CENPF

CENPF
Identifikatori
Aliasi	CENPF
Vanjski ID-jevi	OMIM: 600236 MGI: 1313302 HomoloGene: 22969 GeneCards: CENPF
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	214,664,571 bp
Lokacija gena (miš)
Hrom.	Hromosom 1 (miš)
Kraj	189,420,283 bp
Ontologija gena
Molekularna funkcija	• protein homodimerization activity; • transcription factor binding; • chromatin binding; • protein C-terminus binding; • GO:0001948, GO:0016582 vezivanje za proteine; • dynein complex binding;
Ćelijska komponenta	• citoplazma; • ciliary basal body; • citosol; • centrosom; • spindle pole; • nuclear envelope; • nuclear matrix; • Diobeno vreteno; • nukleoplazma; • ciliary transition fiber; • hromosom; • midbody; • outer kinetochore; • perinuklearno područje citoplazme; • pronucleus; • GO:0035085 Aksonema; • Hromatin; • Primarno suženje; • citoskelet; • jedro; • kinetohor;
Biološki proces	• regulation of G2/M transition of mitotic cell cycle; • regulation of striated muscle tissue development; • Ćelijska diferencijacija; • metaphase plate congression; • DNA biosynthetic process; • Nefrogeneza; • hromosomska segregacija; • muscle organ development; • ventricular system development; • mitotic spindle assembly checkpoint signaling; • regulation of cell cycle; • Ćelijska dioba; • multicellular organism development; • protein transport; • ćelijski ciklus; • Ćelijska proliferacija; • GO:0045996 negative regulation of transcription, DNA-templated; • kinetochore assembly; • GO:0007067 Mitoza;
	Izvori:Amigo / QuickGO
Ortolozi
	1063
	108000
	ENSG00000117724
	ENSMUSG00000026605
	P49454
	n/a
	NM_016343
	NM_001081363
	NP_057427
	n/a
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Centromerni protein F jest protein koji je kod ljudi kodiran genom CENPF sa hromosoma 1.^[5]^[6]^[7] Uključen je u segregaciju hromosoma tokom ćelijske diobe. Također ima ulogu u orijentaciji mikrotubula u formiranju ćelijskih cilija.^[8]^[9]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 3.210 aminokiselina, a molekulska težina 367.764 Da.^[10]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
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

Funkcija

CENPF je dio jedarnog matriksa tokom G2-faze ćelijskog ciklusa (faza brze sinteze proteina u pripremi za mitozu). U kasnoj G2, protein čini dio kinetohorskog, proteinskog kompleksa u obliku diska koji omogućava centromerama dviju sestrinskih hromatida da se veže za mikrotubule (formirajući aparat vretena) kako bi ih mikrotubule razdvojile u procesu ćelijske diobe. Ostaje dio kinetohora tokom rane anafaze (faza podjele hromosoma). U kasnoj anafazi, CENPF odlazi na srednju zonu vretena, a u telofazi (faza dijeljenja ćelija) sdolazi na međućelijski most. Smatra se da se naknadno degradira. Mutacije u "CENPF" dovode do poremećene diobe ćelija tokom ranog razvoja. Utvrđeno je da mitozaa traje duže kada je gen mutiran.^[8]^[9]

Mikrotubule su proteinske strukture koje su dio citoskeleta i neophodne su kako bi ćelije imale različite, složene oblike i sposobnost migraciona. Njih pravi centrosom, koji sadrži par cilindričnih centriola pod pravim uglom jedna u odnosu na drugu. Prije podjele, CENPF se lokalizira na kraju jedne od centriola (matične centriole), kako bi ispravno orijentirao mikrotubule u formiranju tankih ćelijskih projekcija koje se nazivaju cilije. Većina cilija su primarne cilije, koje su uključene u ćelijsku signalizaciju da bi pokrenule migraciju, diobu ili diferencijaciju. Mutacije u "CENPF" remete ovu sposobnost formiranja cilija; utvrđeno je da su cilije malobrbrojnije i kraće kada je gen mutiran.^[8]^[11]

Smatra se da CENPF formira ili homodimer ili heterodimer.

Klinički značaj

Mutacije u obje kopije CENPF uzrokuju Strømmeov sindrom, karakteriziran mikrocefalijom, abnormalnostima očne jabučice i jejunumskom atrezijom.^[9] Autoantitijela protiv CENPF-a pronađena bolesti u kod pacijenata s rakom ili bolesti reakcije transplantata protiv domaćina.^[7]

Također pogledajte

CENPE
CENPJ
CENPT

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000117724 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026605 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Rattner JB, Rao A, Fritzler MJ, Valencia DW, Yen TJ (Mar 1994). "CENP-F is a .ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization". Cell Motil Cytoskeleton. 26 (3): 214–26. doi:10.1002/cm.970260305. PMID 7904902.
^ Testa JR, Zhou JY, Bell DW, Yen TJ (Mar 1995). "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 (3): 691–3. doi:10.1006/geno.1994.1558. PMID 7851898.
^ ^a ^b "Entrez Gene: CENPF centromere protein F, 350/400ka (mitosin)".
^ ^a ^b ^c Waters, Aoife M.; Asfahani, Rowan; Carroll, Paula; Bicknell, Louise; Lescai, Francesco; Bright, Alison; Chanudet, Estelle; Brooks, Anthony; Christou-Savina, Sonja; Osman, Guled; Walsh, Patrick (mart 2015). "The kinetochore protein, CENPF, is mutated in human ciliopathy and microcephaly phenotypes". Journal of Medical Genetics. 52 (3): 147–156. doi:10.1136/jmedgenet-2014-102691. ISSN 1468-6244. PMC 4345935. PMID 25564561.
^ ^a ^b ^c Filges, Isabel; Bruder, Elisabeth; Brandal, Kristin; Meier, Stephanie; Undlien, Dag Erik; Waage, Trine Rygvold; Hoesli, Irene; Schubach, Max; de Beer, Tjaart; Sheng, Ying; Hoeller, Sylvia (april 2016). "Strømme Syndrome Is a Ciliary Disorder Caused by Mutations in CENPF". Human Mutation. 37 (4): 359–363. doi:10.1002/humu.22960. ISSN 1098-1004. PMID 26820108. S2CID 1495539.
^ "UniProt, P49454" (jezik: en.). Pristupljeno 8. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ "OMIM Entry - # 243605 - STROMME SYNDROME; STROMS". www.omim.org (jezik: engleski). Pristupljeno 27. 9. 2018.

Dopunska literatura

Ma L, Zhao X, Zhu X (2006). "Mitosin/CENP-F in mitosis, transcriptional control, and differentiation". J. Biomed. Sci. 13 (2): 205–13. doi:10.1007/s11373-005-9057-3. PMID 16456711.
Liao H, Winkfein RJ, Mack G, et al. (1995). "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 (3): 507–18. doi:10.1083/jcb.130.3.507. PMC 2120529. PMID 7542657.
Li Q, Ke Y, Kapp JA, et al. (1995). "A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain sufficient for nuclear localization". Biochem. Biophys. Res. Commun. 212 (1): 220–8. doi:10.1006/bbrc.1995.1959. PMID 7612011.
Zhu X, Chang KH, He D, et al. (1995). "The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization". J. Biol. Chem. 270 (33): 19545–50. doi:10.1074/jbc.270.33.19545. PMID 7642639.
Zhu X, Mancini MA, Chang KH, et al. (1995). "Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression". Mol. Cell. Biol. 15 (9): 5017–29. doi:10.1128/MCB.15.9.5017. PMC 230749. PMID 7651420.
Li S, Ku CY, Farmer AA, et al. (1998). "Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs". J. Biol. Chem. 273 (11): 6183–9. doi:10.1074/jbc.273.11.6183. PMID 9497340.
Chan GK, Schaar BT, Yen TJ (1998). "Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1". J. Cell Biol. 143 (1): 49–63. doi:10.1083/jcb.143.1.49. PMC 2132809. PMID 9763420.
Zhu X (1999). "Structural requirements and dynamics of mitosin-kinetochore interaction in M phase". Mol. Cell. Biol. 19 (2): 1016–24. doi:10.1128/MCB.19.2.1016. PMC 116032. PMID 9891037.
Erlanson M, Casiano CA, Tan EM, et al. (1999). "Immunohistochemical analysis of the proliferation associated nuclear antigen CENP-F in non-Hodgkin's lymphoma". Mod. Pathol. 12 (1): 69–74. PMID 9950165.
Goodwin RL, Pabón-Peña LM, Foster GC, Bader D (1999). "The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family". J. Biol. Chem. 274 (26): 18597–604. doi:10.1074/jbc.274.26.18597. PMID 10373470.
Ashar HR, James L, Gray K, et al. (2000). "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules". J. Biol. Chem. 275 (39): 30451–7. doi:10.1074/jbc.M003469200. PMID 10852915.
Kobayashi M, Hanai R (2001). "M phase-specific association of human topoisomerase IIIbeta with chromosomes". Biochem. Biophys. Res. Commun. 287 (1): 282–7. doi:10.1006/bbrc.2001.5580. PMID 11549288.
Hussein D, Taylor SS (2003). "Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis". J. Cell Sci. 115 (Pt 17): 3403–14. doi:10.1242/jcs.115.17.3403. PMID 12154071.
Holstein SA, Hohl RJ (2003). "Synergistic interaction of lovastatin and paclitaxel in human cancer cells". Mol. Cancer Ther. 1 (2): 141–9. PMID 12467231.
Konstantinidou AE, Korkolopoulou P, Kavantzas N, et al. (2003). "Mitosin, a novel marker of cell proliferation and early recurrence in intracranial meningiomas". Histol. Histopathol. 18 (1): 67–74. PMID 12507285.
Yang ZY, Guo J, Li N, et al. (2004). "Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic dynein-mediated poleward transport". Cell Res. 13 (4): 275–83. doi:10.1038/sj.cr.7290172. PMID 12974617.
Laoukili J, Kooistra MR, Brás A, et al. (2005). "FoxM1 is required for execution of the mitotic programme and chromosome stability". Nat. Cell Biol. 7 (2): 126–36. doi:10.1038/ncb1217. PMID 15654331. S2CID 11732068.
Zhou X, Wang R, Fan L, et al. (2005). "Mitosin/CENP-F as a negative regulator of activating transcription factor-4". J. Biol. Chem. 280 (14): 13973–7. doi:10.1074/jbc.M414310200. PMID 15677469.

Vanjski linkovi

Lokacija ljudskog genoma CENPF i stranica sa detaljima o genu CENPF u UCSC Genome Browseru.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000117724 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026605 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7904902-5] Rattner JB, Rao A, Fritzler MJ, Valencia DW, Yen TJ (Mar 1994). "CENP-F is a .ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization". Cell Motil Cytoskeleton. 26 (3): 214–26. doi:10.1002/cm.970260305. PMID 7904902.

[pmid7851898-6] Testa JR, Zhou JY, Bell DW, Yen TJ (Mar 1995). "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 (3): 691–3. doi:10.1006/geno.1994.1558. PMID 7851898.

[entrez-7] "Entrez Gene: CENPF centromere protein F, 350/400ka (mitosin)".

[:5-8] Waters, Aoife M.; Asfahani, Rowan; Carroll, Paula; Bicknell, Louise; Lescai, Francesco; Bright, Alison; Chanudet, Estelle; Brooks, Anthony; Christou-Savina, Sonja; Osman, Guled; Walsh, Patrick (mart 2015). "The kinetochore protein, CENPF, is mutated in human ciliopathy and microcephaly phenotypes". Journal of Medical Genetics. 52 (3): 147–156. doi:10.1136/jmedgenet-2014-102691. ISSN 1468-6244. PMC 4345935. PMID 25564561.

[:72-9] Filges, Isabel; Bruder, Elisabeth; Brandal, Kristin; Meier, Stephanie; Undlien, Dag Erik; Waage, Trine Rygvold; Hoesli, Irene; Schubach, Max; de Beer, Tjaart; Sheng, Ying; Hoeller, Sylvia (april 2016). "Strømme Syndrome Is a Ciliary Disorder Caused by Mutations in CENPF". Human Mutation. 37 (4): 359–363. doi:10.1002/humu.22960. ISSN 1098-1004. PMID 26820108. S2CID 1495539.

[UniProt-10] "UniProt, P49454" (jezik: en.). Pristupljeno 8. 12. 2021.CS1 održavanje: nepoznati jezik (link)

[:0-11] "OMIM Entry - # 243605 - STROMME SYNDROME; STROMS". www.omim.org (jezik: engleski). Pristupljeno 27. 9. 2018.

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