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P49454

- CENPF_HUMAN

UniProt

P49454 - CENPF_HUMAN

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Protein

Centromere protein F

Gene

CENPF

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chromatin binding Source: UniProtKB
  2. dynein binding Source: UniProtKB
  3. protein C-terminus binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. cell proliferation Source: UniProtKB
  3. chromosome segregation Source: UniProtKB
  4. DNA replication Source: UniProtKB-KW
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. kinetochore assembly Source: UniProtKB
  7. metaphase plate congression Source: UniProtKB
  8. mitotic cell cycle Source: UniProtKB
  9. mitotic nuclear division Source: UniProtKB-KW
  10. mitotic spindle assembly checkpoint Source: UniProtKB
  11. muscle organ development Source: UniProtKB-KW
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. protein transport Source: UniProtKB
  14. regulation of cell cycle Source: Reactome
  15. regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
  16. regulation of striated muscle tissue development Source: UniProtKB
  17. response to drug Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. 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
ProteomesiUP000005640: 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

  1. chromosome, centromeric region Source: UniProtKB
  2. condensed chromosome outer kinetochore Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. kinetochore Source: UniProtKB
  6. midbody Source: UniProtKB
  7. nuclear envelope Source: UniProtKB
  8. nuclear matrix Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. pronucleus Source: Ensembl
  11. spindle Source: UniProtKB
  12. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26401.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 32073207Centromere protein FPRO_0000089477Add
BLAST
Propeptidei3208 – 32103Removed in mature formCuratedPRO_0000396744

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei144 – 1441Phosphothreonine1 Publication
Modified residuei151 – 1511Phosphothreonine1 Publication
Modified residuei154 – 1541Phosphothreonine1 Publication
Modified residuei158 – 1581Phosphotyrosine1 Publication
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei773 – 7731Phosphoserine1 Publication
Modified residuei783 – 7831Phosphoserine1 Publication
Modified residuei821 – 8211Phosphoserine1 Publication
Modified residuei834 – 8341Phosphoserine1 Publication
Modified residuei876 – 8761Phosphoserine1 Publication
Modified residuei1248 – 12481Phosphoserine2 Publications
Modified residuei1255 – 12551Phosphoserine1 Publication
Modified residuei1259 – 12591Phosphoserine1 Publication
Modified residuei1747 – 17471Phosphoserine3 Publications
Modified residuei1748 – 17481Phosphoserine1 Publication
Modified residuei1750 – 17501Phosphoserine3 Publications
Modified residuei1988 – 19881Phosphoserine1 Publication
Modified residuei2512 – 25121Phosphoserine1 Publication
Modified residuei2513 – 25131Phosphoserine2 Publications
Modified residuei2875 – 28751N6-acetyllysine1 Publication
Modified residuei2996 – 29961Phosphoserine3 Publications
Modified residuei3007 – 30071Phosphoserine3 Publications
Modified residuei3018 – 30181Phosphoserine1 Publication
Modified residuei3045 – 30451Phosphothreonine1 Publication
Modified residuei3048 – 30481Phosphoserine1 Publication
Modified residuei3094 – 30941Phosphoserine1 Publication
Modified residuei3119 – 31191Phosphoserine4 Publications
Modified residuei3122 – 31221Phosphoserine2 Publications
Modified residuei3150 – 31501Phosphoserine4 Publications
Modified residuei3175 – 31751Phosphoserine2 Publications
Modified residuei3179 – 31791Phosphoserine2 Publications
Modified residuei3207 – 32071Cysteine methyl esterCurated
Lipidationi3207 – 32071S-farnesyl cysteine1 Publication

Post-translational modificationi

Hyperphosphorylated during mitosis.

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP49454.
PaxDbiP49454.
PRIDEiP49454.

PTM databases

PhosphoSiteiP49454.

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

BgeeiP49454.
CleanExiHS_CENPF.
GenevestigatoriP49454.

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

Protein-protein interaction databases

BioGridi107492. 21 interactions.
IntActiP49454. 11 interactions.
MINTiMINT-2803614.
STRINGi9606.ENSP00000355922.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1435 – 1530961-1Add
BLAST
Repeati1531 – 1626961-2Add
BLAST
Repeati2207 – 23861802-1Add
BLAST
Repeati2389 – 25681802-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 481481Interaction with SNAP25 and required for localization to the cytoplasmBy similarityAdd
BLAST
Regioni1435 – 16261922 X 96 AA approximate tandem repeatsAdd
BLAST
Regioni2122 – 2447326Interaction with NDE1 and NDEL1Add
BLAST
Regioni2207 – 25683622 X 177 AA tandem repeatsAdd
BLAST
Regioni2488 – 3113626Sufficient for centromere localizationAdd
BLAST
Regioni2488 – 2925438Sufficient for self-associationAdd
BLAST
Regioni2927 – 3113187Sufficient for nuclear localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili14 – 197184Sequence AnalysisAdd
BLAST
Coiled coili273 – 769497Sequence AnalysisAdd
BLAST
Coiled coili823 – 1328506Sequence AnalysisAdd
BLAST
Coiled coili1642 – 1746105Sequence AnalysisAdd
BLAST
Coiled coili1862 – 29871126Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3015 – 303218Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the centromere protein F family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG050893.
InParanoidiP49454.
KOiK11499.
OrthoDBiEOG7FV3PD.
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

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → T in AAA82889. (PubMed:7542657)Curated
Sequence conflicti48 – 481L → P in AAA82889. (PubMed:7542657)Curated
Sequence conflicti48 – 481L → P in AAA82935. (PubMed:7651420)Curated
Sequence conflicti52 – 521K → T in AAA82889. (PubMed:7542657)Curated
Sequence conflicti52 – 521K → T in AAA82935. (PubMed:7651420)Curated
Sequence conflicti611 – 6111Missing in AAA82935. (PubMed:7651420)Curated
Sequence conflicti1811 – 18111V → L in AAA82935. (PubMed:7651420)Curated
Sequence conflicti2242 – 22432ER → DG in AAA86889. (PubMed:15489334)Curated
Sequence conflicti2335 – 23351L → Q in AAA86889. (PubMed:15489334)Curated
Sequence conflicti2492 – 24921N → D in AAA82889. (PubMed:7542657)Curated
Sequence conflicti2492 – 24921N → D in AAA86889. (PubMed:15489334)Curated
Sequence conflicti2545 – 256117ELNER…QEACK → SSMREWQPCIMTKKPVS in AAA86889. (PubMed:15489334)CuratedAdd
BLAST
Sequence conflicti3039 – 30391R → G in AAA82889. (PubMed:7542657)Curated
Sequence conflicti3039 – 30391R → G in AAA82935. (PubMed:7651420)Curated
Sequence conflicti3039 – 30391R → G in AAA86889. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti250 – 2501Q → L.1 Publication
Corresponds to variant rs1050065 [ dbSNP | Ensembl ].
VAR_055049
Natural varianti272 – 2721D → G.1 Publication
Corresponds to variant rs1050066 [ dbSNP | Ensembl ].
VAR_055050
Natural varianti300 – 3001R → C.
Corresponds to variant rs17023281 [ dbSNP | Ensembl ].
VAR_034712
Natural varianti494 – 4941H → Q.
Corresponds to variant rs2070065 [ dbSNP | Ensembl ].
VAR_034713
Natural varianti701 – 7011M → V.
Corresponds to variant rs3795524 [ dbSNP | Ensembl ].
VAR_034714
Natural varianti754 – 7541Q → E.
Corresponds to variant rs3795523 [ dbSNP | Ensembl ].
VAR_034715
Natural varianti815 – 8151R → H.
Corresponds to variant rs3795522 [ dbSNP | Ensembl ].
VAR_034716
Natural varianti1018 – 10181Y → D.
Corresponds to variant rs3795519 [ dbSNP | Ensembl ].
VAR_034717
Natural varianti1033 – 10331G → R.
Corresponds to variant rs3795518 [ dbSNP | Ensembl ].
VAR_034718
Natural varianti1105 – 11051T → I.
Corresponds to variant rs12067133 [ dbSNP | Ensembl ].
VAR_034719
Natural varianti1412 – 14121L → S.
Corresponds to variant rs3795517 [ dbSNP | Ensembl ].
VAR_034720
Natural varianti1515 – 15151A → T.
Corresponds to variant rs2666839 [ dbSNP | Ensembl ].
VAR_034721
Natural varianti1516 – 161196Missing.1 Publication
VAR_036701Add
BLAST
Natural varianti1539 – 15391K → R.
Corresponds to variant rs3795514 [ dbSNP | Ensembl ].
VAR_034722
Natural varianti1864 – 18641D → N.
Corresponds to variant rs3748692 [ dbSNP | Ensembl ].
VAR_055638
Natural varianti2011 – 20111E → A.
Corresponds to variant rs3790647 [ dbSNP | Ensembl ].
VAR_034723
Natural varianti3202 – 32021N → K.3 Publications
Corresponds to variant rs7289 [ dbSNP | Ensembl ].
VAR_014839

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi156630875.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi PC4035.
RefSeqi NP_057427.3. NM_016343.3.
UniGenei Hs.497741.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107492. 21 interactions.
IntActi P49454. 11 interactions.
MINTi MINT-2803614.
STRINGi 9606.ENSP00000355922.

PTM databases

PhosphoSitei P49454.

Polymorphism databases

DMDMi 156630875.

Proteomic databases

MaxQBi P49454.
PaxDbi P49454.
PRIDEi P49454.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366955 ; ENSP00000355922 ; ENSG00000117724 .
GeneIDi 1063.
KEGGi hsa:1063.
UCSCi uc001hkm.3. human.

Organism-specific databases

CTDi 1063.
GeneCardsi GC01P214776.
H-InvDB HIX0028827.
HGNCi HGNC:1857. CENPF.
HPAi CAB009581.
HPA052382.
MIMi 600236. gene.
neXtProti NX_P49454.
PharmGKBi PA26401.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG050893.
InParanoidi P49454.
KOi K11499.
OrthoDBi EOG7FV3PD.
PhylomeDBi P49454.
TreeFami TF101133.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi CENPF. human.
GeneWikii CENPF.
GenomeRNAii 1063.
NextBioi 4446.
PROi P49454.
SOURCEi Search...

Gene expression databases

Bgeei P49454.
CleanExi HS_CENPF.
Genevestigatori P49454.

Family and domain databases

InterProi IPR018302. CenpF/LEK1_Rb-prot-bd.
IPR019513. Centromere_CenpF_leu-rich_rpt.
IPR018463. Centromere_CenpF_N.
[Graphical view ]
Pfami PF10490. CENP-F_C_Rb_bdg. 1 hit.
PF10473. CENP-F_leu_zip. 3 hits.
PF10481. CENP-F_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747 AND SER-1750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NDEL1 AND NDE1, SUBCELLULAR LOCATION.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996 AND SER-3007, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2875, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; THR-154; TYR-158; SER-276; SER-773; SER-783; SER-821; SER-876; SER-1248; SER-1255; SER-1259; SER-1747; SER-1750; SER-1988; SER-2513; SER-2996; SER-3007; SER-3018; THR-3045; SER-3048; SER-3094; SER-3119; SER-3122; SER-3150; SER-3175 AND SER-3179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3119 AND SER-3150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 150 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

External Data

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