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UniProtKB/Swiss-Prot entry P24864


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCNE1_HUMAN
Primary accession number P24864
Secondary accession numbers Q14091 Q8NFG1 Q92501
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 94)
Name and origin of the protein
Protein name G1/S-specific cyclin-E1
Synonyms None
Gene name
Name: CCNE1
Synonyms: CCNE
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-410.
DOI=10.1016/0092-8674(91)90044-Y; PubMed=1833068 [NCBI, ExPASy, EBI, Israel, Japan]
Koff A., Cross F., Fisher A., Schumacher J., le Guellec K., Philippe M., Roberts J.M.;
"Human cyclin E, a new cyclin that interacts with two members of the CDC2 gene family.";
Cell 66:1217-1228(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-410.
DOI=10.1016/0092-8674(91)90042-W; PubMed=1833066 [NCBI, ExPASy, EBI, Israel, Japan]
Lew D.J., Dulic V., Reed S.I.;
"Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast.";
Cell 66:1197-1206(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1L).
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
PubMed=8649818 [NCBI, ExPASy, EBI, Israel, Japan]
Geng Y., Eaton E.N., Picon M., Roberts J.M., Lundberg A.S., Gifford A., Sardet C., Weinberg R.A.;
"Regulation of cyclin E transcription by E2Fs and retinoblastoma protein.";
Oncogene 12:1173-1180(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-370.
DOI=10.1006/geno.1996.0112; PubMed=8833152 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J.;
"Molecular cloning and chromosomal localization of the human cyclin C (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human tumors.";
Genomics 32:253-259(1996).
[7]
ALTERNATIVE SPLICING.
PubMed=8207080 [NCBI, ExPASy, EBI, Israel, Japan]
Sewing A., Roenicke V., Buerger C., Funk M., Mueller R.;
"Alternative splicing of human cyclin E.";
J. Cell Sci. 107:581-588(1994).
[8]
PHOSPHORYLATION AT THR-395.
PubMed=8861947 [NCBI, ExPASy, EBI, Israel, Japan]
Won K.A., Reed S.I.;
"Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E.";
EMBO J. 15:4182-4193(1996).
[9]
TISSUE SPECIFICITY.
DOI=10.1038/sj.onc.1202505; PubMed=9840943 [NCBI, ExPASy, EBI, Israel, Japan]
Zariwala M., Liu J., Xiong Y.;
"Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and CDK3, is induced by viral oncoproteins.";
Oncogene 17:2787-2798(1998).
[10]
PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399.
DOI=10.1016/S1097-2765(03)00287-9; PubMed=14536078 [NCBI, ExPASy, EBI, Israel, Japan]
Welcker M., Singer J., Loeb K.R., Grim J., Bloecher A., Gurien-West M., Clurman B.E., Roberts J.M.;
"Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation.";
Mol. Cell 12:381-392(2003).
[11]
IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CDK2.
DOI=10.1016/j.bbrc.2004.04.190; PubMed=15178429 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y., Mori T., Hata H., Homma Y., Kochi H.;
"NIRF induces G1 arrest and associates with Cdk2.";
Biochem. Biophys. Res. Commun. 319:464-468(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M73812; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
M74093; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AF518727; AAM54043.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035498; AAH35498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X95406; CAA64687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X95406; CAA64688.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40788; AAA83269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40787; AAA83269.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40270; A40270.
RefSeq NP_001229.1; -.
UniGene Hs.244723
3D structure databases
PDB
1W98; X-ray; 2.15 A; B=96-378.[ExPASy / RCSB / EBI]
PDBsum 1W98; -.
ModBase P24864.
Protein-protein interaction databases
DIP DIP:149N; -.
IntAct P24864; -.
PTM databases
PhosphoSite P24864; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
Polymorphism databases
NIEHS-SNPs CCNE1.
Organism-specific databases
H-InvDB HIX0027517; -.
HGNC HGNC:1589; CCNE1.
GenAtlas CCNE1.
HPA CAB000308; -.
CAB016682; -.
MIM 123837; gene. [NCBI / EBI]
PharmGKB PA96; -.
GeneCards P24864.
Gene expression databases
ArrayExpress P24864; -.
CleanEx HS_CCNE1; -.
GermOnline ENSG00000105173; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0050681; Molecular function: androgen receptor binding (non-traceable author statement from UniProtKB).
GO:0003713; Molecular function: transcription coactivator activity (non-traceable author statement from UniProtKB).
GO:0030521; Biological process: androgen receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (non-traceable author statement from UniProtKB).
GO:0045893; Biological process: positive regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006670; Cyclin.
IPR014400; Cyclin_A_B_D_E.
IPR004367; Cyclin_C.
IPR006671; Cyclin_N.
IPR013763; Cyclin_related.
Graphical view of domain structure.
Gene3D G3DSA:1.10.472.10; Cyclin_related; 1.
Pfam PF02984; Cyclin_C; 1.
PF00134; Cyclin_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001771; Cyclin_A_B_D_E; 1.
SMART SM00385; CYCLIN; 1.
SMART graphical view of domain structure.
PROSITE PS00292; CYCLINS; 1.
BLOCKS P24864.
ProtoNet P24864.
Genome annotation databases
Ensembl ENSG00000105173; Homo sapiens. [Contig view]
GeneID 898; -.
KEGG hsa:898; -.
Phylogenomic databases
HOGENOM P24864; -.
HOVERGEN P24864; -.
Other
NextBio 3708; -.
SOURCE CCNE1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   410  410     G1/S-specific cyclin-E1. PRO_0000080449
MOD_RES   59    59        Phosphoserine. 
MOD_RES   77    77        Phosphothreonine. 
MOD_RES   387   387        Phosphoserine. 
MOD_RES   395   395        Phosphothreonine; by GSK3. 
MOD_RES   399   399        Phosphoserine; by CDK2. 
VAR_SEQ   154   196        Missing (in isoform E1S). VSP_001253
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      
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      
Sequence information
Length: 410 AA [This is the length of the unprocessed precursor] Molecular weight: 47077 Da [This is the MW of the unprocessed precursor] CRC64: 424DF0B253B7047E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRERRERDA KERDTMKEDG GAEFSARSRK RKANVTVFLQ DPDEEMAKID RTARDQCGSQ 

        70         80         90        100        110        120 
PWDNNAVCAD PCSLIPTPDK EDDDRVYPNS TCKPRIIAPS RGSPLPVLSW ANREEVWKIM 

       130        140        150        160        170        180 
LNKEKTYLRD QHFLEQHPLL QPKMRAILLD WLMEVCEVYK LHRETFYLAQ DFFDRYMATQ 

       190        200        210        220        230        240 
ENVVKTLLQL IGISSLFIAA KLEEIYPPKL HQFAYVTDGA CSGDEILTME LMIMKALKWR 

       250        260        270        280        290        300 
LSPLTIVSWL NVYMQVAYLN DLHEVLLPQY PQQIFIQIAE LLDLCVLDVD CLEFPYGILA 

       310        320        330        340        350        360 
ASALYHFSSS ELMQKVSGYQ WCDIENCVKW MVPFAMVIRE TGSSKLKHFR GVADEDAHNI 

       370        380        390        400        410 
QTHRDSLDLL DKARAKKAML SEQNRASPLP SGLLTPPQSG KKQSSGPEMA 

P24864 in FASTA format

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