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Protein

G1/S-specific cyclin-E1

Gene

CCNE1

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

Functioni

Essential for the control of the cell cycle at the G1/S (start) transition.1 Publication

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase regulator activity Source: Ensembl
  • kinase activity Source: Ensembl
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • androgen receptor signaling pathway Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • DNA replication initiation Source: Ensembl
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein phosphorylation Source: MGI
  • regulation of cell cycle Source: Ensembl
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  • Wnt signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1625. p53-Dependent G1 DNA Damage Response.
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
SignaLinkiP24864.

Names & Taxonomyi

Protein namesi
Recommended name:
G1/S-specific cyclin-E1
Gene namesi
Name:CCNE1
Synonyms:CCNE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1589. CCNE1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cyclin-dependent protein kinase holoenzyme complex Source: Ensembl
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA96.

Polymorphism and mutation databases

BioMutaiCCNE1.
DMDMi3041657.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410G1/S-specific cyclin-E1PRO_0000080449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphothreonine2 Publications
Modified residuei103 – 1031Phosphoserine2 Publications
Modified residuei387 – 3871Phosphoserine3 Publications
Modified residuei395 – 3951Phosphothreonine; by GSK34 Publications
Modified residuei399 – 3991Phosphoserine; by CDK22 Publications

Post-translational modificationi

Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway. Phosphorylation at Thr-77 creates a low affinity degron also recognized by FBXW7.4 Publications
Ubiquitinated by UHRF2; appears to occur independently of phosphorylation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP24864.
PaxDbiP24864.
PRIDEiP24864.

PTM databases

PhosphoSiteiP24864.

Miscellaneous databases

PMAP-CutDBP24864.

Expressioni

Tissue specificityi

Highly expressed in testis and placenta. Low levels in bronchial epithelial cells.1 Publication

Gene expression databases

BgeeiP24864.
CleanExiHS_CCNE1.
ExpressionAtlasiP24864. baseline and differential.
GenevisibleiP24864. HS.

Organism-specific databases

HPAiCAB000308.
CAB016682.
HPA018169.

Interactioni

Subunit structurei

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. Found in a complex with CDK2, CABLES1 and CCNA1 (By similarity). Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts directly with UHRF2; the interaction ubiquitinates CCNE1 and appears to occur independently of CCNE1 phosphorylation.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383982EBI-519526,EBI-349905
CDK2P2494112EBI-519526,EBI-375096
CDKN1AP389369EBI-519526,EBI-375077
CDKN1BP465277EBI-519526,EBI-519280
FOXM1Q080502EBI-519526,EBI-866480
UHRF2Q96PU44EBI-519526,EBI-625304

Protein-protein interaction databases

BioGridi107338. 69 interactions.
DIPiDIP-149N.
IntActiP24864. 15 interactions.
MINTiMINT-1514839.
STRINGi9606.ENSP00000262643.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi109 – 1113Combined sources
Helixi113 – 12311Combined sources
Turni124 – 1263Combined sources
Helixi133 – 1364Combined sources
Helixi142 – 15817Combined sources
Helixi163 – 17917Combined sources
Helixi185 – 1873Combined sources
Helixi188 – 20316Combined sources
Helixi210 – 2156Combined sources
Turni216 – 2194Combined sources
Helixi223 – 23614Combined sources
Turni237 – 2393Combined sources
Helixi246 – 25712Combined sources
Beta strandi265 – 2673Combined sources
Helixi272 – 28716Combined sources
Helixi289 – 2935Combined sources
Helixi296 – 30611Combined sources
Helixi310 – 3167Combined sources
Helixi321 – 34121Combined sources
Helixi354 – 3596Combined sources
Helixi366 – 3705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W98X-ray2.15B96-378[»]
ProteinModelPortaliP24864.
SMRiP24864. Positions 103-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24864.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin E subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231743.
HOVERGENiHBG050834.
InParanoidiP24864.
KOiK06626.
OMAiPFAMVIR.
OrthoDBiEOG7HB595.
PhylomeDBiP24864.
TreeFamiTF101005.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF71. PTHR10177:SF71. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform E1L (identifier: P24864-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPRERRERDA KERDTMKEDG GAEFSARSRK RKANVTVFLQ DPDEEMAKID
60 70 80 90 100
RTARDQCGSQ PWDNNAVCAD PCSLIPTPDK EDDDRVYPNS TCKPRIIAPS
110 120 130 140 150
RGSPLPVLSW ANREEVWKIM LNKEKTYLRD QHFLEQHPLL QPKMRAILLD
160 170 180 190 200
WLMEVCEVYK LHRETFYLAQ DFFDRYMATQ ENVVKTLLQL IGISSLFIAA
210 220 230 240 250
KLEEIYPPKL HQFAYVTDGA CSGDEILTME LMIMKALKWR LSPLTIVSWL
260 270 280 290 300
NVYMQVAYLN DLHEVLLPQY PQQIFIQIAE LLDLCVLDVD CLEFPYGILA
310 320 330 340 350
ASALYHFSSS ELMQKVSGYQ WCDIENCVKW MVPFAMVIRE TGSSKLKHFR
360 370 380 390 400
GVADEDAHNI QTHRDSLDLL DKARAKKAML SEQNRASPLP SGLLTPPQSG
410
KKQSSGPEMA
Length:410
Mass (Da):47,077
Last modified:July 15, 1998 - v2
Checksum:i424DF0B253B7047E
GO
Isoform E1S (identifier: P24864-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:367
Mass (Da):41,982
Checksum:i526E59736D99D3C6
GO
Isoform 3 (identifier: P24864-3) [UniParc]FASTAAdd to basket

Also known as: E-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Show »
Length:395
Mass (Da):45,150
Checksum:i4E55D1F80BCFB3EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → K no nucleotide entry (PubMed:7739542).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515Missing in isoform 3. 3 PublicationsVSP_037381Add
BLAST
Alternative sequencei154 – 19643Missing in isoform E1S. CuratedVSP_001253Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AH003247 Genomic DNA. Translation: AAA83269.1.
CCDSiCCDS12419.1. [P24864-1]
PIRiA40270.
RefSeqiNP_001229.1. NM_001238.2. [P24864-1]
XP_006723520.1. XM_006723457.2. [P24864-3]
UniGeneiHs.244723.

Genome annotation databases

EnsembliENST00000262643; ENSP00000262643; ENSG00000105173. [P24864-1]
ENST00000444983; ENSP00000410179; ENSG00000105173. [P24864-3]
GeneIDi898.
KEGGihsa:898.
UCSCiuc002nsn.3. human. [P24864-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AH003247 Genomic DNA. Translation: AAA83269.1.
CCDSiCCDS12419.1. [P24864-1]
PIRiA40270.
RefSeqiNP_001229.1. NM_001238.2. [P24864-1]
XP_006723520.1. XM_006723457.2. [P24864-3]
UniGeneiHs.244723.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W98X-ray2.15B96-378[»]
ProteinModelPortaliP24864.
SMRiP24864. Positions 103-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107338. 69 interactions.
DIPiDIP-149N.
IntActiP24864. 15 interactions.
MINTiMINT-1514839.
STRINGi9606.ENSP00000262643.

Chemistry

BindingDBiP24864.
ChEMBLiCHEMBL3038471.

PTM databases

PhosphoSiteiP24864.

Polymorphism and mutation databases

BioMutaiCCNE1.
DMDMi3041657.

Proteomic databases

MaxQBiP24864.
PaxDbiP24864.
PRIDEiP24864.

Protocols and materials databases

DNASUi898.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262643; ENSP00000262643; ENSG00000105173. [P24864-1]
ENST00000444983; ENSP00000410179; ENSG00000105173. [P24864-3]
GeneIDi898.
KEGGihsa:898.
UCSCiuc002nsn.3. human. [P24864-1]

Organism-specific databases

CTDi898.
GeneCardsiGC19P030302.
HGNCiHGNC:1589. CCNE1.
HPAiCAB000308.
CAB016682.
HPA018169.
MIMi123837. gene.
neXtProtiNX_P24864.
PharmGKBiPA96.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231743.
HOVERGENiHBG050834.
InParanoidiP24864.
KOiK06626.
OMAiPFAMVIR.
OrthoDBiEOG7HB595.
PhylomeDBiP24864.
TreeFamiTF101005.

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1625. p53-Dependent G1 DNA Damage Response.
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
SignaLinkiP24864.

Miscellaneous databases

ChiTaRSiCCNE1. human.
EvolutionaryTraceiP24864.
GeneWikiiCyclin_E1.
GenomeRNAii898.
NextBioi3708.
PMAP-CutDBP24864.
PROiP24864.
SOURCEiSearch...

Gene expression databases

BgeeiP24864.
CleanExiHS_CCNE1.
ExpressionAtlasiP24864. baseline and differential.
GenevisibleiP24864. HS.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF71. PTHR10177:SF71. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
    , 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 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399.
  13. Cited for: IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CDK2.
  14. "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-103; SER-387 AND THR-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
    Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
    Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
  18. "The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles."
    Honda R., Lowe E.D., Dubinina E., Skamnaki V., Cook A., Brown N.R., Johnson L.N.
    EMBO J. 24:452-463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 96-378 IN COMPLEX WITH CDK2.
  19. "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases."
    Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.
    Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 73-80 IN COMPLEX WITH SKP1 AND FBXW7, PHOSPHORYLATION AT THR-77; THR-395 AND SER-399.

Entry informationi

Entry nameiCCNE1_HUMAN
AccessioniPrimary (citable) accession number: P24864
Secondary accession number(s): A8K684
, Q14091, Q8NFG1, Q92501, Q9UD21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 167 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. 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.