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Reviewed, UniProtKB/Swiss-Prot P31323 (KAP3_HUMAN)

Last modified January 19, 2010. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-beta regulatory subunit
Gene names
Name: PRKAR2B
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 length418 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.

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.5 Ref.6 Ref.8 Ref.9

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 By similarity
Chain2 – 418417cAMP-dependent protein kinase type II-beta regulatory subunit
PRO_0000205390

Regions

Nucleotide binding154 – 275122cAMP 1
Nucleotide binding276 – 418143cAMP 2
Region2 – 153152Dimerization and phosphorylation

Sites

Binding site2231cAMP 1
Binding site2321cAMP 1
Binding site3521cAMP 2
Binding site3611cAMP 2

Amino acid modifications

Modified residue21N-acetylserine Probable
Modified residue831Phosphoserine Ref.8 Ref.9
Modified residue851Phosphoserine Ref.8 Ref.9
Modified residue1141Phosphoserine Ref.5 Ref.6 Ref.9

Natural variations

Natural variant3351E → D: dbSNP rs3729881.
VAR_046549

Experimental info

Sequence conflict341 – 3422IA → MP in AAA60099. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P31323-1 [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: 83F402CCFFEFD186

FASTA41846,302
        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

« Hide

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References

« Hide '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: 2851102] [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. expand/collapse author list , 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: 14702039] [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. expand/collapse author list , 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: 12690205] [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. expand/collapse author list , 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]"Phosphoproteomic analysis of synaptosomes from human cerebral cortex."
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.
J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
Tissue: Brain cortex.
[6]"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-114, MASS SPECTROMETRY.
Tissue: Liver.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"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-83 AND SER-85, MASS SPECTROMETRY.
[9]"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-83; SER-85 AND SER-114, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

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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.
IPIIPI00554752.
PIROKHUR2. A40915.
RefSeqNP_002727.2.
UniGeneHs.433068

3D structure databases

SMRP31323. Positions 3-41, 132-414.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-554N.
STRINGP31323.

PTM databases

PhosphoSiteP31323.

2-D gel databases

OGPP31323.

Proteomic databases

PRIDEP31323.

Genome annotation databases

EnsemblENST00000265717; ENSP00000265717; ENSG00000005249; Homo sapiens. [Genome view]
GeneID5577.
KEGGhsa:5577.

Organism-specific databases

CTD5577.
GeneCardsGC07P106472.
H-InvDBHIX0025309.
HGNCHGNC:9392. PRKAR2B.
HPAHPA008421.
MIM176912. gene.
PharmGKBPA33758.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG736470.
HOVERGENP31323.
InParanoidP31323.
OMATYDIYVK.
OrthoDBEOG9909VX.
PhylomeDBP31323.

Enzyme and pathway databases

ReactomeREACT_11061. Signalling by NGF.
REACT_1505. Integration of energy metabolism.
REACT_152. Cell Cycle, Mitotic.
REACT_15295. Opioid Signalling.
REACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpressP31323.
BgeeP31323.
CleanExHS_PRKAR2B.
GenevestigatorP31323.
GermOnlineENSG00000005249. 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

NextBio21624.
SOURCESearch...

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Entry information

Entry nameKAP3_HUMAN
AccessionPrimary (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: January 19, 2010
This is version 93 of the entry and version 3 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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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents