Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461ATPPROSITE-ProRule annotation
Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 319ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell surface receptor signaling pathway Source: ProtInc
  • mitotic nuclear division Source: UniProtKB-KW
  • peptidyl-serine phosphorylation Source: GO_Central
  • phagocytosis Source: GO_Central
  • positive regulation of canonical Wnt signaling pathway Source: Reactome
  • protein phosphorylation Source: UniProtKB
  • regulation of cell shape Source: GO_Central
  • 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

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_267753. Activation of SMO.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
SignaLinkiP48729.

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
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2451. CSNK1A1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • primary cilium Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26951.

Polymorphism and mutation databases

BioMutaiCSNK1A1.
DMDMi31077177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 337336Casein kinase I isoform alphaPRO_0000192822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei8 – 81N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP48729.
PaxDbiP48729.
PRIDEiP48729.

PTM databases

PhosphoSiteiP48729.

Expressioni

Gene expression databases

BgeeiP48729.
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.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107836. 80 interactions.
DIPiDIP-40367N.
IntActiP48729. 41 interactions.
MINTiMINT-193806.
STRINGi9606.ENSP00000421689.

Structurei

3D structure databases

ProteinModelPortaliP48729.
SMRiP48729. Positions 17-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 285269Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119040.
HOGENOMiHOG000182055.
HOVERGENiHBG000176.
InParanoidiP48729.
KOiK08957.
OMAiCKPPITE.
OrthoDBiEOG7CZK5W.
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]
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

Note: Contains a phosphoserine at position 156.1 Publication
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.

Note: Contains a phosphothreonine at position 321.1 Publication
Show »
Length:325
Mass (Da):37,567
Checksum:iB84DC84BDDC17854
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451V → L in CAA56710 (PubMed:8050587).Curated
Sequence conflicti74 – 741P → T in AAV38633 (Ref. 6) Curated
Sequence conflicti122 – 1221S → A AA sequence (PubMed:1409656).Curated
Sequence conflicti129 – 1291T → TK AA sequence (PubMed:1409656).Curated
Sequence conflicti231 – 2311Q → K in AAH08717 (PubMed:15489334).Curated
Sequence conflicti250 – 2501K → E in AAY84562 (Ref. 7) Curated
Sequence conflicti330 – 3301T → S in CAA56710 (PubMed:8050587).Curated
Sequence conflicti330 – 3301T → S in AAV38632 (Ref. 6) Curated
Sequence conflicti330 – 3301T → S in AAV38633 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti297 – 2971D → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_042073

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 1521K → KCLESPVGKRKRSMTVSTSQ DPSFSGLNQ in isoform 2. 1 PublicationVSP_035455
Alternative sequencei324 – 33512Missing in isoform 3. 2 PublicationsVSP_055131Add
BLAST

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.2. human. [P48729-2]
uc003lqx.2. human. [P48729-1]
uc003lqy.2. human.

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

ProteinModelPortaliP48729.
SMRiP48729. Positions 17-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107836. 80 interactions.
DIPiDIP-40367N.
IntActiP48729. 41 interactions.
MINTiMINT-193806.
STRINGi9606.ENSP00000421689.

Chemistry

BindingDBiP48729.
ChEMBLiCHEMBL3038493.
GuidetoPHARMACOLOGYi1995.

PTM databases

PhosphoSiteiP48729.

Polymorphism and mutation databases

BioMutaiCSNK1A1.
DMDMi31077177.

Proteomic databases

MaxQBiP48729.
PaxDbiP48729.
PRIDEiP48729.

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.2. human. [P48729-2]
uc003lqx.2. human. [P48729-1]
uc003lqy.2. human.

Organism-specific databases

CTDi1452.
GeneCardsiGC05M148854.
HGNCiHGNC:2451. CSNK1A1.
HPAiCAB016680.
HPA045614.
MIMi600505. gene.
neXtProtiNX_P48729.
PharmGKBiPA26951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119040.
HOGENOMiHOG000182055.
HOVERGENiHBG000176.
InParanoidiP48729.
KOiK08957.
OMAiCKPPITE.
OrthoDBiEOG7CZK5W.
PhylomeDBiP48729.
TreeFamiTF354246.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_267753. Activation of SMO.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
SignaLinkiP48729.

Miscellaneous databases

ChiTaRSiCSNK1A1. human.
GeneWikiiCasein_kinase_1,_alpha_1.
GenomeRNAii1452.
NextBioi5955.
PROiP48729.
SOURCEiSearch...

Gene expression databases

BgeeiP48729.
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]
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

« Hide 'large scale' publications
  1. "Cloning and chromosomal localization of the gene coding for human protein kinase CK1."
    Tapia C., Featherstone T., Gomez C., Taillon-Miller P., Allende C.C., Allende J.E.
    FEBS Lett. 349:307-312(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family."
    Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.
    J. Biol. Chem. 270:14875-14883(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Li H., Yang S.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  8. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  11. "Cell cycle-dependent localization of casein kinase I to mitotic spindles."
    Brockman J.L., Gross S.D., Sussman M.R., Anderson R.A.
    Proc. Natl. Acad. Sci. U.S.A. 89:9454-9458(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 65-83; 111-152 AND 179-204, FUNCTION, SUBCELLULAR LOCATION.
  12. "Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism."
    Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X., He X.
    Cell 108:837-847(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN WNT SIGNALING.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
    Gonzales M.L., Mellman D.L., Anderson R.A.
    J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUT1, SUBCELLULAR LOCATION.
  15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-297.

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: June 24, 2015
This is version 162 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

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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.