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P49454 (CENPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein F

Short name=CENP-F
Alternative name(s):
AH antigen
Kinetochore protein CENPF
Mitosin
Gene names
Name:CENPF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.12

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.12

Subcellular location

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. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.9 Ref.12

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.

Sequence similarities

Belongs to the centromere protein F family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
DNA synthesis
Mitosis
Myogenesis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
   Molecular functionDevelopmental protein
   PTMAcetylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Non-traceable author statement PubMed 12507285PubMed 15927522. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype PubMed 16252009. Source: UniProtKB

kinetochore assembly

Non-traceable author statement PubMed 16252009. Source: UniProtKB

metaphase plate congression

Inferred from direct assay PubMed 15870278. Source: UniProtKB

mitotic G2 phase

Inferred from mutant phenotype PubMed 12154071Ref.2. Source: UniProtKB

mitotic M phase

Inferred from direct assay Ref.1. Source: UniProtKB

mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Non-traceable author statement Ref.9. Source: UniProtKB

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15677469. 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 cell cycle

Traceable author statement. Source: Reactome

regulation of striated muscle tissue development

Inferred from sequence or structural similarity PubMed 10373470. Source: UniProtKB

response to drug

Non-traceable author statement PubMed 12467231. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from direct assay Ref.1Ref.2. Source: UniProtKB

condensed chromosome outer kinetochore

Inferred from direct assay Ref.1Ref.6PubMed 7904902. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay PubMed 17363900Ref.1. Source: UniProtKB

midbody

Inferred from direct assay Ref.2. Source: UniProtKB

nuclear envelope

Inferred from direct assay PubMed 12154071. Source: UniProtKB

nuclear matrix

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1Ref.6Ref.2. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

pronucleus

Inferred from electronic annotation. Source: Ensembl

spindle

Inferred from direct assay Ref.2. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionchromatin binding

Non-traceable author statement PubMed 9891037. 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 binding

Inferred from physical interaction PubMed 17363900Ref.12Ref.2Ref.7. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.6. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15677469. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NDEL1Q9GZM85EBI-968343,EBI-928842
NUP133Q8WUM02EBI-968343,EBI-295695

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 32073207Centromere protein F
PRO_0000089477
Propeptide3208 – 32103Removed in mature form Probable
PRO_0000396744

Regions

Repeat1435 – 1530961-1
Repeat1531 – 1626961-2
Repeat2207 – 23861802-1
Repeat2389 – 25681802-2
Region1 – 481481Interaction with SNAP25 and required for localization to the cytoplasm By similarity
Region1435 – 16261922 X 96 AA approximate tandem repeats
Region2122 – 2447326Interaction with NDE1 and NDEL1
Region2207 – 25683622 X 177 AA tandem repeats
Region2488 – 3113626Sufficient for centromere localization
Region2488 – 2925438Sufficient for self-association
Region2927 – 3113187Sufficient for nuclear localization
Coiled coil14 – 197184 Potential
Coiled coil273 – 769497 Potential
Coiled coil823 – 1328506 Potential
Coiled coil1642 – 1746105 Potential
Coiled coil1862 – 29871126 Potential
Motif3015 – 303218Nuclear localization signal Potential

Amino acid modifications

Modified residue1061Phosphoserine Ref.16
Modified residue1441Phosphothreonine Ref.16
Modified residue1511Phosphothreonine Ref.20
Modified residue1541Phosphothreonine Ref.20
Modified residue1581Phosphotyrosine Ref.20
Modified residue2761Phosphoserine Ref.20
Modified residue7731Phosphoserine Ref.20
Modified residue7831Phosphoserine Ref.20
Modified residue8211Phosphoserine Ref.20
Modified residue8341Phosphoserine Ref.16
Modified residue8761Phosphoserine Ref.20
Modified residue12481Phosphoserine Ref.16 Ref.20
Modified residue12551Phosphoserine Ref.20
Modified residue12591Phosphoserine Ref.20
Modified residue17471Phosphoserine Ref.11 Ref.16 Ref.20
Modified residue17481Phosphoserine Ref.16
Modified residue17501Phosphoserine Ref.11 Ref.16 Ref.20
Modified residue19881Phosphoserine Ref.20
Modified residue25121Phosphoserine Ref.16
Modified residue25131Phosphoserine Ref.16 Ref.20
Modified residue28751N6-acetyllysine Ref.19
Modified residue29961Phosphoserine Ref.16 Ref.18 Ref.20
Modified residue30071Phosphoserine Ref.16 Ref.18 Ref.20
Modified residue30181Phosphoserine Ref.20
Modified residue30451Phosphothreonine Ref.20
Modified residue30481Phosphoserine Ref.20
Modified residue30941Phosphoserine Ref.20
Modified residue31191Phosphoserine Ref.13 Ref.16 Ref.20 Ref.22
Modified residue31221Phosphoserine Ref.16 Ref.20
Modified residue31501Phosphoserine Ref.15 Ref.16 Ref.20 Ref.22
Modified residue31751Phosphoserine Ref.16 Ref.20
Modified residue31791Phosphoserine Ref.16 Ref.20
Modified residue32071Cysteine methyl ester Probable
Lipidation32071S-farnesyl cysteine Ref.8

Natural variations

Natural variant2501Q → L. Ref.1
Corresponds to variant rs1050065 [ dbSNP | Ensembl ].
VAR_055049
Natural variant2721D → G. Ref.1
Corresponds to variant rs1050066 [ dbSNP | Ensembl ].
VAR_055050
Natural variant3001R → C.
Corresponds to variant rs17023281 [ dbSNP | Ensembl ].
VAR_034712
Natural variant4941H → Q.
Corresponds to variant rs2070065 [ dbSNP | Ensembl ].
VAR_034713
Natural variant7011M → V.
Corresponds to variant rs3795524 [ dbSNP | Ensembl ].
VAR_034714
Natural variant7541Q → E.
Corresponds to variant rs3795523 [ dbSNP | Ensembl ].
VAR_034715
Natural variant8151R → H.
Corresponds to variant rs3795522 [ dbSNP | Ensembl ].
VAR_034716
Natural variant10181Y → D.
Corresponds to variant rs3795519 [ dbSNP | Ensembl ].
VAR_034717
Natural variant10331G → R.
Corresponds to variant rs3795518 [ dbSNP | Ensembl ].
VAR_034718
Natural variant11051T → I.
Corresponds to variant rs12067133 [ dbSNP | Ensembl ].
VAR_034719
Natural variant14121L → S.
Corresponds to variant rs3795517 [ dbSNP | Ensembl ].
VAR_034720
Natural variant15151A → T.
Corresponds to variant rs2666839 [ dbSNP | Ensembl ].
VAR_034721
Natural variant1516 – 161196Missing.
VAR_036701
Natural variant15391K → R.
Corresponds to variant rs3795514 [ dbSNP | Ensembl ].
VAR_034722
Natural variant18641D → N.
Corresponds to variant rs3748692 [ dbSNP | Ensembl ].
VAR_055638
Natural variant20111E → A.
Corresponds to variant rs3790647 [ dbSNP | Ensembl ].
VAR_034723
Natural variant32021N → K. Ref.1 Ref.2 Ref.5
Corresponds to variant rs7289 [ dbSNP | Ensembl ].
VAR_014839

Experimental info

Sequence conflict161A → T in AAA82889. Ref.1
Sequence conflict481L → P in AAA82889. Ref.1
Sequence conflict481L → P in AAA82935. Ref.2
Sequence conflict521K → T in AAA82889. Ref.1
Sequence conflict521K → T in AAA82935. Ref.2
Sequence conflict6111Missing in AAA82935. Ref.2
Sequence conflict18111V → L in AAA82935. Ref.2
Sequence conflict2242 – 22432ER → DG in AAA86889. Ref.4
Sequence conflict23351L → Q in AAA86889. Ref.4
Sequence conflict24921N → D in AAA82889. Ref.1
Sequence conflict24921N → D in AAA86889. Ref.4
Sequence conflict2545 – 256117ELNER…QEACK → SSMREWQPCIMTKKPVS in AAA86889. Ref.4
Sequence conflict30391R → G in AAA82889. Ref.1
Sequence conflict30391R → G in AAA82935. Ref.2
Sequence conflict30391R → G in AAA86889. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P49454 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: FF20F99216257BAD

FASTA3,210367,764
        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 

« Hide

References

« Hide '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] [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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [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, 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]"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] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

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.
PIRPC4035.
RefSeqNP_057427.3. NM_016343.3.
UniGeneHs.497741.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107492. 18 interactions.
IntActP49454. 11 interactions.
MINTMINT-2803614.
STRING9606.ENSP00000355922.

PTM databases

PhosphoSiteP49454.

Polymorphism databases

DMDM156630875.

Proteomic databases

MaxQBP49454.
PaxDbP49454.
PRIDEP49454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366955; ENSP00000355922; ENSG00000117724.
GeneID1063.
KEGGhsa:1063.
UCSCuc001hkm.3. human.

Organism-specific databases

CTD1063.
GeneCardsGC01P214776.
H-InvDBHIX0028827.
HGNCHGNC:1857. CENPF.
HPACAB009581.
HPA052382.
MIM600236. gene.
neXtProtNX_P49454.
PharmGKBPA26401.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG050893.
KOK11499.
OrthoDBEOG7FV3PD.
PhylomeDBP49454.
TreeFamTF101133.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeP49454.
CleanExHS_CENPF.
GenevestigatorP49454.

Family and domain databases

InterProIPR018302. CenpF/LEK1_Rb-prot-bd.
IPR019513. Centromere_CenpF_leu-rich_rpt.
IPR018463. Centromere_CenpF_N.
[Graphical view]
PfamPF10490. CENP-F_C_Rb_bdg. 1 hit.
PF10473. CENP-F_leu_zip. 3 hits.
PF10481. CENP-F_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCENPF. human.
GeneWikiCENPF.
GenomeRNAi1063.
NextBio4446.
PROP49454.
SOURCESearch...

Entry information

Entry nameCENPF_HUMAN
AccessionPrimary (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: June 11, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM