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P25389 (KCC4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable serine/threonine-protein kinase KCC4

EC=2.7.11.1
Gene names
Name:KCC4
Ordered Locus Names:YCL024W
ORF Names:YCL24W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with septin proteins, primarily with CDC11. Interacts with SWE1 and NAP1. Ref.2 Ref.7 Ref.9

Subcellular location

Bud neck Ref.1 Ref.7.

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Cell shape
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbudding cell bud growth

Inferred from mutant phenotype Ref.1. Source: SGD

cytokinesis checkpoint

Inferred from mutant phenotype Ref.1. Source: SGD

protein phosphorylation

Inferred from sequence or structural similarity PubMed 9813093. Source: SGD

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

septin ring assembly

Inferred from mutant phenotype Ref.1. Source: SGD

   Cellular_componentcellular bud neck

Inferred from direct assay PubMed 15282802Ref.1. Source: SGD

cellular bud neck septin collar

Inferred from direct assay PubMed 15901837. Source: SGD

incipient cellular bud site

Inferred from direct assay PubMed 15901837. Source: SGD

plasma membrane

Inferred from direct assay PubMed 21145462. Source: UniProtKB

septin ring

Inferred from direct assay PubMed 15901837. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidic acid binding

Inferred from direct assay PubMed 21145462. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay PubMed 21145462. Source: UniProtKB

phosphatidylserine binding

Inferred from direct assay PubMed 21145462. Source: UniProtKB

protein kinase activity

Inferred from sequence or structural similarity PubMed 9813093. Source: SGD

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NAP1P252936EBI-9607,EBI-11850

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10371037Probable serine/threonine-protein kinase KCC4
PRO_0000086109

Regions

Domain21 – 285265Protein kinase
Nucleotide binding27 – 359ATP By similarity
Compositional bias388 – 499112Ser-rich

Sites

Active site1521Proton acceptor By similarity
Binding site501ATP By similarity

Amino acid modifications

Modified residue3961Phosphoserine Ref.11
Modified residue6751Phosphoserine Ref.10
Modified residue7071Phosphoserine Ref.11
Modified residue7771Phosphoserine Ref.11
Modified residue8221Phosphoserine Ref.10
Modified residue8251Phosphoserine Ref.10
Modified residue8711Phosphoserine Ref.11

Secondary structure

........................ 1037
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25389 [UniParc].

Last modified June 27, 2003. Version 3.
Checksum: 2F5FF36DA8C5B1A3

FASTA1,037116,475
        10         20         30         40         50         60 
MTVANTETHS AAKPSSTIGP WKLGETLGFG STGKVQLAQH ERTGHRTAVK VISKSIFNNN 

        70         80         90        100        110        120 
GNHSNDDSVL PYNIEREIVI MKLLSHPNVL SLYDVWETNN NLYLILEYAE KGELFNLLVD 

       130        140        150        160        170        180 
HGPLPEREAI NCFRQIIIGI SYCHALGIVH RDLKPENLLL DSFYNIKIAD FGMAALQTDA 

       190        200        210        220        230        240 
DLLETSCGSP HYAAPEIVSG LPYEGFASDV WSCGVILFAL LTGRLPFDEE NGNVRDLLLK 

       250        260        270        280        290        300 
VQKGQFEMPN DTEISRDAQD LIGKILVVDP RQRIKIRDIL SHPLLKKYQT IKDSKSIKDL 

       310        320        330        340        350        360 
PRENTYLYPL ADSNNHTSAS IDDSILQNLV VLWHGRHADD IVSKLKENGT NKEKILYALL 

       370        380        390        400        410        420 
YRFKLDSVRG SNKKNRNKIK KTKKNKRSST LSSSSSLLLN NRSIQSTPRR RTSKRHSREF 

       430        440        450        460        470        480 
SSSRKRSSFL LSSNPTDSSP IPLRSSKRIT HINVASANTQ ATPSGVPNPH KRNSKKRSSK 

       490        500        510        520        530        540 
RLSYMPNTKR SSLTSKSLSN FTNLIDDDDW EYIEKDAKRT SSNFATLIDE IFEPEKFELA 

       550        560        570        580        590        600 
KREKAELQRK VQEAKRQSVN AQKINEDEFG SEVSDGMKEL KKINDKVSSP LINYEFSQQE 

       610        620        630        640        650        660 
LLQDIDTLLT NRYQLSSYTR PISRLDPGLT PVTETLPNNL KEKTALLQDT EKKIIETIRR 

       670        680        690        700        710        720 
SKFLGSLLNV RGGLSPGKSE LAPIEESPIV STTPLIYNDR MEPRRISDVE VPHFTRKSKH 

       730        740        750        760        770        780 
FTTANNRRSV LSLYAKDSIK DLNEFLIKED PDLPPQGSTD NESRSEDPEI AESITDSRNI 

       790        800        810        820        830        840 
QYDEDDSKDG DNVNNDNILS DFPQGVGISQ EYDMKDKNPN QSPISKSAEP TLVVKLPSLS 

       850        860        870        880        890        900 
SFQGKNASGL GLYQREPSKV TLPSLTSNNS SVGENIEDGA EKGTESEKIA ASLSDDDLKE 

       910        920        930        940        950        960 
DNDKKDNDTV NAPTTVKKPP NSVLLKKFSK GKILELEIHA KIPEKRLYEG LHKLLEGWKQ 

       970        980        990       1000       1010       1020 
YGLKNLVFNI TNMIITGKLV NDSILFLRST LFEIMVLPNG DGRSLIKFNK KTGSTKTLTK 

      1030 
LATEIQIILQ KEGVLDK 

« Hide

References

« Hide 'large scale' references
[1]"Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast."
Barral Y., Parra M., Bidlingmaier S., Snyder M.
Genes Dev. 13:176-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]"The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct but partially-overlapping cellular functions."
Okuzaki D., Watanabe T., Tanaka S., Nojima H.
Genes Genet. Syst. 78:113-126(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH SWE1.
[3]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Kcc4 associates with septin proteins of Saccharomyces cerevisiae."
Okuzaki D., Nojima H.
FEBS Lett. 489:197-201(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPTIN PROTEINS, SUBCELLULAR LOCATION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-822 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-707; SER-777 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAC42961.1.
BK006937 Genomic DNA. Translation: DAA07461.1.
PIRS74283.
RefSeqNP_009907.2. NM_001178670.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OSMX-ray1.70A917-1037[»]
3OSTX-ray1.69A917-1037[»]
ProteinModelPortalP25389.
SMRP25389. Positions 15-361, 918-1036.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30960. 85 interactions.
DIPDIP-1779N.
IntActP25389. 14 interactions.
MINTMINT-397998.

Proteomic databases

PaxDbP25389.
PRIDEP25389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL024W; YCL024W; YCL024W.
GeneID850334.
KEGGsce:YCL024W.

Organism-specific databases

CYGDYCL024w.
SGDS000000529. KCC4.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117372.
HOGENOMHOG000057100.
KOK08286.
OrthoDBEOG793BK1.

Enzyme and pathway databases

BioCycYEAST:G3O-29286-MONOMER.

Gene expression databases

GenevestigatorP25389.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25389.
NextBio965772.
PROP25389.

Entry information

Entry nameKCC4_YEAST
AccessionPrimary (citable) accession number: P25389
Secondary accession number(s): D6VQZ2, P87005, Q8NKJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references