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UniProtKB - P43565 (RIM15_YEAST)

Entry version 211 (23 Feb 2022)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
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Protein

Serine/threonine-protein kinase RIM15

Gene

RIM15

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

Protein kinase that positively regulates proper entry into stationary phase of cells under nutrient starvation conditions. Involved in glycogen and trehalose accumulation, derepression of stress-induced genes, induction of thermotolerance and starvation resistance, and proper G1 cell cycle arrest. Also involved in the activation of a meiotic genes activation pathway. Phosphorylates IGO1 and IGO2, both involved in the TORC1 control of gene expression and chronological life span.

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei823ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei918Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi800 – 808ATPPROSITE-ProRule annotation9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processMeiosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1, 984

<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%5Fand%5Ftaxonomy%5Fsection">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:
Serine/threonine-protein kinase RIM15 (EC:2.7.11.1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:RIM15
Synonyms:TAK1
Ordered Locus Names:YFL033C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 VI

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001861, RIM15

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YFL033C

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi823K → Y: Loss of kinase activity. 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 '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_00000866051 – 1770Serine/threonine-protein kinase RIM15Add BLAST1770

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 residuei380PhosphoserineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei704PhosphothreonineCombined sources1
Modified residuei709PhosphoserineCombined sources1
Modified residuei733PhosphoserineCombined sources1
Modified residuei736PhosphoserineCombined sources1
Modified residuei737PhosphoserineCombined sources1
Modified residuei747PhosphothreonineCombined sources1
Modified residuei1044PhosphoserineCombined sources1
Modified residuei1048PhosphoserineCombined sources1
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1075Phosphothreonine; by PHO851 Publication1
Modified residuei1421PhosphoserineCombined sources1
Modified residuei1531PhosphoserineCombined sources1
Modified residuei1538PhosphoserineCombined sources1
Modified residuei1542PhosphoserineCombined sources1
Modified residuei1565PhosphoserineCombined sources1
Modified residuei1764PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Autophosphorylated. Phosphorylation by PKA strongly inhibits kinase activity. Phosphorylation by cyclin-CDK PHO80-PHO85 under favorable growth condition causes inactivation of RIM15 by promoting its export to the cytoplasm.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P43565

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

More...PaxDbi		P43565

PRoteomics IDEntifications database

More...PRIDEi		P43565

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P43565

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P43565

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with the cyclin-dependent kinase (CDK) PHO85 and IGO1.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		31114, 385 interactors

Database of interacting proteins

More...DIPi		DIP-2510N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P43565

Protein interaction database and analysis system

More...IntActi		P43565, 16 interactors

Molecular INTeraction database

More...MINTi		P43565

STRING: functional protein association networks

More...STRINGi		4932.YFL033C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P43565, 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

3D structure databases

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

More...SMRi		P43565

Database of comparative protein structure models

More...ModBasei		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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini794 – 1254Protein kinasePROSITE-ProRule annotationAdd BLAST461
Domaini1255 – 1320AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST66
Domaini1636 – 1750Response regulatoryPROSITE-ProRule annotationAdd BLAST115

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>Regioni334 – 358DisorderedSequence analysisAdd BLAST25
Regioni530 – 563DisorderedSequence analysisAdd BLAST34
Regioni583 – 694DisorderedSequence analysisAdd BLAST112
Regioni970 – 1032DisorderedSequence analysisAdd BLAST63
Regioni1378 – 1403DisorderedSequence analysisAdd BLAST26
Regioni1448 – 1507DisorderedSequence analysisAdd BLAST60
Regioni1519 – 1572DisorderedSequence analysisAdd BLAST54

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 biasi336 – 358Polar residuesSequence analysisAdd BLAST23
Compositional biasi583 – 635Polar residuesSequence analysisAdd BLAST53
Compositional biasi636 – 656Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi657 – 694Polar residuesSequence analysisAdd BLAST38
Compositional biasi970 – 993Polar residuesSequence analysisAdd BLAST24
Compositional biasi1001 – 1032Polar residuesSequence analysisAdd BLAST32
Compositional biasi1378 – 1402Polar residuesSequence analysisAdd BLAST25
Compositional biasi1458 – 1507Polar residuesSequence analysisAdd BLAST50

<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

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0605, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157002

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000709_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P43565

Identification of Orthologs from Complete Genome Data

More...OMAi		ISQVLQW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000961, AGC-kinase_C
IPR011006, CheY-like_superfamily
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS
IPR001789, Sig_transdc_resp-reg_receiver

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00069, Pkinase, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00448, REC, 1 hit
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52172, SSF52172, 1 hit
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit
PS50110, RESPONSE_REGULATORY, 1 hit

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P43565-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNRSNTAGG SQAMKEGLGI NKLSPISSNS NPSSLTSSNY EKYLQLATEK 
        60         70         80         90        100
NPCMILELEL DGKVRYGSPQ WNTITGVADD SGSSPTYIAD LILGSDQDKG 
       110        120        130        140        150
VFQKATDMLL MNDDTSCTIT FKIKAADYEG SAGCDDESTI TTLEARGILI 
       160        170        180        190        200
RDGHTQLPSH TMWIVKPRTN DWSDFYANED AQDDMVIQLS DNCDDIDIQL 
       210        220        230        240        250
PEEFAKTLGF GAKIFVQYLK RIRLEMIIDE FNLPLPKMEL CRVCENFVPV 
       260        270        280        290        300
WWLETHSQSC VCEHRTESLI QLLHDNLLEQ QAILANFTKD SEYKGSQIQV 
       310        320        330        340        350
RSNNFLNQVL DSLRELCQDA IDINPSEMVP DLYHSLSTFP QDNGNNNNNN 
       360        370        380        390        400
NNNNNNNNAL LDQFPIQKDT VSLNSYFQFS PRTNHNIQNV TSWQSRFFLN 
       410        420        430        440        450
DDQDPGLALL IHDTLDLARK KVDAVLRLDN AMTYSLKIKN EVNNYVVQLI 
       460        470        480        490        500
REQIEINKHA ILTHPMNLRS SSIFHSPLPQ IHSQQPEAEN LIYSSSTPLQ 
       510        520        530        540        550
VQHDQCASFE APSKSHLEPI PFPVSSIEET PTANDIRHPS PLPRSCSNTV 
       560        570        580        590        600
MKLPTPRRKL DSNGLFSDAY LNADIIPNPS IESTISIDRD NNTNSRGSSM 
       610        620        630        640        650
KQYGIGEATD SRTSNSERPS SSSSRLGIRS RSITPRQKIE YSHVDNDDRT 
       660        670        680        690        700
NEMLSRDKDS LQPQPSVDTT ITSSTQATTT GTKTNSNNST NSVLPKLMTS 
       710        720        730        740        750
ISLTPRRGSP SFGNLASHSM QQTNSFKLIH DKSPISSPFT FSKDFLTPEQ 
       760        770        780        790        800
HPSNIARTDS INNAMLTSPN MPLSPLLLAT NQTVKSPTPS IKDYDILKPI 
       810        820        830        840        850
SKGAYGSVYL ARKKLTGDYF AIKVLRKSDM IAKNQVTNVK SERAIMMVQS 
       860        870        880        890        900
DKPYVARLFA SFQNKDNLFL VMEYLPGGDL ATLIKMMGYL PDQWAKQYLT 
       910        920        930        940        950
EIVVGVNDMH QNGIIHHDLK PENLLIDNAG HVKLTDFGLS RAGLIRRHKF 
       960        970        980        990       1000
VPHKSSLSIS STLPIDNPAN NFTMNNNNSN HSQLSTPDSF TSDHKQYNRS 
      1010       1020       1030       1040       1050
KKSSLGQQYE HSEYSSTSNS HSMTPTPSTN TVVYPSYYRG KDRSHGSSNI 
      1060       1070       1080       1090       1100
DLPASLRRSE SQLSFSLLDI SRSSTPPLAN PTNSNANNIM RRKSLTENKS 
      1110       1120       1130       1140       1150
FSNDLLSSDA IAATNTNINS NNNISLSPAP SDLALFYPDD SKQNKKFFGT 
      1160       1170       1180       1190       1200
PDYLAPETIE GKGEDNKQCD WWSVGCIFFE LLLGYPPFHA ETPDAVFKKI 
      1210       1220       1230       1240       1250
LSGVIQWPEF KNEEEEREFL TPEAKDLIEK LLVVDPAKRL GAKGIQEIKD 
      1260       1270       1280       1290       1300
HPYFKNVDWD HVYDEEASFV PTIDNPEDTD YFDLRGAELQ DFGDDIENDN 
      1310       1320       1330       1340       1350
ANILFGKHGI NTDVSELSAA NLSPPLNHKN ILSRKLSMSN TTNRSSNNSN 
      1360       1370       1380       1390       1400
SSVHDFGAHT PVNKLSIASV LESVPQETGY ITPNGTGTTT TSAKNSPNLK 
      1410       1420       1430       1440       1450
NLSLAIPPHM RDRRSSKLND SQTEFGSFNF RNLSALDKAN KDAINRLKSE 
      1460       1470       1480       1490       1500
HFSEQPGVHR RTSSASLMGS SSDGSVSTPG SNASNTTSGG KLKIHKPTIS 
      1510       1520       1530       1540       1550
GSPSTFGTFP KTFLRSDSFS TRSYSPERSI SIDSSTLSRK GSIIGDNQQT 
      1560       1570       1580       1590       1600
TANSSDSPTM TKFKSPLSPA NTTTVSSYFS RQRVLSKSFS QRTNSSDLSA 
      1610       1620       1630       1640       1650
EESDRLQAIS RVNSLRNRRR SGRKSSSTSE IGYHMDVLVC EPIPIHRYRV 
      1660       1670       1680       1690       1700
TKDLENLGCT VVSVGAGDEL VSRATSGVSF DLIMTALKLP KLGAIDIVQL 
      1710       1720       1730       1740       1750
LKQTNGANST TPIVAITNYF QEAATSRVFD DVLEKPVKLD ELKKLVAKYA 
      1760       1770
LKKSQEDEEH TILSDSDETH
Length:1,770
Mass (Da):196,531
Last modified:November 1, 1995 - v1
<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:iDC1064825000FAFF
GO

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
D50617 Genomic DNA Translation: BAA09206.1
U83459 Genomic DNA Translation: AAB64088.1
AJ001030 Genomic DNA Translation: CAA04486.1
BK006940 Genomic DNA Translation: DAA12408.1

Protein sequence database of the Protein Information Resource

More...PIRi		S56221

NCBI Reference Sequences

More...RefSeqi		NP_116620.1, NM_001179933.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YFL033C_mRNA; YFL033C; YFL033C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		850511

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YFL033C

<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
D50617 Genomic DNA Translation: BAA09206.1
U83459 Genomic DNA Translation: AAB64088.1
AJ001030 Genomic DNA Translation: CAA04486.1
BK006940 Genomic DNA Translation: DAA12408.1
PIRiS56221
RefSeqiNP_116620.1, NM_001179933.1

3D structure databases

SMRiP43565
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi31114, 385 interactors
DIPiDIP-2510N
ELMiP43565
IntActiP43565, 16 interactors
MINTiP43565
STRINGi4932.YFL033C

PTM databases

CarbonylDBiP43565
iPTMnetiP43565

Proteomic databases

MaxQBiP43565
PaxDbiP43565
PRIDEiP43565

Genome annotation databases

EnsemblFungiiYFL033C_mRNA; YFL033C; YFL033C
GeneIDi850511
KEGGisce:YFL033C

Organism-specific databases

SGDiS000001861, RIM15
VEuPathDBiFungiDB:YFL033C

Phylogenomic databases

eggNOGiKOG0605, Eukaryota
GeneTreeiENSGT00940000157002
HOGENOMiCLU_000709_4_0_1
InParanoidiP43565
OMAiISQVLQW

Enzyme and pathway databases

BRENDAi2.7.11.1, 984

Miscellaneous databases

Protein Ontology

More...PROi		PR:P43565
RNActiP43565, protein

Family and domain databases

InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR011006, CheY-like_superfamily
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS
IPR001789, Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF00069, Pkinase, 2 hits
SMARTiView protein in SMART
SM00448, REC, 1 hit
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF52172, SSF52172, 1 hit
SSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit
PS50110, RESPONSE_REGULATORY, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiRIM15_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: P43565
Secondary accession number(s): D6VTJ8
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 23, 2022
This is version 211 of the entry and version 1 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

Reference proteome

Documents

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