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Protein

Casein kinase I isoform alpha

Gene

CSNK1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis (PubMed:11955436, PubMed:1409656, PubMed:18305108). May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (PubMed:23902688).4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi23 – 31ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • beta-catenin destruction complex assembly Source: Reactome
  • beta-catenin destruction complex disassembly Source: Reactome
  • cell division Source: UniProtKB-KW
  • cell morphogenesis Source: Ensembl
  • cell surface receptor signaling pathway Source: ProtInc
  • Golgi organization Source: ParkinsonsUK-UCL
  • intermediate filament cytoskeleton organization Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • phagocytosis Source: GO_Central
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Reactome
  • protein phosphorylation Source: UniProtKB
  • regulation of cell shape Source: GO_Central
  • regulation of GTP binding Source: ParkinsonsUK-UCL
  • signal transduction Source: ProtInc
  • Wnt signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS03709-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5635838. Activation of SMO.
SignaLinkiP48729.
SIGNORiP48729.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase I isoform alpha (EC:2.7.11.1)
Short name:
CKI-alpha
Alternative name(s):
CK1
Gene namesi
Name:CSNK1A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2451. CSNK1A1.

Subcellular locationi

GO - Cellular componenti

  • beta-catenin destruction complex Source: ParkinsonsUK-UCL
  • centrosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: Ensembl
  • membrane Source: UniProtKB
  • nuclear speck Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1452.
OpenTargetsiENSG00000113712.
PharmGKBiPA26951.

Chemistry databases

ChEMBLiCHEMBL2793.
GuidetoPHARMACOLOGYi1995.

Polymorphism and mutation databases

BioMutaiCSNK1A1.
DMDMi31077177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001928222 – 337Casein kinase I isoform alphaAdd BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei4PhosphoserineCombined sources1
Modified residuei8N6-acetyllysineCombined sources1
Isoform 2 (identifier: P48729-2)
Modified residuei156PhosphoserineCombined sources1
Isoform 3 (identifier: P48729-3)
Modified residuei321PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP48729.
MaxQBiP48729.
PeptideAtlasiP48729.
PRIDEiP48729.
TopDownProteomicsiP48729-1. [P48729-1]

PTM databases

iPTMnetiP48729.
PhosphoSitePlusiP48729.
SwissPalmiP48729.

Expressioni

Gene expression databases

BgeeiENSG00000113712.
CleanExiHS_CSNK1A1.
ExpressionAtlasiP48729. baseline and differential.
GenevisibleiP48729. HS.

Organism-specific databases

HPAiCAB016680.
HPA045614.

Interactioni

Subunit structurei

Monomer. Interacts with the Axin complex. Interacts with TUT1, leading to TUT1 phosphorylation. Interacts with FAM83H; recruits CSNK1A1 to keratin filaments (PubMed:23902688).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-10106282,EBI-5323863
MDM2Q009873EBI-2040168,EBI-389668
MDM4O151512EBI-1383726,EBI-398437
RIPK1Q135465EBI-1383726,EBI-358507

Protein-protein interaction databases

BioGridi107836. 106 interactors.
DIPiDIP-40367N.
IntActiP48729. 59 interactors.
MINTiMINT-193806.

Chemistry databases

BindingDBiP48729.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni14 – 16Combined sources3
Beta strandi17 – 24Combined sources8
Beta strandi27 – 36Combined sources10
Turni37 – 39Combined sources3
Beta strandi42 – 49Combined sources8
Helixi57 – 67Combined sources11
Beta strandi76 – 82Combined sources7
Beta strandi85 – 91Combined sources7
Helixi97 – 103Combined sources7
Helixi110 – 129Combined sources20
Helixi139 – 141Combined sources3
Beta strandi142 – 144Combined sources3
Helixi147 – 149Combined sources3
Beta strandi153 – 155Combined sources3
Turni167 – 169Combined sources3
Turni185 – 187Combined sources3
Helixi190 – 193Combined sources4
Helixi200 – 215Combined sources16
Beta strandi216 – 218Combined sources3
Turni220 – 223Combined sources4
Helixi229 – 242Combined sources14
Helixi245 – 248Combined sources4
Turni249 – 251Combined sources3
Helixi254 – 264Combined sources11
Helixi274 – 287Combined sources14
Helixi297 – 301Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FQDX-ray2.45C/F1-337[»]
ProteinModelPortaliP48729.
SMRiP48729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 285Protein kinasePROSITE-ProRule annotationAdd BLAST269

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119040.
HOGENOMiHOG000182055.
HOVERGENiHBG000176.
InParanoidiP48729.
KOiK08957.
OMAiHIGYRED.
OrthoDBiEOG091G0AFG.
PhylomeDBiP48729.
TreeFamiTF354246.

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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48729-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ
60 70 80 90 100
KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL
110 120 130 140 150
FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC
160 170 180 190 200
NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR
210 220 230 240 250
RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK
260 270 280 290 300
GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM
310 320 330
LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF
Length:337
Mass (Da):38,915
Last modified:May 23, 2003 - v2
Checksum:i1B2085AE33CAFAC2
GO
Isoform 2 (identifier: P48729-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: K → KCLESPVGKRKRSMTVSTSQDPSFSGLNQ

Show »
Length:365
Mass (Da):41,937
Checksum:i11756FB15947D9F5
GO
Isoform 3 (identifier: P48729-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-335: Missing.

Show »
Length:325
Mass (Da):37,567
Checksum:iB84DC84BDDC17854
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45V → L in CAA56710 (PubMed:8050587).Curated1
Sequence conflicti74P → T in AAV38633 (Ref. 6) Curated1
Sequence conflicti122S → A AA sequence (PubMed:1409656).Curated1
Sequence conflicti129T → TK AA sequence (PubMed:1409656).Curated1
Sequence conflicti231Q → K in AAH08717 (PubMed:15489334).Curated1
Sequence conflicti250K → E in AAY84562 (Ref. 7) Curated1
Sequence conflicti330T → S in CAA56710 (PubMed:8050587).Curated1
Sequence conflicti330T → S in AAV38632 (Ref. 6) Curated1
Sequence conflicti330T → S in AAV38633 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042073297D → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035455152K → KCLESPVGKRKRSMTVSTSQ DPSFSGLNQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_055131324 – 335Missing in isoform 3. 2 PublicationsAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80693 mRNA. Translation: CAA56710.1.
L37042 mRNA. Translation: AAC41760.1.
AF218004 mRNA. Translation: AAG17246.1.
AK294942 mRNA. Translation: BAG58018.1.
CR542206 mRNA. Translation: CAG47002.1.
BT019829 mRNA. Translation: AAV38632.1.
BT019830 mRNA. Translation: AAV38633.1.
DQ082865 mRNA. Translation: AAY84562.1.
AC021078 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61767.1.
CH471062 Genomic DNA. Translation: EAW61769.1.
CH471062 Genomic DNA. Translation: EAW61773.1.
CH471062 Genomic DNA. Translation: EAW61774.1.
CH471062 Genomic DNA. Translation: EAW61776.1.
BC008717 mRNA. Translation: AAH08717.1.
CCDSiCCDS47303.1. [P48729-1]
CCDS47304.1. [P48729-2]
CCDS64291.1. [P48729-3]
PIRiA57011.
S46254.
RefSeqiNP_001020276.1. NM_001025105.2. [P48729-2]
NP_001258670.1. NM_001271741.1. [P48729-3]
NP_001258671.1. NM_001271742.1.
NP_001883.4. NM_001892.5. [P48729-1]
UniGeneiHs.529862.
Hs.712555.

Genome annotation databases

EnsembliENST00000261798; ENSP00000261798; ENSG00000113712. [P48729-3]
ENST00000377843; ENSP00000367074; ENSG00000113712. [P48729-1]
ENST00000515768; ENSP00000421689; ENSG00000113712. [P48729-2]
GeneIDi1452.
KEGGihsa:1452.
UCSCiuc003lqw.3. human. [P48729-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80693 mRNA. Translation: CAA56710.1.
L37042 mRNA. Translation: AAC41760.1.
AF218004 mRNA. Translation: AAG17246.1.
AK294942 mRNA. Translation: BAG58018.1.
CR542206 mRNA. Translation: CAG47002.1.
BT019829 mRNA. Translation: AAV38632.1.
BT019830 mRNA. Translation: AAV38633.1.
DQ082865 mRNA. Translation: AAY84562.1.
AC021078 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61767.1.
CH471062 Genomic DNA. Translation: EAW61769.1.
CH471062 Genomic DNA. Translation: EAW61773.1.
CH471062 Genomic DNA. Translation: EAW61774.1.
CH471062 Genomic DNA. Translation: EAW61776.1.
BC008717 mRNA. Translation: AAH08717.1.
CCDSiCCDS47303.1. [P48729-1]
CCDS47304.1. [P48729-2]
CCDS64291.1. [P48729-3]
PIRiA57011.
S46254.
RefSeqiNP_001020276.1. NM_001025105.2. [P48729-2]
NP_001258670.1. NM_001271741.1. [P48729-3]
NP_001258671.1. NM_001271742.1.
NP_001883.4. NM_001892.5. [P48729-1]
UniGeneiHs.529862.
Hs.712555.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FQDX-ray2.45C/F1-337[»]
ProteinModelPortaliP48729.
SMRiP48729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107836. 106 interactors.
DIPiDIP-40367N.
IntActiP48729. 59 interactors.
MINTiMINT-193806.

Chemistry databases

BindingDBiP48729.
ChEMBLiCHEMBL2793.
GuidetoPHARMACOLOGYi1995.

PTM databases

iPTMnetiP48729.
PhosphoSitePlusiP48729.
SwissPalmiP48729.

Polymorphism and mutation databases

BioMutaiCSNK1A1.
DMDMi31077177.

Proteomic databases

EPDiP48729.
MaxQBiP48729.
PeptideAtlasiP48729.
PRIDEiP48729.
TopDownProteomicsiP48729-1. [P48729-1]

Protocols and materials databases

DNASUi1452.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261798; ENSP00000261798; ENSG00000113712. [P48729-3]
ENST00000377843; ENSP00000367074; ENSG00000113712. [P48729-1]
ENST00000515768; ENSP00000421689; ENSG00000113712. [P48729-2]
GeneIDi1452.
KEGGihsa:1452.
UCSCiuc003lqw.3. human. [P48729-1]

Organism-specific databases

CTDi1452.
DisGeNETi1452.
GeneCardsiCSNK1A1.
HGNCiHGNC:2451. CSNK1A1.
HPAiCAB016680.
HPA045614.
MIMi600505. gene.
neXtProtiNX_P48729.
OpenTargetsiENSG00000113712.
PharmGKBiPA26951.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119040.
HOGENOMiHOG000182055.
HOVERGENiHBG000176.
InParanoidiP48729.
KOiK08957.
OMAiHIGYRED.
OrthoDBiEOG091G0AFG.
PhylomeDBiP48729.
TreeFamiTF354246.

Enzyme and pathway databases

BioCyciZFISH:HS03709-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5635838. Activation of SMO.
SignaLinkiP48729.
SIGNORiP48729.

Miscellaneous databases

ChiTaRSiCSNK1A1. human.
GeneWikiiCasein_kinase_1,_alpha_1.
GenomeRNAii1452.
PROiP48729.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113712.
CleanExiHS_CSNK1A1.
ExpressionAtlasiP48729. baseline and differential.
GenevisibleiP48729. HS.

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...

Entry informationi

Entry nameiKC1A_HUMAN
AccessioniPrimary (citable) accession number: P48729
Secondary accession number(s): D3DQG0
, D3DQG1, Q4JJA0, Q5U046, Q5U047, Q6FGA2, Q71TU5, Q96HD2, Q9UDK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 23, 2003
Last modified: November 30, 2016
This is version 178 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.