 260122cAMP 1
Nucleotide binding261 – 404144cAMP 2
Region2 – 138137Dimerization and phosphorylation

Sites

Binding site2081cAMP 1
Binding site2171cAMP 1
Binding site3381cAMP 2
Binding site3471cAMP 2

Amino acid modifications

Modified residue21N-acetylserine Probable
Modified residue541Phosphothreonine Ref.8 Ref.12
Modified residue581Phosphoserine Ref.8 Ref.12
Modified residue781Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17
Modified residue801Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17
Modified residue991Phosphoserine; by PKA Ref.5 Ref.12 Ref.13 Ref.17

Secondary structure

1 ..... 404
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13861-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C7D6E8E476E1DB65

FASTA40445,518
        10         20         30         40         50         60 
MSHIQIPPGL TELLQGYTVE VLRQQPPDLV EFAVEYFTRL REARAPASVL PAATPRQSLG 

        70         80         90        100        110        120 
HPPPEPGPDR VADAKGDSES EEDEDLEVPV PSRFNRRVSV CAETYNPDEE EEDTDPRVIH 

       130        140        150        160        170        180 
PKTDEQRCRL QEACKDILLF KNLDQEQLSQ VLDAMFERIV KADEHVIDQG DDGDNFYVIE 

       190        200        210        220        230        240 
RGTYDILVTK DNQTRSVGQY DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI 

       250        260        270        280        290        300 
IVKNNAKKRK MFESFIESVP LLKSLEVSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI 

       310        320        330        340        350        360 
IESGEVSILI RSRTKSNKDG GNQEVEIARC HKGQYFGELA LVTNKPRAAS AYAVGDVKCL 

       370        380        390        400 
VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSVDLG NLGQ

« Hide

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References

« Hide 'large scale' references
[1]"Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent protein kinase encodes an alternate amino-terminal region."
Oyen O., Myklebust F., Scott J.D., Hansson V., Jahnsen T.
FEBS Lett. 246:57-64(1989) [PubMed: 2540040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Molecular cloning, upstream sequence and promoter studies of the human gene for the regulatory subunit RII alpha of cAMP-dependent protein kinase."
Foss K.B., Solberg R., Simard J., Myklebust F., Hansson V., Jahnsen T., Tasken K.
Biochim. Biophys. Acta 1350:98-108(1997) [PubMed: 9003463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
[3]"Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes."
Schillace R.V., Andrews S.F., Liberty G.A., Davey M.P., Carr D.W.
J. Immunol. 168:1590-1599(2002) [PubMed: 11823486] [Abstract]
Cited for: INTERACTION WITH CBFA2T3.
[4]"Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation."
Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.
J. Biol. Chem. 278:11579-11589(2003) [PubMed: 12509440] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
Tissue: Sperm.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
Tissue: Pituitary.
[7]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
[8]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78 AND SER-80, MASS SPECTROMETRY.
[9]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, MASS SPECTROMETRY.
[10]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
Tissue: Platelet.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80 AND SER-99, MASS SPECTROMETRY.
[13]"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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99, MASS SPECTROMETRY.
Tissue: Liver.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
[16]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, MASS SPECTROMETRY.
[17]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X14968 mRNA. Translation: CAA33094.1.
X99455 Genomic DNA. Translation: CAA67817.1.
IPIIPI00219774.
PIROKHU2R. S03885.
RefSeqNP_004148.1.
UniGeneHs.631923

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IZXX-ray1.30A/B4-43[»]
SMRP13861. Positions 96-396.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-552N.
STRINGP13861.

PTM databases

PhosphoSiteP13861.

2-D gel databases

OGPP13861.

Proteomic databases

PRIDEP13861.

Genome annotation databases

EnsemblENST00000265563; ENSP00000265563; ENSG00000114302; Homo sapiens. [Genome view]
ENST00000454963; ENSP00000394041; ENSG00000114302; Homo sapiens. [Genome view]
GeneID5576.
KEGGhsa:5576.
UCSCuc003cux.1. human.

Organism-specific databases

CTD5576.
GeneCardsGC03M048762.
H-InvDBHIX0022012.
HGNCHGNC:9391. PRKAR2A.
HPACAB005023.
MIM176910. gene.
PharmGKBPA33757.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13076.
HOGENOMHBG736470.
HOVERGENP13861.
InParanoidP13861.
OMADQQRCRL.
PhylomeDBP13861.

Enzyme and pathway databases

ReactomeREACT_11061. Signalling by NGF.
REACT_1505. Integration of energy metabolism.
REACT_15295. Opioid Signalling.
REACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpressP13861.
BgeeP13861.
CleanExHS_PRKAR2A.
GenevestigatorP13861.
GermOnlineENSG00000114302. Homo sapiens.

Family and domain databases

InterProIPR003117. cAMP-dep_prot_kin_reg_I/II_a/b.
IPR002373. cAMP/cGMP_kin.
IPR000595. cNMP_bd.
IPR018490. cNMP_bd-like.
IPR018488. cNMP_bd_CS.
IPR012198. PK_regulatory.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21620.
SOURCESearch...

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Entry information

Entry nameKAP2_HUMAN
AccessionPrimary (citable) accession number: P13861
Secondary accession number(s): Q16823
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents