Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00289
Entry Name
UniProt Accession
Theoretical PI
5.03
Molecular Weight
367764.44
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
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
3207
Canonical
ESNGSENCKVQ****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Ashar HR, James L, Gray K, Carr D, Black S, Armstrong L, Bishop WR,Kirschmeier P. Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. J BiolChem. 2000 Sep 29;275(39):30451-7.[PMID:10852915]
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
Region: 1 481 Interaction with SNAP25 and required forlocalization to the cytoplasm.
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.
Modified residue: 106 106 Phosphoserine.
Modified residue: 144 144 Phosphothreonine.
Modified residue: 151 151 Phosphothreonine.
Modified residue: 154 154 Phosphothreonine.
Modified residue: 158 158 Phosphotyrosine.
Modified residue: 276 276 Phosphoserine.
Modified residue: 773 773 Phosphoserine.
Modified residue: 783 783 Phosphoserine.
Modified residue: 821 821 Phosphoserine.
Modified residue: 834 834 Phosphoserine.
Modified residue: 876 876 Phosphoserine.
Modified residue: 1248 1248 Phosphoserine.
Modified residue: 1255 1255 Phosphoserine.
Modified residue: 1259 1259 Phosphoserine.
Modified residue: 1747 1747 Phosphoserine.
Modified residue: 1748 1748 Phosphoserine.
Modified residue: 1750 1750 Phosphoserine.
Modified residue: 1988 1988 Phosphoserine.
Modified residue: 2512 2512 Phosphoserine.
Modified residue: 2513 2513 Phosphoserine.
Modified residue: 2875 2875 N6-acetyllysine.
Modified residue: 2996 2996 Phosphoserine.
Modified residue: 3007 3007 Phosphoserine.
Modified residue: 3018 3018 Phosphoserine.
Modified residue: 3045 3045 Phosphothreonine.
Modified residue: 3048 3048 Phosphoserine.
Modified residue: 3094 3094 Phosphoserine.
Modified residue: 3119 3119 Phosphoserine.
Modified residue: 3122 3122 Phosphoserine.
Modified residue: 3150 3150 Phosphoserine.
Modified residue: 3175 3175 Phosphoserine.
Modified residue: 3179 3179 Phosphoserine.
Modified residue: 3207 3207 Cysteine methyl ester.
Protein Length
3210 AA.
Protein Sequence
(Canonical)
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
FASTA
(Canonical)
>LipidDB-9606-00289|P49454
MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKT
EGTNLKRENQRLMEICESLEKTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKR
CKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYSGSKYEDLKEKYNKEVEERKR
LEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRD
FSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELR
LQGHEKEMKGQVNKFQELQLQLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTAL
EQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEELSRQQRSFQTLDQECIQMKAR
LTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRS
MEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDL
QEKINQQENSLTLEKLKLAVADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLS
ALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENLQSKINHLETCLKTQQIKSHE
YNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIEN
MCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDH
QRSLLAFDQQPAMHHSFANIIGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLE
SQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAETSQRISKLQEDTSAHQNVVA
ETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSS
IISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQ
EKLILLQRCEETGNAYEDLSQKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAK
EHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNNSKSEAGGLKQEIMTLKEEQN
KMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKE
ISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISG
LKDCEIDAEEKYISGPHELSTSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTE
LNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGELVEDIPGGEFGEQPNEQHPVS
LAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVD
SLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALL
EQTGDMSLLSNLEGAVSANQCSVDEVFCSSLQTYVDSLKAENLVLSTNLRNFQGDLVKEM
QLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGVVSANQCSVD
EVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQEL
EQLLSSERQELDCLRKQYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQ
LQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSETTERTPKHDVHQICDKDAQQDLNL
DIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPMDFLG
NQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEA
CIELEKIVGELKKENSDLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGD
NVAKVNDSWKERFLDVENELSRIRSEKASIEHEALYLEADLEVVQTEKLCLEKDNENKQK
VIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLHCIQV
AEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKE
KELLVKESESLQARLSESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKL
RVRIEADEKKQLHIAEKLKERERENDSLKDKVENLERELQMSEENQELVILDAENSKAEV
ETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLLEEKE
QAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIE
KLRARLEADEKKQLCVLQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKG
EVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNELQKEQERISELEIINSSFENILQE
KEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLELEKAQ
LLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQV
EGEHQLWKEQNLELRNLTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDK
MSFVEKVNKMTAKETELQREMHEMAQKTAELQEELSGEKNRLAGELQLLLEEIKSSKDQL
KELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQYEVE
IQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQL
KKENERAQGKMKLLIKSCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIK
ELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEMLETQVAHLCSQQSKQDSRGSPLLG
PVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKAVMSG
IHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSP
LSLGKENLAESSKPTAGGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSP
REGLRVKRGRLVPSPKAGLESNGSENCKVQ
Gene Ontology
GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB
GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0000776; C:kinetochore; IDA:UniProtKB
GO:0030496; C:midbody; IDA:UniProtKB
GO:0005635; C:nuclear envelope; IDA:UniProtKB
GO:0016363; C:nuclear matrix; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0045120; C:pronucleus; IEA:Ensembl
GO:0005819; C:spindle; IDA:UniProtKB
GO:0000922; C:spindle pole; IDA:UniProtKB
GO:0003682; F:chromatin binding; NAS:UniProtKB
GO:0045502; F:dynein binding; IDA:UniProtKB
GO:0008022; F:protein C-terminus binding; IPI:UniProtKB
GO:0042803; F:protein homodimerization activity; IPI:UniProtKB
GO:0008134; F:transcription factor binding; IPI:UniProtKB
GO:0030154; P:cell differentiation; IEA:UniProtKB-KW
GO:0008283; P:cell proliferation; NAS:UniProtKB
GO:0007059; P:chromosome segregation; IMP:UniProtKB
GO:0006260; P:DNA replication; IEA:UniProtKB-KW
GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome
GO:0051382; P:kinetochore assembly; NAS:UniProtKB
GO:0051310; P:metaphase plate congression; IDA:UniProtKB
GO:0000278; P:mitotic cell cycle; IMP:UniProtKB
GO:0007067; P:mitotic nuclear division; 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-templated; IDA:UniProtKB
GO:0015031; P:protein transport; IDA:UniProtKB
GO:0051726; P:regulation of cell cycle; TAS:Reactome
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
InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd
InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt
InterPro; IPR018463; Centromere_CenpF_N
Pfam
Pfam; PF10490; CENP-F_C_Rb_bdg;
Pfam; PF10473; CENP-F_leu_zip;
Pfam; PF10481; CENP-F_N;
SMART
PROSITE
PRINTS