Reviewed, UniProtKB/Swiss-Prot Q10156 (LKH1_SCHPO)

Names and origin

Protein names

Recommended name:
    Dual specificity protein kinase lkh1
    EC=2.7.12.1

Gene names

Name:	lkh1
Synonyms:	kic1
ORF Names:	SPAC1D4.11c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that may act as a negative regulator of filamentous growth and flocculation. Appears to have a role in normal cell wall and septum formation and in cell seperation. May have antagonistic function in the regulation of beta-glucan distribution between the sites for cell wall and septum assembly. Ref.1 Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Post-translational modification	Autophosphorylates on all three types of residues Probable.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from mutant phenotype. Source: GeneDB_SPombe intracellular signaling cascade Ref.2 Traceable author statement. Source: GeneDB_SPombe negative regulation of filamentous growth Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe negative regulation of flocculation Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe protein amino acid phosphorylation Inferred by curator. Source: GeneDB_SPombe regulation of barrier septum formation Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of cell separation during cytokinesis Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of fungal-type cell wall organization Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: GeneDB_SPombe protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 690	690	Dual specificity protein kinase lkh1		PRO_0000086236
Regions
	Domain	362 – 682	321	Protein kinase
	Nucleotide binding	368 – 376	9	ATP By similarity
	Compositional bias	132 – 233	102	Pro-rich
Sites
	Active site	488	1	Proton acceptor By similarity
	Binding site	391	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10156-1 [UniParc]. Last modified May 30, 2006. Version 3. Checksum: AE85C3A27E4DE03E	FASTA	690	77,494
	10 20 30 40 50 60 MHSLKRRRNH APDWQDFYKN GVPQEVIVIE DSASPRLTPN LPPPFSVHQL QSFVPPQPPS 70 80 90 100 110 120 SSSPSTTGTV AVPINGANAV YPSTNSVSLP QSYDPWLDAN GVVPLPHDVA SHPSYMVQSP 130 140 150 160 170 180 TSYHACSNNQ SPFPHSHHPP LHNPLPVSCQ PVLRPPPVPQ VPSHWYPVSL PSPNLPHQPI 190 200 210 220 230 240 SKPPVIPNLP KLQVHPNRLP HPIHNHPYSS PTSYPPPLCP ATYCPSNPPQ LAPATAIAPS 250 260 270 280 290 300 SQSSQHKSVN YSVTPSSINN HTAVPLSPTL AVWLPMTQPT FQPPSANVYQ PASNANQVIT 310 320 330 340 350 360 PVSISDYRPP KKRKRAAWPP YKKVDRVNVP VVHDTTAFDP STFDDDDGHY KVVPNSKFAN 370 380 390 400 410 420 RYTVVRLLGH GTFGKVIQCY DQSTGRHCAI KVTRAIPKYR EASLIELRVL QTIAHSDPTN 430 440 450 460 470 480 ENKCIQLRDY FDYRKHICIV TDLFGWSVFD FLKNNNYIPF PLKHIQMLSQ QLFKSVAFLH 490 500 510 520 530 540 SLGLVHTDLK PENVLLVSNA SRTIRLPYRN YSQKVLNSCE IRLIDFGSAT FEDEYHSSVV 550 560 570 580 590 600 STRHYRAPEI ILGLGWSYPC DVWSIGCILV ELFTGQALFQ THEDSEHLCM MEKILGPFDR 610 620 630 640 650 660 NMISRSSRTS QRFFKSDGKV RYPLSNTPKK SINYLQSLQT LEQIFAVSSP EVALLLDLLK 670 680 690 KVFVYDPKRR ITAKEALWHP FFTQPISSNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Negative regulation of filamentous growth and flocculation by Lkh1, a fission yeast LAMMER kinase homolog." Kim K.-H., Cho Y.-M., Kang W.-H., Kim J.-H., Byun K.-H., Park Y.-D., Bae K.-S., Park H.-M. Biochem. Biophys. Res. Commun. 289:1237-1242(2001) [PubMed: 11741326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"The kic1 kinase of schizosaccharomyces pombe is a CLK/STY orthologue that regulates cell-cell separation." Tang Z., Mandel L.L., Yean S.-L., Lin C.X., Chen T., Yanagida M., Lin R.-J. Exp. Cell Res. 283:101-115(2003) [PubMed: 12565823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION.
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF334941 mRNA. Translation: AAK12335.1. Different initiation. CU329670 Genomic DNA. Translation: CAD29835.2.
PIR	JC7794.
RefSeq	NP_001018187.2.
3D structure databases
HSSP	HSSP built from PDB template 1LEZ based on UniProtKB P47811.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10156.
Genome annotation databases
GeneID	3361532.
GenomeReviews	Gene locus lkh1 in contig CU329670_GR.
KEGG	spo:SPAC1D4.11c.
NMPDR	fig|4896.1.peg.2994.
Organism-specific databases
GeneDB_Spombe	SPAC1D4.11c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000745-MON.
BRENDA	2.7.12.1. 653.
Gene expression databases
ArrayExpress	Q10156.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKH1_SCHPO

Accession

Primary (citable) accession number: Q10156
Secondary accession number(s): Q9C3Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2006
Last modified:	September 22, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)