CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008156
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centromere protein F 
Protein Synonyms/Alias
 CENP-F; AH antigen; Kinetochore protein CENPF; Mitosin 
Gene Name
 CENPF 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19LPTRALQKIQELEGQubiquitination[1, 2]
163SQYYSGSKYEDLKEKubiquitination[3]
223VFSWQQEKTPSHLSSubiquitination[4, 5]
263RSTLQIGKRDANSSFubiquitination[5, 6]
284PHLLDQLKAQNQELRubiquitination[5, 7]
314EMKGQVNKFQELQLQubiquitination[1, 2]
356QYDQASTKYTALEQKubiquitination[1, 2]
457ENNLEEFKQKLCRAEubiquitination[8]
513EAELKNIKQCLNQSQubiquitination[5, 6]
527QNFAEEMKAKNTSQEubiquitination[5]
543MLRDLQEKINQQENSubiquitination[5, 6, 7]
555ENSLTLEKLKLAVADubiquitination[1, 2, 5]
557SLTLEKLKLAVADLEubiquitination[5]
587HIEQLNDKLSKTEKEubiquitination[5]
628CWKSENEKLLTQMESubiquitination[5]
657CLKTQQIKSHEYNERubiquitination[5]
689LHNVLDSKSVEVETQubiquitination[4, 7]
697SVEVETQKLAYMELQubiquitination[3, 4, 5, 6, 7]
706AYMELQQKAEFSDQKubiquitination[3, 4, 5, 7]
768ESLRDLLKSKDASLVubiquitination[1, 2]
770LRDLLKSKDASLVTNubiquitination[1, 2, 5, 6, 7]
823LEADQSPKNSAILQNubiquitination[1, 2, 3, 4, 5, 6, 7, 9]
911SALENKEKELQLLNDubiquitination[1, 2]
919ELQLLNDKVETEQAEubiquitination[3, 7]
956ETLSLEKKEMSSIISubiquitination[1, 2]
1022SDQYKQEKLILLQRCubiquitination[1, 2]
1088EHQEFLTKLAFAEERubiquitination[1, 2]
1122TDNQNNSKSEAGGLKubiquitination[7]
1136KQEIMTLKEEQNKMQubiquitination[7]
1314CEILQAEKYELVTELubiquitination[5]
1334ECITATRKMAEEVGKubiquitination[1, 2]
1341KMAEEVGKLLNEVKIacetylation[6, 10, 11]
1341KMAEEVGKLLNEVKIubiquitination[1, 2]
1410HFAELQEKFLSLQSEubiquitination[1, 2]
1675SQGIMKNKEIQELEQubiquitination[5, 7]
1906EMKELDSKLHLQEVQubiquitination[1, 2]
2079ALDQLSEKMKEKTQEubiquitination[1, 2]
2132DKTHLQEKLQSLEKDubiquitination[1, 2]
2671KIQVLQSKNASLQDTubiquitination[3]
2831YREKLTSKEECLSSQubiquitination[9]
2870LEELKKTKMDNLKYVacetylation[12]
2875KTKMDNLKYVNQLKKacetylation[6, 10, 11, 13]
2881LKYVNQLKKENERAQacetylation[12]
2940DELTTEIKELKETLEubiquitination[1, 2]
3092FADIPTGKTSPYILRubiquitination[9]
3115SPRLAAQKLALSPLSubiquitination[9]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [12] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [13] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 1435 1530 1-1.
 REPEAT 1531 1626 1-2.
 REPEAT 2207 2386 2-1.
 REPEAT 2389 2568 2-2.
 REGION 1 481 Interaction with SNAP25 and required for
 REGION 1435 1626 2 X 96 AA approximate tandem repeats.
 REGION 2122 2447 Interaction with NDE1 and NDEL1.
 REGION 2207 2568 2 X 177 AA tandem repeats.
 REGION 2488 3113 Sufficient for centromere localization.
 REGION 2488 2925 Sufficient for self-association.
 REGION 2927 3113 Sufficient for nuclear localization.
 MOTIF 3015 3032 Nuclear localization signal (Potential).
 MOD_RES 106 106 Phosphoserine.
 MOD_RES 144 144 Phosphothreonine.
 MOD_RES 151 151 Phosphothreonine.
 MOD_RES 154 154 Phosphothreonine.
 MOD_RES 158 158 Phosphotyrosine.
 MOD_RES 276 276 Phosphoserine.
 MOD_RES 773 773 Phosphoserine.
 MOD_RES 783 783 Phosphoserine.
 MOD_RES 821 821 Phosphoserine.
 MOD_RES 834 834 Phosphoserine.
 MOD_RES 876 876 Phosphoserine.
 MOD_RES 1248 1248 Phosphoserine.
 MOD_RES 1255 1255 Phosphoserine.
 MOD_RES 1259 1259 Phosphoserine.
 MOD_RES 1747 1747 Phosphoserine.
 MOD_RES 1748 1748 Phosphoserine.
 MOD_RES 1750 1750 Phosphoserine.
 MOD_RES 1988 1988 Phosphoserine.
 MOD_RES 2512 2512 Phosphoserine.
 MOD_RES 2513 2513 Phosphoserine.
 MOD_RES 2875 2875 N6-acetyllysine.
 MOD_RES 2996 2996 Phosphoserine.
 MOD_RES 3007 3007 Phosphoserine.
 MOD_RES 3018 3018 Phosphoserine.
 MOD_RES 3045 3045 Phosphothreonine.
 MOD_RES 3048 3048 Phosphoserine.
 MOD_RES 3094 3094 Phosphoserine.
 MOD_RES 3119 3119 Phosphoserine.
 MOD_RES 3122 3122 Phosphoserine.
 MOD_RES 3150 3150 Phosphoserine.
 MOD_RES 3175 3175 Phosphoserine.
 MOD_RES 3179 3179 Phosphoserine.
 MOD_RES 3207 3207 Cysteine methyl ester (Probable).
 LIPID 3207 3207 S-farnesyl cysteine.  
Keyword
 Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; DNA synthesis; Kinetochore; Lipoprotein; Methylation; Mitosis; Myogenesis; Nucleus; Phosphoprotein; Polymorphism; Prenylation; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3210 AA 
Protein Sequence
MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT 60
EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR 120
CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR 180
LEAEVKALQA KKASQTLPQA TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD 240
FSASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR 300
LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKYTAL 360
EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQMKAR 420
LTQELQQAKN MHNVLQAELD KLTSVKQQLE NNLEEFKQKL CRAEQAFQAS QIKENELRRS 480
MEEMKKENNL LKSHSEQKAR EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL 540
QEKINQQENS LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS 600
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE 660
YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY MELQQKAEFS DQKHQKEIEN 720
MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH 780
QRSLLAFDQQ PAMHHSFANI IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE 840
SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA 900
ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET LSLEKKEMSS 960
IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ 1020
EKLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK 1080
EHQEFLTKLA FAEERNQNLM LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN 1140
KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE 1200
ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL QDMQSQEISG 1260
LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL NELEKICEIL QAEKYELVTE 1320
LNDSRSECIT ATRKMAEEVG KLLNEVKILN DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS 1380
LAPLDESNSY EHLTLSDKEV QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD 1440
SLKAENLVLS TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL 1500
EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQTYVDSLKA ENLVLSTNLR NFQGDLVKEM 1560
QLGLEEGLVP SLSSSCVPDS SSLSSLGDSS FYRALLEQTG DMSLLSNLEG VVSANQCSVD 1620
EVFCSSLQEE NLTRKETPSA PAKGVEELES LCEVYRQSLE KLEEKMESQG IMKNKEIQEL 1680
EQLLSSERQE LDCLRKQYLS ENEQWQQKLT SVTLEMESKL AAEKKQTEQL SLELEVARLQ 1740
LQGLDLSSRS LLGIDTEDAI QGRNESCDIS KEHTSETTER TPKHDVHQIC DKDAQQDLNL 1800
DIEKITETGA VKPTGECSGE QSPDTNYEPP GEDKTQGSSE CISELSFSGP NALVPMDFLG 1860
NQEDIHNLQL RVKETSNENL RLLHVIEDRD RKVESLLNEM KELDSKLHLQ EVQLMTKIEA 1920
CIELEKIVGE LKKENSDLSE KLEYFSCDHQ ELLQRVETSE GLNSDLEMHA DKSSREDIGD 1980
NVAKVNDSWK ERFLDVENEL SRIRSEKASI EHEALYLEAD LEVVQTEKLC LEKDNENKQK 2040
VIVCLEEELS VVTSERNQLR GELDTMSKKT TALDQLSEKM KEKTQELESH QSECLHCIQV 2100
AEAEVKEKTE LLQTLSSDVS ELLKDKTHLQ EKLQSLEKDS QALSLTKCEL ENQIAQLNKE 2160
KELLVKESES LQARLSESDY EKLNVSKALE AALVEKGEFA LRLSSTQEEV HQLRRGIEKL 2220
RVRIEADEKK QLHIAEKLKE RERENDSLKD KVENLERELQ MSEENQELVI LDAENSKAEV 2280
ETLKTQIEEM ARSLKVFELD LVTLRSEKEN LTKQIQEKQG QLSELDKLLS SFKSLLEEKE 2340
QAEIQIKEES KTAVEMLQNQ LKELNEAVAA LCGDQEIMKA TEQSLDPPIE EEHQLRNSIE 2400
KLRARLEADE KKQLCVLQQL KESEHHADLL KGRVENLERE LEIARTNQEH AALEAENSKG 2460
EVETLKAKIE GMTQSLRGLE LDVVTIRSEK ENLTNELQKE QERISELEII NSSFENILQE 2520
KEQEKVQMKE KSSTAMEMLQ TQLKELNERV AALHNDQEAC KAKEQNLSSQ VECLELEKAQ 2580
LLQGLDEAKN NYIVLQSSVN GLIQEVEDGK QKLEKKDEEI SRLKNQIQDQ EQLVSKLSQV 2640
EGEHQLWKEQ NLELRNLTVE LEQKIQVLQS KNASLQDTLE VLQSSYKNLE NELELTKMDK 2700
MSFVEKVNKM TAKETELQRE MHEMAQKTAE LQEELSGEKN RLAGELQLLL EEIKSSKDQL 2760
KELTLENSEL KKSLDCMHKD QVEKEGKVRE EIAEYQLRLH EAEKKHQALL LDTNKQYEVE 2820
IQTYREKLTS KEECLSSQKL EIDLLKSSKE ELNNSLKATT QILEELKKTK MDNLKYVNQL 2880
KKENERAQGK MKLLIKSCKQ LEEEKEILQK ELSQLQAAQE KQKTGTVMDT KVDELTTEIK 2940
ELKETLEEKT KEADEYLDKY CSLLISHEKL EKAKEMLETQ VAHLCSQQSK QDSRGSPLLG 3000
PVVPGPSPIP SVTEKRLSSG QNKASGKRQR SSGIWENGRG PTPATPESFS KKSKKAVMSG 3060
IHPAEDTEGT EFEPEGLPEV VKKGFADIPT GKTSPYILRR TTMATRTSPR LAAQKLALSP 3120
LSLGKENLAE SSKPTAGGSR SQKVKVAQRS PVDSGTILRE PTTKSVPVNN LPERSPTDSP 3180
REGLRVKRGR LVPSPKAGLE SNGSENCKVQ 3210 
Gene Ontology
 GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; NAS:UniProtKB.
 GO:0045502; F:dynein binding; IDA:UniProtKB.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0000085; P:G2 phase of mitotic cell cycle; IMP:UniProtKB.
 GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
 GO:0000087; P:M phase of mitotic cell cycle; IDA:UniProtKB.
 GO:0051310; P:metaphase plate congression; IDA:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; NAS:UniProtKB.
 GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0015031; P:protein transport; IDA:UniProtKB.
 GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
 GO:0042493; P:response to drug; NAS:UniProtKB. 
Interpro
 IPR019513; Centromere_CenpF_leu-rich_rpt.
 IPR018463; Centromere_CenpF_N.
 IPR018302; Centromere_CenpF_Rb-prot-bd. 
Pfam
 PF10473; Cenp-F_leu_zip
 PF10481; Cenp-F_N
 PF10490; Rb-bdg_C_Cenp-F 
SMART
  
PROSITE
  
PRINTS