Full text data of CENPF
CENPF
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Centromere protein F; CENP-F (AH antigen; Kinetochore protein CENPF; Mitosin; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Centromere protein F; CENP-F (AH antigen; Kinetochore protein CENPF; Mitosin; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49454
ID CENPF_HUMAN Reviewed; 3210 AA.
AC P49454; Q13171; Q13246; Q5VVM7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-AUG-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Centromere protein F;
DE Short=CENP-F;
DE AltName: Full=AH antigen;
DE AltName: Full=Kinetochore protein CENPF;
DE AltName: Full=Mitosin;
DE Flags: Precursor;
GN Name=CENPF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND VARIANTS LEU-250; GLY-272 AND LYS-3202.
RC TISSUE=Mammary carcinoma;
RX PubMed=7542657; DOI=10.1083/jcb.130.3.507;
RA Liao H., Winkfein R.J., Mack G., Rattner J.B., Yen T.J.;
RT "CENP-F is a protein of the nuclear matrix that assembles onto
RT kinetochores at late G2 and is rapidly degraded after mitosis.";
RL J. Cell Biol. 130:507-518(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1,
RP SUBCELLULAR LOCATION, AND VARIANTS 1516-VAL--VAL-1611 DEL AND
RP LYS-3202.
RX PubMed=7651420;
RA Zhu X., Mancini M.A., Chang K.-H., Liu C.-Y., Chen C.-F., Shan B.,
RA Jones D., Yang-Feng T.L., Lee W.-H.;
RT "Characterization of a novel 350-kilodalton nuclear phosphoprotein
RT that is specifically involved in mitotic-phase progression.";
RL Mol. Cell. Biol. 15:5017-5029(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT
RP 1516-VAL--VAL-1611.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT
RP 1516-VAL--VAL-1611.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2194-3210, SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, AND VARIANT LYS-3202.
RX PubMed=7612011; DOI=10.1006/bbrc.1995.1959;
RA Li Q., Ke Y., Kapp J.A., Fertig N., Medsger T.A. Jr., Joshi H.C.;
RT "A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal
RT domain sufficient for nuclear localization.";
RL Biochem. Biophys. Res. Commun. 212:220-228(1995).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=7642639; DOI=10.1074/jbc.270.33.19545;
RA Zhu X., Chang K.-H., He D., Mancini M.A., Brinkley W.R., Lee W.-H.;
RT "The C-terminus of mitosin is essential for its nuclear localization,
RT centromere/kinetochore targeting, and dimerization.";
RL J. Biol. Chem. 270:19545-19550(1995).
RN [7]
RP INTERACTION WITH BUBR1 AND CENPE, AND SUBCELLULAR LOCATION.
RX PubMed=9763420; DOI=10.1083/jcb.143.1.49;
RA Chan G.K.T., Schaar B.T., Yen T.J.;
RT "Characterization of the kinetochore binding domain of CENP-E reveals
RT interactions with the kinetochore proteins CENP-F and hBUBR1.";
RL J. Cell Biol. 143:49-63(1998).
RN [8]
RP ISOPRENYLATION AT CYS-3207.
RX PubMed=10852915; DOI=10.1074/jbc.M003469200;
RA Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L.,
RA Bishop W.R., Kirschmeier P.;
RT "Farnesyl transferase inhibitors block the farnesylation of CENP-E and
RT CENP-F and alter the association of CENP-E with the microtubules.";
RL J. Biol. Chem. 275:30451-30457(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12974617; DOI=10.1038/sj.cr.7290172;
RA Yang Z.Y., Guo J., Li N., Qian M., Wang S.N., Zhu X.L.;
RT "Mitosin/CENP-F is a conserved kinetochore protein subjected to
RT cytoplasmic dynein-mediated poleward transport.";
RL Cell Res. 13:275-283(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747 AND SER-1750, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP FUNCTION, INTERACTION WITH NDEL1 AND NDE1, AND SUBCELLULAR LOCATION.
RX PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
RA Vergnolle M.A.S., Taylor S.S.;
RT "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
RT complexes.";
RL Curr. Biol. 17:1173-1179(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3150, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-144; SER-834;
RP SER-1248; SER-1747; SER-1748; SER-1750; SER-2512; SER-2513; SER-2996;
RP SER-3007; SER-3119; SER-3122; SER-3150; SER-3175 AND SER-3179, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996 AND SER-3007, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2875, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; THR-154; TYR-158;
RP SER-276; SER-773; SER-783; SER-821; SER-876; SER-1248; SER-1255;
RP SER-1259; SER-1747; SER-1750; SER-1988; SER-2513; SER-2996; SER-3007;
RP SER-3018; THR-3045; SER-3048; SER-3094; SER-3119; SER-3122; SER-3150;
RP SER-3175 AND SER-3179, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119 AND SER-3150, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for kinetochore function and chromosome
CC segregation in mitosis. Required for kinetochore localization of
CC dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma
CC membrane by acting as a link between recycling vesicles and the
CC microtubule network though its association with STX4 and SNAP25.
CC Acts as a potential inhibitor of pocket protein-mediated cellular
CC processes during development by regulating the activity of RB
CC proteins during cell division and proliferation. May play a
CC regulatory or permissive role in the normal embryonic
CC cardiomyocyte cell cycle and in promoting continued mitosis in
CC transformed, abnormally dividing neonatal cardiomyocytes.
CC Interaction with RB directs embryonic stem cells toward a cardiac
CC lineage. Involved in the regulation of DNA synthesis and hence
CC cell cycle progression, via its C-terminus. Has a potential role
CC regulating skeletal myogenesis and in cell differentiation in
CC embryogenesis. Involved in dendritic cell regulation of T-cell
CC immunity against chlamydia.
CC -!- SUBUNIT: Interacts with and STX4 (via C-terminus) (By similarity).
CC Interacts (via N-terminus) with RBL1, RBL2 and SNAP25 (By
CC similarity). Self-associates. Interacts with CENP-E and BUBR1 (via
CC C-terminus). Interacts (via C-terminus) with NDE1, NDEL1 and RB1.
CC -!- INTERACTION:
CC Q9GZM8:NDEL1; NbExp=5; IntAct=EBI-968343, EBI-928842;
CC Q8WUM0:NUP133; NbExp=2; IntAct=EBI-968343, EBI-295695;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus
CC matrix. Chromosome, centromere, kinetochore. Cytoplasm,
CC cytoskeleton, spindle. Note=Relocalizes to the
CC kinetochore/centromere (coronal surface of the outer plate) and
CC the spindle during mitosis. Observed in nucleus during interphase
CC but not in the nucleolus. At metaphase becomes localized to areas
CC including kinetochore and mitotic apparatus as well as cytoplasm.
CC By telophase, is concentrated within the intracellular bridge at
CC either side of the mid-body.
CC -!- DEVELOPMENTAL STAGE: Gradually accumulates during the cell cycle,
CC reaching peak levels in G2 and M phase, and is rapidly degraded
CC upon completion of mitosis.
CC -!- PTM: Hyperphosphorylated during mitosis.
CC -!- SIMILARITY: Belongs to the centromere protein F family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CENPFID40057ch1q41.html";
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DR EMBL; U19769; AAA82889.1; -; mRNA.
DR EMBL; U30872; AAA82935.1; -; mRNA.
DR EMBL; AL445666; CAH71810.1; -; Genomic_DNA.
DR EMBL; AL445305; CAH71810.1; JOINED; Genomic_DNA.
DR EMBL; AL445305; CAH73032.1; -; Genomic_DNA.
DR EMBL; AL445666; CAH73032.1; JOINED; Genomic_DNA.
DR EMBL; BC172232; AAI72232.1; -; mRNA.
DR EMBL; U25725; AAA86889.1; -; mRNA.
DR PIR; PC4035; PC4035.
DR RefSeq; NP_057427.3; NM_016343.3.
DR UniGene; Hs.497741; -.
DR IntAct; P49454; 11.
DR MINT; MINT-2803614; -.
DR STRING; 9606.ENSP00000355922; -.
DR PhosphoSite; P49454; -.
DR DMDM; 156630875; -.
DR PaxDb; P49454; -.
DR PRIDE; P49454; -.
DR Ensembl; ENST00000366955; ENSP00000355922; ENSG00000117724.
DR GeneID; 1063; -.
DR KEGG; hsa:1063; -.
DR UCSC; uc001hkm.3; human.
DR CTD; 1063; -.
DR GeneCards; GC01P214776; -.
DR H-InvDB; HIX0028827; -.
DR HGNC; HGNC:1857; CENPF.
DR HPA; CAB009581; -.
DR MIM; 600236; gene.
DR neXtProt; NX_P49454; -.
DR PharmGKB; PA26401; -.
DR eggNOG; NOG12793; -.
DR HOVERGEN; HBG050893; -.
DR KO; K11499; -.
DR OrthoDB; EOG7FV3PD; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; CENPF; human.
DR GeneWiki; CENPF; -.
DR GenomeRNAi; 1063; -.
DR NextBio; 4446; -.
DR PRO; PR:P49454; -.
DR Bgee; P49454; -.
DR CleanEx; HS_CENPF; -.
DR Genevestigator; P49454; -.
DR GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0045502; F:dynein binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; IDA:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000085; P:mitotic G2 phase; IMP:UniProtKB.
DR GO; GO:0000087; P:mitotic M phase; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; NAS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; NAS:UniProtKB.
DR InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR InterPro; IPR018463; Centromere_CenpF_N.
DR Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR Pfam; PF10473; CENP-F_leu_zip; 3.
DR Pfam; PF10481; CENP-F_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; DNA synthesis; Kinetochore;
KW Lipoprotein; Methylation; Mitosis; Myogenesis; Nucleus;
KW Phosphoprotein; Polymorphism; Prenylation; Reference proteome; Repeat.
FT CHAIN 1 3207 Centromere protein F.
FT /FTId=PRO_0000089477.
FT PROPEP 3208 3210 Removed in mature form (Probable).
FT /FTId=PRO_0000396744.
FT REPEAT 1435 1530 1-1.
FT REPEAT 1531 1626 1-2.
FT REPEAT 2207 2386 2-1.
FT REPEAT 2389 2568 2-2.
FT REGION 1 481 Interaction with SNAP25 and required for
FT localization to the cytoplasm (By
FT similarity).
FT REGION 1435 1626 2 X 96 AA approximate tandem repeats.
FT REGION 2122 2447 Interaction with NDE1 and NDEL1.
FT REGION 2207 2568 2 X 177 AA tandem repeats.
FT REGION 2488 3113 Sufficient for centromere localization.
FT REGION 2488 2925 Sufficient for self-association.
FT REGION 2927 3113 Sufficient for nuclear localization.
FT COILED 14 197 Potential.
FT COILED 273 769 Potential.
FT COILED 823 1328 Potential.
FT COILED 1642 1746 Potential.
FT COILED 1862 2987 Potential.
FT MOTIF 3015 3032 Nuclear localization signal (Potential).
FT MOD_RES 106 106 Phosphoserine.
FT MOD_RES 144 144 Phosphothreonine.
FT MOD_RES 151 151 Phosphothreonine.
FT MOD_RES 154 154 Phosphothreonine.
FT MOD_RES 158 158 Phosphotyrosine.
FT MOD_RES 276 276 Phosphoserine.
FT MOD_RES 773 773 Phosphoserine.
FT MOD_RES 783 783 Phosphoserine.
FT MOD_RES 821 821 Phosphoserine.
FT MOD_RES 834 834 Phosphoserine.
FT MOD_RES 876 876 Phosphoserine.
FT MOD_RES 1248 1248 Phosphoserine.
FT MOD_RES 1255 1255 Phosphoserine.
FT MOD_RES 1259 1259 Phosphoserine.
FT MOD_RES 1747 1747 Phosphoserine.
FT MOD_RES 1748 1748 Phosphoserine.
FT MOD_RES 1750 1750 Phosphoserine.
FT MOD_RES 1988 1988 Phosphoserine.
FT MOD_RES 2512 2512 Phosphoserine.
FT MOD_RES 2513 2513 Phosphoserine.
FT MOD_RES 2875 2875 N6-acetyllysine.
FT MOD_RES 2996 2996 Phosphoserine.
FT MOD_RES 3007 3007 Phosphoserine.
FT MOD_RES 3018 3018 Phosphoserine.
FT MOD_RES 3045 3045 Phosphothreonine.
FT MOD_RES 3048 3048 Phosphoserine.
FT MOD_RES 3094 3094 Phosphoserine.
FT MOD_RES 3119 3119 Phosphoserine.
FT MOD_RES 3122 3122 Phosphoserine.
FT MOD_RES 3150 3150 Phosphoserine.
FT MOD_RES 3175 3175 Phosphoserine.
FT MOD_RES 3179 3179 Phosphoserine.
FT MOD_RES 3207 3207 Cysteine methyl ester (Probable).
FT LIPID 3207 3207 S-farnesyl cysteine.
FT VARIANT 250 250 Q -> L (in dbSNP:rs1050065).
FT /FTId=VAR_055049.
FT VARIANT 272 272 D -> G (in dbSNP:rs1050066).
FT /FTId=VAR_055050.
FT VARIANT 300 300 R -> C (in dbSNP:rs17023281).
FT /FTId=VAR_034712.
FT VARIANT 494 494 H -> Q (in dbSNP:rs2070065).
FT /FTId=VAR_034713.
FT VARIANT 701 701 M -> V (in dbSNP:rs3795524).
FT /FTId=VAR_034714.
FT VARIANT 754 754 Q -> E (in dbSNP:rs3795523).
FT /FTId=VAR_034715.
FT VARIANT 815 815 R -> H (in dbSNP:rs3795522).
FT /FTId=VAR_034716.
FT VARIANT 1018 1018 Y -> D (in dbSNP:rs3795519).
FT /FTId=VAR_034717.
FT VARIANT 1033 1033 G -> R (in dbSNP:rs3795518).
FT /FTId=VAR_034718.
FT VARIANT 1105 1105 T -> I (in dbSNP:rs12067133).
FT /FTId=VAR_034719.
FT VARIANT 1412 1412 L -> S (in dbSNP:rs3795517).
FT /FTId=VAR_034720.
FT VARIANT 1515 1515 A -> T (in dbSNP:rs2666839).
FT /FTId=VAR_034721.
FT VARIANT 1516 1611 Missing.
FT /FTId=VAR_036701.
FT VARIANT 1539 1539 K -> R (in dbSNP:rs3795514).
FT /FTId=VAR_034722.
FT VARIANT 1864 1864 D -> N (in dbSNP:rs3748692).
FT /FTId=VAR_055638.
FT VARIANT 2011 2011 E -> A (in dbSNP:rs3790647).
FT /FTId=VAR_034723.
FT VARIANT 3202 3202 N -> K (in dbSNP:rs7289).
FT /FTId=VAR_014839.
FT CONFLICT 16 16 A -> T (in Ref. 1; AAA82889).
FT CONFLICT 48 48 L -> P (in Ref. 1; AAA82889 and 2;
FT AAA82935).
FT CONFLICT 52 52 K -> T (in Ref. 1; AAA82889 and 2;
FT AAA82935).
FT CONFLICT 611 611 Missing (in Ref. 2; AAA82935).
FT CONFLICT 1811 1811 V -> L (in Ref. 2; AAA82935).
FT CONFLICT 2242 2243 ER -> DG (in Ref. 4; AAA86889).
FT CONFLICT 2335 2335 L -> Q (in Ref. 4; AAA86889).
FT CONFLICT 2492 2492 N -> D (in Ref. 1; AAA82889 and 4;
FT AAA86889).
FT CONFLICT 2545 2561 ELNERVAALHNDQEACK -> SSMREWQPCIMTKKPVS
FT (in Ref. 4; AAA86889).
FT CONFLICT 3039 3039 R -> G (in Ref. 1; AAA82889, 2; AAA82935
FT and 4; AAA86889).
SQ SEQUENCE 3210 AA; 367764 MW; FF20F99216257BAD CRC64;
MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT
EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR
CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR
LEAEVKALQA KKASQTLPQA TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD
FSASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR
LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKYTAL
EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQMKAR
LTQELQQAKN MHNVLQAELD KLTSVKQQLE NNLEEFKQKL CRAEQAFQAS QIKENELRRS
MEEMKKENNL LKSHSEQKAR EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL
QEKINQQENS LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE
YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY MELQQKAEFS DQKHQKEIEN
MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH
QRSLLAFDQQ PAMHHSFANI IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE
SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET LSLEKKEMSS
IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ
EKLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK
EHQEFLTKLA FAEERNQNLM LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN
KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE
ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL QDMQSQEISG
LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL NELEKICEIL QAEKYELVTE
LNDSRSECIT ATRKMAEEVG KLLNEVKILN DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS
LAPLDESNSY EHLTLSDKEV QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD
SLKAENLVLS TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL
EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR NFQGDLVKEM
QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG DMSLLSNLEG VVSANQCSVD
EVFCSSLQEE NLTRKETPSA PAKGVEELES LCEVYRQSLE KLEEKMESQG IMKNKEIQEL
EQLLSSERQE LDCLRKQYLS ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ
LQGLDLSSRS LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL
DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP NALVPMDFLG
NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM KELDSKLHLQ EVQLMTKIEA
CIELEKIVGE LKKENSDLSE KLEYFSCDHQ ELLQRVETSE GLNSDLEMHA DKSSREDIGD
NVAKVNDSWK ERFLDVENEL SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK
VIVCLEEELS VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV
AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL ENQIAQLNKE
KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA LRLSSTQEEV HQLRRGIEKL
RVRIEADEKK QLHIAEKLKE RERENDSLKD KVENLERELQ MSEENQELVI LDAENSKAEV
ETLKTQIEEM ARSLKVFELD LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE
QAEIQIKEES KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE
KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH AALEAENSKG
EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE QERISELEII NSSFENILQE
KEQEKVQMKE KSSTAMEMLQ TQLKELNERV AALHNDQEAC KAKEQNLSSQ VECLELEKAQ
LLQGLDEAKN NYIVLQSSVN GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV
EGEHQLWKEQ NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK
MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL EEIKSSKDQL
KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH EAEKKHQALL LDTNKQYEVE
IQTYREKLTS KEECLSSQKL EIDLLKSSKE ELNNSLKATT QILEELKKTK MDNLKYVNQL
KKENERAQGK MKLLIKSCKQ LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK
ELKETLEEKT KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG
PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS KKSKKAVMSG
IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR TTMATRTSPR LAAQKLALSP
LSLGKENLAE SSKPTAGGSR SQKVKVAQRS PVDSGTILRE PTTKSVPVNN LPERSPTDSP
REGLRVKRGR LVPSPKAGLE SNGSENCKVQ
//
ID CENPF_HUMAN Reviewed; 3210 AA.
AC P49454; Q13171; Q13246; Q5VVM7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-AUG-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Centromere protein F;
DE Short=CENP-F;
DE AltName: Full=AH antigen;
DE AltName: Full=Kinetochore protein CENPF;
DE AltName: Full=Mitosin;
DE Flags: Precursor;
GN Name=CENPF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND VARIANTS LEU-250; GLY-272 AND LYS-3202.
RC TISSUE=Mammary carcinoma;
RX PubMed=7542657; DOI=10.1083/jcb.130.3.507;
RA Liao H., Winkfein R.J., Mack G., Rattner J.B., Yen T.J.;
RT "CENP-F is a protein of the nuclear matrix that assembles onto
RT kinetochores at late G2 and is rapidly degraded after mitosis.";
RL J. Cell Biol. 130:507-518(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1,
RP SUBCELLULAR LOCATION, AND VARIANTS 1516-VAL--VAL-1611 DEL AND
RP LYS-3202.
RX PubMed=7651420;
RA Zhu X., Mancini M.A., Chang K.-H., Liu C.-Y., Chen C.-F., Shan B.,
RA Jones D., Yang-Feng T.L., Lee W.-H.;
RT "Characterization of a novel 350-kilodalton nuclear phosphoprotein
RT that is specifically involved in mitotic-phase progression.";
RL Mol. Cell. Biol. 15:5017-5029(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT
RP 1516-VAL--VAL-1611.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT
RP 1516-VAL--VAL-1611.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2194-3210, SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, AND VARIANT LYS-3202.
RX PubMed=7612011; DOI=10.1006/bbrc.1995.1959;
RA Li Q., Ke Y., Kapp J.A., Fertig N., Medsger T.A. Jr., Joshi H.C.;
RT "A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal
RT domain sufficient for nuclear localization.";
RL Biochem. Biophys. Res. Commun. 212:220-228(1995).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=7642639; DOI=10.1074/jbc.270.33.19545;
RA Zhu X., Chang K.-H., He D., Mancini M.A., Brinkley W.R., Lee W.-H.;
RT "The C-terminus of mitosin is essential for its nuclear localization,
RT centromere/kinetochore targeting, and dimerization.";
RL J. Biol. Chem. 270:19545-19550(1995).
RN [7]
RP INTERACTION WITH BUBR1 AND CENPE, AND SUBCELLULAR LOCATION.
RX PubMed=9763420; DOI=10.1083/jcb.143.1.49;
RA Chan G.K.T., Schaar B.T., Yen T.J.;
RT "Characterization of the kinetochore binding domain of CENP-E reveals
RT interactions with the kinetochore proteins CENP-F and hBUBR1.";
RL J. Cell Biol. 143:49-63(1998).
RN [8]
RP ISOPRENYLATION AT CYS-3207.
RX PubMed=10852915; DOI=10.1074/jbc.M003469200;
RA Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L.,
RA Bishop W.R., Kirschmeier P.;
RT "Farnesyl transferase inhibitors block the farnesylation of CENP-E and
RT CENP-F and alter the association of CENP-E with the microtubules.";
RL J. Biol. Chem. 275:30451-30457(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12974617; DOI=10.1038/sj.cr.7290172;
RA Yang Z.Y., Guo J., Li N., Qian M., Wang S.N., Zhu X.L.;
RT "Mitosin/CENP-F is a conserved kinetochore protein subjected to
RT cytoplasmic dynein-mediated poleward transport.";
RL Cell Res. 13:275-283(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747 AND SER-1750, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP FUNCTION, INTERACTION WITH NDEL1 AND NDE1, AND SUBCELLULAR LOCATION.
RX PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
RA Vergnolle M.A.S., Taylor S.S.;
RT "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
RT complexes.";
RL Curr. Biol. 17:1173-1179(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3150, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-144; SER-834;
RP SER-1248; SER-1747; SER-1748; SER-1750; SER-2512; SER-2513; SER-2996;
RP SER-3007; SER-3119; SER-3122; SER-3150; SER-3175 AND SER-3179, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996 AND SER-3007, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2875, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; THR-154; TYR-158;
RP SER-276; SER-773; SER-783; SER-821; SER-876; SER-1248; SER-1255;
RP SER-1259; SER-1747; SER-1750; SER-1988; SER-2513; SER-2996; SER-3007;
RP SER-3018; THR-3045; SER-3048; SER-3094; SER-3119; SER-3122; SER-3150;
RP SER-3175 AND SER-3179, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119 AND SER-3150, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for kinetochore function and chromosome
CC segregation in mitosis. Required for kinetochore localization of
CC dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma
CC membrane by acting as a link between recycling vesicles and the
CC microtubule network though its association with STX4 and SNAP25.
CC Acts as a potential inhibitor of pocket protein-mediated cellular
CC processes during development by regulating the activity of RB
CC proteins during cell division and proliferation. May play a
CC regulatory or permissive role in the normal embryonic
CC cardiomyocyte cell cycle and in promoting continued mitosis in
CC transformed, abnormally dividing neonatal cardiomyocytes.
CC Interaction with RB directs embryonic stem cells toward a cardiac
CC lineage. Involved in the regulation of DNA synthesis and hence
CC cell cycle progression, via its C-terminus. Has a potential role
CC regulating skeletal myogenesis and in cell differentiation in
CC embryogenesis. Involved in dendritic cell regulation of T-cell
CC immunity against chlamydia.
CC -!- SUBUNIT: Interacts with and STX4 (via C-terminus) (By similarity).
CC Interacts (via N-terminus) with RBL1, RBL2 and SNAP25 (By
CC similarity). Self-associates. Interacts with CENP-E and BUBR1 (via
CC C-terminus). Interacts (via C-terminus) with NDE1, NDEL1 and RB1.
CC -!- INTERACTION:
CC Q9GZM8:NDEL1; NbExp=5; IntAct=EBI-968343, EBI-928842;
CC Q8WUM0:NUP133; NbExp=2; IntAct=EBI-968343, EBI-295695;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus
CC matrix. Chromosome, centromere, kinetochore. Cytoplasm,
CC cytoskeleton, spindle. Note=Relocalizes to the
CC kinetochore/centromere (coronal surface of the outer plate) and
CC the spindle during mitosis. Observed in nucleus during interphase
CC but not in the nucleolus. At metaphase becomes localized to areas
CC including kinetochore and mitotic apparatus as well as cytoplasm.
CC By telophase, is concentrated within the intracellular bridge at
CC either side of the mid-body.
CC -!- DEVELOPMENTAL STAGE: Gradually accumulates during the cell cycle,
CC reaching peak levels in G2 and M phase, and is rapidly degraded
CC upon completion of mitosis.
CC -!- PTM: Hyperphosphorylated during mitosis.
CC -!- SIMILARITY: Belongs to the centromere protein F family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CENPFID40057ch1q41.html";
CC -----------------------------------------------------------------------
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DR EMBL; U19769; AAA82889.1; -; mRNA.
DR EMBL; U30872; AAA82935.1; -; mRNA.
DR EMBL; AL445666; CAH71810.1; -; Genomic_DNA.
DR EMBL; AL445305; CAH71810.1; JOINED; Genomic_DNA.
DR EMBL; AL445305; CAH73032.1; -; Genomic_DNA.
DR EMBL; AL445666; CAH73032.1; JOINED; Genomic_DNA.
DR EMBL; BC172232; AAI72232.1; -; mRNA.
DR EMBL; U25725; AAA86889.1; -; mRNA.
DR PIR; PC4035; PC4035.
DR RefSeq; NP_057427.3; NM_016343.3.
DR UniGene; Hs.497741; -.
DR IntAct; P49454; 11.
DR MINT; MINT-2803614; -.
DR STRING; 9606.ENSP00000355922; -.
DR PhosphoSite; P49454; -.
DR DMDM; 156630875; -.
DR PaxDb; P49454; -.
DR PRIDE; P49454; -.
DR Ensembl; ENST00000366955; ENSP00000355922; ENSG00000117724.
DR GeneID; 1063; -.
DR KEGG; hsa:1063; -.
DR UCSC; uc001hkm.3; human.
DR CTD; 1063; -.
DR GeneCards; GC01P214776; -.
DR H-InvDB; HIX0028827; -.
DR HGNC; HGNC:1857; CENPF.
DR HPA; CAB009581; -.
DR MIM; 600236; gene.
DR neXtProt; NX_P49454; -.
DR PharmGKB; PA26401; -.
DR eggNOG; NOG12793; -.
DR HOVERGEN; HBG050893; -.
DR KO; K11499; -.
DR OrthoDB; EOG7FV3PD; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; CENPF; human.
DR GeneWiki; CENPF; -.
DR GenomeRNAi; 1063; -.
DR NextBio; 4446; -.
DR PRO; PR:P49454; -.
DR Bgee; P49454; -.
DR CleanEx; HS_CENPF; -.
DR Genevestigator; P49454; -.
DR GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0045502; F:dynein binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; IDA:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000085; P:mitotic G2 phase; IMP:UniProtKB.
DR GO; GO:0000087; P:mitotic M phase; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; NAS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; NAS:UniProtKB.
DR InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR InterPro; IPR018463; Centromere_CenpF_N.
DR Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR Pfam; PF10473; CENP-F_leu_zip; 3.
DR Pfam; PF10481; CENP-F_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; DNA synthesis; Kinetochore;
KW Lipoprotein; Methylation; Mitosis; Myogenesis; Nucleus;
KW Phosphoprotein; Polymorphism; Prenylation; Reference proteome; Repeat.
FT CHAIN 1 3207 Centromere protein F.
FT /FTId=PRO_0000089477.
FT PROPEP 3208 3210 Removed in mature form (Probable).
FT /FTId=PRO_0000396744.
FT REPEAT 1435 1530 1-1.
FT REPEAT 1531 1626 1-2.
FT REPEAT 2207 2386 2-1.
FT REPEAT 2389 2568 2-2.
FT REGION 1 481 Interaction with SNAP25 and required for
FT localization to the cytoplasm (By
FT similarity).
FT REGION 1435 1626 2 X 96 AA approximate tandem repeats.
FT REGION 2122 2447 Interaction with NDE1 and NDEL1.
FT REGION 2207 2568 2 X 177 AA tandem repeats.
FT REGION 2488 3113 Sufficient for centromere localization.
FT REGION 2488 2925 Sufficient for self-association.
FT REGION 2927 3113 Sufficient for nuclear localization.
FT COILED 14 197 Potential.
FT COILED 273 769 Potential.
FT COILED 823 1328 Potential.
FT COILED 1642 1746 Potential.
FT COILED 1862 2987 Potential.
FT MOTIF 3015 3032 Nuclear localization signal (Potential).
FT MOD_RES 106 106 Phosphoserine.
FT MOD_RES 144 144 Phosphothreonine.
FT MOD_RES 151 151 Phosphothreonine.
FT MOD_RES 154 154 Phosphothreonine.
FT MOD_RES 158 158 Phosphotyrosine.
FT MOD_RES 276 276 Phosphoserine.
FT MOD_RES 773 773 Phosphoserine.
FT MOD_RES 783 783 Phosphoserine.
FT MOD_RES 821 821 Phosphoserine.
FT MOD_RES 834 834 Phosphoserine.
FT MOD_RES 876 876 Phosphoserine.
FT MOD_RES 1248 1248 Phosphoserine.
FT MOD_RES 1255 1255 Phosphoserine.
FT MOD_RES 1259 1259 Phosphoserine.
FT MOD_RES 1747 1747 Phosphoserine.
FT MOD_RES 1748 1748 Phosphoserine.
FT MOD_RES 1750 1750 Phosphoserine.
FT MOD_RES 1988 1988 Phosphoserine.
FT MOD_RES 2512 2512 Phosphoserine.
FT MOD_RES 2513 2513 Phosphoserine.
FT MOD_RES 2875 2875 N6-acetyllysine.
FT MOD_RES 2996 2996 Phosphoserine.
FT MOD_RES 3007 3007 Phosphoserine.
FT MOD_RES 3018 3018 Phosphoserine.
FT MOD_RES 3045 3045 Phosphothreonine.
FT MOD_RES 3048 3048 Phosphoserine.
FT MOD_RES 3094 3094 Phosphoserine.
FT MOD_RES 3119 3119 Phosphoserine.
FT MOD_RES 3122 3122 Phosphoserine.
FT MOD_RES 3150 3150 Phosphoserine.
FT MOD_RES 3175 3175 Phosphoserine.
FT MOD_RES 3179 3179 Phosphoserine.
FT MOD_RES 3207 3207 Cysteine methyl ester (Probable).
FT LIPID 3207 3207 S-farnesyl cysteine.
FT VARIANT 250 250 Q -> L (in dbSNP:rs1050065).
FT /FTId=VAR_055049.
FT VARIANT 272 272 D -> G (in dbSNP:rs1050066).
FT /FTId=VAR_055050.
FT VARIANT 300 300 R -> C (in dbSNP:rs17023281).
FT /FTId=VAR_034712.
FT VARIANT 494 494 H -> Q (in dbSNP:rs2070065).
FT /FTId=VAR_034713.
FT VARIANT 701 701 M -> V (in dbSNP:rs3795524).
FT /FTId=VAR_034714.
FT VARIANT 754 754 Q -> E (in dbSNP:rs3795523).
FT /FTId=VAR_034715.
FT VARIANT 815 815 R -> H (in dbSNP:rs3795522).
FT /FTId=VAR_034716.
FT VARIANT 1018 1018 Y -> D (in dbSNP:rs3795519).
FT /FTId=VAR_034717.
FT VARIANT 1033 1033 G -> R (in dbSNP:rs3795518).
FT /FTId=VAR_034718.
FT VARIANT 1105 1105 T -> I (in dbSNP:rs12067133).
FT /FTId=VAR_034719.
FT VARIANT 1412 1412 L -> S (in dbSNP:rs3795517).
FT /FTId=VAR_034720.
FT VARIANT 1515 1515 A -> T (in dbSNP:rs2666839).
FT /FTId=VAR_034721.
FT VARIANT 1516 1611 Missing.
FT /FTId=VAR_036701.
FT VARIANT 1539 1539 K -> R (in dbSNP:rs3795514).
FT /FTId=VAR_034722.
FT VARIANT 1864 1864 D -> N (in dbSNP:rs3748692).
FT /FTId=VAR_055638.
FT VARIANT 2011 2011 E -> A (in dbSNP:rs3790647).
FT /FTId=VAR_034723.
FT VARIANT 3202 3202 N -> K (in dbSNP:rs7289).
FT /FTId=VAR_014839.
FT CONFLICT 16 16 A -> T (in Ref. 1; AAA82889).
FT CONFLICT 48 48 L -> P (in Ref. 1; AAA82889 and 2;
FT AAA82935).
FT CONFLICT 52 52 K -> T (in Ref. 1; AAA82889 and 2;
FT AAA82935).
FT CONFLICT 611 611 Missing (in Ref. 2; AAA82935).
FT CONFLICT 1811 1811 V -> L (in Ref. 2; AAA82935).
FT CONFLICT 2242 2243 ER -> DG (in Ref. 4; AAA86889).
FT CONFLICT 2335 2335 L -> Q (in Ref. 4; AAA86889).
FT CONFLICT 2492 2492 N -> D (in Ref. 1; AAA82889 and 4;
FT AAA86889).
FT CONFLICT 2545 2561 ELNERVAALHNDQEACK -> SSMREWQPCIMTKKPVS
FT (in Ref. 4; AAA86889).
FT CONFLICT 3039 3039 R -> G (in Ref. 1; AAA82889, 2; AAA82935
FT and 4; AAA86889).
SQ SEQUENCE 3210 AA; 367764 MW; FF20F99216257BAD CRC64;
MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT
EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR
CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR
LEAEVKALQA KKASQTLPQA TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD
FSASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR
LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKYTAL
EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQMKAR
LTQELQQAKN MHNVLQAELD KLTSVKQQLE NNLEEFKQKL CRAEQAFQAS QIKENELRRS
MEEMKKENNL LKSHSEQKAR EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL
QEKINQQENS LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE
YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY MELQQKAEFS DQKHQKEIEN
MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH
QRSLLAFDQQ PAMHHSFANI IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE
SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET LSLEKKEMSS
IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ
EKLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK
EHQEFLTKLA FAEERNQNLM LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN
KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE
ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL QDMQSQEISG
LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL NELEKICEIL QAEKYELVTE
LNDSRSECIT ATRKMAEEVG KLLNEVKILN DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS
LAPLDESNSY EHLTLSDKEV QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD
SLKAENLVLS TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL
EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR NFQGDLVKEM
QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG DMSLLSNLEG VVSANQCSVD
EVFCSSLQEE NLTRKETPSA PAKGVEELES LCEVYRQSLE KLEEKMESQG IMKNKEIQEL
EQLLSSERQE LDCLRKQYLS ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ
LQGLDLSSRS LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL
DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP NALVPMDFLG
NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM KELDSKLHLQ EVQLMTKIEA
CIELEKIVGE LKKENSDLSE KLEYFSCDHQ ELLQRVETSE GLNSDLEMHA DKSSREDIGD
NVAKVNDSWK ERFLDVENEL SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK
VIVCLEEELS VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV
AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL ENQIAQLNKE
KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA LRLSSTQEEV HQLRRGIEKL
RVRIEADEKK QLHIAEKLKE RERENDSLKD KVENLERELQ MSEENQELVI LDAENSKAEV
ETLKTQIEEM ARSLKVFELD LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE
QAEIQIKEES KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE
KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH AALEAENSKG
EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE QERISELEII NSSFENILQE
KEQEKVQMKE KSSTAMEMLQ TQLKELNERV AALHNDQEAC KAKEQNLSSQ VECLELEKAQ
LLQGLDEAKN NYIVLQSSVN GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV
EGEHQLWKEQ NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK
MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL EEIKSSKDQL
KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH EAEKKHQALL LDTNKQYEVE
IQTYREKLTS KEECLSSQKL EIDLLKSSKE ELNNSLKATT QILEELKKTK MDNLKYVNQL
KKENERAQGK MKLLIKSCKQ LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK
ELKETLEEKT KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG
PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS KKSKKAVMSG
IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR TTMATRTSPR LAAQKLALSP
LSLGKENLAE SSKPTAGGSR SQKVKVAQRS PVDSGTILRE PTTKSVPVNN LPERSPTDSP
REGLRVKRGR LVPSPKAGLE SNGSENCKVQ
//
MIM
600236
*RECORD*
*FIELD* NO
600236
*FIELD* TI
*600236 CENTROMERIC PROTEIN F; CENPF
*FIELD* TX
Rattner et al. (1993) identified a human kinetochore protein with a
read moremolecular weight of approximately 400 kD. Designated centromeric protein
F, it was only transiently associated with kinetochores from the onset
of mitosis to metaphase.
Liao et al. (1995) reported the cDNA sequence of CENPF, together with
its expression and localization patterns at different stages of the HeLa
cell cycle. CENPF is a protein of the nuclear matrix that gradually
accumulates during the cell cycle until it reaches peak levels in G2 and
M phase cells and is rapidly degraded upon completion of mitosis. CENPF
is first detected at the prekinetochore complex during late G2, and by
prophase is clearly detectable as paired foci that correspond to all the
centromeres. During mitosis, CENPF is associated with kinetochores from
prometaphase until early anaphase and then is detected at the spindle
midzone throughout the remainder of anaphase. By telophase, CENPF is
concentrated within the intracellular bridge at either side of the
midbody. The predicted structure of the 367-kD CENPF protein consists of
two 1,600-amino acid-long coil domains that flank a central flexible
core.
Using CENPF cDNA in fluorescence in situ hybridization, Testa et al.
(1994) mapped the CENPF gene to 1q32-q41. By interspecific backcross
analysis, Fowler et al. (1998) mapped the mouse Cenpf gene to the distal
region of chromosome 1.
*FIELD* RF
1. Fowler, K. J.; Saffery, R.; Irvine, D. V.; Trowell, H. E.; Choo,
K. H. A.: Mouse centromere protein F (Cenpf) gene maps to the distal
region of chromosome 1 by interspecific backcross analysis. Cytogenet.
Cell Genet. 82: 180-181, 1998.
2. Liao, H.; Winkfein, R. J.; Mack, G.; Rattner, J. B.; Yen, T. J.
: CENP-F is a protein of the nuclear matrix that assembles onto kinetochores
at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130:
507-518, 1995.
3. Rattner, J. B.; Rao, A.; Fritzler, M. J.; Valencia, D. W.; Yen,
T. J.: CENP-F is a ca 400 kDa kinetochore protein that exhibits a
cell-cycle dependent localization. Cell Motil. Cytoskeleton 26:
214-226, 1993.
4. Testa, J. R.; Zhou, J.; Bell, D. W.; Yen, T. J.: Chromosomal localization
of the genes encoding the kinetochore proteins CENPE and CENPF to
human chromosomes 4q24-q25 and 1q32-q41, respectively, by fluorescence
in situ hybridization. Genomics 23: 691-693, 1994.
*FIELD* CN
Carol A. Bocchini - updated: 3/24/1999
*FIELD* CD
Victor A. McKusick: 12/13/1994
*FIELD* ED
carol: 04/27/2000
terry: 3/25/1999
carol: 3/24/1999
jamie: 1/17/1997
mark: 10/13/1995
carol: 12/13/1994
*RECORD*
*FIELD* NO
600236
*FIELD* TI
*600236 CENTROMERIC PROTEIN F; CENPF
*FIELD* TX
Rattner et al. (1993) identified a human kinetochore protein with a
read moremolecular weight of approximately 400 kD. Designated centromeric protein
F, it was only transiently associated with kinetochores from the onset
of mitosis to metaphase.
Liao et al. (1995) reported the cDNA sequence of CENPF, together with
its expression and localization patterns at different stages of the HeLa
cell cycle. CENPF is a protein of the nuclear matrix that gradually
accumulates during the cell cycle until it reaches peak levels in G2 and
M phase cells and is rapidly degraded upon completion of mitosis. CENPF
is first detected at the prekinetochore complex during late G2, and by
prophase is clearly detectable as paired foci that correspond to all the
centromeres. During mitosis, CENPF is associated with kinetochores from
prometaphase until early anaphase and then is detected at the spindle
midzone throughout the remainder of anaphase. By telophase, CENPF is
concentrated within the intracellular bridge at either side of the
midbody. The predicted structure of the 367-kD CENPF protein consists of
two 1,600-amino acid-long coil domains that flank a central flexible
core.
Using CENPF cDNA in fluorescence in situ hybridization, Testa et al.
(1994) mapped the CENPF gene to 1q32-q41. By interspecific backcross
analysis, Fowler et al. (1998) mapped the mouse Cenpf gene to the distal
region of chromosome 1.
*FIELD* RF
1. Fowler, K. J.; Saffery, R.; Irvine, D. V.; Trowell, H. E.; Choo,
K. H. A.: Mouse centromere protein F (Cenpf) gene maps to the distal
region of chromosome 1 by interspecific backcross analysis. Cytogenet.
Cell Genet. 82: 180-181, 1998.
2. Liao, H.; Winkfein, R. J.; Mack, G.; Rattner, J. B.; Yen, T. J.
: CENP-F is a protein of the nuclear matrix that assembles onto kinetochores
at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130:
507-518, 1995.
3. Rattner, J. B.; Rao, A.; Fritzler, M. J.; Valencia, D. W.; Yen,
T. J.: CENP-F is a ca 400 kDa kinetochore protein that exhibits a
cell-cycle dependent localization. Cell Motil. Cytoskeleton 26:
214-226, 1993.
4. Testa, J. R.; Zhou, J.; Bell, D. W.; Yen, T. J.: Chromosomal localization
of the genes encoding the kinetochore proteins CENPE and CENPF to
human chromosomes 4q24-q25 and 1q32-q41, respectively, by fluorescence
in situ hybridization. Genomics 23: 691-693, 1994.
*FIELD* CN
Carol A. Bocchini - updated: 3/24/1999
*FIELD* CD
Victor A. McKusick: 12/13/1994
*FIELD* ED
carol: 04/27/2000
terry: 3/25/1999
carol: 3/24/1999
jamie: 1/17/1997
mark: 10/13/1995
carol: 12/13/1994