P25389 (KCC4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable serine/threonine-protein kinase KCC4
EC=2.7.11.1

Gene names

Name:	KCC4
Ordered Locus Names:	YCL024W
ORF Names:	YCL24W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1037 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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 process	Cell cycle Cell division Cell shape
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	budding cell bud growth Inferred from genetic interaction Ref.1. Source: SGD regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW septin checkpoint Inferred from mutant phenotype Ref.1. Source: SGD septin ring assembly Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	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_function	ATP 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 direct assay PubMed 16319894. Source: SGD protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAP1	P25293	6	EBI-9607,EBI-11850

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1037

1037

Probable serine/threonine-protein kinase KCC4

PRO_0000086109

Regions

Domain

21 – 285

265

Protein kinase

Nucleotide binding

27 – 35

9

ATP By similarity

Compositional bias

388 – 499

112

Ser-rich

Sites

Active site

152

1

Proton acceptor By similarity

Binding site

50

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

Phosphothreonine Ref.12

Modified residue

396

1

Phosphoserine Ref.12

Modified residue

439

1

Phosphoserine Ref.12

Modified residue

675

1

Phosphoserine Ref.10 Ref.12

Modified residue

679

1

Phosphoserine Ref.12

Modified residue

729

1

Phosphoserine Ref.12

Modified residue

773

1

Phosphoserine Ref.12

Modified residue

775

1

Phosphothreonine Ref.12

Modified residue

822

1

Phosphoserine Ref.12

Modified residue

825

1

Phosphoserine Ref.12

Modified residue

838

1

Phosphoserine Ref.12

Modified residue

841

1

Phosphoserine Ref.12

Modified residue

848

1

Phosphoserine Ref.9

Secondary structure

1

.

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.

.

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.

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.

.

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1037

Helix Strand Turn

Details...

Helix

921 – 924

4

Helix

925 – 927

3

Beta strand

930 – 933

4

Beta strand

938 – 942

5

Helix

944 – 956

13

Helix

959 – 961

3

Beta strand

963 – 969

7

Turn

970 – 973

4

Beta strand

974 – 979

6

Beta strand

984 – 986

3

Beta strand

990 – 998

9

Beta strand

1004 – 1013

10

Helix

1015 – 1031

17

Sequences

	Sequence		Length	Mass (Da)
	P25389 [UniParc]. Last modified June 27, 2003. Version 3. Checksum: 2F5FF36DA8C5B1A3	FASTA	1,037	116,475
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY.
[12]	"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 THR-2; SER-396; SER-439; SER-675; SER-679; SER-729; SER-773; THR-775; SER-822; SER-825; SER-838 AND SER-841, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59720 Genomic DNA. Translation: CAC42961.1.
BK006937 Genomic DNA. Translation: DAA07461.1.

PIR

S74283.

RefSeq

NP_009907.2. NM_001178670.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OSM	X-ray	1.70	A	917-1037	[»]
3OST	X-ray	1.69	A	917-1037	[»]

ProteinModelPortal

P25389.

SMR

P25389. Positions 18-361, 918-1036.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1779N.

IntAct

P25389. 12 interactions.

MINT

MINT-397998.

Proteomic databases

PaxDb

P25389.

PRIDE

P25389.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YCL024W; YCL024W; YCL024W.

GeneID

850334.

KEGG

sce:YCL024W.

Organism-specific databases

CYGD

YCL024w.

SGD

S000000529. KCC4.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00700000104008.

HOGENOM

HOG000057100.

KO

K08286.

OrthoDB

EOG4B2X58.

Gene expression databases

ArrayExpress

P25389.

Genevestigator

P25389.

GermOnline

YCL024W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25389.

NextBio

965772.

Entry information

Entry name

KCC4_YEAST

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program