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P49454

- CENPF_HUMAN

UniProt

P49454 - CENPF_HUMAN

Protein

Centromere protein F

Gene

CENPF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (21 Aug 2007)
      Previous versions | rss
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    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 binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. 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 G2 phase Source: UniProtKB
    10. mitotic M phase Source: UniProtKB
    11. mitotic nuclear division Source: UniProtKB-KW
    12. mitotic spindle assembly checkpoint Source: UniProtKB
    13. muscle organ development Source: UniProtKB-KW
    14. negative regulation of transcription, DNA-templated Source: UniProtKB
    15. protein transport Source: UniProtKB
    16. regulation of cell cycle Source: Reactome
    17. regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
    18. regulation of striated muscle tissue development Source: UniProtKB
    19. response to drug Source: UniProtKB

    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. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    11. pronucleus Source: Ensembl
    12. spindle Source: UniProtKB
    13. spindle pole Source: UniProtKB

    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. 18 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.
    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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    MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK     50
    QKQKVENEKT EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ 100
    EGQLNSGKKQ IEKLEQELKR CKSELERSQQ AAQSADVSLN PCNTPQKIFT 150
    TPLTPSQYYS GSKYEDLKEK YNKEVEERKR LEAEVKALQA KKASQTLPQA 200
    TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD FSASYFSGEQ 250
    EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR 300
    LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY 350
    DQASTKYTAL EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL 400
    SRQQRSFQTL DQECIQMKAR LTQELQQAKN MHNVLQAELD KLTSVKQQLE 450
    NNLEEFKQKL CRAEQAFQAS QIKENELRRS MEEMKKENNL LKSHSEQKAR 500
    EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL QEKINQQENS 550
    LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS 600
    ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC 650
    LKTQQIKSHE YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY 700
    MELQQKAEFS DQKHQKEIEN MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD 750
    RCYQDLHAEY ESLRDLLKSK DASLVTNEDH QRSLLAFDQQ PAMHHSFANI 800
    IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE SQKQMNSDLQ 850
    KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA 900
    ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET 950
    LSLEKKEMSS IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF 1000
    ANYIDEREKS ISELSDQYKQ EKLILLQRCE ETGNAYEDLS QKYKAAQEKN 1050
    SKLECLLNEC TSLCENRKNE LEQLKEAFAK EHQEFLTKLA FAEERNQNLM 1100
    LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN KMQKEVNDLL 1150
    QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE 1200
    ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL 1250
    QDMQSQEISG LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL 1300
    NELEKICEIL QAEKYELVTE LNDSRSECIT ATRKMAEEVG KLLNEVKILN 1350
    DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS LAPLDESNSY EHLTLSDKEV 1400
    QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD SLKAENLVLS 1450
    TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL 1500
    EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR 1550
    NFQGDLVKEM QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG 1600
    DMSLLSNLEG VVSANQCSVD EVFCSSLQEE NLTRKETPSA PAKGVEELES 1650
    LCEVYRQSLE KLEEKMESQG IMKNKEIQEL EQLLSSERQE LDCLRKQYLS 1700
    ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ LQGLDLSSRS 1750
    LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL 1800
    DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP 1850
    NALVPMDFLG NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM 1900
    KELDSKLHLQ EVQLMTKIEA CIELEKIVGE LKKENSDLSE KLEYFSCDHQ 1950
    ELLQRVETSE GLNSDLEMHA DKSSREDIGD NVAKVNDSWK ERFLDVENEL 2000
    SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK VIVCLEEELS 2050
    VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV 2100
    AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL 2150
    ENQIAQLNKE KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA 2200
    LRLSSTQEEV HQLRRGIEKL RVRIEADEKK QLHIAEKLKE RERENDSLKD 2250
    KVENLERELQ MSEENQELVI LDAENSKAEV ETLKTQIEEM ARSLKVFELD 2300
    LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE QAEIQIKEES 2350
    KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE 2400
    KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH 2450
    AALEAENSKG EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE 2500
    QERISELEII NSSFENILQE KEQEKVQMKE KSSTAMEMLQ TQLKELNERV 2550
    AALHNDQEAC KAKEQNLSSQ VECLELEKAQ LLQGLDEAKN NYIVLQSSVN 2600
    GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV EGEHQLWKEQ 2650
    NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK 2700
    MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL 2750
    EEIKSSKDQL KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH 2800
    EAEKKHQALL LDTNKQYEVE IQTYREKLTS KEECLSSQKL EIDLLKSSKE 2850
    ELNNSLKATT QILEELKKTK MDNLKYVNQL KKENERAQGK MKLLIKSCKQ 2900
    LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK ELKETLEEKT 2950
    KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG 3000
    PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS 3050
    KKSKKAVMSG IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR 3100
    TTMATRTSPR LAAQKLALSP LSLGKENLAE SSKPTAGGSR SQKVKVAQRS 3150
    PVDSGTILRE PTTKSVPVNN LPERSPTDSP REGLRVKRGR LVPSPKAGLE 3200
    SNGSENCKVQ 3210
    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.
    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. 18 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.
    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

    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 1, 2014
    This is version 149 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

    Dasty 3