P49454 (CENPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein F
Short name=CENP-F

Alternative name(s):
AH antigen
Kinetochore protein CENPF
Mitosin

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 further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing neonatal cardiomyocytes. Interaction with RB directs embryonic stem cells toward a cardiac lineage. Involved in the regulation of DNA synthesis and hence cell cycle progression, via its C-terminus. Has a potential role regulating skeletal myogenesis and in cell differentiation in embryogenesis. Involved in dendritic cell regulation of T-cell immunity against chlamydia. Ref.1 Ref.2 Ref.9 Ref.10
Subunit structure	Interacts with and STX4 (via C-terminus) By similarity. Interacts (via N-terminus) with RBL1, RBL2 and SNAP25 By similarity. Self-associates. Interacts with CENP-E and BUBR1 (via C-terminus). Interacts (via C-terminus) with NDE1, NDEL1 and RB1. Ref.2 Ref.6 Ref.7 Ref.10
Subcellular location	Cytoplasm › perinuclear region. Nucleus matrix. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. Note: Relocalizes to the kinetochore/centromere (coronal surface of the outer plate) and the spindle during mitosis. Observed in nucleus during interphase but not in the nucleolus. At metaphase becomes localized to areas including kinetochore and mitotic apparatus as well as cytoplasm. By telophase, is concentrated within the intracellular bridge at either side of the mid-body. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10
Developmental stage	Gradually accumulates during the cell cycle, reaching peak levels in G2 and M phase, and is rapidly degraded upon completion of mitosis. Ref.1
Post-translational modification	Hyperphosphorylated during mitosis. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the centromere protein F family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA synthesis Differentiation Mitosis Myogenesis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Molecular function	Developmental protein
PTM	Acetylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW G2 phase of mitotic cell cycle Inferred from mutant phenotype Ref.2. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW 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 mitotic cell cycle spindle assembly checkpoint Non-traceable author statement Ref.9. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome muscle organ development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB protein transport Inferred from direct assay Ref.9. Source: UniProtKB regulation of G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.2. Source: UniProtKB regulation of striated muscle tissue development Inferred from sequence or structural similarity. Source: UniProtKB response to drug Non-traceable author statement. Source: UniProtKB
Cellular component	condensed chromosome outer kinetochore Inferred from direct assay Ref.1Ref.6. Source: UniProtKB cytosol Traceable author statement. Source: Reactome midbody Inferred from direct assay Ref.2. Source: UniProtKB nuclear envelope Inferred from direct assay. Source: UniProtKB nuclear matrix Inferred from direct assay Ref.1. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	chromatin binding Non-traceable author statement. Source: UniProtKB dynein binding Inferred from direct assay Ref.9. Source: UniProtKB protein C-terminus binding Inferred from physical interaction Ref.6. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.6. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDEL1	Q9GZM8	5	EBI-968343,EBI-928842

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3207	3207	Centromere protein F		PRO_0000089477
	Propeptide	3208 – 3210	3	Removed in mature form Probable		PRO_0000396744
Regions
	Repeat	1435 – 1530	96	1-1
	Repeat	1531 – 1626	96	1-2
	Repeat	2207 – 2386	180	2-1
	Repeat	2389 – 2568	180	2-2
	Region	1 – 481	481	Interaction with SNAP25 and required for localization to the cytoplasm By similarity
	Region	1435 – 1626	192	2 X 96 AA approximate tandem repeats
	Region	2122 – 2447	326	Interaction with NDE1 and NDEL1
	Region	2207 – 2568	362	2 X 177 AA tandem repeats
	Region	2488 – 3113	626	Sufficient for centromere localization
	Region	2488 – 2925	438	Sufficient for self-association
	Region	2927 – 3113	187	Sufficient for nuclear localization
	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 Ref.19
	Modified residue	144	1	Phosphothreonine Ref.19
	Modified residue	154	1	Phosphothreonine Ref.20
	Modified residue	253	1	Phosphothreonine Ref.17
	Modified residue	268	1	Phosphoserine Ref.15
	Modified residue	274	1	Phosphoserine Ref.15
	Modified residue	276	1	Phosphoserine Ref.15
	Modified residue	769	1	Phosphoserine By similarity
	Modified residue	821	1	Phosphoserine Ref.13
	Modified residue	834	1	Phosphoserine Ref.19
	Modified residue	1248	1	Phosphoserine Ref.19
	Modified residue	1255	1	Phosphoserine Ref.16
	Modified residue	1282	1	Phosphoserine Ref.16
	Modified residue	1315	1	Phosphotyrosine Ref.14
	Modified residue	1319	1	Phosphothreonine Ref.14
	Modified residue	1324	1	Phosphoserine Ref.13
	Modified residue	1590	1	Phosphoserine Ref.17
	Modified residue	1747	1	Phosphoserine Ref.12 Ref.13 Ref.19 Ref.20
	Modified residue	1748	1	Phosphoserine Ref.19
	Modified residue	1750	1	Phosphoserine Ref.12 Ref.13 Ref.19 Ref.21
	Modified residue	1988	1	Phosphoserine Ref.13
	Modified residue	2512	1	Phosphoserine Ref.19
	Modified residue	2513	1	Phosphoserine Ref.13 Ref.19
	Modified residue	2638	1	Phosphoserine Ref.16
	Modified residue	2875	1	N6-acetyllysine Ref.22
	Modified residue	2996	1	Phosphoserine Ref.13 Ref.19 Ref.20 Ref.21
	Modified residue	3007	1	Phosphoserine Ref.13 Ref.19 Ref.20 Ref.21
	Modified residue	3094	1	Phosphoserine Ref.13 Ref.17
	Modified residue	3119	1	Phosphoserine Ref.12 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
	Modified residue	3122	1	Phosphoserine Ref.19
	Modified residue	3150	1	Phosphoserine Ref.11 Ref.14 Ref.17 Ref.18 Ref.19
	Modified residue	3175	1	Phosphoserine Ref.13 Ref.18 Ref.19
	Modified residue	3179	1	Phosphoserine Ref.13 Ref.19
	Modified residue	3207	1	Cysteine methyl ester Probable
	Lipidation	3207	1	S-farnesyl cysteine Ref.8
Natural variations
	Natural variant	250	1	Q → L. Ref.1 Corresponds to variant rs1050065 [ dbSNP | Ensembl ].		VAR_055049
	Natural variant	272	1	D → G. Ref.1 Corresponds to variant rs1050066 [ dbSNP | Ensembl ].		VAR_055050
	Natural variant	300	1	R → C. Corresponds to variant rs17023281 [ dbSNP | Ensembl ].		VAR_034712
	Natural variant	494	1	H → Q. Corresponds to variant rs2070065 [ dbSNP | Ensembl ].		VAR_034713
	Natural variant	701	1	M → V. Corresponds to variant rs3795524 [ dbSNP | Ensembl ].		VAR_034714
	Natural variant	754	1	Q → E. Corresponds to variant rs3795523 [ dbSNP | Ensembl ].		VAR_034715
	Natural variant	815	1	R → H. Corresponds to variant rs3795522 [ dbSNP | Ensembl ].		VAR_034716
	Natural variant	1018	1	Y → D. Corresponds to variant rs3795519 [ dbSNP | Ensembl ].		VAR_034717
	Natural variant	1033	1	G → R. Corresponds to variant rs3795518 [ dbSNP | Ensembl ].		VAR_034718
	Natural variant	1105	1	T → I. Corresponds to variant rs12067133 [ dbSNP | Ensembl ].		VAR_034719
	Natural variant	1412	1	L → S. Corresponds to variant rs3795517 [ dbSNP | Ensembl ].		VAR_034720
	Natural variant	1515	1	A → T. Corresponds to variant rs2666839 [ dbSNP | Ensembl ].		VAR_034721
	Natural variant	1516 – 1611	96	Missing.		VAR_036701
	Natural variant	1539	1	K → R. Corresponds to variant rs3795514 [ dbSNP | Ensembl ].		VAR_034722
	Natural variant	1864	1	D → N. Corresponds to variant rs3748692 [ dbSNP | Ensembl ].		VAR_055638
	Natural variant	2011	1	E → A. Corresponds to variant rs3790647 [ dbSNP | Ensembl ].		VAR_034723
	Natural variant	3202	1	N → K. Ref.1 Ref.2 Ref.5 Corresponds to variant rs7289 [ dbSNP | Ensembl ].		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	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 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[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., Rattner J.B., Yen T.J. J. Cell Biol. 130:507-518(1995) [PubMed: 7542657] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, VARIANTS LEU-250; GLY-272 AND LYS-3202. Tissue: Mammary carcinoma.
[2]	"Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression." Zhu X., Mancini M.A., Chang K.-H., Liu C.-Y., Chen C.-F., Shan B., Jones D., Yang-Feng T.L., Lee W.-H. Mol. Cell. Biol. 15:5017-5029(1995) [PubMed: 7651420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1, SUBCELLULAR LOCATION, VARIANTS 1516-VAL--VAL-1611 DEL AND LYS-3202.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT 1516-VAL--VAL-1611.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT 1516-VAL--VAL-1611.
[5]	"A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain sufficient for nuclear localization." Li Q., Ke Y., Kapp J.A., Fertig N., Medsger T.A. Jr., Joshi H.C. Biochem. Biophys. Res. Commun. 212:220-228(1995) [PubMed: 7612011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2194-3210, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, VARIANT LYS-3202.
[6]	"The C-terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization." Zhu X., Chang K.-H., He D., Mancini M.A., Brinkley W.R., Lee W.-H. J. Biol. Chem. 270:19545-19550(1995) [PubMed: 7642639] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[7]	"Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1." Chan G.K.T., Schaar B.T., Yen T.J. J. Cell Biol. 143:49-63(1998) [PubMed: 9763420] [Abstract] Cited for: INTERACTION WITH BUBR1 AND CENPE, SUBCELLULAR LOCATION.
[8]	"Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules." Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L., Bishop W.R., Kirschmeier P. J. Biol. Chem. 275:30451-30457(2000) [PubMed: 10852915] [Abstract] Cited for: ISOPRENYLATION AT CYS-3207.
[9]	"Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic dynein-mediated poleward transport." Yang Z.Y., Guo J., Li N., Qian M., Wang S.N., Zhu X.L. Cell Res. 13:275-283(2003) [PubMed: 12974617] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor complexes." Vergnolle M.A.S., Taylor S.S. Curr. Biol. 17:1173-1179(2007) [PubMed: 17600710] [Abstract] Cited for: FUNCTION, INTERACTION WITH NDEL1 AND NDE1, SUBCELLULAR LOCATION.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3150, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747; SER-1750 AND SER-3119, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821; SER-1324; SER-1747; SER-1750; SER-1988; SER-2513; SER-2996; SER-3007; SER-3094; SER-3119; SER-3175 AND SER-3179, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1315; THR-1319; SER-3119 AND SER-3150, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-274 AND SER-276, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255; SER-1282 AND SER-2638, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-253; SER-1590; SER-3094 AND SER-3150, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3150 AND SER-3175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-144; SER-834; SER-1248; SER-1747; SER-1748; SER-1750; SER-2512; SER-2513; SER-2996; SER-3007; SER-3119; SER-3122; SER-3150; SER-3175 AND SER-3179, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154; SER-1747; SER-2996; SER-3007 AND SER-3119, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1750; SER-2996; SER-3007 AND SER-3119, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2875, MASS SPECTROMETRY.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19769 mRNA. Translation: AAA82889.1. U30872 mRNA. Translation: AAA82935.1. AL445666, AL445305 Genomic DNA. Translation: CAH71810.1. AL445305, AL445666 Genomic DNA. Translation: CAH73032.1. BC172232 mRNA. Translation: AAI72232.1. U25725 mRNA. Translation: AAA86889.1.
IPI	IPI00855998.
PIR	PC4035.
RefSeq	NP_057427.3. NM_016343.3.
UniGene	Hs.497741.
3D structure databases
ProteinModelPortal	P49454.
SMR	P49454. Positions 3-34.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49454. 7 interactions.
MINT	MINT-2803614.
STRING	P49454.
PTM databases
PhosphoSite	P49454.
Polymorphism databases
DMDM	156630875.
Proteomic databases
PRIDE	P49454.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1063.
KEGG	hsa:1063.
UCSC	uc001hkm.1. human.
Organism-specific databases
CTD	1063.
GeneCards	GC01P214776.
H-InvDB	HIX0028827.
HGNC	HGNC:1857. CENPF.
MIM	600236. gene.
neXtProt	NX_P49454.
PharmGKB	PA26401.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG050893.
Enzyme and pathway databases
Pathway_Interaction_DB	foxm1pathway. FOXM1 transcription factor network.
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
CleanEx	HS_CENPF.
Genevestigator	P49454.
Family and domain databases
InterPro	IPR019513. Centromere_CenpF_leu-rich_rpt. IPR018463. Centromere_CenpF_N. IPR018302. Centromere_CenpF_Rb-prot-bd. [Graphical view]
KO	K11499.
Pfam	PF10473. Cenp-F_leu_zip. 2 hits. PF10481. Cenp-F_N. 1 hit. PF10490. Rb-bdg_C_Cenp-F. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	4446.
SOURCE	Search...

Entry information

Entry name

CENPF_HUMAN

Accession

Primary (citable) accession number: P49454
Secondary accession number(s): Q13171, Q13246, Q5VVM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.