Reviewed, UniProtKB/Swiss-Prot P49454 (CENPF_HUMAN)

Names and origin

Protein names

Recommended name:
    Centromere protein F
Alternative name(s):
    Kinetochore protein CENP-F
    Mitosin
    AH antigen

Gene names

Name:

CENPF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	3210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably required for kinetochore function, involved in chromosome segregation during mitosis. Interacts with retinoblastoma protein (RB), CENP-E and BUBR1.
Subunit structure	Homo- or heterodimer.
Subcellular location	Nucleus matrix. Kinetochore. Note= But not in the nucleolus, reorganization to the kinetochore/centromere (coronal surface of the outer plate) and the spindle during mitosis.
Developmental stage	Gradually accumulates during the cell cycle.
Post-translational modification	Hyperphosphorylated during mitosis. Phosphorylated upon DNA damage, probably by ATM or ATR.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosomal protein Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
PTM	Lipoprotein Phosphoprotein Prenylation
Gene Ontology (GO)
Biological process	G2 phase of mitotic cell cycle Ref.2 Inferred from mutant phenotype. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Non-traceable author statement. Source: UniProtKB kinetochore assembly Non-traceable author statement. Source: UniProtKB metaphase plate congression Inferred from direct assay. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle assembly checkpoint Non-traceable author statement. Source: UniProtKB negative regulation of transcription Inferred from direct assay. Source: UniProtKB regulation of striated muscle development Inferred from sequence or structural similarity. Source: UniProtKB response to drug Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB nuclear envelope Inferred from direct assay. Source: UniProtKB nuclear matrix Ref.1 Inferred from direct assay. Source: UniProtKB outer kinetochore of condensed chromosome Ref.1 Inferred from direct assay. Source: UniProtKB spindle pole Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	chromatin binding Non-traceable author statement. Source: UniProtKB dynein binding Inferred from direct assay. Source: UniProtKB protein C-terminus binding Ref.5 Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Ref.5 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.5 Inferred from physical interaction. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CENPE	Q02224	2	EBI-968343,EBI-1375040

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3210	3210	Centromere protein F		PRO_0000089477
Regions
	Repeat	1435 – 1530	96	1-1
	Repeat	1531 – 1626	96	2-1
	Repeat	2207 – 2386	180	1-2
	Repeat	2389 – 2568	180	2-2
	Region	1435 – 1626	192	3 X 96 AA approximate tandem repeats
	Region	2207 – 2568	362	2 X 177 AA tandem repeats
	Coiled coil	14 – 197	184	Potential
	Coiled coil	273 – 769	497	Potential
	Coiled coil	823 – 1328	506	Potential
	Coiled coil	1642 – 1746	105	Potential
	Coiled coil	1862 – 2987	1126	Potential
	Motif	3015 – 3032	18	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	106	1	Phosphoserine
	Modified residue	144	1	Phosphothreonine
	Modified residue	268	1	Phosphoserine
	Modified residue	274	1	Phosphoserine
	Modified residue	276	1	Phosphoserine
	Modified residue	821	1	Phosphoserine
	Modified residue	834	1	Phosphoserine
	Modified residue	1248	1	Phosphoserine
	Modified residue	1255	1	Phosphoserine
	Modified residue	1282	1	Phosphoserine
	Modified residue	1315	1	Phosphotyrosine
	Modified residue	1319	1	Phosphothreonine
	Modified residue	1324	1	Phosphoserine
	Modified residue	1747	1	Phosphoserine
	Modified residue	1748	1	Phosphoserine
	Modified residue	1750	1	Phosphoserine
	Modified residue	1988	1	Phosphoserine
	Modified residue	2512	1	Phosphoserine
	Modified residue	2513	1	Phosphoserine
	Modified residue	2638	1	Phosphoserine
	Modified residue	2996	1	Phosphoserine
	Modified residue	3007	1	Phosphoserine
	Modified residue	3094	1	Phosphoserine
	Modified residue	3119	1	Phosphoserine
	Modified residue	3122	1	Phosphoserine
	Modified residue	3150	1	Phosphoserine
	Modified residue	3175	1	Phosphoserine
	Modified residue	3179	1	Phosphoserine
	Lipidation	3207	1	S-farnesyl cysteine
Natural variations
	Natural variant	300	1	R → C: dbSNP rs17023281.		VAR_034712
	Natural variant	494	1	H → Q: dbSNP rs2070065.		VAR_034713
	Natural variant	701	1	M → V: dbSNP rs3795524.		VAR_034714
	Natural variant	754	1	Q → E: dbSNP rs3795523.		VAR_034715
	Natural variant	815	1	R → H: dbSNP rs3795522.		VAR_034716
	Natural variant	1018	1	Y → D: dbSNP rs3795519.		VAR_034717
	Natural variant	1033	1	G → R: dbSNP rs3795518.		VAR_034718
	Natural variant	1105	1	T → I: dbSNP rs12067133.		VAR_034719
	Natural variant	1412	1	L → S: dbSNP rs3795517.		VAR_034720
	Natural variant	1515	1	A → T: dbSNP rs2666839.		VAR_034721
	Natural variant	1516 – 1611	96	Missing		VAR_036701
	Natural variant	1539	1	K → R: dbSNP rs3795514.		VAR_034722
	Natural variant	2011	1	E → A: dbSNP rs3790647.		VAR_034723
	Natural variant	3202	1	N → K: dbSNP rs7289.		VAR_014839
Experimental info
	Sequence conflict	16	1	A → T in AAA82889. Ref.1
	Sequence conflict	48	1	L → P in AAA82889. Ref.1
	Sequence conflict	48	1	L → P in AAA82935. Ref.2
	Sequence conflict	52	1	K → T in AAA82889. Ref.1
	Sequence conflict	52	1	K → T in AAA82935. Ref.2
	Sequence conflict	250	1	Q → L in AAA82889. Ref.1
	Sequence conflict	272	1	D → G in AAA82889. Ref.1
	Sequence conflict	611	1	Missing in AAA82935. Ref.2
	Sequence conflict	1811	1	V → L in AAA82935. Ref.2
	Sequence conflict	2242 – 2243	2	ER → DG in AAA86889. Ref.4
	Sequence conflict	2335	1	L → Q in AAA86889. Ref.4
	Sequence conflict	2492	1	N → D in AAA82889. Ref.1
	Sequence conflict	2492	1	N → D in AAA86889. Ref.4
	Sequence conflict	2545 – 2561	17	ELNER…QEACK → SSMREWQPCIMTKKPVS in AAA86889. Ref.4
	Sequence conflict	3039	1	R → G in AAA82889. Ref.1
	Sequence conflict	3039	1	R → G in AAA82935. Ref.2
	Sequence conflict	3039	1	R → G in AAA86889. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P49454-1 [UniParc]. Last modified August 21, 2007. Version 2. Checksum: FF20F99216257BAD	FASTA	3,210	367,764
	10 20 30 40 50 60 MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT 70 80 90 100 110 120 EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR 130 140 150 160 170 180 CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR 190 200 210 220 230 240 LEAEVKALQA KKASQTLPQA TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD 250 260 270 280 290 300 FSASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR 310 320 330 340 350 360 LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKYTAL 370 380 390 400 410 420 EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQMKAR 430 440 450 460 470 480 LTQELQQAKN MHNVLQAELD KLTSVKQQLE NNLEEFKQKL CRAEQAFQAS QIKENELRRS 490 500 510 520 530 540 MEEMKKENNL LKSHSEQKAR EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL 550 560 570 580 590 600 QEKINQQENS LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS 610 620 630 640 650 660 ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE 670 680 690 700 710 720 YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY MELQQKAEFS DQKHQKEIEN 730 740 750 760 770 780 MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH 790 800 810 820 830 840 QRSLLAFDQQ PAMHHSFANI IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE 850 860 870 880 890 900 SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA 910 920 930 940 950 960 ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET LSLEKKEMSS 970 980 990 1000 1010 1020 IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ 1030 1040 1050 1060 1070 1080 EKLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK 1090 1100 1110 1120 1130 1140 EHQEFLTKLA FAEERNQNLM LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN 1150 1160 1170 1180 1190 1200 KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE 1210 1220 1230 1240 1250 1260 ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL QDMQSQEISG 1270 1280 1290 1300 1310 1320 LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL NELEKICEIL QAEKYELVTE 1330 1340 1350 1360 1370 1380 LNDSRSECIT ATRKMAEEVG KLLNEVKILN DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS 1390 1400 1410 1420 1430 1440 LAPLDESNSY EHLTLSDKEV QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD 1450 1460 1470 1480 1490 1500 SLKAENLVLS TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL 1510 1520 1530 1540 1550 1560 EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR NFQGDLVKEM 1570 1580 1590 1600 1610 1620 QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG DMSLLSNLEG VVSANQCSVD 1630 1640 1650 1660 1670 1680 EVFCSSLQEE NLTRKETPSA PAKGVEELES LCEVYRQSLE KLEEKMESQG IMKNKEIQEL 1690 1700 1710 1720 1730 1740 EQLLSSERQE LDCLRKQYLS ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ 1750 1760 1770 1780 1790 1800 LQGLDLSSRS LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL 1810 1820 1830 1840 1850 1860 DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP NALVPMDFLG 1870 1880 1890 1900 1910 1920 NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM KELDSKLHLQ EVQLMTKIEA 1930 1940 1950 1960 1970 1980 CIELEKIVGE LKKENSDLSE KLEYFSCDHQ ELLQRVETSE GLNSDLEMHA DKSSREDIGD 1990 2000 2010 2020 2030 2040 NVAKVNDSWK ERFLDVENEL SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK 2050 2060 2070 2080 2090 2100 VIVCLEEELS VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV 2110 2120 2130 2140 2150 2160 AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL ENQIAQLNKE 2170 2180 2190 2200 2210 2220 KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA LRLSSTQEEV HQLRRGIEKL 2230 2240 2250 2260 2270 2280 RVRIEADEKK QLHIAEKLKE RERENDSLKD KVENLERELQ MSEENQELVI LDAENSKAEV 2290 2300 2310 2320 2330 2340 ETLKTQIEEM ARSLKVFELD LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE 2350 2360 2370 2380 2390 2400 QAEIQIKEES KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE 2410 2420 2430 2440 2450 2460 KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH AALEAENSKG 2470 2480 2490 2500 2510 2520 EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE QERISELEII NSSFENILQE 2530 2540 2550 2560 2570 2580 KEQEKVQMKE KSSTAMEMLQ TQLKELNERV AALHNDQEAC KAKEQNLSSQ VECLELEKAQ 2590 2600 2610 2620 2630 2640 LLQGLDEAKN NYIVLQSSVN GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV 2650 2660 2670 2680 2690 2700 EGEHQLWKEQ NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK 2710 2720 2730 2740 2750 2760 MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL EEIKSSKDQL 2770 2780 2790 2800 2810 2820 KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH EAEKKHQALL LDTNKQYEVE 2830 2840 2850 2860 2870 2880 IQTYREKLTS KEECLSSQKL EIDLLKSSKE ELNNSLKATT QILEELKKTK MDNLKYVNQL 2890 2900 2910 2920 2930 2940 KKENERAQGK MKLLIKSCKQ LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK 2950 2960 2970 2980 2990 3000 ELKETLEEKT KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG 3010 3020 3030 3040 3050 3060 PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS KKSKKAVMSG 3070 3080 3090 3100 3110 3120 IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR TTMATRTSPR LAAQKLALSP 3130 3140 3150 3160 3170 3180 LSLGKENLAE SSKPTAGGSR SQKVKVAQRS PVDSGTILRE PTTKSVPVNN LPERSPTDSP 3190 3200 3210 REGLRVKRGR LVPSPKAGLE SNGSENCKVQ

References

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[1]	"CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis." Liao H., Winkfein R.J., Mack G.