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Protein

Serine/threonine-protein kinase Haspin homolog ALK1

Gene

ALK1

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

Functioni

Serine/threonine haspin-like protein kinase involved in cell cycle regulation.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei510 – 5101ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi474 – 4829ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • intracellular signal transduction Source: GO_Central
  • mitotic nuclear division Source: SGD
  • protein phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30541-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Haspin homolog ALK1 (EC:2.7.11.1)
Alternative name(s):
DNA damage-responsive protein ALK1
Gene namesi
Name:ALK1
Ordered Locus Names:YGL021W
ORF Names:G3686
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL021W.
SGDiS000002989. ALK1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi606 – 6105EHRNL → AAAAA: Reduces strongly kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 760760Serine/threonine-protein kinase Haspin homolog ALK1PRO_0000064557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei79 – 791PhosphoserineCombined sources

Post-translational modificationi

Periodically phosphorylated during the cell cycle with a phosphorylation peak during mitosis and hyperphosphorylated after DNA damage.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43633.

PTM databases

iPTMnetiP43633.

Expressioni

Inductioni

Absent in G1-arrested cells and accumulates in G2-M.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi33225. 15 interactions.
DIPiDIP-4816N.
IntActiP43633. 3 interactions.
MINTiMINT-527379.

Structurei

3D structure databases

ProteinModelPortaliP43633.
SMRiP43633. Positions 507-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 760293Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi200 – 2023KEN box
Motifi224 – 2329D box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 449356Ser-richAdd
BLAST
Compositional biasi240 – 2456Poly-Gln
Compositional biasi264 – 2696Poly-Ser
Compositional biasi351 – 3566Poly-Ser

Domaini

The KEN and D (destructive) boxes are required for the cell cycle-controlled ALK1 degradation by the anaphase promoting complex (APC) pathway.1 Publication
The protein kinase domain is predicted to be catalytically inactive. However, weak kinase activity was experimentally demonstrated.1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.Curated

Phylogenomic databases

GeneTreeiENSGT00530000068001.
HOGENOMiHOG000033904.
InParanoidiP43633.
OMAiSSKKRWS.
OrthoDBiEOG7GFBG3.

Family and domain databases

InterProiIPR024604. GSG2_C.
IPR011009. Kinase-like_dom.
[Graphical view]
PfamiPF12330. DUF3635. 1 hit.
[Graphical view]
SMARTiSM01331. DUF3635. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequencei

Sequence statusi: Complete.

P43633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLHFDIVIQ LLSSHTLKSH QVEPPMDFET SFEEFVEDKR FIALEVSDND
60 70 80 90 100
DDCDTDLTAD TADELESSAI LKMRESDASL NVTTGNNTSR KTTSNSKKRW
110 120 130 140 150
SLLSNHSAVS SSKSKKRWSV LSSSFTSESH KDRESRNVLQ QKRKSLQSYS
160 170 180 190 200
SLDTVASNSS ISASSSLKRS STGLSLRQLF TKIGINDDIS QPGIGIPQGK
210 220 230 240 250
ENLPPTMGKK NSSIASTSSE NRLRTPLKPL VNHSKRPTSQ PQQQQPLYNA
260 270 280 290 300
SLSSRRSSIS STVSSSSSSK WRFWKRNKNQ TPALLQPDHH SLKTFPAVNR
310 320 330 340 350
RDSMTPVEPR NMVKHKTSFS DFHKTIFSSN TYSESSDTIS SMEITLKNKA
360 370 380 390 400
SSSSLSLNVL KKRNSQSSLK HKSSHASLQK FKRNKGKSSM IAPSTATNSS
410 420 430 440 450
NDDSCSYSSK NSTLSHRISL PVPDQVSRDK IQNKLRYSTS LLSLNSKSSL
460 470 480 490 500
PMNKNDHDET LLRQILLNCD IKRILNPAKG DVLPLINDVN HLSSIQLTSN
510 520 530 540 550
VWQIGEVICK KVSLGTIDDI TWDRKFLSLQ ELEKLKIMQQ KFDGIPQLLK
560 570 580 590 600
SFVVKEANGG LYLYLLFKDH GTPISLISLK NWKQILKIFW SCAGIIHGLE
610 620 630 640 650
KNLKFEHRNL TLDNILIDGN GNITIIDFKC SRLQTPQDDV LYLRLDHPLF
660 670 680 690 700
FLNGKDKSKI NEYQYQFEFE IYQSMRILLN MDASAFEPMT NLYWLYYLSR
710 720 730 740 750
VLLKFGDRKL GKNDANRDKM ARVINHLEMN LAVHKRGGQL FKRLETEDIK
760
NTGDLLKLYK
Length:760
Mass (Da):86,087
Last modified:October 1, 1996 - v2
Checksum:i3FD169AD789ED60A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti758 – 7603LYK → AL in CAA61012 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87672 Genomic DNA. Translation: CAA61012.1.
Z72543 Genomic DNA. Translation: CAA96721.1.
BK006941 Genomic DNA. Translation: DAA08077.1.
PIRiS64023.
RefSeqiNP_011494.1. NM_001180886.1.

Genome annotation databases

EnsemblFungiiYGL021W; YGL021W; YGL021W.
GeneIDi852863.
KEGGisce:YGL021W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87672 Genomic DNA. Translation: CAA61012.1.
Z72543 Genomic DNA. Translation: CAA96721.1.
BK006941 Genomic DNA. Translation: DAA08077.1.
PIRiS64023.
RefSeqiNP_011494.1. NM_001180886.1.

3D structure databases

ProteinModelPortaliP43633.
SMRiP43633. Positions 507-633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33225. 15 interactions.
DIPiDIP-4816N.
IntActiP43633. 3 interactions.
MINTiMINT-527379.

PTM databases

iPTMnetiP43633.

Proteomic databases

MaxQBiP43633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL021W; YGL021W; YGL021W.
GeneIDi852863.
KEGGisce:YGL021W.

Organism-specific databases

EuPathDBiFungiDB:YGL021W.
SGDiS000002989. ALK1.

Phylogenomic databases

GeneTreeiENSGT00530000068001.
HOGENOMiHOG000033904.
InParanoidiP43633.
OMAiSSKKRWS.
OrthoDBiEOG7GFBG3.

Enzyme and pathway databases

BioCyciYEAST:G3O-30541-MONOMER.

Miscellaneous databases

PROiP43633.

Family and domain databases

InterProiIPR024604. GSG2_C.
IPR011009. Kinase-like_dom.
[Graphical view]
PfamiPF12330. DUF3635. 1 hit.
[Graphical view]
SMARTiSM01331. DUF3635. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-76 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiALK1_YEAST
AccessioniPrimary (citable) accession number: P43633
Secondary accession number(s): D6VUB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2190 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.