Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P25389

- KCC4_YEAST

UniProt

P25389 - KCC4_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable serine/threonine-protein kinase KCC4

Gene

KCC4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501ATPPROSITE-ProRule annotation
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphatidic acid binding Source: UniProtKB
  3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  4. phosphatidylserine binding Source: UniProtKB
  5. protein kinase activity Source: SGD
  6. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. budding cell bud growth Source: SGD
  2. cytokinesis checkpoint Source: SGD
  3. protein phosphorylation Source: SGD
  4. regulation of cell shape Source: UniProtKB-KW
  5. septin ring assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29286-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable serine/threonine-protein kinase KCC4 (EC:2.7.11.1)
Gene namesi
Name:KCC4
Ordered Locus Names:YCL024W
ORF Names:YCL24W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCL024w.
SGDiS000000529. KCC4.

Subcellular locationi

Bud neck 2 Publications

GO - Cellular componenti

  1. cellular bud neck Source: SGD
  2. cellular bud neck septin collar Source: SGD
  3. incipient cellular bud site Source: SGD
  4. plasma membrane Source: UniProtKB
  5. septin ring Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10371037Probable serine/threonine-protein kinase KCC4PRO_0000086109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei396 – 3961Phosphoserine1 Publication
Modified residuei675 – 6751Phosphoserine1 Publication
Modified residuei707 – 7071Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei822 – 8221Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication
Modified residuei871 – 8711Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25389.
PaxDbiP25389.
PRIDEiP25389.

Expressioni

Gene expression databases

GenevestigatoriP25389.

Interactioni

Subunit structurei

Interacts with septin proteins, primarily with CDC11. Interacts with SWE1 and NAP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NAP1P252936EBI-9607,EBI-11850

Protein-protein interaction databases

BioGridi30960. 85 interactions.
DIPiDIP-1779N.
IntActiP25389. 14 interactions.
MINTiMINT-397998.

Structurei

Secondary structure

1
1037
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi921 – 9244Combined sources
Helixi925 – 9273Combined sources
Beta strandi930 – 9334Combined sources
Beta strandi938 – 9425Combined sources
Helixi944 – 95613Combined sources
Helixi959 – 9613Combined sources
Beta strandi963 – 9697Combined sources
Turni970 – 9734Combined sources
Beta strandi974 – 9796Combined sources
Beta strandi984 – 9863Combined sources
Beta strandi990 – 9989Combined sources
Beta strandi1004 – 101310Combined sources
Helixi1015 – 103117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OSMX-ray1.70A917-1037[»]
3OSTX-ray1.69A917-1037[»]
ProteinModelPortaliP25389.
SMRiP25389. Positions 18-361, 918-1036.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25389.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 285265Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi388 – 499112Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119244.
HOGENOMiHOG000057100.
InParanoidiP25389.
KOiK08286.
OrthoDBiEOG793BK1.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25389-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVANTETHS AAKPSSTIGP WKLGETLGFG STGKVQLAQH ERTGHRTAVK
60 70 80 90 100
VISKSIFNNN GNHSNDDSVL PYNIEREIVI MKLLSHPNVL SLYDVWETNN
110 120 130 140 150
NLYLILEYAE KGELFNLLVD HGPLPEREAI NCFRQIIIGI SYCHALGIVH
160 170 180 190 200
RDLKPENLLL DSFYNIKIAD FGMAALQTDA DLLETSCGSP HYAAPEIVSG
210 220 230 240 250
LPYEGFASDV WSCGVILFAL LTGRLPFDEE NGNVRDLLLK VQKGQFEMPN
260 270 280 290 300
DTEISRDAQD LIGKILVVDP RQRIKIRDIL SHPLLKKYQT IKDSKSIKDL
310 320 330 340 350
PRENTYLYPL ADSNNHTSAS IDDSILQNLV VLWHGRHADD IVSKLKENGT
360 370 380 390 400
NKEKILYALL YRFKLDSVRG SNKKNRNKIK KTKKNKRSST LSSSSSLLLN
410 420 430 440 450
NRSIQSTPRR RTSKRHSREF SSSRKRSSFL LSSNPTDSSP IPLRSSKRIT
460 470 480 490 500
HINVASANTQ ATPSGVPNPH KRNSKKRSSK RLSYMPNTKR SSLTSKSLSN
510 520 530 540 550
FTNLIDDDDW EYIEKDAKRT SSNFATLIDE IFEPEKFELA KREKAELQRK
560 570 580 590 600
VQEAKRQSVN AQKINEDEFG SEVSDGMKEL KKINDKVSSP LINYEFSQQE
610 620 630 640 650
LLQDIDTLLT NRYQLSSYTR PISRLDPGLT PVTETLPNNL KEKTALLQDT
660 670 680 690 700
EKKIIETIRR SKFLGSLLNV RGGLSPGKSE LAPIEESPIV STTPLIYNDR
710 720 730 740 750
MEPRRISDVE VPHFTRKSKH FTTANNRRSV LSLYAKDSIK DLNEFLIKED
760 770 780 790 800
PDLPPQGSTD NESRSEDPEI AESITDSRNI QYDEDDSKDG DNVNNDNILS
810 820 830 840 850
DFPQGVGISQ EYDMKDKNPN QSPISKSAEP TLVVKLPSLS SFQGKNASGL
860 870 880 890 900
GLYQREPSKV TLPSLTSNNS SVGENIEDGA EKGTESEKIA ASLSDDDLKE
910 920 930 940 950
DNDKKDNDTV NAPTTVKKPP NSVLLKKFSK GKILELEIHA KIPEKRLYEG
960 970 980 990 1000
LHKLLEGWKQ YGLKNLVFNI TNMIITGKLV NDSILFLRST LFEIMVLPNG
1010 1020 1030
DGRSLIKFNK KTGSTKTLTK LATEIQIILQ KEGVLDK
Length:1,037
Mass (Da):116,475
Last modified:June 27, 2003 - v3
Checksum:i2F5FF36DA8C5B1A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42961.1.
BK006937 Genomic DNA. Translation: DAA07461.1.
PIRiS74283.
RefSeqiNP_009907.2. NM_001178670.1.

Genome annotation databases

EnsemblFungiiYCL024W; YCL024W; YCL024W.
GeneIDi850334.
KEGGisce:YCL024W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42961.1 .
BK006937 Genomic DNA. Translation: DAA07461.1 .
PIRi S74283.
RefSeqi NP_009907.2. NM_001178670.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OSM X-ray 1.70 A 917-1037 [» ]
3OST X-ray 1.69 A 917-1037 [» ]
ProteinModelPortali P25389.
SMRi P25389. Positions 18-361, 918-1036.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30960. 85 interactions.
DIPi DIP-1779N.
IntActi P25389. 14 interactions.
MINTi MINT-397998.

Proteomic databases

MaxQBi P25389.
PaxDbi P25389.
PRIDEi P25389.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCL024W ; YCL024W ; YCL024W .
GeneIDi 850334.
KEGGi sce:YCL024W.

Organism-specific databases

CYGDi YCL024w.
SGDi S000000529. KCC4.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119244.
HOGENOMi HOG000057100.
InParanoidi P25389.
KOi K08286.
OrthoDBi EOG793BK1.

Enzyme and pathway databases

BioCyci YEAST:G3O-29286-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25389.
NextBioi 965772.
PROi P25389.

Gene expression databases

Genevestigatori P25389.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiKCC4_YEAST
AccessioniPrimary (citable) accession number: P25389
Secondary accession number(s): D6VQZ2, P87005, Q8NKJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: November 26, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3