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Entry version 208 (29 Sep 2021)
Sequence version 4 (23 Jan 2007)
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Protein

cAMP-dependent protein kinase regulatory subunit

Gene

BCY1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.

4 Publications

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2493',5'-cAMP 11 Publication1
Binding sitei2583',5'-cAMP 11 Publication1
Binding sitei3683',5'-cAMP 21 Publication1
Binding sitei3773',5'-cAMP 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi184 – 3013',5'-cAMP 11 PublicationAdd BLAST118
Nucleotide bindingi302 – 4163',5'-cAMP 21 PublicationAdd BLAST115

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandcAMP, cAMP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
cAMP-dependent protein kinase regulatory subunit
Short name:
cAPK regulatory subunit
Alternative name(s):
Bypass of cyclase mutations protein 1
Protein kinase A regulatory subunit
Short name:
PKA regulatory subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BCY1
Synonyms:REG1, SRA1
Ordered Locus Names:YIL033C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IX

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000001295, BCY1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YIL033C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi129T → D: Confers increased sensitivity to rapamycin and enhanced accumulation of glycogen upon TORC1 inhibition. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved3 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002054182 – 416cAMP-dependent protein kinase regulatory subunitAdd BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3PhosphoserineCurated1
Modified residuei4PhosphoserineCurated1
Modified residuei9PhosphoserineCurated1
Modified residuei68Phosphoserine1 Publication1
Modified residuei70Phosphoserine1 Publication1
Modified residuei74Phosphoserine1 Publication1
Modified residuei77Phosphoserine1 Publication1
Modified residuei79Phosphoserine1 Publication1
Modified residuei81Phosphoserine1 Publication1
Modified residuei83PhosphoserineCombined sources1 Publication1
Modified residuei84Phosphoserine1 Publication1
Modified residuei129Phosphothreonine1 Publication1
Modified residuei130Phosphoserine1 Publication1
Modified residuei131Phosphothreonine1 Publication1
Modified residuei144Phosphothreonine1 Publication1
Modified residuei145Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei147Phosphoserine1 Publication1
Modified residuei150PhosphothreonineCombined sources1 Publication1
Modified residuei160Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clustered in several groups, all localized in the N-terminal part. The first cluster termed cluster I (CI) is located close to the N-terminus and includes Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and Ser-84. This cluster of phosphorylation sites, termed cluster II (CII), is important for BCY1 cytoplasmic localization and function (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-150, and Thr-160. This cluster falls within or near the so-called autoinhibitory domain where the catalytic subunit of PKA autophosphorylates the highly conserved Ser-145 to inhibit BCY1 (PubMed:20702584). A last cluster of phosphorylated residues included Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites in CIII (and to a lesser extent in CII) are hyperphosphorylated in response to rapamycin (PubMed:20702584).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07278

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07278

PRoteomics IDEntifications database

More...
PRIDEi
P07278

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P07278

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07278

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer, composed of 2 regulatory subunits (R, encoded by BCY1) and two catalytic subunits (C, encoded by the 3 partially redundant TPK1, TPK2, and TPK3 genes). Activation by cAMP causes dissociation of the holoenzyme, producing 2 active catalytic monomers C and a regulatory dimer R2.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
34957, 365 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-536, cAMP-dependent protein kinase complex variant 1
CPX-537, cAMP-dependent protein kinase complex variant 2
CPX-571, cAMP-dependent protein kinase complex variant 3
CPX-572, cAMP-dependent protein kinase complex variant 4
CPX-573, cAMP-dependent protein kinase complex variant 5
CPX-574, cAMP-dependent protein kinase complex variant 6

Database of interacting proteins

More...
DIPi
DIP-551N

Protein interaction database and analysis system

More...
IntActi
P07278, 23 interactors

Molecular INTeraction database

More...
MINTi
P07278

STRING: functional protein association networks

More...
STRINGi
4932.YIL033C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P07278, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07278

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 183Dimerization and phosphorylationAdd BLAST182
Regioni8 – 45Dimerization/docking domain (D/D)Add BLAST38
Regioni65 – 138DisorderedSequence analysisAdd BLAST74

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi142 – 146Inhibitor sequence (IS)5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi69 – 88Polar residuesSequence analysisAdd BLAST20
Compositional biasi113 – 127Basic and acidic residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The inhibitor sequence (IS) is a substrate recognition motif that docks to the active site cleft of the catalytic subunit rendering the holoenzyme inactive.
Binding of cAMP to the 2 tandem cyclic-nucleotide binding domains (CNB-A and CNB-B) induces a conformational change in BCY1, causing the interaction surface with the catalytic subunit to be destroyed and eventually the dissociation of the R dimer from the C subunits.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1113, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000168302

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018310_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07278

Identification of Orthologs from Complete Genome Data

More...
OMAi
QYNFGRR

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00038, CAP_ED, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00027, cNMP_binding, 2 hits
PF02197, RIIa, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000548, PK_regulatory, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00100, cNMP, 2 hits
SM00394, RIIa, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51206, SSF51206, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00888, CNMP_BINDING_1, 2 hits
PS00889, CNMP_BINDING_2, 2 hits
PS50042, CNMP_BINDING_3, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P07278-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSSLPKESQ AELQLFQNEI NAANPSDFLQ FSANYFNKRL EQQRAFLKAR
60 70 80 90 100
EPEFKAKNIV LFPEPEESFS RPQSAQSQSR SRSSVMFKSP FVNEDPHSNV
110 120 130 140 150
FKSGFNLDPH EQDTHQQAQE EQQHTREKTS TPPLPMHFNA QRRTSVSGET
160 170 180 190 200
LQPNNFDDWT PDHYKEKSEQ QLQRLEKSIR NNFLFNKLDS DSKRLVINCL
210 220 230 240 250
EEKSVPKGAT IIKQGDQGDY FYVVEKGTVD FYVNDNKVNS SGPGSSFGEL
260 270 280 290 300
ALMYNSPRAA TVVATSDCLL WALDRLTFRK ILLGSSFKKR LMYDDLLKSM
310 320 330 340 350
PVLKSLTTYD RAKLADALDT KIYQPGETII REGDQGENFY LIEYGAVDVS
360 370 380 390 400
KKGQGVINKL KDHDYFGEVA LLNDLPRQAT VTATKRTKVA TLGKSGFQRL
410
LGPAVDVLKL NDPTRH
Length:416
Mass (Da):47,219
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6D7D97D8E4340AF3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti264A → P in CAA28726 (PubMed:3547325).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M15756 Genomic DNA Translation: AAA34468.1
M17223 Genomic DNA Translation: AAA66934.1
X05051 Genomic DNA Translation: CAA28726.1
Z46861 Genomic DNA Translation: CAA86918.1
AY558087 Genomic DNA Translation: AAS56413.1
BK006942 Genomic DNA Translation: DAA08515.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25868, OKBYRC

NCBI Reference Sequences

More...
RefSeqi
NP_012231.1, NM_001179383.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YIL033C_mRNA; YIL033C; YIL033C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854778

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YIL033C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15756 Genomic DNA Translation: AAA34468.1
M17223 Genomic DNA Translation: AAA66934.1
X05051 Genomic DNA Translation: CAA28726.1
Z46861 Genomic DNA Translation: CAA86918.1
AY558087 Genomic DNA Translation: AAS56413.1
BK006942 Genomic DNA Translation: DAA08515.1
PIRiA25868, OKBYRC
RefSeqiNP_012231.1, NM_001179383.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OF1X-ray2.21A171-416[»]
6XQKX-ray2.56A/B/C/D/E/F/G/H1-50[»]
SMRiP07278
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34957, 365 interactors
ComplexPortaliCPX-536, cAMP-dependent protein kinase complex variant 1
CPX-537, cAMP-dependent protein kinase complex variant 2
CPX-571, cAMP-dependent protein kinase complex variant 3
CPX-572, cAMP-dependent protein kinase complex variant 4
CPX-573, cAMP-dependent protein kinase complex variant 5
CPX-574, cAMP-dependent protein kinase complex variant 6
DIPiDIP-551N
IntActiP07278, 23 interactors
MINTiP07278
STRINGi4932.YIL033C

PTM databases

iPTMnetiP07278

Proteomic databases

MaxQBiP07278
PaxDbiP07278
PRIDEiP07278
TopDownProteomicsiP07278

Genome annotation databases

EnsemblFungiiYIL033C_mRNA; YIL033C; YIL033C
GeneIDi854778
KEGGisce:YIL033C

Organism-specific databases

SGDiS000001295, BCY1
VEuPathDBiFungiDB:YIL033C

Phylogenomic databases

eggNOGiKOG1113, Eukaryota
GeneTreeiENSGT00940000168302
HOGENOMiCLU_018310_0_1_1
InParanoidiP07278
OMAiQYNFGRR

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
REG1, yeast

Protein Ontology

More...
PROi
PR:P07278
RNActiP07278, protein

Family and domain databases

CDDicd00038, CAP_ED, 2 hits
Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
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
PfamiView protein in Pfam
PF00027, cNMP_binding, 2 hits
PF02197, RIIa, 1 hit
PIRSFiPIRSF000548, PK_regulatory, 1 hit
SMARTiView protein in SMART
SM00100, cNMP, 2 hits
SM00394, RIIa, 1 hit
SUPFAMiSSF51206, SSF51206, 2 hits
PROSITEiView protein in PROSITE
PS00888, CNMP_BINDING_1, 2 hits
PS00889, CNMP_BINDING_2, 2 hits
PS50042, CNMP_BINDING_3, 2 hits

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKAPR_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07278
Secondary accession number(s): D6VVP9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 208 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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