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Database: UniProt
Entry: CENPF_HUMAN
LinkDB: CENPF_HUMAN
Original site: CENPF_HUMAN 
ID   CENPF_HUMAN             Reviewed;        3114 AA.
AC   P49454; Q13171; Q13246; Q5VVM7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 3.
DT   10-FEB-2021, entry version 205.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND VARIANTS LEU-250; GLY-272 AND LYS-3106.
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 kinetochores
RT   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, SUBCELLULAR
RP   LOCATION, AND VARIANT LYS-3106.
RX   PubMed=7651420; DOI=10.1128/mcb.15.9.5017;
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 that is
RT   specifically involved in mitotic-phase progression.";
RL   Mol. Cell. Biol. 15:5017-5029(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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].
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2098-3114, SUBCELLULAR LOCATION, NUCLEAR
RP   LOCALIZATION SIGNAL, AND VARIANT LYS-3106.
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 domain
RT   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-3111.
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 cytoplasmic
RT   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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651 AND SER-1654, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT   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-3023, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   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, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   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-3054, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   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-1651; SER-1652; SER-1654; SER-2416; SER-2417; SER-2900;
RP   SER-2911; SER-3023; SER-3026; SER-3054; SER-3079 AND SER-3083, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2900 AND SER-2911, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-2779, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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; SER-1259;
RP   SER-1651; SER-1654; SER-1892; SER-2417; SER-2900; SER-2911; SER-2922;
RP   THR-2949; SER-2952; SER-2998; SER-3023; SER-3026; SER-3054; SER-3079 AND
RP   SER-3083, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   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., Buerckstuemmer T.,
RA   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-3023 AND SER-3054, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-154; SER-242;
RP   SER-276; SER-821; SER-838; SER-876; SER-1255; SER-1651; SER-1654; SER-1726;
RP   THR-1862; SER-1868; SER-2936; THR-2949; SER-2998; SER-3023; SER-3054 AND
RP   SER-3079, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   INVOLVEMENT IN STROMS.
RX   PubMed=25564561; DOI=10.1136/jmedgenet-2014-102691;
RA   Waters A.M., Asfahani R., Carroll P., Bicknell L., Lescai F., Bright A.,
RA   Chanudet E., Brooks A., Christou-Savina S., Osman G., Walsh P.,
RA   Bacchelli C., Chapgier A., Vernay B., Bader D.M., Deshpande C.,
RA   O'Sullivan M., Ocaka L., Stanescu H., Stewart H.S., Hildebrandt F.,
RA   Otto E., Johnson C.A., Szymanska K., Katsanis N., Davis E., Kleta R.,
RA   Hubank M., Doxsey S., Jackson A., Stupka E., Winey M., Beales P.L.;
RT   "The kinetochore protein, CENPF, is mutated in human ciliopathy and
RT   microcephaly phenotypes.";
RL   J. Med. Genet. 52:147-156(2015).
RN   [25]
RP   INVOLVEMENT IN STROMS.
RX   PubMed=26820108; DOI=10.1002/humu.22960;
RA   Filges I., Bruder E., Brandal K., Meier S., Undlien D.E., Waage T.R.,
RA   Hoesli I., Schubach M., de Beer T., Sheng Y., Hoeller S., Schulzke S.,
RA   Roesby O., Miny P., Tercanli S., Oppedal T., Meyer P., Selmer K.K.,
RA   Stroemme P.;
RT   "Stroemme Syndrome Is a Ciliary Disorder Caused by Mutations in CENPF.";
RL   Hum. Mutat. 37:359-363(2016).
CC   -!- FUNCTION: Required for kinetochore function and chromosome segregation
CC       in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1
CC       and NDEL1. Regulates recycling of the plasma membrane by acting as a
CC       link between recycling vesicles and the microtubule network though its
CC       association with STX4 and SNAP25. Acts as a potential inhibitor of
CC       pocket protein-mediated cellular processes during development by
CC       regulating the activity of RB proteins during cell division and
CC       proliferation. May play a regulatory or permissive role in the normal
CC       embryonic cardiomyocyte cell cycle and in promoting continued mitosis
CC       in 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 cell
CC       cycle progression, via its C-terminus. Has a potential role regulating
CC       skeletal myogenesis and in cell differentiation in embryogenesis.
CC       Involved in dendritic cell regulation of T-cell immunity against
CC       chlamydia. {ECO:0000269|PubMed:12974617, ECO:0000269|PubMed:17600710,
CC       ECO:0000269|PubMed:7542657, ECO:0000269|PubMed:7651420}.
CC   -!- SUBUNIT: Interacts with and STX4 (via C-terminus) (By similarity).
CC       Interacts (via N-terminus) with RBL1, RBL2 and SNAP25 (By similarity).
CC       Self-associates. Interacts with CENP-E and BUBR1 (via C-terminus).
CC       Interacts (via C-terminus) with NDE1, NDEL1 and RB1. {ECO:0000250,
CC       ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:7642639,
CC       ECO:0000269|PubMed:7651420, ECO:0000269|PubMed:9763420}.
CC   -!- INTERACTION:
CC       P49454; Q9GZM8: NDEL1; NbExp=6; IntAct=EBI-968343, EBI-928842;
CC       P49454; Q8WUM0: NUP133; NbExp=2; IntAct=EBI-968343, EBI-295695;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus matrix.
CC       Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle.
CC       Note=Relocalizes to the kinetochore/centromere (coronal surface of the
CC       outer plate) and the spindle during mitosis. Observed in nucleus during
CC       interphase but not in the nucleolus. At metaphase becomes localized to
CC       areas including kinetochore and mitotic apparatus as well as cytoplasm.
CC       By telophase, is concentrated within the intracellular bridge at either
CC       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 upon
CC       completion of mitosis. {ECO:0000269|PubMed:7542657}.
CC   -!- PTM: Hyperphosphorylated during mitosis.
CC   -!- DISEASE: Stromme syndrome (STROMS) [MIM:243605]: An autosomal recessive
CC       congenital disorder characterized by intestinal atresia, ocular
CC       anomalies, microcephaly, and renal and cardiac abnormalities in some
CC       patients. The disease has features of a ciliopathy, and lethality in
CC       early childhood is observed in severe cases.
CC       {ECO:0000269|PubMed:25564561, ECO:0000269|PubMed:26820108}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the centromere protein F family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA82889.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CENPFID40057ch1q41.html";
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DR   EMBL; U19769; AAA82889.1; ALT_SEQ; mRNA.
DR   EMBL; U30872; AAA82935.1; -; mRNA.
DR   EMBL; AL445666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC172232; AAI72232.1; -; mRNA.
DR   EMBL; U25725; AAA86889.1; -; mRNA.
DR   CCDS; CCDS31023.1; -.
DR   PIR; PC4035; PC4035.
DR   RefSeq; NP_057427.3; NM_016343.3.
DR   RefSeq; XP_016855575.1; XM_017000086.1.
DR   SMR; P49454; -.
DR   BioGRID; 107492; 66.
DR   IntAct; P49454; 51.
DR   MINT; P49454; -.
DR   STRING; 9606.ENSP00000355922; -.
DR   CarbonylDB; P49454; -.
DR   iPTMnet; P49454; -.
DR   MetOSite; P49454; -.
DR   PhosphoSitePlus; P49454; -.
DR   BioMuta; CENPF; -.
DR   DMDM; 156630875; -.
DR   EPD; P49454; -.
DR   jPOST; P49454; -.
DR   MassIVE; P49454; -.
DR   MaxQB; P49454; -.
DR   PaxDb; P49454; -.
DR   PeptideAtlas; P49454; -.
DR   PRIDE; P49454; -.
DR   ProteomicsDB; 56015; -.
DR   Antibodypedia; 4038; 260 antibodies.
DR   Ensembl; ENST00000366955; ENSP00000355922; ENSG00000117724.
DR   GeneID; 1063; -.
DR   KEGG; hsa:1063; -.
DR   UCSC; uc001hkm.4; human.
DR   CTD; 1063; -.
DR   DisGeNET; 1063; -.
DR   GeneCards; CENPF; -.
DR   HGNC; HGNC:1857; CENPF.
DR   HPA; ENSG00000117724; Group enriched (bone marrow, lymphoid tissue).
DR   MalaCards; CENPF; -.
DR   MIM; 243605; phenotype.
DR   MIM; 600236; gene.
DR   neXtProt; NX_P49454; -.
DR   OpenTargets; ENSG00000117724; -.
DR   Orphanet; 444069; Lethal fetal brain malformation-duodenal atresia-bilateral renal hypoplasia syndrome.
DR   Orphanet; 506307; Stromme syndrome.
DR   PharmGKB; PA26401; -.
DR   VEuPathDB; HostDB:ENSG00000117724.12; -.
DR   eggNOG; ENOG502QVMD; Eukaryota.
DR   GeneTree; ENSGT00730000111187; -.
DR   HOGENOM; CLU_000551_0_0_1; -.
DR   InParanoid; P49454; -.
DR   OMA; YNAQLVQ; -.
DR   OrthoDB; 205405at2759; -.
DR   PhylomeDB; P49454; -.
DR   TreeFam; TF101133; -.
DR   PathwayCommons; P49454; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SIGNOR; P49454; -.
DR   BioGRID-ORCS; 1063; 61 hits in 892 CRISPR screens.
DR   ChiTaRS; CENPF; human.
DR   GeneWiki; CENPF; -.
DR   GenomeRNAi; 1063; -.
DR   Pharos; P49454; Tbio.
DR   PRO; PR:P49454; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P49454; protein.
DR   Bgee; ENSG00000117724; Expressed in ventricular zone and 168 other tissues.
DR   ExpressionAtlas; P49454; baseline and differential.
DR   Genevisible; P49454; HS.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0097539; C:ciliary transition fiber; IMP:GO_Central.
DR   GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; 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:0005819; C:spindle; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0001822; P:kidney development; IMP:GO_Central.
DR   GO; GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
DR   GO; GO:0051310; P:metaphase plate congression; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP: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-templated; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
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   GO; GO:0021591; P:ventricular system development; IMP:GO_Central.
DR   InterPro; IPR043513; Cenp-F.
DR   InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR   InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR   InterPro; IPR018463; Centromere_CenpF_N.
DR   PANTHER; PTHR18874; PTHR18874; 2.
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; Ciliopathy;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Differentiation; DNA synthesis; Kinetochore; Lipoprotein; Methylation;
KW   Mitosis; Myogenesis; Nucleus; Phosphoprotein; Prenylation;
KW   Primary ciliary dyskinesia; Reference proteome; Repeat.
FT   CHAIN           1..3111
FT                   /note="Centromere protein F"
FT                   /id="PRO_0000089477"
FT   PROPEP          3112..3114
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000396744"
FT   REPEAT          2111..2290
FT                   /note="1"
FT   REPEAT          2293..2472
FT                   /note="2"
FT   REGION          1..481
FT                   /note="Interaction with SNAP25 and required for
FT                   localization to the cytoplasm"
FT                   /evidence="ECO:0000250"
FT   REGION          2026..2351
FT                   /note="Interaction with NDE1 and NDEL1"
FT                   /evidence="ECO:0000269|PubMed:17600710"
FT   REGION          2111..2472
FT                   /note="2 X 177 AA tandem repeats"
FT   REGION          2392..3017
FT                   /note="Sufficient for centromere localization"
FT   REGION          2392..2829
FT                   /note="Sufficient for self-association"
FT   REGION          2831..3017
FT                   /note="Sufficient for nuclear localization"
FT   COILED          13..131
FT                   /evidence="ECO:0000255"
FT   COILED          280..685
FT                   /evidence="ECO:0000255"
FT   COILED          899..989
FT                   /evidence="ECO:0000255"
FT   COILED          1196..1244
FT                   /evidence="ECO:0000255"
FT   COILED          1549..1646
FT                   /evidence="ECO:0000255"
FT   COILED          1890..2078
FT                   /evidence="ECO:0000255"
FT   COILED          2107..2891
FT                   /evidence="ECO:0000255"
FT   MOTIF           2919..2936
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         144
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         158
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         834
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         1255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         1654
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1726
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1862
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1868
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         2416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         2417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         2779
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         2900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231"
FT   MOD_RES         2911
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231"
FT   MOD_RES         2922
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         2936
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         2949
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         2952
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         2998
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         3023
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17924679,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         3026
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         3054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18220336,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         3079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   MOD_RES         3083
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         3111
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           3111
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10852915"
FT   VARIANT         250
FT                   /note="Q -> L (in dbSNP:rs1050065)"
FT                   /evidence="ECO:0000269|PubMed:7542657"
FT                   /id="VAR_055049"
FT   VARIANT         272
FT                   /note="D -> G (in dbSNP:rs1050066)"
FT                   /evidence="ECO:0000269|PubMed:7542657"
FT                   /id="VAR_055050"
FT   VARIANT         300
FT                   /note="R -> C (in dbSNP:rs17023281)"
FT                   /id="VAR_034712"
FT   VARIANT         494
FT                   /note="H -> Q (in dbSNP:rs2070065)"
FT                   /id="VAR_034713"
FT   VARIANT         701
FT                   /note="M -> V (in dbSNP:rs3795524)"
FT                   /id="VAR_034714"
FT   VARIANT         754
FT                   /note="Q -> E (in dbSNP:rs3795523)"
FT                   /id="VAR_034715"
FT   VARIANT         815
FT                   /note="R -> H (in dbSNP:rs3795522)"
FT                   /id="VAR_034716"
FT   VARIANT         1018
FT                   /note="Y -> D (in dbSNP:rs3795519)"
FT                   /id="VAR_034717"
FT   VARIANT         1033
FT                   /note="G -> R (in dbSNP:rs3795518)"
FT                   /id="VAR_034718"
FT   VARIANT         1105
FT                   /note="T -> I (in dbSNP:rs12067133)"
FT                   /id="VAR_034719"
FT   VARIANT         1412
FT                   /note="L -> S (in dbSNP:rs3795517)"
FT                   /id="VAR_034720"
FT   VARIANT         1768
FT                   /note="D -> N (in dbSNP:rs3748692)"
FT                   /id="VAR_055638"
FT   VARIANT         1915
FT                   /note="E -> A (in dbSNP:rs3790647)"
FT                   /id="VAR_034723"
FT   VARIANT         3106
FT                   /note="N -> K (in dbSNP:rs7289)"
FT                   /evidence="ECO:0000269|PubMed:7542657,
FT                   ECO:0000269|PubMed:7612011, ECO:0000269|PubMed:7651420"
FT                   /id="VAR_014839"
FT   CONFLICT        16
FT                   /note="A -> T (in Ref. 1; AAA82889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="L -> P (in Ref. 1; AAA82889 and 2; AAA82935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="K -> T (in Ref. 1; AAA82889 and 2; AAA82935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611
FT                   /note="Missing (in Ref. 2; AAA82935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1515
FT                   /note="A -> V (in Ref. 1; AAA82889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1715
FT                   /note="V -> L (in Ref. 2; AAA82935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2146..2147
FT                   /note="ER -> DG (in Ref. 5; AAA86889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2239
FT                   /note="L -> Q (in Ref. 5; AAA86889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2396
FT                   /note="N -> D (in Ref. 1; AAA82889 and 5; AAA86889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2449..2465
FT                   /note="ELNERVAALHNDQEACK -> SSMREWQPCIMTKKPVS (in Ref. 5;
FT                   AAA86889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2943
FT                   /note="R -> G (in Ref. 1; AAA82889, 2; AAA82935 and 5;
FT                   AAA86889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3114 AA;  357527 MW;  1FC81972F947B375 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 LQEENLTRKE TPSAPAKGVE ELESLCEVYR
     QSLEKLEEKM ESQGIMKNKE IQELEQLLSS ERQELDCLRK QYLSENEQWQ QKLTSVTLEM
     ESKLAAEKKQ TEQLSLELEV ARLQLQGLDL SSRSLLGIDT EDAIQGRNES CDISKEHTSE
     TTERTPKHDV HQICDKDAQQ DLNLDIEKIT ETGAVKPTGE CSGEQSPDTN YEPPGEDKTQ
     GSSECISELS FSGPNALVPM DFLGNQEDIH NLQLRVKETS NENLRLLHVI EDRDRKVESL
     LNEMKELDSK LHLQEVQLMT KIEACIELEK IVGELKKENS DLSEKLEYFS CDHQELLQRV
     ETSEGLNSDL EMHADKSSRE DIGDNVAKVN DSWKERFLDV ENELSRIRSE KASIEHEALY
     LEADLEVVQT EKLCLEKDNE NKQKVIVCLE EELSVVTSER NQLRGELDTM SKKTTALDQL
     SEKMKEKTQE LESHQSECLH CIQVAEAEVK EKTELLQTLS SDVSELLKDK THLQEKLQSL
     EKDSQALSLT KCELENQIAQ LNKEKELLVK ESESLQARLS ESDYEKLNVS KALEAALVEK
     GEFALRLSST QEEVHQLRRG IEKLRVRIEA DEKKQLHIAE KLKEREREND SLKDKVENLE
     RELQMSEENQ ELVILDAENS KAEVETLKTQ IEEMARSLKV FELDLVTLRS EKENLTKQIQ
     EKQGQLSELD KLLSSFKSLL EEKEQAEIQI KEESKTAVEM LQNQLKELNE AVAALCGDQE
     IMKATEQSLD PPIEEEHQLR NSIEKLRARL EADEKKQLCV LQQLKESEHH ADLLKGRVEN
     LERELEIART NQEHAALEAE NSKGEVETLK AKIEGMTQSL RGLELDVVTI RSEKENLTNE
     LQKEQERISE LEIINSSFEN ILQEKEQEKV QMKEKSSTAM EMLQTQLKEL NERVAALHND
     QEACKAKEQN LSSQVECLEL EKAQLLQGLD EAKNNYIVLQ SSVNGLIQEV EDGKQKLEKK
     DEEISRLKNQ IQDQEQLVSK LSQVEGEHQL WKEQNLELRN LTVELEQKIQ VLQSKNASLQ
     DTLEVLQSSY KNLENELELT KMDKMSFVEK VNKMTAKETE LQREMHEMAQ KTAELQEELS
     GEKNRLAGEL QLLLEEIKSS KDQLKELTLE NSELKKSLDC MHKDQVEKEG KVREEIAEYQ
     LRLHEAEKKH QALLLDTNKQ YEVEIQTYRE KLTSKEECLS SQKLEIDLLK SSKEELNNSL
     KATTQILEEL KKTKMDNLKY VNQLKKENER AQGKMKLLIK SCKQLEEEKE ILQKELSQLQ
     AAQEKQKTGT VMDTKVDELT TEIKELKETL EEKTKEADEY LDKYCSLLIS HEKLEKAKEM
     LETQVAHLCS QQSKQDSRGS PLLGPVVPGP SPIPSVTEKR LSSGQNKASG KRQRSSGIWE
     NGRGPTPATP ESFSKKSKKA VMSGIHPAED TEGTEFEPEG LPEVVKKGFA DIPTGKTSPY
     ILRRTTMATR TSPRLAAQKL ALSPLSLGKE NLAESSKPTA GGSRSQKVKV AQRSPVDSGT
     ILREPTTKSV PVNNLPERSP TDSPREGLRV KRGRLVPSPK AGLESNGSEN CKVQ
//
DBGET integrated database retrieval system