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Protein

Casein kinase II subunit alpha

Gene

ACK2

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATP
Active sitei151 – 1511Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATP

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 6752.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha (EC:2.7.11.1)
Alternative name(s):
CK II
CK2-alpha
Gene namesi
Name:ACK2
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Chromosome 2

Organism-specific databases

MaizeGDBi30032.

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Casein kinase II subunit alphaPRO_0000085901Add
BLAST

Proteomic databases

PaxDbiP28523.
PRIDEiP28523.

Expressioni

Gene expression databases

ExpressionAtlasiP28523. baseline.
GenevisibleiP28523. ZM.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains (possible).

Protein-protein interaction databases

IntActiP28523. 1 interaction.
STRINGi4577.GRMZM2G143602_P03.

Chemistry

BindingDBiP28523.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi10 – 134Combined sources
Helixi16 – 194Combined sources
Helixi21 – 233Combined sources
Helixi31 – 333Combined sources
Beta strandi34 – 4310Combined sources
Beta strandi46 – 538Combined sources
Turni54 – 574Combined sources
Beta strandi58 – 658Combined sources
Helixi70 – 8314Combined sources
Beta strandi92 – 976Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1096Combined sources
Helixi116 – 1194Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 14420Combined sources
Helixi154 – 1563Combined sources
Beta strandi157 – 1604Combined sources
Turni161 – 1644Combined sources
Beta strandi165 – 1684Combined sources
Helixi171 – 1733Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 1984Combined sources
Helixi207 – 22216Combined sources
Beta strandi225 – 2284Combined sources
Helixi233 – 24412Combined sources
Helixi246 – 25510Combined sources
Helixi262 – 2687Combined sources
Helixi276 – 2794Combined sources
Turni282 – 2843Combined sources
Helixi285 – 2873Combined sources
Helixi290 – 29910Combined sources
Helixi304 – 3063Combined sources
Helixi310 – 3156Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 3267Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DAWX-ray2.20A2-328[»]
1DAYX-ray2.20A2-328[»]
1DS5X-ray3.16A/B/C/D1-332[»]
1F0QX-ray2.63A1-332[»]
1J91X-ray2.22A/B1-332[»]
1JAMX-ray2.18A1-332[»]
1LP4X-ray1.86A1-332[»]
1LPUX-ray1.86A1-332[»]
1LR4X-ray2.00A1-332[»]
1M2PX-ray2.00A2-326[»]
1M2QX-ray1.79A2-328[»]
1M2RX-ray1.70A2-328[»]
1OM1X-ray1.68A1-332[»]
1ZOEX-ray1.77A1-332[»]
1ZOGX-ray2.30A1-332[»]
1ZOHX-ray1.81A1-332[»]
2OXDX-ray2.30A1-332[»]
2OXXX-ray2.30A1-332[»]
2OXYX-ray1.81A/B1-332[»]
2PVHX-ray2.20A1-332[»]
2PVJX-ray1.70A1-332[»]
2PVKX-ray1.90A1-332[»]
2PVLX-ray1.90A1-332[»]
2PVMX-ray2.00A1-332[»]
2PVNX-ray2.00A1-332[»]
2QC6X-ray1.85A1-332[»]
3BE9X-ray2.00A1-332[»]
3FL5X-ray2.30A1-332[»]
3KXGX-ray1.70A2-328[»]
3KXHX-ray1.70A2-328[»]
3KXMX-ray1.75A2-328[»]
3KXNX-ray2.00A2-328[»]
3PVGX-ray1.50A2-332[»]
3PWDX-ray2.20A1-332[»]
3PZHX-ray1.92A1-332[»]
4ANMX-ray1.70A2-332[»]
4DGMX-ray1.65A2-327[»]
4DGNX-ray1.75A2-327[»]
4DGOX-ray1.96A2-326[»]
4RLKX-ray1.24A1-332[»]
ProteinModelPortaliP28523.
SMRiP28523. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 319286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
HOGENOMiHOG000233021.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

P28523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKARVYADV NVLRPKEYWD YEALTVQWGE QDDYEVVRKV GRGKYSEVFE
60 70 80 90 100
GINVNNNEKC IIKILKPVKK KKIKREIKIL QNLCGGPNIV KLLDIVRDQH
110 120 130 140 150
SKTPSLIFEY VNNTDFKVLY PTLTDYDIRY YIYELLKALD YCHSQGIMHR
160 170 180 190 200
DVKPHNVMID HELRKLRLID WGLAEFYHPG KEYNVRVASR YFKGPELLVD
210 220 230 240 250
LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG HDNHDQLVKI AKVLGTDGLN
260 270 280 290 300
VYLNKYRIEL DPQLEALVGR HSRKPWLKFM NADNQHLVSP EAIDFLDKLL
310 320 330
RYDHQERLTA LEAMTHPYFQ QVRAAENSRT RA
Length:332
Mass (Da):39,230
Last modified:December 1, 1992 - v1
Checksum:i85513A5A5C77235A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61387 mRNA. Translation: CAA43659.1.
PIRiS19726.
RefSeqiXP_008668648.1. XM_008670426.1.
UniGeneiZm.569.

Genome annotation databases

EnsemblPlantsiGRMZM2G143602_T01; GRMZM2G143602_P01; GRMZM2G143602.
GeneIDi542637.
GrameneiGRMZM2G143602_T01; GRMZM2G143602_P01; GRMZM2G143602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61387 mRNA. Translation: CAA43659.1.
PIRiS19726.
RefSeqiXP_008668648.1. XM_008670426.1.
UniGeneiZm.569.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DAWX-ray2.20A2-328[»]
1DAYX-ray2.20A2-328[»]
1DS5X-ray3.16A/B/C/D1-332[»]
1F0QX-ray2.63A1-332[»]
1J91X-ray2.22A/B1-332[»]
1JAMX-ray2.18A1-332[»]
1LP4X-ray1.86A1-332[»]
1LPUX-ray1.86A1-332[»]
1LR4X-ray2.00A1-332[»]
1M2PX-ray2.00A2-326[»]
1M2QX-ray1.79A2-328[»]
1M2RX-ray1.70A2-328[»]
1OM1X-ray1.68A1-332[»]
1ZOEX-ray1.77A1-332[»]
1ZOGX-ray2.30A1-332[»]
1ZOHX-ray1.81A1-332[»]
2OXDX-ray2.30A1-332[»]
2OXXX-ray2.30A1-332[»]
2OXYX-ray1.81A/B1-332[»]
2PVHX-ray2.20A1-332[»]
2PVJX-ray1.70A1-332[»]
2PVKX-ray1.90A1-332[»]
2PVLX-ray1.90A1-332[»]
2PVMX-ray2.00A1-332[»]
2PVNX-ray2.00A1-332[»]
2QC6X-ray1.85A1-332[»]
3BE9X-ray2.00A1-332[»]
3FL5X-ray2.30A1-332[»]
3KXGX-ray1.70A2-328[»]
3KXHX-ray1.70A2-328[»]
3KXMX-ray1.75A2-328[»]
3KXNX-ray2.00A2-328[»]
3PVGX-ray1.50A2-332[»]
3PWDX-ray2.20A1-332[»]
3PZHX-ray1.92A1-332[»]
4ANMX-ray1.70A2-332[»]
4DGMX-ray1.65A2-327[»]
4DGNX-ray1.75A2-327[»]
4DGOX-ray1.96A2-326[»]
4RLKX-ray1.24A1-332[»]
ProteinModelPortaliP28523.
SMRiP28523. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28523. 1 interaction.
STRINGi4577.GRMZM2G143602_P03.

Chemistry

BindingDBiP28523.
ChEMBLiCHEMBL4514.

Proteomic databases

PaxDbiP28523.
PRIDEiP28523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGRMZM2G143602_T01; GRMZM2G143602_P01; GRMZM2G143602.
GeneIDi542637.
GrameneiGRMZM2G143602_T01; GRMZM2G143602_P01; GRMZM2G143602.

Organism-specific databases

MaizeGDBi30032.

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
HOGENOMiHOG000233021.

Enzyme and pathway databases

BRENDAi2.7.11.1. 6752.

Miscellaneous databases

EvolutionaryTraceiP28523.
PROiP28523.

Gene expression databases

ExpressionAtlasiP28523. baseline.
GenevisibleiP28523. ZM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of the casein kinase 2 alpha subunit from Zea mays."
    Dobrowolska G., Boldyreff B., Issinger O.-G.
    Biochim. Biophys. Acta 1129:139-140(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. B73 Inbred.
  2. "Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1-A resolution."
    Niefind K., Guerra B., Pinna L.A., Issinger O.G., Schomburg D.
    EMBO J. 17:2451-2462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiCSK2A_MAIZE
AccessioniPrimary (citable) accession number: P28523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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.