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Protein

cAMP-dependent protein kinase regulatory subunit

Gene

cgs1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei224 – 2241cAMP 1
Binding sitei233 – 2331cAMP 1
Binding sitei344 – 3441cAMP 2
Binding sitei353 – 3531cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi143 – 277135cAMP 1; high affinityAdd
BLAST
Nucleotide bindingi278 – 412135cAMP 2; low affinityAdd
BLAST

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase regulator activity Source: PomBase

GO - Biological processi

  • negative regulation of meiotic cell cycle Source: PomBase
  • positive regulation of protein export from nucleus Source: PomBase
  • signal transduction Source: PomBase
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-163615. PKA activation.
R-SPO-164378. PKA activation in glucagon signalling.
R-SPO-180024. DARPP-32 events.
R-SPO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SPO-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase regulatory subunit
Short name:
PKA regulatory subunit
Gene namesi
Name:cgs1
ORF Names:SPAC8C9.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC8C9.03.
PomBaseiSPAC8C9.03. cgs1.

Subcellular locationi

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412cAMP-dependent protein kinase regulatory subunitPRO_0000205414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36600.

PTM databases

iPTMnetiP36600.

Interactioni

Subunit structurei

Tetramer, composed of 2 regulatory (R) and 2 catalytic (C) subunits. In the presence of cAMP it dissociates into 2 active monomeric C subunits and an R dimer.

Protein-protein interaction databases

BioGridi279773. 20 interactions.
MINTiMINT-4688868.

Structurei

3D structure databases

ProteinModelPortaliP36600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 142142Dimerization and phosphorylationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi101 – 1055Pseudophosphorylation motif

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000196669.
InParanoidiP36600.
KOiK04739.
OMAiSTRVYND.
OrthoDBiEOG7034TC.
PhylomeDBiP36600.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEEVYEEL KALVDEQNPS DVLQFCYDFF GEKLKAERSV FRRGDTITES
60 70 80 90 100
FSDGDESDFL SELNDMVAGP EAIGPDAKYV PELGGLKEMN VSYPQNYNLL
110 120 130 140 150
RRQSVSTESM NPSAFALETK RTFPPKDPED LKRLKRSVAG NFLFKNLDEE
160 170 180 190 200
HYNEVLNAMT EKRIGEAGVA VIVQGAVGDY FYIVEQGEFD VYKRPELNIT
210 220 230 240 250
PEEVLSSGYG NYITTISPGE YFGELALMYN APRAASVVSK TPNNVIYALD
260 270 280 290 300
RTSFRRIVFE NAYRQRMLYE SLLEEVPILS SLDKYQRQKI ADALQTVVYQ
310 320 330 340 350
AGSIVIRQGD IGNQFYLIED GEAEVVKNGK GVVVTLTKGD YFGELALIHE
360 370 380 390 400
TVRNATVQAK TRLKLATFDK PTFNRLLGNA IDLMRNQPRA RMGMDNEYGD
410
QSLHRSPPST KA
Length:412
Mass (Da):46,468
Last modified:January 11, 2001 - v2
Checksum:iCA6D4D53D308EF2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741E → Q in AAB20314 (PubMed:1657594).Curated
Sequence conflicti295 – 2951Q → L in AAB20314 (PubMed:1657594).Curated
Sequence conflicti326 – 3261Missing in AAB20314 (PubMed:1657594).Curated
Sequence conflicti336 – 3361L → Q in AAB20314 (PubMed:1657594).Curated
Sequence conflicti356 – 3561T → P in AAB20314 (PubMed:1657594).Curated
Sequence conflicti397 – 3971E → K in AAB20314 (PubMed:1657594).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64905 Genomic DNA. Translation: AAB20314.1.
CU329670 Genomic DNA. Translation: CAB16291.2.
PIRiS18634.
T39140.
RefSeqiNP_594274.1. NM_001019697.2.

Genome annotation databases

EnsemblFungiiSPAC8C9.03.1; SPAC8C9.03.1:pep; SPAC8C9.03.
GeneIDi2543351.
KEGGispo:SPAC8C9.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64905 Genomic DNA. Translation: AAB20314.1.
CU329670 Genomic DNA. Translation: CAB16291.2.
PIRiS18634.
T39140.
RefSeqiNP_594274.1. NM_001019697.2.

3D structure databases

ProteinModelPortaliP36600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279773. 20 interactions.
MINTiMINT-4688868.

PTM databases

iPTMnetiP36600.

Proteomic databases

MaxQBiP36600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC8C9.03.1; SPAC8C9.03.1:pep; SPAC8C9.03.
GeneIDi2543351.
KEGGispo:SPAC8C9.03.

Organism-specific databases

EuPathDBiFungiDB:SPAC8C9.03.
PomBaseiSPAC8C9.03. cgs1.

Phylogenomic databases

HOGENOMiHOG000196669.
InParanoidiP36600.
KOiK04739.
OMAiSTRVYND.
OrthoDBiEOG7034TC.
PhylomeDBiP36600.

Enzyme and pathway databases

ReactomeiR-SPO-163615. PKA activation.
R-SPO-164378. PKA activation in glucagon signalling.
R-SPO-180024. DARPP-32 events.
R-SPO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SPO-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP36600.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction between ran1+ protein kinase and cAMP dependent protein kinase as negative regulators of fission yeast meiosis."
    Devoti J., Seydoux G., Beach D., McLeod M.
    EMBO J. 10:3759-3768(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiKAPR_SCHPO
AccessioniPrimary (citable) accession number: P36600
Secondary accession number(s): O14272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: July 6, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.