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Protein

Centromere protein F

Gene

CENPF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • dynein binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell proliferation Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • DNA biosynthetic process Source: UniProtKB-KW
  • kidney development Source: GO_Central
  • kinetochore assembly Source: UniProtKB
  • metaphase plate congression Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle assembly checkpoint Source: UniProtKB
  • muscle organ development Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • protein transport Source: UniProtKB
  • regulation of cell cycle Source: Reactome
  • regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
  • regulation of striated muscle tissue development Source: UniProtKB
  • response to drug Source: UniProtKB
  • sister chromatid cohesion Source: Reactome
  • ventricular system development Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, DNA synthesis, Mitosis, Myogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117724-MONOMER.
ReactomeiR-HSA-156711. Polo-like kinase mediated events.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein F
Short name:
CENP-F
Alternative name(s):
AH antigen
Kinetochore protein CENPF
Mitosin
Gene namesi
Name:CENPF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1857. CENPF.

Subcellular locationi

  • Cytoplasmperinuclear region
  • Nucleus matrix
  • Chromosomecentromerekinetochore
  • Cytoplasmcytoskeletonspindle

  • 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.

GO - Cellular componenti

  • axoneme Source: Ensembl
  • centrosome Source: Ensembl
  • chromosome, centromeric region Source: UniProtKB
  • ciliary basal body Source: Ensembl
  • ciliary transition fiber Source: GO_Central
  • condensed chromosome outer kinetochore Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • midbody Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • pronucleus Source: Ensembl
  • spindle Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

Stromme syndrome (STROMS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive congenital disorder characterized by intestinal atresia, ocular anomalies, microcephaly, and renal and cardiac abnormalities in some patients. The disease has features of a ciliopathy, and lethality in early childhood is observed in severe cases.
See also OMIM:243605

Keywords - Diseasei

Ciliopathy, Primary ciliary dyskinesia

Organism-specific databases

DisGeNETi1063.
MIMi243605. phenotype.
PharmGKBiPA26401.

Polymorphism and mutation databases

BioMutaiCENPF.
DMDMi156630875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000894771 – 3207Centromere protein FAdd BLAST3207
PropeptideiPRO_00003967443208 – 3210Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei106PhosphoserineCombined sources1
Modified residuei144PhosphothreonineCombined sources1
Modified residuei151PhosphothreonineCombined sources1
Modified residuei154PhosphothreonineCombined sources1
Modified residuei158PhosphotyrosineCombined sources1
Modified residuei242PhosphoserineCombined sources1
Modified residuei276PhosphoserineCombined sources1
Modified residuei773PhosphoserineCombined sources1
Modified residuei783PhosphoserineCombined sources1
Modified residuei821PhosphoserineCombined sources1
Modified residuei834PhosphoserineCombined sources1
Modified residuei838PhosphoserineCombined sources1
Modified residuei876PhosphoserineCombined sources1
Modified residuei1248PhosphoserineCombined sources1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1747PhosphoserineCombined sources1
Modified residuei1748PhosphoserineCombined sources1
Modified residuei1750PhosphoserineCombined sources1
Modified residuei1822PhosphoserineCombined sources1
Modified residuei1958PhosphothreonineCombined sources1
Modified residuei1964PhosphoserineCombined sources1
Modified residuei1988PhosphoserineCombined sources1
Modified residuei2512PhosphoserineCombined sources1
Modified residuei2513PhosphoserineCombined sources1
Modified residuei2875N6-acetyllysineCombined sources1
Modified residuei2996PhosphoserineCombined sources1
Modified residuei3007PhosphoserineCombined sources1
Modified residuei3018PhosphoserineCombined sources1
Modified residuei3032PhosphoserineCombined sources1
Modified residuei3045PhosphothreonineCombined sources1
Modified residuei3048PhosphoserineCombined sources1
Modified residuei3094PhosphoserineCombined sources1
Modified residuei3119PhosphoserineCombined sources1
Modified residuei3122PhosphoserineCombined sources1
Modified residuei3150PhosphoserineCombined sources1
Modified residuei3175PhosphoserineCombined sources1
Modified residuei3179PhosphoserineCombined sources1
Modified residuei3207Cysteine methyl esterCurated1
Lipidationi3207S-farnesyl cysteine1 Publication1

Post-translational modificationi

Hyperphosphorylated during mitosis.

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiP49454.
MaxQBiP49454.
PaxDbiP49454.
PeptideAtlasiP49454.
PRIDEiP49454.

PTM databases

iPTMnetiP49454.
PhosphoSitePlusiP49454.

Expressioni

Developmental stagei

Gradually accumulates during the cell cycle, reaching peak levels in G2 and M phase, and is rapidly degraded upon completion of mitosis.1 Publication

Gene expression databases

BgeeiENSG00000117724.
CleanExiHS_CENPF.
ExpressionAtlasiP49454. baseline and differential.
GenevisibleiP49454. HS.

Organism-specific databases

HPAiCAB009581.
HPA052382.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NDEL1Q9GZM85EBI-968343,EBI-928842
NUP133Q8WUM02EBI-968343,EBI-295695

GO - Molecular functioni

  • dynein binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107492. 47 interactors.
IntActiP49454. 27 interactors.
MINTiMINT-2803614.
STRINGi9606.ENSP00000355922.

Structurei

3D structure databases

ProteinModelPortaliP49454.
SMRiP49454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1435 – 15301-1Add BLAST96
Repeati1531 – 16261-2Add BLAST96
Repeati2207 – 23862-1Add BLAST180
Repeati2389 – 25682-2Add BLAST180

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 481Interaction with SNAP25 and required for localization to the cytoplasmBy similarityAdd BLAST481
Regioni1435 – 16262 X 96 AA approximate tandem repeatsAdd BLAST192
Regioni2122 – 2447Interaction with NDE1 and NDEL11 PublicationAdd BLAST326
Regioni2207 – 25682 X 177 AA tandem repeatsAdd BLAST362
Regioni2488 – 3113Sufficient for centromere localizationAdd BLAST626
Regioni2488 – 2925Sufficient for self-associationAdd BLAST438
Regioni2927 – 3113Sufficient for nuclear localizationAdd BLAST187

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili14 – 197Sequence analysisAdd BLAST184
Coiled coili273 – 769Sequence analysisAdd BLAST497
Coiled coili823 – 1328Sequence analysisAdd BLAST506
Coiled coili1642 – 1746Sequence analysisAdd BLAST105
Coiled coili1862 – 2987Sequence analysisAdd BLAST1126

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3015 – 3032Nuclear localization signalSequence analysisAdd BLAST18

Sequence similaritiesi

Belongs to the centromere protein F family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IGJF. Eukaryota.
ENOG410XS5F. LUCA.
HOVERGENiHBG050893.
InParanoidiP49454.
KOiK11499.
OrthoDBiEOG091G01XR.
PhylomeDBiP49454.
TreeFamiTF101133.

Family and domain databases

InterProiIPR018302. CenpF/LEK1_Rb-prot-bd.
IPR019513. Centromere_CenpF_leu-rich_rpt.
IPR018463. Centromere_CenpF_N.
[Graphical view]
PfamiPF10490. CENP-F_C_Rb_bdg. 1 hit.
PF10473. CENP-F_leu_zip. 3 hits.
PF10481. CENP-F_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49454-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK
60 70 80 90 100
QKQKVENEKT EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ
110 120 130 140 150
EGQLNSGKKQ IEKLEQELKR CKSELERSQQ AAQSADVSLN PCNTPQKIFT
160 170 180 190 200
TPLTPSQYYS GSKYEDLKEK YNKEVEERKR LEAEVKALQA KKASQTLPQA
210 220 230 240 250
TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD FSASYFSGEQ
260 270 280 290 300
EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR
310 320 330 340 350
LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY
360 370 380 390 400
DQASTKYTAL EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL
410 420 430 440 450
SRQQRSFQTL DQECIQMKAR LTQELQQAKN MHNVLQAELD KLTSVKQQLE
460 470 480 490 500
NNLEEFKQKL CRAEQAFQAS QIKENELRRS MEEMKKENNL LKSHSEQKAR
510 520 530 540 550
EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL QEKINQQENS
560 570 580 590 600
LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
610 620 630 640 650
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC
660 670 680 690 700
LKTQQIKSHE YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY
710 720 730 740 750
MELQQKAEFS DQKHQKEIEN MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD
760 770 780 790 800
RCYQDLHAEY ESLRDLLKSK DASLVTNEDH QRSLLAFDQQ PAMHHSFANI
810 820 830 840 850
IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE SQKQMNSDLQ
860 870 880 890 900
KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
910 920 930 940 950
ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET
960 970 980 990 1000
LSLEKKEMSS IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF
1010 1020 1030 1040 1050
ANYIDEREKS ISELSDQYKQ EKLILLQRCE ETGNAYEDLS QKYKAAQEKN
1060 1070 1080 1090 1100
SKLECLLNEC TSLCENRKNE LEQLKEAFAK EHQEFLTKLA FAEERNQNLM
1110 1120 1130 1140 1150
LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN KMQKEVNDLL
1160 1170 1180 1190 1200
QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE
1210 1220 1230 1240 1250
ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL
1260 1270 1280 1290 1300
QDMQSQEISG LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL
1310 1320 1330 1340 1350
NELEKICEIL QAEKYELVTE LNDSRSECIT ATRKMAEEVG KLLNEVKILN
1360 1370 1380 1390 1400
DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS LAPLDESNSY EHLTLSDKEV
1410 1420 1430 1440 1450
QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD SLKAENLVLS
1460 1470 1480 1490 1500
TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL
1510 1520 1530 1540 1550
EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR
1560 1570 1580 1590 1600
NFQGDLVKEM QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG
1610 1620 1630 1640 1650
DMSLLSNLEG VVSANQCSVD EVFCSSLQEE NLTRKETPSA PAKGVEELES
1660 1670 1680 1690 1700
LCEVYRQSLE KLEEKMESQG IMKNKEIQEL EQLLSSERQE LDCLRKQYLS
1710 1720 1730 1740 1750
ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ LQGLDLSSRS
1760 1770 1780 1790 1800
LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL
1810 1820 1830 1840 1850
DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP
1860 1870 1880 1890 1900
NALVPMDFLG NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM
1910 1920 1930 1940 1950
KELDSKLHLQ EVQLMTKIEA CIELEKIVGE LKKENSDLSE KLEYFSCDHQ
1960 1970 1980 1990 2000
ELLQRVETSE GLNSDLEMHA DKSSREDIGD NVAKVNDSWK ERFLDVENEL
2010 2020 2030 2040 2050
SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK VIVCLEEELS
2060 2070 2080 2090 2100
VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV
2110 2120 2130 2140 2150
AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL
2160 2170 2180 2190 2200
ENQIAQLNKE KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA
2210 2220 2230 2240 2250
LRLSSTQEEV HQLRRGIEKL RVRIEADEKK QLHIAEKLKE RERENDSLKD
2260 2270 2280 2290 2300
KVENLERELQ MSEENQELVI LDAENSKAEV ETLKTQIEEM ARSLKVFELD
2310 2320 2330 2340 2350
LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE QAEIQIKEES
2360 2370 2380 2390 2400
KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE
2410 2420 2430 2440 2450
KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH
2460 2470 2480 2490 2500
AALEAENSKG EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE
2510 2520 2530 2540 2550
QERISELEII NSSFENILQE KEQEKVQMKE KSSTAMEMLQ TQLKELNERV
2560 2570 2580 2590 2600
AALHNDQEAC KAKEQNLSSQ VECLELEKAQ LLQGLDEAKN NYIVLQSSVN
2610 2620 2630 2640 2650
GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV EGEHQLWKEQ
2660 2670 2680 2690 2700
NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK
2710 2720 2730 2740 2750
MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL
2760 2770 2780 2790 2800
EEIKSSKDQL KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH
2810 2820 2830 2840 2850
EAEKKHQALL LDTNKQYEVE IQTYREKLTS KEECLSSQKL EIDLLKSSKE
2860 2870 2880 2890 2900
ELNNSLKATT QILEELKKTK MDNLKYVNQL KKENERAQGK MKLLIKSCKQ
2910 2920 2930 2940 2950
LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK ELKETLEEKT
2960 2970 2980 2990 3000
KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG
3010 3020 3030 3040 3050
PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS
3060 3070 3080 3090 3100
KKSKKAVMSG IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR
3110 3120 3130 3140 3150
TTMATRTSPR LAAQKLALSP LSLGKENLAE SSKPTAGGSR SQKVKVAQRS
3160 3170 3180 3190 3200
PVDSGTILRE PTTKSVPVNN LPERSPTDSP REGLRVKRGR LVPSPKAGLE
3210
SNGSENCKVQ
Length:3,210
Mass (Da):367,764
Last modified:August 21, 2007 - v2
Checksum:iFF20F99216257BAD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16A → T in AAA82889 (PubMed:7542657).Curated1
Sequence conflicti48L → P in AAA82889 (PubMed:7542657).Curated1
Sequence conflicti48L → P in AAA82935 (PubMed:7651420).Curated1
Sequence conflicti52K → T in AAA82889 (PubMed:7542657).Curated1
Sequence conflicti52K → T in AAA82935 (PubMed:7651420).Curated1
Sequence conflicti611Missing in AAA82935 (PubMed:7651420).Curated1
Sequence conflicti1811V → L in AAA82935 (PubMed:7651420).Curated1
Sequence conflicti2242 – 2243ER → DG in AAA86889 (PubMed:15489334).Curated2
Sequence conflicti2335L → Q in AAA86889 (PubMed:15489334).Curated1
Sequence conflicti2492N → D in AAA82889 (PubMed:7542657).Curated1
Sequence conflicti2492N → D in AAA86889 (PubMed:15489334).Curated1
Sequence conflicti2545 – 2561ELNER…QEACK → SSMREWQPCIMTKKPVS in AAA86889 (PubMed:15489334).CuratedAdd BLAST17
Sequence conflicti3039R → G in AAA82889 (PubMed:7542657).Curated1
Sequence conflicti3039R → G in AAA82935 (PubMed:7651420).Curated1
Sequence conflicti3039R → G in AAA86889 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055049250Q → L.1 PublicationCorresponds to variant rs1050065dbSNPEnsembl.1
Natural variantiVAR_055050272D → G.1 PublicationCorresponds to variant rs1050066dbSNPEnsembl.1
Natural variantiVAR_034712300R → C.Corresponds to variant rs17023281dbSNPEnsembl.1
Natural variantiVAR_034713494H → Q.Corresponds to variant rs2070065dbSNPEnsembl.1
Natural variantiVAR_034714701M → V.Corresponds to variant rs3795524dbSNPEnsembl.1
Natural variantiVAR_034715754Q → E.Corresponds to variant rs3795523dbSNPEnsembl.1
Natural variantiVAR_034716815R → H.Corresponds to variant rs3795522dbSNPEnsembl.1
Natural variantiVAR_0347171018Y → D.Corresponds to variant rs3795519dbSNPEnsembl.1
Natural variantiVAR_0347181033G → R.Corresponds to variant rs3795518dbSNPEnsembl.1
Natural variantiVAR_0347191105T → I.Corresponds to variant rs12067133dbSNPEnsembl.1
Natural variantiVAR_0347201412L → S.Corresponds to variant rs3795517dbSNPEnsembl.1
Natural variantiVAR_0347211515A → T.Corresponds to variant rs2666839dbSNPEnsembl.1
Natural variantiVAR_0367011516 – 1611Missing .1 PublicationAdd BLAST96
Natural variantiVAR_0347221539K → R.Corresponds to variant rs3795514dbSNPEnsembl.1
Natural variantiVAR_0556381864D → N.Corresponds to variant rs3748692dbSNPEnsembl.1
Natural variantiVAR_0347232011E → A.Corresponds to variant rs3790647dbSNPEnsembl.1
Natural variantiVAR_0148393202N → K.3 PublicationsCorresponds to variant rs7289dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiPC4035.
RefSeqiNP_057427.3. NM_016343.3.
UniGeneiHs.497741.

Genome annotation databases

EnsembliENST00000366955; ENSP00000355922; ENSG00000117724.
GeneIDi1063.
KEGGihsa:1063.
UCSCiuc001hkm.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiPC4035.
RefSeqiNP_057427.3. NM_016343.3.
UniGeneiHs.497741.

3D structure databases

ProteinModelPortaliP49454.
SMRiP49454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107492. 47 interactors.
IntActiP49454. 27 interactors.
MINTiMINT-2803614.
STRINGi9606.ENSP00000355922.

PTM databases

iPTMnetiP49454.
PhosphoSitePlusiP49454.

Polymorphism and mutation databases

BioMutaiCENPF.
DMDMi156630875.

Proteomic databases

EPDiP49454.
MaxQBiP49454.
PaxDbiP49454.
PeptideAtlasiP49454.
PRIDEiP49454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366955; ENSP00000355922; ENSG00000117724.
GeneIDi1063.
KEGGihsa:1063.
UCSCiuc001hkm.4. human.

Organism-specific databases

CTDi1063.
DisGeNETi1063.
GeneCardsiCENPF.
H-InvDBHIX0028827.
HGNCiHGNC:1857. CENPF.
HPAiCAB009581.
HPA052382.
MIMi243605. phenotype.
600236. gene.
neXtProtiNX_P49454.
PharmGKBiPA26401.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGJF. Eukaryota.
ENOG410XS5F. LUCA.
HOVERGENiHBG050893.
InParanoidiP49454.
KOiK11499.
OrthoDBiEOG091G01XR.
PhylomeDBiP49454.
TreeFamiTF101133.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117724-MONOMER.
ReactomeiR-HSA-156711. Polo-like kinase mediated events.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiCENPF. human.
GeneWikiiCENPF.
GenomeRNAii1063.
PROiP49454.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117724.
CleanExiHS_CENPF.
ExpressionAtlasiP49454. baseline and differential.
GenevisibleiP49454. HS.

Family and domain databases

InterProiIPR018302. CenpF/LEK1_Rb-prot-bd.
IPR019513. Centromere_CenpF_leu-rich_rpt.
IPR018463. Centromere_CenpF_N.
[Graphical view]
PfamiPF10490. CENP-F_C_Rb_bdg. 1 hit.
PF10473. CENP-F_leu_zip. 3 hits.
PF10481. CENP-F_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCENPF_HUMAN
AccessioniPrimary (citable) accession number: P49454
Secondary accession number(s): Q13171, Q13246, Q5VVM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.