Hmdb loader
Survey
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.

Showing Protein cAMP-dependent protein kinase type II-alpha regulatory subunit (HMDBP08138)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP08138
Secondary Accession Numbers
  • 13849
Name cAMP-dependent protein kinase type II-alpha regulatory subunit
Synonyms Not Available
Gene Name PRKAR2A
Protein Type Unknown
Biological Properties
General Function Involved in cAMP-dependent protein kinase regulator activity
Specific Function Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase
Pathways Not Available
Reactions Not Available
GO Classification
Component
macromolecular complex
protein complex
camp-dependent protein kinase complex
Function
enzyme regulator activity
kinase regulator activity
protein kinase regulator activity
camp-dependent protein kinase regulator activity
Process
regulation of cellular protein metabolic process
regulation of protein modification process
regulation of protein amino acid phosphorylation
biological regulation
regulation of biological process
regulation of metabolic process
regulation of cellular process
signal transduction
regulation of cellular metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:3
Locus 3p21.3-p21.2
SNPs PRKAR2A
Gene Sequence 
>1215 bp
ATGAGCCACATCCAGATCCCGCCGGGGCTCACGGAGCTGCTGCAGGGCTACACGGTGGAG
GTGCTGCGACAGCAGCCGCCTGACCTCGTCGAATTCGCAGTGGAGTACTTCACCCGCCTG
CGCGAGGCCCGCGCCCCAGCCTCAGTCCTGCCCGCCGCCACCCCACGCCAGAGCCTGGGC
CACCCCCCGCCAGAACCCGGCCCGGACCGTGTCGCCGACGCCAAAGGGGACAGCGAGTCG
GAGGAGGACGAGGACTTGGAAGTTCCAGTTCCTAGCAGATTTAATAGACGAGTATCAGTC
TGTGCTGAGACCTATAACCCTGATGAGGAAGAGGAAGATACAGATCCAAGGGTGATTCAT
CCTAAAACTGATGAACAGAGATGCAGACTTCAGGAAGCTTGCAAAGATATTCTCCTTTTC
AAAAATCTTGATCAGGAACAGCTTTCTCAAGTTCTCGATGCCATGTTTGAAAGGATAGTC
AAAGCTGATGAGCATGTCATTGACCAAGGAGATGATGGAGACAACTTTTATGTCATAGAA
CGGGGAACTTATGACATTTTAGTAACAAAAGATAATCAAACCCGCTCTGTTGGTCAATAT
GACAACCGTGGCAGTTTTGGAGAACTAGCTCTGATGTACAACACCCCGAGAGCTGCTACC
ATTGTTGCTACCTCAGAAGGCTCCCTTTGGGGACTGGACCGGGTGACTTTTAGAAGAATC
ATAGTGAAAAATAATGCAAAGAAGAGGAAGATGTTTGAATCATTTATTGAGTCTGTGCCC
CTCCTTAAATCACTAGAGGTGTCAGAACGAATGAAGATTGTGGATGTAATAGGAGAGAAG
ATCTATAAGGATGGAGAACGCATAATCACTCAGGGTGAAAAGGCTGATAGCTTTTACATC
ATAGAGTCTGGCGAAGTGAGCATCTTGATTAGAAGCAGGACTAAATCAAACAAGGATGGT
GGGAACCAGGAGGTCGAGATTGCCCGCTGCCATAAGGGGCAGTACTTTGGAGAGCTTGCC
CTGGTCACCAACAAACCCAGAGCTGCCTCAGCTTATGCAGTTGGAGATGTCAAATGCTTA
GTTATGGATGTACAAGCATTCGAGAGGCTTCTGGGGCCCTGCATGGACATCATGAAGAGG
AACATCTCACACTATGAGGAACAGCTGGTGAAGATGTTTGGCTCCAGCGTGGATCTGGGC
AACCTCGGGCAGTAG
Protein Properties
Number of Residues 404
Molecular Weight 45518.0
Theoretical pI 4.7
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>cAMP-dependent protein kinase type II-alpha regulatory subunit
MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLG
HPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIH
PKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIE
RGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRI
IVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYI
IESGEVSILIRSRTKSNKDGGNQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCL
VMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSVDLGNLGQ
GenBank ID Protein 29648
UniProtKB/Swiss-Prot ID P13861
UniProtKB/Swiss-Prot Entry Name KAP2_HUMAN
PDB IDs Not Available
GenBank Gene ID X14968
GeneCard ID PRKAR2A
GenAtlas ID PRKAR2A
HGNC ID HGNC:9391
References
General References
  1. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  2. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  8. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed:17487921 ]
  9. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  10. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. doi: 10.1002/pmic.200700884. [PubMed:18318008 ]
  11. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. doi: 10.1021/ac801708p. [PubMed:19007248 ]
  12. Ficarro S, Chertihin O, Westbrook VA, White F, Jayes F, Kalab P, Marto JA, Shabanowitz J, Herr JC, Hunt DF, Visconti PE: Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J Biol Chem. 2003 Mar 28;278(13):11579-89. Epub 2002 Dec 30. [PubMed:12509440 ]
  13. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [PubMed:16807684 ]
  14. Oyen O, Myklebust F, Scott JD, Hansson V, Jahnsen T: Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent protein kinase encodes an alternate amino-terminal region. FEBS Lett. 1989 Mar 27;246(1-2):57-64. [PubMed:2540040 ]
  15. Foss KB, Solberg R, Simard J, Myklebust F, Hansson V, Jahnsen T, Tasken K: Molecular cloning, upstream sequence and promoter studies of the human gene for the regulatory subunit RII alpha of cAMP-dependent protein kinase. Biochim Biophys Acta. 1997 Jan 3;1350(1):98-108. [PubMed:9003463 ]
  16. Schillace RV, Andrews SF, Liberty GA, Davey MP, Carr DW: Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes. J Immunol. 2002 Feb 15;168(4):1590-9. [PubMed:11823486 ]