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Entry version 183 (16 Oct 2019)
Sequence version 2 (01 Oct 1996)
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Protein

Checkpoint serine/threonine-protein kinase BUB1

Gene

BUB1

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

Involved in cell cycle checkpoint enforcement. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism. Catalyzes the phosphorylation of BUB3 and its autophosphorylation. Associates with centromere (CEN) DNA via interaction with SKP1. The association with SKP1 is required for the mitotic delay induced by kinetochore tension defects, but not for the arrest induced by spindle depolymerization or kinetochore assembly defects.1 Publication

Miscellaneous

Present with 414 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

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 sitei733ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei833Proton acceptorPROSITE-ProRule annotation1

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 bindingi711 – 719ATPPROSITE-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

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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30878-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-SCE-179409 APC-Cdc20 mediated degradation of Nek2A

<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:
Checkpoint serine/threonine-protein kinase BUB1 (EC:2.7.11.1)
<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:BUB1
Ordered Locus Names:YGR188C
ORF Names:G7542
<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 VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGR188C

Saccharomyces Genome Database

More...
SGDi
S000003420 BUB1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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>Mutagenesisi733K → R: Loss of activity. 1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000856761 – 1021Checkpoint serine/threonine-protein kinase BUB1Add BLAST1021

<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

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P41695

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

More...
PaxDbi
P41695

PRoteomics IDEntifications database

More...
PRIDEi
P41695

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P41695

<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

Part of complex consisting of MAD1, BUB1 and BUB3 after activation of spindle checkpoint.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33440, 718 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-154 Bub1-Bub3 complex
CPX-3212 Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex

Database of interacting proteins

More...
DIPi
DIP-2236N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P41695

Protein interaction database and analysis system

More...
IntActi
P41695, 16 interactors

Molecular INTeraction database

More...
MINTi
P41695

STRING: functional protein association networks

More...
STRINGi
4932.YGR188C

<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

11021
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
P41695

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P41695

<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_and_domains_section">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>Domaini47 – 212BUB1 N-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini705 – 1021Protein kinasePROSITE-ProRule annotationAdd BLAST317

<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. BUB1 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000248151

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P41695

KEGG Orthology (KO)

More...
KOi
K02178

Identification of Orthologs from Complete Genome Data

More...
OMAi
DNCMIRF

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015661 Bub1/Mad3
IPR011009 Kinase-like_dom_sf
IPR013212 Mad3/Bub1_I
IPR012572 Mad3/Bub1_II
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR14030 PTHR14030, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08311 Mad3_BUB1_I, 1 hit
PF08171 Mad3_BUB1_II, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00777 Mad3_BUB1_I, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51489 BUB1_N, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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_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.

P41695-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLDLGSTVR GYESDKDTFP QSKGVSSSQK EQHSQLNQTK IAYEQRLLND
60 70 80 90 100
LEDMDDPLDL FLDYMIWIST SYIEVDSESG QEVLRSTMER CLIYIQDMET
110 120 130 140 150
YRNDPRFLKI WIWYINLFLS NNFHESENTF KYMFNKGIGT KLSLFYEEFS
160 170 180 190 200
KLLENAQFFL EAKVLLELGA ENNCRPYNRL LRSLSNYEDR LREMNIVENQ
210 220 230 240 250
NSVPDSRERL KGRLIYRTAP FFIRKFLTSS LMTDDKENRA NLNSNVGVGK
260 270 280 290 300
SAPNVYQDSI VVADFKSETE RLNLNSSKQP SNQRLKNGNK KTSIYADQKQ
310 320 330 340 350
SNNPVYKLIN TPGRKPERIV FNFNLIYPEN DEEFNTEEIL AMIKGLYKVQ
360 370 380 390 400
RRGKKHTEDY TSDKNRKKRK LDVLVERRQD LPSSQPPVVP KSTRIEVFKD
410 420 430 440 450
DDNPSQSTHH KNTQVQVQTT TSILPLKPVV DGNLAHETPV KPSLTSNASR
460 470 480 490 500
SPTVTAFSKD AINEVFSMFN QHYSTPGALL DGDDTTTSKF NVFENFTQEF
510 520 530 540 550
TAKNIEDLTE VKDPKQETVS QQTTSTNETN DRYERLSNSS TRPEKADYMT
560 570 580 590 600
PIKETTETDV VPIIQTPKEQ IRTEDKKSGD NTETQTQLTS TTIQSSPFLT
610 620 630 640 650
QPEPQAEKLL QTAEHSEKSK EHYPTIIPPF TKIKNQPPVI IENPLSNNLR
660 670 680 690 700
AKFLSEISPP LFQYNTFYNY NQELKMSSLL KKIHRVSRNE NKNPIVDFKK
710 720 730 740 750
TGDLYCIRGE LGEGGYATVY LAESSQGHLR ALKVEKPASV WEYYIMSQVE
760 770 780 790 800
FRLRKSTILK SIINASALHL FLDESYLVLN YASQGTVLDL INLQREKAID
810 820 830 840 850
GNGIMDEYLC MFITVELMKV LEKIHEVGII HGDLKPDNCM IRLEKPGEPL
860 870 880 890 900
GAHYMRNGED GWENKGIYLI DFGRSFDMTL LPPGTKFKSN WKADQQDCWE
910 920 930 940 950
MRAGKPWSYE ADYYGLAGVI HSMLFGKFIE TIQLQNGRCK LKNPFKRYWK
960 970 980 990 1000
KEIWGVIFDL LLNSGQASNQ ALPMTEKIVE IRNLIESHLE QHAENHLRNV
1010 1020
ILSIEEELSH FQYKGKPSRR F
Length:1,021
Mass (Da):117,868
Last modified:October 1, 1996 - v2
<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:i6D76FC980775D3F9
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 conflicti531D → V in AAA64894 (PubMed:7969164).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
L32027 Genomic DNA Translation: AAA64894.1
Z72973 Genomic DNA Translation: CAA97214.1
X99074 Genomic DNA Translation: CAA67524.1
BK006941 Genomic DNA Translation: DAA08282.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64506

NCBI Reference Sequences

More...
RefSeqi
NP_011704.3, NM_001181317.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGR188C_mRNA; YGR188C; YGR188C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853100

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGR188C

<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
L32027 Genomic DNA Translation: AAA64894.1
Z72973 Genomic DNA Translation: CAA97214.1
X99074 Genomic DNA Translation: CAA67524.1
BK006941 Genomic DNA Translation: DAA08282.1
PIRiS64506
RefSeqiNP_011704.3, NM_001181317.3

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
2I3SX-ray1.90B/D/F315-350[»]
3ESLX-ray1.74A/B29-230[»]
4BL0X-ray1.95B/E289-359[»]
SMRiP41695
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33440, 718 interactors
ComplexPortaliCPX-154 Bub1-Bub3 complex
CPX-3212 Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex
DIPiDIP-2236N
ELMiP41695
IntActiP41695, 16 interactors
MINTiP41695
STRINGi4932.YGR188C

PTM databases

iPTMnetiP41695

Proteomic databases

MaxQBiP41695
PaxDbiP41695
PRIDEiP41695

Genome annotation databases

EnsemblFungiiYGR188C_mRNA; YGR188C; YGR188C
GeneIDi853100
KEGGisce:YGR188C

Organism-specific databases

EuPathDBiFungiDB:YGR188C
SGDiS000003420 BUB1

Phylogenomic databases

HOGENOMiHOG000248151
InParanoidiP41695
KOiK02178
OMAiDNCMIRF

Enzyme and pathway databases

BioCyciYEAST:G3O-30878-MONOMER
BRENDAi2.7.11.1 984
ReactomeiR-SCE-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-SCE-179409 APC-Cdc20 mediated degradation of Nek2A

Miscellaneous databases

EvolutionaryTraceiP41695

Protein Ontology

More...
PROi
PR:P41695

Family and domain databases

InterProiView protein in InterPro
IPR015661 Bub1/Mad3
IPR011009 Kinase-like_dom_sf
IPR013212 Mad3/Bub1_I
IPR012572 Mad3/Bub1_II
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR14030 PTHR14030, 1 hit
PfamiView protein in Pfam
PF08311 Mad3_BUB1_I, 1 hit
PF08171 Mad3_BUB1_II, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00777 Mad3_BUB1_I, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51489 BUB1_N, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiBUB1_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: P41695
Secondary accession number(s): D6VUX1
<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: November 1, 1995
Last sequence update: October 1, 1996
Last modified: October 16, 2019
This is version 183 of the entry and version 2 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, Complete proteome, Reference proteome

Documents

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