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P31321

- KAP1_HUMAN

UniProt

P31321 - KAP1_HUMAN

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Protein

cAMP-dependent protein kinase type I-beta regulatory subunit

Gene
PRKAR1B
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  3. cAMP-dependent protein kinase regulator activity Source: UniProtKB
  4. protein kinase A catalytic subunit binding Source: BHF-UCL

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. activation of protein kinase A activity Source: Reactome
  3. blood coagulation Source: Reactome
  4. cellular response to glucagon stimulus Source: Reactome
  5. energy reserve metabolic process Source: Reactome
  6. epidermal growth factor receptor signaling pathway Source: Reactome
  7. fibroblast growth factor receptor signaling pathway Source: Reactome
  8. innate immune response Source: Reactome
  9. learning or memory Source: Ensembl
  10. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
  11. neurotrophin TRK receptor signaling pathway Source: Reactome
  12. protein phosphorylation Source: UniProtKB
  13. regulation of insulin secretion Source: Reactome
  14. signal transduction Source: Reactome
  15. small molecule metabolic process Source: Reactome
  16. transmembrane transport Source: Reactome
  17. water transport Source: Reactome
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. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

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: Chromosome 7

Organism-specific databases

HGNCiHGNC:9390. PRKAR1B.

Subcellular locationi

Cell membrane 1 Publication

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By 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-acetylalanine Inferred
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 – 831Phosphoserine2 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

ArrayExpressiP31321.
BgeeiP31321.
CleanExiHS_PRKAR1B.
GenevestigatoriP31321.

Organism-specific databases

HPAiHPA026719.

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. 14 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 – 246
Turni27 – 315
Helixi32 – 4110
Helixi46 – 6823

3D structure databases

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

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP31321.
KOiK04739.
OMAiCKQIMAR.
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

MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL    50
REHFEKLEKE ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV 100
SAEVYTEEDA VSYVRKVIPK DYKTMTALAK AISKNVLFAH LDDNERSDIF 150
DAMFPVTHIA GETVIQQGNE GDNFYVVDQG EVDVYVNGEW VTNISEGGSF 200
GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL RKRKMYEEFL 250
SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA 300
SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL 350
DRPRFERVLG PCSEILKRNI QRYNSFISLT V 381
Length:381
Mass (Da):43,073
Last modified:May 5, 2009 - v4
Checksum:i1ED7BFEC30897191
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701A → R in AAC37564. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi229463042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34579.1.
PIRi JH0392. OKHUR1.
RefSeqi NP_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.
UniGenei Hs.520851.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DIN X-ray 3.70 B 1-381 [» ]
4F9K X-ray 2.80 A/B/C/D 11-73 [» ]
ProteinModelPortali P31321.
SMRi P31321. Positions 14-380.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111561. 14 interactions.
IntActi P31321. 8 interactions.
MINTi MINT-240609.
STRINGi 9606.ENSP00000353415.

Chemistry

BindingDBi P31321.

PTM databases

PhosphoSitei P31321.

Polymorphism databases

DMDMi 229463042.

Proteomic databases

MaxQBi P31321.
PaxDbi P31321.
PRIDEi P31321.

Protocols and materials databases

DNASUi 5575.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360274 ; ENSP00000353415 ; ENSG00000188191 .
ENST00000403562 ; ENSP00000385349 ; ENSG00000188191 .
ENST00000406797 ; ENSP00000385749 ; ENSG00000188191 .
ENST00000537384 ; ENSP00000440449 ; ENSG00000188191 .
ENST00000544935 ; ENSP00000444487 ; ENSG00000188191 .
GeneIDi 5575.
KEGGi hsa:5575.
UCSCi uc003siu.2. human.

Organism-specific databases

CTDi 5575.
GeneCardsi GC07M000588.
HGNCi HGNC:9390. PRKAR1B.
HPAi HPA026719.
MIMi 176911. gene.
neXtProti NX_P31321.
PharmGKBi PA33756.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0664.
HOGENOMi HOG000196669.
HOVERGENi HBG002025.
InParanoidi P31321.
KOi K04739.
OMAi CKQIMAR.
OrthoDBi EOG72JWG6.
PhylomeDBi P31321.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_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. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi PRKAR1B. human.
GeneWikii PRKAR1B.
GenomeRNAii 5575.
NextBioi 21612.
PROi P31321.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31321.
Bgeei P31321.
CleanExi HS_PRKAR1B.
Genevestigatori P31321.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR002373. 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 ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 139 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

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