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P41002

- CCNF_HUMAN

UniProt

P41002 - CCNF_HUMAN

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Protein

Cyclin-F

Gene

CCNF

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

Functioni

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication.1 Publication

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. negative regulation of centrosome duplication Source: UniProtKB
  3. placenta development Source: Ensembl
  4. protein ubiquitination Source: UniProtKB
  5. re-entry into mitotic cell cycle Source: Ensembl
  6. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

SignaLinkiP41002.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-F
Alternative name(s):
F-box only protein 1
Gene namesi
Name:CCNF
Synonyms:FBX1, FBXO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:1591. CCNF.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
Note: Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Also localizes to the nucleus.

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 362LP → AA: Impairs interaction with SKP1 and CUL1 and prevents degradation of CP110, leading to promote the formation of micronuclei. 1 Publication
Mutagenesisi309 – 3091M → A: Abolishes ability to interact with CP110; when associated with A-352. 1 Publication
Mutagenesisi352 – 3521L → A: Abolishes ability to interact with CP110; when associated with A-309. 1 Publication

Organism-specific databases

PharmGKBiPA26156.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Cyclin-FPRO_0000080463Add
BLAST

Post-translational modificationi

Degraded when the spindle assembly checkpoint is activated during the G2-M transition. Degradation is not dependent on the proteasome or ubiquitin and depends on the C-terminal PEST sequence.
Phosphorylated just before cells enter into mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41002.
PaxDbiP41002.
PRIDEiP41002.

PTM databases

PhosphoSiteiP41002.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Appears in S phase, peaks in G2 phase and disappears as cells enter into mitosis (at protein level).1 Publication

Gene expression databases

BgeeiP41002.
CleanExiHS_CCNF.
ExpressionAtlasiP41002. baseline and differential.
GenevestigatoriP41002.

Interactioni

Subunit structurei

Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Interacts with CCNB1; interaction is required for nuclear localization of CCNB1. Interacts with CCP110; this interaction leads to CCP110 ubiquitination and degradation via the proteasome pathway.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCP110O433033EBI-1207574,EBI-1566217
RRM2P3135012EBI-1207574,EBI-2339245
SKP1P632086EBI-1207574,EBI-307486

Protein-protein interaction databases

BioGridi107339. 11 interactions.
DIPiDIP-44939N.
IntActiP41002. 6 interactions.
MINTiMINT-1543357.
STRINGi9606.ENSP00000380256.

Structurei

3D structure databases

ProteinModelPortaliP41002.
SMRiP41002. Positions 302-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 7648F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini292 – 405114Cyclin N-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni582 – 766185PESTAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 289Nuclear localization signal 11 Publication
Motifi568 – 5747Nuclear localization signal 21 Publication

Domaini

The nuclear localization signals mediate the localization to the nucleus and are required for CCNB1 localization to the nucleus.1 Publication

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated
Contains 1 cyclin N-terminal domain.Curated
Contains 1 F-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG283043.
GeneTreeiENSGT00730000111208.
HOGENOMiHOG000285971.
HOVERGENiHBG050838.
InParanoidiP41002.
KOiK10289.
OMAiKSCLQCR.
OrthoDBiEOG7WDN1V.
PhylomeDBiP41002.
TreeFamiTF101006.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
1.25.40.10. 2 hits.
InterProiIPR028857. CCNF_metazoan.
IPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
IPR001810. F-box_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR10177:SF183. PTHR10177:SF183. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
PF00646. F-box. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
SSF81383. SSF81383. 1 hit.
PROSITEiPS00292. CYCLINS. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41002-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSGGVVHCR CAKCFCYPTK RRIRRRPRNL TILSLPEDVL FHILKWLSVE
60 70 80 90 100
DILAVRAVHS QLKDLVDNHA SVWACASFQE LWPSPGNLKL FERAAEKGNF
110 120 130 140 150
EAAVKLGIAY LYNEGLSVSD EARAEVNGLK ASRFFSLAER LNVGAAPFIW
160 170 180 190 200
LFIRPPWSVS GSCCKAVVHE SLRAECQLQR THKASILHCL GRVLSLFEDE
210 220 230 240 250
EKQQQAHDLF EEAAHQGCLT SSYLLWESDR RTDVSDPGRC LHSFRKLRDY
260 270 280 290 300
AAKGCWEAQL SLAKACANAN QLGLEVRASS EIVCQLFQAS QAVSKQQVFS
310 320 330 340 350
VQKGLNDTMR YILIDWLVEV ATMKDFTSLC LHLTVECVDR YLRRRLVPRY
360 370 380 390 400
RLQLLGIACM VICTRFISKE ILTIREAVWL TDNTYKYEDL VRMMGEIVSA
410 420 430 440 450
LEGKIRVPTV VDYKEVLLTL VPVELRTQHL CSFLCELSLL HTSLSAYAPA
460 470 480 490 500
RLAAAALLLA RLTHGQTQPW TTQLWDLTGF SYEDLIPCVL SLHKKCFHDD
510 520 530 540 550
APKDYRQVSL TAVKQRFEDK RYGEISQEEV LSYSQLCAAL GVTQDSPDPP
560 570 580 590 600
TFLSTGEIHA FLSSPSGRRT KRKRENSLQE DRGSFVTTPT AELSSQEETL
610 620 630 640 650
LGSFLDWSLD CCSGYEGDQE SEGEKEGDVT APSGILDVTV VYLNPEQHCC
660 670 680 690 700
QESSDEEACP EDKGPQDPQA LALDTQIPAT PGPKPLVRTS REPGKDVTTS
710 720 730 740 750
GYSSVSTASP TSSVDGGLGA LPQPTSVLSL DSDSHTQPCH HQARKSCLQC
760 770 780
RPPSPPESSV PQQQVKRINL CIHSEEEDMN LGLVRL
Length:786
Mass (Da):87,640
Last modified:April 16, 2002 - v2
Checksum:iADB2FE41BC708898
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521A → R in CAA85308. (PubMed:7896286)Curated
Sequence conflicti324 – 3241K → N in CAA85308. (PubMed:7896286)Curated
Sequence conflicti434 – 4341L → H in BAG36170. (PubMed:14702039)Curated
Sequence conflicti600 – 6001L → V in CAA85308. (PubMed:7896286)Curated
Sequence conflicti662 – 6621D → A in CAA85308. (PubMed:7896286)Curated
Sequence conflicti710 – 7101P → S in AAB60342. (PubMed:7813445)Curated
Sequence conflicti731 – 7311D → H in CAA85308. (PubMed:7896286)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17105 mRNA. Translation: AAB60342.1.
Z36714 mRNA. Translation: CAA85308.1.
AK313371 mRNA. Translation: BAG36170.1.
AC106820 Genomic DNA. No translation available.
BC012349 mRNA. Translation: AAH12349.1.
CCDSiCCDS10467.1.
PIRiA55501.
RefSeqiNP_001752.2. NM_001761.2.
UniGeneiHs.1973.

Genome annotation databases

EnsembliENST00000397066; ENSP00000380256; ENSG00000162063.
GeneIDi899.
KEGGihsa:899.
UCSCiuc002cqd.1. human.

Polymorphism databases

DMDMi20178283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17105 mRNA. Translation: AAB60342.1 .
Z36714 mRNA. Translation: CAA85308.1 .
AK313371 mRNA. Translation: BAG36170.1 .
AC106820 Genomic DNA. No translation available.
BC012349 mRNA. Translation: AAH12349.1 .
CCDSi CCDS10467.1.
PIRi A55501.
RefSeqi NP_001752.2. NM_001761.2.
UniGenei Hs.1973.

3D structure databases

ProteinModelPortali P41002.
SMRi P41002. Positions 302-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107339. 11 interactions.
DIPi DIP-44939N.
IntActi P41002. 6 interactions.
MINTi MINT-1543357.
STRINGi 9606.ENSP00000380256.

PTM databases

PhosphoSitei P41002.

Polymorphism databases

DMDMi 20178283.

Proteomic databases

MaxQBi P41002.
PaxDbi P41002.
PRIDEi P41002.

Protocols and materials databases

DNASUi 899.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397066 ; ENSP00000380256 ; ENSG00000162063 .
GeneIDi 899.
KEGGi hsa:899.
UCSCi uc002cqd.1. human.

Organism-specific databases

CTDi 899.
GeneCardsi GC16P002479.
HGNCi HGNC:1591. CCNF.
MIMi 600227. gene.
neXtProti NX_P41002.
PharmGKBi PA26156.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283043.
GeneTreei ENSGT00730000111208.
HOGENOMi HOG000285971.
HOVERGENi HBG050838.
InParanoidi P41002.
KOi K10289.
OMAi KSCLQCR.
OrthoDBi EOG7WDN1V.
PhylomeDBi P41002.
TreeFami TF101006.

Enzyme and pathway databases

SignaLinki P41002.

Miscellaneous databases

ChiTaRSi CCNF. human.
GeneWikii CCNF.
GenomeRNAii 899.
NextBioi 3714.
PROi P41002.
SOURCEi Search...

Gene expression databases

Bgeei P41002.
CleanExi HS_CCNF.
ExpressionAtlasi P41002. baseline and differential.
Genevestigatori P41002.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
1.25.40.10. 2 hits.
InterProi IPR028857. CCNF_metazoan.
IPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
IPR001810. F-box_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
PANTHERi PTHR10177:SF183. PTHR10177:SF183. 1 hit.
Pfami PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
PF00646. F-box. 1 hit.
[Graphical view ]
SMARTi SM00385. CYCLIN. 2 hits.
SM00256. FBOX. 1 hit.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
SSF81383. SSF81383. 1 hit.
PROSITEi PS00292. CYCLINS. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cyclin F."
    Bai C., Richman R., Elledge S.J.
    EMBO J. 13:6087-6098(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  2. "A novel cyclin gene (CCNF) in the region of the polycystic kidney disease gene (PKD1)."
    Kraus B., Pohlschmidt M., Leung A.L.S., Germino G.G., Snarey A., Schneider M.C., Reeders S.T., Frischauf A.-M.
    Genomics 24:27-33(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Thymus.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Eye.
  6. "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box."
    Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J.
    Cell 86:263-274(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1.
  7. "Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction."
    Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.
    EMBO J. 19:1378-1388(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, DOMAIN, INTERACTION WITH CCNB1.
  8. "Cyclin F is degraded during G2-M by mechanisms fundamentally different from other cyclins."
    Fung T.K., Siu W.Y., Yam C.H., Lau A., Poon R.Y.
    J. Biol. Chem. 277:35140-35149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1, DEGRADATION.
  9. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
    D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
    Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SCF(CCNF) COMPLEX WITH SKP1 AND CUL1, INTERACTION WITH CP110, MUTAGENESIS OF 35-LEU-PRO-36; MET-309 AND LEU-352.
  10. "Neurl4, a novel daughter centriole protein, prevents formation of ectopic microtubule organizing centres."
    Li J., Kim S., Kobayashi T., Liang F.X., Korzeniewski N., Duensing S., Dynlacht B.D.
    EMBO Rep. 13:547-553(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCP110.

Entry informationi

Entry nameiCCNF_HUMAN
AccessioniPrimary (citable) accession number: P41002
Secondary accession number(s): B2R8H3, Q96EG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 16, 2002
Last modified: November 26, 2014
This is version 140 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

Miscellaneous

Founding member of the F-box domain protein family, which obtained its name from cyclin-F.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3