P43633 (ALK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Haspin homolog ALK1
EC=2.7.11.1

Alternative name(s):
DNA damage-responsive protein ALK1

Gene names

Name:	ALK1
Ordered Locus Names:	YGL021W
ORF Names:	G3686

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Induction	Absent in G1-arrested cells and accumulates in G2-M. Ref.5
Domain	The KEN and D (destructive) boxes are required for the cell cycle-controled ALK1 degradation by the anaphase promoting complex (APC) pathway. Ref.5 The protein kinase domain is predicted to be catalytically inactive. However, weak kinase activity was experimentally demonstrated. Ref.5
Post-translational modification	Periodically phosphorylated during the cell cycle with a phosphorylation peak during mitosis and hyperphosphorylated after DNA damage. Ref.6 Ref.7
Miscellaneous	Present with 2190 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle DNA damage
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitosis Inferred from expression pattern Ref.5. Source: SGD response to DNA damage stimulus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine 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 – 760	760	Serine/threonine-protein kinase Haspin homolog ALK1		PRO_0000064557
Regions
	Domain	468 – 760	293	Protein kinase
	Nucleotide binding	474 – 482	9	ATP By similarity
	Motif	200 – 202	3	KEN box
	Motif	224 – 232	9	D box
	Compositional bias	94 – 449	356	Ser-rich
	Compositional bias	240 – 245	6	Poly-Gln
	Compositional bias	264 – 269	6	Poly-Ser
	Compositional bias	351 – 356	6	Poly-Ser
Sites
	Binding site	510	1	ATP By similarity
Amino acid modifications
	Modified residue	172	1	Phosphothreonine Ref.6
	Modified residue	318	1	Phosphoserine Ref.6
	Modified residue	351	1	Phosphoserine Ref.7
	Modified residue	439	1	Phosphothreonine Ref.7
Experimental info
	Mutagenesis	606 – 610	5	EHRNL → AAAAA: Reduces strongly kinase activity. Ref.5
	Sequence conflict	758 – 760	3	LYK → AL in CAA61012. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P43633 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 3FD169AD789ED60A	FASTA	760	86,087
	10 20 30 40 50 60 MLLHFDIVIQ LLSSHTLKSH QVEPPMDFET SFEEFVEDKR FIALEVSDND DDCDTDLTAD 70 80 90 100 110 120 TADELESSAI LKMRESDASL NVTTGNNTSR KTTSNSKKRW SLLSNHSAVS SSKSKKRWSV 130 140 150 160 170 180 LSSSFTSESH KDRESRNVLQ QKRKSLQSYS SLDTVASNSS ISASSSLKRS STGLSLRQLF 190 200 210 220 230 240 TKIGINDDIS QPGIGIPQGK ENLPPTMGKK NSSIASTSSE NRLRTPLKPL VNHSKRPTSQ 250 260 270 280 290 300 PQQQQPLYNA SLSSRRSSIS STVSSSSSSK WRFWKRNKNQ TPALLQPDHH SLKTFPAVNR 310 320 330 340 350 360 RDSMTPVEPR NMVKHKTSFS DFHKTIFSSN TYSESSDTIS SMEITLKNKA SSSSLSLNVL 370 380 390 400 410 420 KKRNSQSSLK HKSSHASLQK FKRNKGKSSM IAPSTATNSS NDDSCSYSSK NSTLSHRISL 430 440 450 460 470 480 PVPDQVSRDK IQNKLRYSTS LLSLNSKSSL PMNKNDHDET LLRQILLNCD IKRILNPAKG 490 500 510 520 530 540 DVLPLINDVN HLSSIQLTSN VWQIGEVICK KVSLGTIDDI TWDRKFLSLQ ELEKLKIMQQ 550 560 570 580 590 600 KFDGIPQLLK SFVVKEANGG LYLYLLFKDH GTPISLISLK NWKQILKIFW SCAGIIHGLE 610 620 630 640 650 660 KNLKFEHRNL TLDNILIDGN GNITIIDFKC SRLQTPQDDV LYLRLDHPLF FLNGKDKSKI 670 680 690 700 710 720 NEYQYQFEFE IYQSMRILLN MDASAFEPMT NLYWLYYLSR VLLKFGDRKL GKNDANRDKM 730 740 750 760 ARVINHLEMN LAVHKRGGQL FKRLETEDIK NTGDLLKLYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel DNA damage-response gene from Saccharomyces cerevisiae with homology to protein kinase." Moen C., Lindstedt B.A., Berdal K.G., Rognes T., Seeberg E.C. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Alk1 and Alk2 are two new cell cycle-regulated haspin-like proteins in budding yeast." Nespoli A., Vercillo R., di Nola L., Diani L., Giannattasio M., Plevani P., Muzi-Falconi M. Cell Cycle 5:1464-1471(2006) [PubMed: 16855400] [Abstract] Cited for: FUNCTION, INDUCTION, DOMAINS, MUTAGENESIS OF 606-E--L-610.
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 AND SER-318, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND THR-439, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X87672 Genomic DNA. Translation: CAA61012.1. Z72543 Genomic DNA. Translation: CAA96721.1. BK006941 Genomic DNA. Translation: DAA08077.1.
PIR	S64023.
RefSeq	NP_011494.1. NM_001180886.1.
3D structure databases
ProteinModelPortal	P43633.
SMR	P43633. Positions 506-636.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4816N.
MINT	MINT-527379.
STRING	P43633.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL021W; YGL021W; YGL021W.
GeneID	852863.
KEGG	sce:YGL021W.
NMPDR	fig|4932.3.peg.2601.
Organism-specific databases
CYGD	YGL021w.
SGD	S000002989. ALK1.
Phylogenomic databases
eggNOG	fuNOG10805.
GeneTree	EFGT00050000003025.
OMA	SSKKRWS.
OrthoDB	EOG483HCS.
Gene expression databases
ArrayExpress	P43633.
Genevestigator	P43633.
GermOnline	YGL021W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR024604. DUF3635. IPR011009. Kinase-like_dom. [Graphical view]
Pfam	PF12330. DUF3635. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50011. PROTEIN_KINASE_DOM. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	972475.

Entry information

Entry name

ALK1_YEAST

Accession

Primary (citable) accession number: P43633
Secondary accession number(s): D6VUB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program