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Protein

cAMP-dependent protein kinase type I-beta regulatory subunit

Gene

PRKAR1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021cAMP 1
Binding sitei211 – 2111cAMP 1
Binding sitei326 – 3261cAMP 2
Binding sitei335 – 3351cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 254118cAMP 1Add
BLAST
Nucleotide bindingi255 – 381127cAMP 2Add
BLAST

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  • cAMP-dependent protein kinase regulator activity Source: UniProtKB
  • protein kinase A catalytic subunit binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_268323. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type I-beta regulatory subunit
Gene namesi
Name:PRKAR1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9390. PRKAR1B.

Subcellular locationi

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: UniProtKB
  • ciliary base Source: Reactome
  • cytosol Source: Reactome
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33756.

Polymorphism and mutation databases

BioMutaiPRKAR1B.
DMDMi229463042.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 381380cAMP-dependent protein kinase type I-beta regulatory subunitPRO_0000205381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCurated
Disulfide bondi18 – 18Interchain (with C-39)By similarity
Modified residuei21 – 211Nitrated tyrosine1 Publication
Disulfide bondi39 – 39Interchain (with C-18)By similarity
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei83 – 831Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP31321.
PaxDbiP31321.
PRIDEiP31321.

PTM databases

PhosphoSiteiP31321.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP31321.
CleanExiHS_PRKAR1B.
ExpressionAtlasiP31321. baseline and differential.
GenevestigatoriP31321.

Organism-specific databases

HPAiHPA026719.
HPA049847.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi111561. 21 interactions.
IntActiP31321. 8 interactions.
MINTiMINT-240609.
STRINGi9606.ENSP00000353415.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 246Combined sources
Turni27 – 315Combined sources
Helixi32 – 4110Combined sources
Helixi46 – 6823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DINX-ray3.70B1-381[»]
4F9KX-ray2.80A/B/C/D11-73[»]
ProteinModelPortaliP31321.
SMRiP31321. Positions 14-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 136135Dimerization and phosphorylationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1005Pseudophosphorylation motif

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP31321.
KOiK04739.
OMAiCEIFVQK.
OrthoDBiEOG72JWG6.
PhylomeDBiP31321.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL
60 70 80 90 100
REHFEKLEKE ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV
110 120 130 140 150
SAEVYTEEDA VSYVRKVIPK DYKTMTALAK AISKNVLFAH LDDNERSDIF
160 170 180 190 200
DAMFPVTHIA GETVIQQGNE GDNFYVVDQG EVDVYVNGEW VTNISEGGSF
210 220 230 240 250
GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL RKRKMYEEFL
260 270 280 290 300
SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA
310 320 330 340 350
SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL
360 370 380
DRPRFERVLG PCSEILKRNI QRYNSFISLT V
Length:381
Mass (Da):43,073
Last modified:May 5, 2009 - v4
Checksum:i1ED7BFEC30897191
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701A → R in AAC37564 (PubMed:1708242).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34579.1.
PIRiJH0392. OKHUR1.
RefSeqiNP_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.
UniGeneiHs.520851.

Genome annotation databases

EnsembliENST00000360274; ENSP00000353415; ENSG00000188191.
ENST00000403562; ENSP00000385349; ENSG00000188191.
ENST00000406797; ENSP00000385749; ENSG00000188191.
ENST00000537384; ENSP00000440449; ENSG00000188191.
ENST00000544935; ENSP00000444487; ENSG00000188191.
GeneIDi5575.
KEGGihsa:5575.
UCSCiuc003siu.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34579.1.
PIRiJH0392. OKHUR1.
RefSeqiNP_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.
UniGeneiHs.520851.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DINX-ray3.70B1-381[»]
4F9KX-ray2.80A/B/C/D11-73[»]
ProteinModelPortaliP31321.
SMRiP31321. Positions 14-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111561. 21 interactions.
IntActiP31321. 8 interactions.
MINTiMINT-240609.
STRINGi9606.ENSP00000353415.

PTM databases

PhosphoSiteiP31321.

Polymorphism and mutation databases

BioMutaiPRKAR1B.
DMDMi229463042.

Proteomic databases

MaxQBiP31321.
PaxDbiP31321.
PRIDEiP31321.

Protocols and materials databases

DNASUi5575.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360274; ENSP00000353415; ENSG00000188191.
ENST00000403562; ENSP00000385349; ENSG00000188191.
ENST00000406797; ENSP00000385749; ENSG00000188191.
ENST00000537384; ENSP00000440449; ENSG00000188191.
ENST00000544935; ENSP00000444487; ENSG00000188191.
GeneIDi5575.
KEGGihsa:5575.
UCSCiuc003siu.2. human.

Organism-specific databases

CTDi5575.
GeneCardsiGC07M000588.
HGNCiHGNC:9390. PRKAR1B.
HPAiHPA026719.
HPA049847.
MIMi176911. gene.
neXtProtiNX_P31321.
PharmGKBiPA33756.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP31321.
KOiK04739.
OMAiCEIFVQK.
OrthoDBiEOG72JWG6.
PhylomeDBiP31321.
TreeFamiTF314920.

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_268323. Hedgehog 'off' state.

Miscellaneous databases

ChiTaRSiPRKAR1B. human.
GeneWikiiPRKAR1B.
GenomeRNAii5575.
NextBioi21612.
PROiP31321.
SOURCEiSearch...

Gene expression databases

BgeeiP31321.
CleanExiHS_PRKAR1B.
ExpressionAtlasiP31321. baseline and differential.
GenevestigatoriP31321.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKAP1_HUMAN
AccessioniPrimary (citable) accession number: P31321
Secondary accession number(s): Q8N422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 5, 2009
Last modified: April 29, 2015
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.