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UniProtKB - P06493 (CDK1_HUMAN)

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Protein

Cyclin-dependent kinase 1

Gene

CDK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (PubMed:26549230).16 Publications
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry.1 Publication

Miscellaneous

As a key regulator of the cell cycle, CDK1 is a potent therapeutic target for inhibitors in cancer treatment.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it. Activated through a multistep process; binding to cyclin-B is required for relocation of cyclin-kinase complexes to the nucleus, activated by CAK/CDK7-mediated phosphorylation on Thr-161, and CDC25-mediated dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15. Inhibited by flavopiridol and derivatives, pyrimidine derivatives, pyridine derivatives, purine derivatives, staurosporine, paullones, oxoindoles, indazole analogs, indolin-2-ones, pyrazolo[3,4-b]pyridines, imidazo[1,2-a]pyridine (AZ703), thiazolinone analogs(RO-3306), thiazol urea, macrocyclic quinoxalin-2-one, pyrrolo[2,3-a]carbazole, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib, SCH 727965), 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine), olomoucine, AG-024322, AT-7519, P276-00, R547/Ro-4584820 and SNS-032/BMS-387032. Repressed by the CDK inhibitors CDKN1A/p21 and CDKN1B/p27 during the G1 phase and by CDKN1A/p21 at the G1-S checkpoint upon DNA damage. Transient activation by rapid and transient dephosphorylation at Tyr-15 triggered by TGFB1.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33ATPPROSITE-ProRule annotation1
Active sitei128Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 18ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: Ensembl
  • cyclin binding Source: MGI
  • cyclin-dependent protein kinase activity Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • histone kinase activity Source: UniProtKB
  • Hsp70 protein binding Source: Ensembl
  • protein kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB
  • RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionHost cell receptor for virus entry, Kinase, Receptor, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiR-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-113507. E2F-enabled inhibition of pre-replication complex formation.
R-HSA-1362300. Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
R-HSA-157881. Cyclin B2 mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-170145. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-380284. Loss of proteins required for interphase microtubule organization from the centrosome.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-539107. Activation of E2F1 target genes at G1/S.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69478. G2/M DNA replication checkpoint.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
SignaLinkiP06493.
SIGNORiP06493.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDK1
Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase
Gene namesi
Name:CDK1
Synonyms:CDC2, CDC28A, CDKN1, P34CDC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1722. CDK1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cyclin B1-CDK1 complex Source: CAFA
  • cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  • cytosol Source: HPA
  • endoplasmic reticulum membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • mitochondrial matrix Source: Ensembl
  • mitochondrion Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4Y → D or E: Constitutive polyubiquitination. 1 Publication1
Mutagenesisi14 – 15TY → AF: Abnormal cell cycle exhibiting only M-phase without completing either karyokinesis or cytokinesis. 1 Publication2

Organism-specific databases

DisGeNETi983.
OpenTargetsiENSG00000170312.
PharmGKBiPA99.

Chemistry databases

ChEMBLiCHEMBL308.
DrugBankiDB04014. Alsterpaullone.
DB05037. AT7519.
DB03496. Flavopiridol.
DB02950. Hymenialdisine.
DB02052. Indirubin-3'-Monoxime.
DB02116. Olomoucine.
DB03428. SU9516.
GuidetoPHARMACOLOGYi1961.

Polymorphism and mutation databases

BioMutaiCDK1.
DMDMi334302921.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000857241 – 297Cyclin-dependent kinase 1Add BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei4Phosphotyrosine; by PKR1 Publication1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei14Phosphothreonine; by PKMYT1Combined sources1 Publication1
Modified residuei15Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCDCombined sources2 Publications1
Modified residuei19PhosphotyrosineCombined sources1
Modified residuei39PhosphoserineCombined sources1
Modified residuei77PhosphotyrosineCombined sources1
Modified residuei141PhosphothreonineCombined sources1
Modified residuei161Phosphothreonine; by CAKCombined sources1 Publication1
Modified residuei178PhosphoserineCombined sources1
Modified residuei222PhosphothreonineCombined sources1
Modified residuei245N6-succinyllysineBy similarity1
Modified residuei248PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity. Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis (G2 to M transition). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2. By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated. Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry. Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation. Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress. This phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest. In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint.5 Publications
Polyubiquitinated upon genotoxic stress.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06493.
MaxQBiP06493.
PaxDbiP06493.
PeptideAtlasiP06493.
PRIDEiP06493.

2D gel databases

SWISS-2DPAGEiP06493.

PTM databases

iPTMnetiP06493.
PhosphoSitePlusiP06493.
SwissPalmiP06493.

Expressioni

Tissue specificityi

Isoform 2 is found in breast cancer tissues.

Inductioni

Follows a cyclic expression; during interphase, accumulates gradually following G1, S to reach a critical threshold at the end of G2, which promotes self-activation and triggers onset of mitosis. Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis, but later repressed. Triggered by CKS1B during mitotic entry in breast cancer cells. Down-regulated under genotoxic stresses triggered by PKR/EIF2AK2-mediated phosphorylation.2 Publications

Gene expression databases

BgeeiENSG00000170312.
CleanExiHS_CDC2.
ExpressionAtlasiP06493. baseline and differential.
GenevisibleiP06493. HS.

Organism-specific databases

HPAiCAB003799.
HPA003387.

Interactioni

Subunit structurei

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with cyclins-B (CCNB1, CCNB2 and CCNB3) to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Can also form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate RB1 in vitro. Binds to RB1 and other transcription factors such as FOXO1 and RUNX2. Promotes G2-M transition when in complex with a cyclin-B. Interacts with DLGAP5. Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Isoform 2 is unable to complex with cyclin-B1 and also fails to bind to CDKN1A/p21. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase. Associates with cyclins-A and B1 during S-phase in regenerating hepatocytes. Interacts with FANCC. Interacts with CEP63; this interaction recruits CDK1 to centrosomes. Interacts with CENPA (PubMed:25556658).7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cyclin binding Source: MGI
  • Hsp70 protein binding Source: Ensembl
Complete GO annotation...

Protein-protein interaction databases

BioGridi107420. 217 interactors.
DIPiDIP-35N.
IntActiP06493. 95 interactors.
MINTiMINT-5000894.
STRINGi9606.ENSP00000378699.

Chemistry databases

BindingDBiP06493.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 3Combined sources3
Beta strandi4 – 12Combined sources9
Beta strandi17 – 23Combined sources7
Turni24 – 26Combined sources3
Beta strandi29 – 34Combined sources6
Helixi40 – 42Combined sources3
Helixi46 – 57Combined sources12
Beta strandi66 – 72Combined sources7
Beta strandi75 – 81Combined sources7
Beta strandi84 – 86Combined sources3
Helixi87 – 92Combined sources6
Helixi102 – 120Combined sources19
Turni121 – 123Combined sources3
Helixi131 – 133Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi142 – 144Combined sources3
Helixi149 – 152Combined sources4
Beta strandi155 – 157Combined sources3
Turni161 – 163Combined sources3
Helixi166 – 169Combined sources4
Helixi172 – 175Combined sources4
Beta strandi179 – 181Combined sources3
Helixi184 – 199Combined sources16
Helixi209 – 220Combined sources12
Turni225 – 227Combined sources3
Helixi231 – 233Combined sources3
Helixi249 – 251Combined sources3
Helixi258 – 267Combined sources10
Turni272 – 274Combined sources3
Helixi278 – 281Combined sources4
Helixi285 – 288Combined sources4
Helixi292 – 295Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LC9model-A1-297[»]
4Y72X-ray2.30A1-297[»]
4YC3X-ray2.70A1-297[»]
4YC6X-ray2.60A/C/E/G1-297[»]
5HQ0X-ray2.30A1-297[»]
5LQFX-ray2.06A/D1-297[»]
ProteinModelPortaliP06493.
SMRiP06493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 287Protein kinasePROSITE-ProRule annotationAdd BLAST284

Sequence similaritiesi

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.Curated

Phylogenomic databases

eggNOGiKOG0594. Eukaryota.
ENOG410XPP3. LUCA.
GeneTreeiENSGT00830000128256.
HOVERGENiHBG014652.
InParanoidiP06493.
KOiK02087.
OMAiEMMLVYD.
PhylomeDBiP06493.
TreeFamiTF101021.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
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: P06493-1) [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
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR 
        60         70         80         90        100
EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM 
       110        120        130        140        150
DSSLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA 
       160        170        180        190        200
RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK 
       210        220        230        240        250
KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA 
       260        270        280        290 
SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM
Length:297
Mass (Da):34,095
Last modified:May 31, 2011 - v3
Checksum:i942D79448EFE490A
GO
Isoform 2 (identifier: P06493-2) [UniParc]FASTAAdd to basket
Also known as: CDC2deltaT

The sequence of this isoform differs from the canonical sequence as follows:
     107-163: Missing.

Show »
Length:240
Mass (Da):27,503
Checksum:i50FC3D192024E38C
GO

Sequence cautioni

The sequence EAW54204 differs from that shown. Reason: Erroneous gene model prediction.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_021375107 – 163Missing in isoform 2. 1 PublicationAdd BLAST57

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05360 mRNA. Translation: CAA28963.1.
Y00272 mRNA. Translation: CAA68376.1.
D88357 mRNA. Translation: BAA26001.1.
AK291939 mRNA. Translation: BAF84628.1.
BT007004 mRNA. Translation: AAP35650.1.
AF512554 Genomic DNA. Translation: AAM34793.1.
AC022390 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54204.1. Sequence problems.
BC014563 mRNA. Translation: AAH14563.1.
CCDSiCCDS44408.1. [P06493-1]
CCDS7260.1. [P06493-2]
PIRiA29539.
RefSeqiNP_001307847.1. NM_001320918.1. [P06493-1]
NP_001777.1. NM_001786.4. [P06493-1]
NP_203698.1. NM_033379.4. [P06493-2]
XP_005270360.1. XM_005270303.3. [P06493-1]
UniGeneiHs.732435.

Genome annotation databases

EnsembliENST00000316629; ENSP00000325970; ENSG00000170312. [P06493-2]
ENST00000373809; ENSP00000362915; ENSG00000170312. [P06493-2]
ENST00000395284; ENSP00000378699; ENSG00000170312. [P06493-1]
GeneIDi983.
KEGGihsa:983.
UCSCiuc001jld.3. human. [P06493-1]

Keywords - Coding sequence diversityi

Alternative splicing

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.

Entry informationi

Entry nameiCDK1_HUMAN
AccessioniPrimary (citable) accession number: P06493
Secondary accession number(s): A8K7C4, C9J497, O60764
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 31, 2011
Last modified: July 5, 2017
This is version 223 of the entry and version 3 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

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families