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 II subunit alpha

Gene

CSNK2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).7 Publications

Miscellaneous

Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has been found to be increased at protein level and up-regulated at the level of enzyme activity in the majority of cancers. However, elevated levels of casein kinase 2 are present in certain normal organs such as brain and testes.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei68ATPPROSITE-ProRule annotation1
Active sitei156Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi45 – 53ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • Hsp90 protein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • kinase activity Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • chaperone-mediated protein folding Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: CAFA
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of protein catabolic process Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of chromosome separation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Biological rhythms, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-1483191 Synthesis of PC
R-HSA-201688 WNT mediated activation of DVL
R-HSA-2514853 Condensation of Prometaphase Chromosomes
R-HSA-445144 Signal transduction by L1
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-8934903 Receptor Mediated Mitophagy
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8948751 Regulation of PTEN stability and activity
SignaLinkiP68400
SIGNORiP68400

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha (EC:2.7.11.1)
Short name:
CK II alpha
Gene namesi
Name:CSNK2A1
Synonyms:CK2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000101266.16
HGNCiHGNC:2457 CSNK2A1
MIMi115440 gene
neXtProtiNX_P68400

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Okur-Chung neurodevelopmental syndrome (OCNDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by developmental delay, intellectual disability, behavioral problems, hypotonia, speech problems, microcephaly, pachygyria and variable dysmorphic features.
See also OMIM:617062
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07704547R → Q in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312845EnsemblClinVar.1
Natural variantiVAR_07704650Y → S in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312849EnsemblClinVar.1
Natural variantiVAR_077047175D → G in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312848EnsemblClinVar.1
Natural variantiVAR_077048198K → R in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312840EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi1457
MalaCardsiCSNK2A1
MIMi617062 phenotype
OpenTargetsiENSG00000101266
PharmGKBiPA26957

Chemistry databases

ChEMBLiCHEMBL3629
DrugBankiDB03127 Benzamidine
DB08846 Ellagic Acid
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB02709 Resveratrol
DB04462 Tetrabromo-2-Benzotriazole
GuidetoPHARMACOLOGYi1549

Polymorphism and mutation databases

BioMutaiCSNK2A1
DMDMi55977123

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858831 – 391Casein kinase II subunit alphaAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei344Phosphothreonine; by CDK11 Publication1
Modified residuei360Phosphothreonine; by CDK11 Publication1
Modified residuei362Phosphoserine; by CDK11 Publication1
Modified residuei370Phosphoserine; by CDK1Combined sources1 Publication1

Post-translational modificationi

Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP68400
MaxQBiP68400
PaxDbiP68400
PeptideAtlasiP68400
PRIDEiP68400

PTM databases

iPTMnetiP68400
PhosphoSitePlusiP68400
SwissPalmiP68400

Miscellaneous databases

PMAP-CutDBB4DYS6

Expressioni

Tissue specificityi

Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000101266
CleanExiHS_CSNK2A1
ExpressionAtlasiP68400 baseline and differential
GenevisibleiP68400 HS

Organism-specific databases

HPAiCAB020680
CAB069395
HPA059206

Interactioni

Subunit structurei

Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1. Interacts with SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2.9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • Hsp90 protein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107841, 469 interactors
CORUMiP68400
DIPiDIP-32682N
IntActiP68400, 285 interactors
MINTiP68400
STRINGi9606.ENSP00000217244

Chemistry databases

BindingDBiP68400

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Turni13 – 18Combined sources6
Helixi21 – 24Combined sources4
Helixi26 – 28Combined sources3
Helixi36 – 38Combined sources3
Beta strandi39 – 47Combined sources9
Beta strandi49 – 58Combined sources10
Turni59 – 61Combined sources3
Beta strandi64 – 70Combined sources7
Turni72 – 74Combined sources3
Helixi75 – 88Combined sources14
Beta strandi97 – 102Combined sources6
Turni104 – 106Combined sources3
Beta strandi107 – 114Combined sources8
Turni118 – 120Combined sources3
Helixi121 – 124Combined sources4
Helixi125 – 127Combined sources3
Helixi130 – 149Combined sources20
Helixi159 – 161Combined sources3
Beta strandi162 – 165Combined sources4
Helixi166 – 168Combined sources3
Beta strandi170 – 173Combined sources4
Helixi176 – 178Combined sources3
Helixi195 – 197Combined sources3
Helixi200 – 203Combined sources4
Helixi212 – 227Combined sources16
Beta strandi230 – 233Combined sources4
Helixi238 – 249Combined sources12
Helixi251 – 261Combined sources11
Helixi267 – 269Combined sources3
Turni270 – 272Combined sources3
Helixi281 – 284Combined sources4
Turni287 – 289Combined sources3
Helixi290 – 292Combined sources3
Helixi295 – 304Combined sources10
Helixi309 – 311Combined sources3
Helixi315 – 318Combined sources4
Helixi322 – 324Combined sources3
Helixi325 – 331Combined sources7
Beta strandi333 – 335Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JWHX-ray3.10A/B1-337[»]
1NA7X-ray2.40A1-329[»]
1PJKX-ray2.50A2-335[»]
2PVRX-ray1.60A2-335[»]
2ZJWX-ray2.40A1-335[»]
3AMYX-ray2.30A1-335[»]
3AT2X-ray1.60A1-335[»]
3AT3X-ray2.60A1-335[»]
3AT4X-ray2.20A1-335[»]
3AXWX-ray2.50A1-335[»]
3BQCX-ray1.50A1-335[»]
3C13X-ray1.95A1-335[»]
3FWQX-ray2.30A/B1-335[»]
3H30X-ray1.56A/B1-334[»]
3JUHX-ray1.66A/B1-335[»]
3MB6X-ray1.75A1-331[»]
3MB7X-ray1.65A1-331[»]
3NGAX-ray2.71A/B1-333[»]
3NSZX-ray1.30A2-331[»]
3OWJX-ray1.85A1-331[»]
3OWKX-ray1.80A1-331[»]
3OWLX-ray2.10A1-331[»]
3PE1X-ray1.60A1-337[»]
3PE2X-ray1.90A1-337[»]
3PE4X-ray1.95B/D340-352[»]
3Q04X-ray1.80A3-330[»]
3Q9WX-ray1.70A1-336[»]
3Q9XX-ray2.20A/B1-336[»]
3Q9YX-ray1.80A1-336[»]
3Q9ZX-ray2.20A/B1-336[»]
3QA0X-ray2.50A/B1-336[»]
3R0TX-ray1.75A1-337[»]
3RPSX-ray2.30A/B1-335[»]
3TAXX-ray1.88B/D340-352[»]
3U4UX-ray2.20A1-333[»]
3U87X-ray2.90A/B1-325[»]
3U9CX-ray3.20A/B1-335[»]
3W8LX-ray2.40A/B1-335[»]
3WARX-ray1.04A1-335[»]
3WIKX-ray2.00A1-335[»]
3WILX-ray2.90A1-335[»]
3WOWX-ray2.50A1-335[»]
4DGLX-ray3.00C/D1-335[»]
4FBXX-ray2.33A1-335[»]
4GRBX-ray2.15A1-333[»]
4GUBX-ray2.20A1-333[»]
4GYWX-ray1.70B/D340-352[»]
4GYYX-ray1.85B/D340-352[»]
4GZ3X-ray1.90B/D340-352[»]
4IB5X-ray2.20A/B/C1-335[»]
4KWPX-ray1.25A1-336[»]
4MD7X-ray3.10E/F/G/H1-391[»]
4MD8X-ray3.30E/F/G/H1-391[»]
4MD9X-ray3.50E/F/G/H/K/L/M/P1-336[»]
4NH1X-ray3.30A/B1-335[»]
4RLLX-ray1.85A1-335[»]
4UB7X-ray2.10A1-335[»]
4UBAX-ray3.00A/B1-335[»]
5B0XX-ray2.30A1-335[»]
5CLPX-ray1.68A/B2-329[»]
5CQUX-ray2.35A1-335[»]
5CQWX-ray2.65A/B1-335[»]
5CS6X-ray1.88A/B2-329[»]
5CSHX-ray1.59A/B2-329[»]
5CSPX-ray1.50A2-329[»]
5CSVX-ray1.38A2-329[»]
5CT0X-ray2.01A/B2-329[»]
5CTPX-ray2.03A/B2-329[»]
5CU0X-ray2.18A/B2-329[»]
5CU2X-ray1.71A/B2-329[»]
5CU3X-ray1.79A/B2-329[»]
5CU4X-ray1.56A2-329[»]
5CU6X-ray1.36A2-329[»]
5CVFX-ray1.63A2-329[»]
5CVGX-ray1.25A2-329[»]
5CVHX-ray1.85A/B2-329[»]
5CX9X-ray1.73A/B2-329[»]
5H8BX-ray2.55A/B1-333[»]
5H8EX-ray2.15A/B1-333[»]
5H8GX-ray2.00A1-333[»]
5HGVX-ray2.05B/D340-352[»]
5KU8X-ray2.22A/B2-332[»]
5KWHX-ray2.12A/B1-333[»]
5M44X-ray2.71A1-335[»]
5M4CX-ray1.94A1-335[»]
5M4FX-ray1.52A1-335[»]
5M4IX-ray2.22A1-335[»]
5MMFX-ray1.99A/B2-329[»]
5MMRX-ray2.00A/B2-329[»]
5MO5X-ray2.04A/B2-329[»]
5MO6X-ray1.82A/B2-329[»]
5MO7X-ray2.15A/B2-329[»]
5MO8X-ray1.82A/B2-329[»]
5MODX-ray2.08A/B2-329[»]
5MOEX-ray1.89A/B2-329[»]
5MOHX-ray1.38A2-329[»]
5MOTX-ray2.09A2-329[»]
5MOVX-ray2.20A3-327[»]
5MOWX-ray1.86A/B2-329[»]
5MP8X-ray1.92A/B2-329[»]
5MPJX-ray2.14A/B2-329[»]
5N1VX-ray2.52A/B1-336[»]
5N9KX-ray1.64A1-335[»]
5N9LX-ray1.79A1-335[»]
5N9NX-ray1.84A1-335[»]
5NQCX-ray2.00A2-335[»]
5OMYX-ray1.95A1-391[»]
5ONIX-ray2.00A/B1-391[»]
5OQUX-ray2.32A/B2-329[»]
5ORHX-ray1.75A/B2-329[»]
5ORJX-ray1.99A/B2-329[»]
5ORKX-ray2.14A/B2-329[»]
5OS7X-ray1.66A/B2-329[»]
5OS8X-ray1.55A2-329[»]
5OSLX-ray1.95A2-329[»]
5OSZX-ray2.00A2-329[»]
5OT5X-ray1.63A/B2-329[»]
5OT6X-ray1.94A/B2-329[»]
5OTDX-ray1.57A/B2-329[»]
5OTHX-ray1.69A/B2-329[»]
5OTIX-ray1.59A2-329[»]
5OTLX-ray1.57A/B2-329[»]
5OTOX-ray1.51A/B2-329[»]
5OTQX-ray1.38A2-329[»]
5OTRX-ray1.52A2-329[»]
5OTYX-ray1.48A2-329[»]
5OTZX-ray1.46A2-329[»]
5OUEX-ray2.01A/B2-329[»]
5OULX-ray1.34A2-329[»]
5OUMX-ray2.05A/B2-329[»]
5OUUX-ray1.81A/B2-329[»]
5OYFX-ray1.54A2-329[»]
5T1HX-ray2.11A/B1-333[»]
5VIEX-ray2.60B/D339-352[»]
5VIFX-ray2.25B339-352[»]
6EHKX-ray1.40A2-329[»]
6EHUX-ray1.95A/B2-329[»]
6EIIX-ray1.94A/B2-329[»]
ProteinModelPortaliP68400
SMRiP68400
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68400

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 324Protein kinasePROSITE-ProRule annotationAdd BLAST286

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 41Interaction with beta subunitBy similarity6

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0668 Eukaryota
ENOG410XNPP LUCA
GeneTreeiENSGT00390000004215
HOGENOMiHOG000233021
HOVERGENiHBG107282
InParanoidiP68400
KOiK03097
OMAiNNTDFRS
PhylomeDBiP68400
TreeFamiTF300483

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68400-1) [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
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY
60 70 80 90 100
SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI
110 120 130 140 150
VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM
160 170 180 190 200
GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP
210 220 230 240 250
ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG
260 270 280 290 300
TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
310 320 330 340 350
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN
360 370 380 390
MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q
Length:391
Mass (Da):45,144
Last modified:November 23, 2004 - v1
Checksum:iD3B6F5D13FF7422D
GO
Isoform 2 (identifier: P68400-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.

Show »
Length:255
Mass (Da):29,181
Checksum:iABCEE52F34E7431B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128L → F in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti256D → G in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti287S → R in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti351M → V in CAA49758 (PubMed:8420794).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07704547R → Q in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312845EnsemblClinVar.1
Natural variantiVAR_07704650Y → S in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312849EnsemblClinVar.1
Natural variantiVAR_077047175D → G in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312848EnsemblClinVar.1
Natural variantiVAR_077048198K → R in OCNDS. 1 PublicationCorresponds to variant dbSNP:rs869312840EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0419251 – 136Missing in isoform 2. 1 PublicationAdd BLAST136

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02853 mRNA Translation: AAA56821.1
M55265 mRNA Translation: AAA35503.1
S53149 mRNA Translation: ABB72474.1
X70251 Genomic DNA Translation: CAA49758.1
AK302583 mRNA Translation: BAG63838.1
BT019792 mRNA Translation: AAV38595.1
AB451279 mRNA Translation: BAG70093.1
AL049761 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10665.1
CH471133 Genomic DNA Translation: EAX10666.1
CH471133 Genomic DNA Translation: EAX10667.1
CH471133 Genomic DNA Translation: EAX10668.1
CH471133 Genomic DNA Translation: EAX10669.1
BC011668 mRNA Translation: AAH11668.1
BC053532 mRNA Translation: AAH53532.1
BC071167 mRNA Translation: AAH71167.1
CCDSiCCDS13003.1 [P68400-1]
CCDS13004.1 [P68400-2]
PIRiA30319
RefSeqiNP_001886.1, NM_001895.3 [P68400-1]
NP_808227.1, NM_177559.2 [P68400-1]
NP_808228.1, NM_177560.2 [P68400-2]
UniGeneiHs.644056
Hs.654675
Hs.741126

Genome annotation databases

EnsembliENST00000217244; ENSP00000217244; ENSG00000101266 [P68400-1]
ENST00000349736; ENSP00000339247; ENSG00000101266 [P68400-1]
ENST00000400217; ENSP00000383076; ENSG00000101266 [P68400-2]
GeneIDi1457
KEGGihsa:1457
UCSCiuc002wdw.2 human [P68400-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCSK21_HUMAN
AccessioniPrimary (citable) accession number: P68400
Secondary accession number(s): B4DYS6
, D3DVV8, P19138, P20426, Q14013, Q5U065
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: May 23, 2018
This is version 165 of the entry and version 1 of the sequence. See 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, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health