Reviewed,
UniProtKB/Swiss-Prot P24864 (CCNE1_HUMAN)
Last modified
May 26, 2009.
Version 100.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: G1/S-specific cyclin-E1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 410 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Essential for the control of the cell cycle at the G1/S (start) transition. |
| Subunit structure | Interacts with a member of the CDK2/CDK protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Interacts with retinoblastoma binding protein 3 and retinoblastoma-like protein 1. Found in a complex with CDK2, CABLES1 and CCNA1 By similarity. Part of a complex consisting of UHRF2, CDK2 and CCNE1. |
| Subcellular location | |
| Tissue specificity | Highly expressed in testis and placenta. Low levels in bronchial epithelial cells. Ref.11 |
| Post-translational modification | Phosphorylation of Thr-395 by GSK3 and of Ser-399 by CDK2 accelerates degradation via the ubiquitin proteasome pathway. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.12 Ref.14 Ref.15 |
| Sequence similarities | Belongs to the cyclin family. Cyclin E subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Cyclin |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | G1/S transition of mitotic cell cycle Ref.9 Non-traceable author statement. Source: UniProtKB androgen receptor signaling pathwayNon-traceable author statement. Source: UniProtKB cell divisionInferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependentNon-traceable author statement. Source: UniProtKB |
| Cellular component | cytosol Inferred from Experiment. Source: Reactome nucleoplasmInferred from Experiment. Source: Reactome |
| Molecular function | androgen receptor binding Non-traceable author statement. Source: UniProtKB transcription coactivator activityNon-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BRCA1 | P38398 | 2 | EBI-519526,EBI-349905 | |
| CDK2 | P24941 | 4 | EBI-519526,EBI-375096 | |
| CDKN1A | P38936 | 3 | EBI-519526,EBI-375077 | |
| CDKN1B | P46527 | 2 | EBI-519526,EBI-519280 | |
| MRE11A | P49959 | 1 | EBI-519526,EBI-396513 | |
| NBN | O60934 | 1 | EBI-519526,EBI-494844 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform E1L (identifier: P24864-1) Also known as: E-L; 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. | ||||||
| Isoform E1S (identifier: P24864-2) The sequence of this isoform differs from the canonical sequence as follows: 154-196: Missing. | ||||||
| Note: Lacks 49 residues within the cyclin box and cannot complex with CDK2. | ||||||
| Isoform 3 (identifier: P24864-3) Also known as: E-S; The sequence of this isoform differs from the canonical sequence as follows: 1-15: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 410 | 410 | G1/S-specific cyclin-E1 | PRO_0000080449 | |||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 59 | 1 | Phosphoserine Ref.14 | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 77 | 1 | Phosphothreonine Ref.12 | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 103 | 1 | Phosphoserine Ref.15 | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 387 | 1 | Phosphoserine Ref.12 Ref.15 | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 395 | 1 | Phosphothreonine; by GSK3 Ref.10 Ref.12 Ref.15 | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 399 | 1 | Phosphoserine; by CDK2 Ref.12 | ||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 15 | 15 | Missing in isoform 3. | VSP_037381 | |||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 154 – 196 | 43 | Missing in isoform E1S. | VSP_001253 | |||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 9 | 1 | D → K Ref.3 | ||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 111 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 113 – 123 | 11 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 124 – 126 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 133 – 136 | 4 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 158 | 17 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 179 | 17 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 187 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 188 – 203 | 16 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 210 – 215 | 6 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 216 – 219 | 4 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 223 – 236 | 14 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 237 – 239 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 246 – 257 | 12 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 265 – 267 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 272 – 287 | 16 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 289 – 293 | 5 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 296 – 306 | 11 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 310 – 316 | 7 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 321 – 341 | 21 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 354 – 359 | 6 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 366 – 370 | 5 | |||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast." Lew D.J., Dulic V., Reed S.I. Cell 66:1197-1206(1991) [PubMed: 1833066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). |
| [2] | "Human cyclin E, a new cyclin that interacts with two members of the CDC2 gene family." Koff A., Cross F., Fisher A., Schumacher J., le Guellec K., Philippe M., Roberts J.M. Cell 66:1217-1228(1991) [PubMed: 1833068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). |
| [3] | "Human cyclin E, a nuclear protein essential for the G1-to-S phase transition." Ohtsubo M., Theodoras A.M., Schumacher J., Roberts J.M., Pagano M. Mol. Cell. Biol. 15:2612-2624(1995) [PubMed: 7739542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E1L AND 3), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING. |
| [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1L). Tissue: Placenta. |
| [5] | NIEHS SNPs program Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [6] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1L). Tissue: Placenta. |
| [7] | "Regulation of cyclin E transcription by E2Fs and retinoblastoma protein." Geng Y., Eaton E.N., Picon M., Roberts J.M., Lundberg A.S., Gifford A., Sardet C., Weinberg R.A. Oncogene 12:1173-1180(1996) [PubMed: 8649818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. |
| [8] | "Molecular cloning and chromosomal localization of the human cyclin C (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human tumors." Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J. Genomics 32:253-259(1996) [PubMed: 8833152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-370. |
| [9] | "Alternative splicing of human cyclin E." Sewing A., Roenicke V., Buerger C., Funk M., Mueller R. J. Cell Sci. 107:581-588(1994) [PubMed: 8207080] [Abstract] Cited for: ALTERNATIVE SPLICING. |
| [10] | "Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E." Won K.A., Reed S.I. EMBO J. 15:4182-4193(1996) [PubMed: 8861947] [Abstract] Cited for: PHOSPHORYLATION AT THR-395. |
| [11] | "Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and CDK3, is induced by viral oncoproteins." Zariwala M., Liu J., Xiong Y. Oncogene 17:2787-2798(1998) [PubMed: 9840943] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [12] | "Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation." Welcker M., Singer J., Loeb K.R., Grim J., Bloecher A., Gurien-West M., Clurman B.E., Roberts J.M. Mol. Cell 12:381-392(2003) [PubMed: 14536078] [Abstract] Cited for: PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399. |
| [13] | "NIRF induces G1 arrest and associates with Cdk2." Li Y., Mori T., Hata H., Homma Y., Kochi H. Biochem. Biophys. Res. Commun. 319:464-468(2004) [PubMed: 15178429] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CDK2. |
| [14] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, MASS SPECTROMETRY. |
| [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-387 AND THR-395, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M74093 mRNA. No translation available. M73812 mRNA. No translation available. AK291549 mRNA. Translation: BAF84238.1. AF518727 Genomic DNA. Translation: AAM54043.1. BC035498 mRNA. Translation: AAH35498.1. X95406 Genomic DNA. Translation: CAA64687.1. X95406 Genomic DNA. Translation: CAA64688.1. U40788, U40787 Genomic DNA. Translation: AAA83269.1. | |||||||||||||
| IPI | IPI00031077. IPI00216040. | ||||||||||||
| PIR | A40270. | ||||||||||||
| RefSeq | NP_001229.1. | ||||||||||||
| UniGene | Hs.244723 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP:149N. | ||||||||||||
| IntAct | P24864. 8 interactions. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P24864. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P24864. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000105173. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 898. | ||||||||||||
| KEGG | hsa:898. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC19P034994. | ||||||||||||
| H-InvDB | HIX0027517. | ||||||||||||
| HGNC | HGNC:1589. CCNE1. | ||||||||||||
| HPA | CAB000308. CAB016682. | ||||||||||||
| MIM | 123837. gene. | ||||||||||||
| PharmGKB | PA96. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P24864. | ||||||||||||
| HOVERGEN | P24864. | ||||||||||||
| OMA | P24864. PLLQPKM. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Pathway_Interaction_DB | bard1pathway. BARD1 signaling events. foxm1pathway. FOXM1 transcription factor network. prlsignalingeventspathway. Signaling events mediated by PRL. | ||||||||||||
| Reactome | REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P24864. | ||||||||||||
| Bgee | P24864. | ||||||||||||
| CleanEx | HS_CCNE1. | ||||||||||||
| GermOnline | ENSG00000105173. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR006670. Cyclin. IPR014400. Cyclin_A_B_D_E. IPR004367. Cyclin_C. IPR006671. Cyclin_N. IPR013763. Cyclin_related. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.472.10. Cyclin_related. 1 hit. | ||||||||||||
| Pfam | PF02984. Cyclin_C. 1 hit. PF00134. Cyclin_N. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF001771. Cyclin_A_B_D_E. 1 hit. | ||||||||||||
| SMART | SM00385. CYCLIN. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00292. CYCLINS. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 3708. | ||||||||||||
| PMAP-CutDB | P24864. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CCNE1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P24864 Secondary accession number(s): A8K684 Q9UD21 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 19 Human chromosome 19: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


