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P31321 (KAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase type I-beta regulatory subunit
Gene names
Name:PRKAR1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Ref.9

Subunit structure

The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. Interacts with PRKX; regulates this cAMP-dependent protein kinase. Interacts with C2orf88/smAKAP; this interaction may target PRKAR1B to the plasma membrane. Ref.9 Ref.10

Subcellular location

Cell membrane Ref.10.

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

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMAcetylation
Disulfide bond
Nitration
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

learning or memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP-dependent protein kinase activity

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

protein phosphorylation

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

water transport

Traceable author statement. Source: Reactome

   Cellular_componentcAMP-dependent protein kinase complex

Non-traceable author statement Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase inhibitor activity

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

cAMP-dependent protein kinase regulator activity

Non-traceable author statement Ref.1. Source: UniProtKB

protein kinase A catalytic subunit binding

Inferred from physical interaction PubMed 21812984. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380cAMP-dependent protein kinase type I-beta regulatory subunit
PRO_0000205381

Regions

Nucleotide binding137 – 254118cAMP 1
Nucleotide binding255 – 381127cAMP 2
Region2 – 136135Dimerization and phosphorylation
Motif96 – 1005Pseudophosphorylation motif

Sites

Binding site2021cAMP 1
Binding site2111cAMP 1
Binding site3261cAMP 2
Binding site3351cAMP 2

Amino acid modifications

Modified residue21N-acetylalanine Probable
Modified residue211Nitrated tyrosine Ref.5
Modified residue771Phosphoserine Ref.7
Modified residue831Phosphoserine Ref.7 Ref.8
Disulfide bond18Interchain (with C-39) By similarity
Disulfide bond39Interchain (with C-18) By similarity

Experimental info

Sequence conflict2701A → R in AAC37564. Ref.1

Secondary structure

........ 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31321 [UniParc].

Last modified May 5, 2009. Version 4.
Checksum: 1ED7BFEC30897191

FASTA38143,073
        10         20         30         40         50         60 
MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL REHFEKLEKE 

        70         80         90        100        110        120 
ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK 

       130        140        150        160        170        180 
DYKTMTALAK AISKNVLFAH LDDNERSDIF DAMFPVTHIA GETVIQQGNE GDNFYVVDQG 

       190        200        210        220        230        240 
EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL 

       250        260        270        280        290        300 
RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA 

       310        320        330        340        350        360 
SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG 

       370        380 
PCSEILKRNI QRYNSFISLT V 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, cDNA structure and tissue-specific expression of the human regulatory subunit RI beta of cAMP-dependent protein kinases."
Solberg R., Tasken K., Keiserud A., Jahnsen T.
Biochem. Biophys. Res. Commun. 176:166-172(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human regulatory subunit RI beta of cAMP-dependent protein kinases: expression, holoenzyme formation and microinjection into living cells."
Solberg R., Tasken K., Wen W., Coghlan V.M., Meinkoth J.L., Scott J.D., Jahnsen T., Taylor S.S.
Exp. Cell Res. 214:595-605(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 98-100.
Tissue: Testis.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala and Brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Cervix.
[5]"Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry."
Zhan X., Desiderio D.M.
Anal. Biochem. 354:279-289(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary adenoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Regulation of cAMP-dependent protein kinases: the human protein kinase X (PrKX) reveals the role of the catalytic subunit alphaH-alphaI loop."
Diskar M., Zenn H.M., Kaupisch A., Kaufholz M., Brockmeyer S., Sohmen D., Berrera M., Zaccolo M., Boshart M., Herberg F.W., Prinz A.
J. Biol. Chem. 285:35910-35918(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKX.
[10]"A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma membrane."
Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A., Ellisman M., Scholten A., Taylor S.S., Heck A.J.
J. Biol. Chem. 287:43789-43797(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C2ORF88/SMAKAP, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65066 mRNA. Translation: AAC37564.1.
AK315951 mRNA. Translation: BAH14322.1.
AK315990 mRNA. Translation: BAH14361.1.
BC026734 mRNA. Translation: AAH26734.1.
BC036828 mRNA. Translation: AAH36828.2.
PIROKHUR1. JH0392.
RefSeqNP_001158230.1. NM_001164758.1.
NP_001158231.1. NM_001164759.1.
NP_001158232.1. NM_001164760.1.
NP_001158233.1. NM_001164761.1.
NP_001158234.1. NM_001164762.1.
NP_002726.1. NM_002735.2.
UniGeneHs.520851.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DINX-ray3.70B1-381[»]
4F9KX-ray2.80A/B/C/D11-73[»]
ProteinModelPortalP31321.
SMRP31321. Positions 14-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111561. 14 interactions.
IntActP31321. 8 interactions.
MINTMINT-240609.
STRING9606.ENSP00000353415.

Chemistry

BindingDBP31321.

PTM databases

PhosphoSiteP31321.

Polymorphism databases

DMDM229463042.

Proteomic databases

PaxDbP31321.
PRIDEP31321.

Protocols and materials databases

DNASU5575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360274; ENSP00000353415; ENSG00000188191.
ENST00000403562; ENSP00000385349; ENSG00000188191.
ENST00000406797; ENSP00000385749; ENSG00000188191.
ENST00000537384; ENSP00000440449; ENSG00000188191.
ENST00000544935; ENSP00000444487; ENSG00000188191.
GeneID5575.
KEGGhsa:5575.
UCSCuc003siu.2. human.

Organism-specific databases

CTD5575.
GeneCardsGC07M000588.
HGNCHGNC:9390. PRKAR1B.
HPAHPA026719.
MIM176911. gene.
neXtProtNX_P31321.
PharmGKBPA33756.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000196669.
HOVERGENHBG002025.
InParanoidP31321.
KOK04739.
OMAIMARQKS.
OrthoDBEOG72JWG6.
PhylomeDBP31321.
TreeFamTF314920.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP31321.
BgeeP31321.
CleanExHS_PRKAR1B.
GenevestigatorP31321.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR002373. 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]
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]
SUPFAMSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAR1B. human.
GeneWikiPRKAR1B.
GenomeRNAi5575.
NextBio21612.
PROP31321.
SOURCESearch...

Entry information

Entry nameKAP1_HUMAN
AccessionPrimary (citable) accession number: P31321
Secondary accession number(s): Q8N422
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM