CENPE_MOUSE - dbPTM
CENPE_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPE_MOUSE
UniProt AC Q6RT24
Protein Name Centromere-associated protein E {ECO:0000312|EMBL:AAR85498.1}
Gene Name Cenpe {ECO:0000312|MGI:MGI:1098230}
Organism Mus musculus (Mouse).
Sequence Length 2474
Subcellular Localization Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Chromosome, centromere . Associates with kinetochores during congression (as early as prometaphase), relocates to the spindle midzone at anaphase, and is quantitatively discarde
Protein Description Microtubule plus-end-directed kinetochore motor which plays an important role in chromosome congression, microtubule-kinetochore conjugation and spindle assembly checkpoint activation. Drives chromosome congression (alignment of chromosomes at the spindle equator resulting in the formation of the metaphase plate) by mediating the lateral sliding of polar chromosomes along spindle microtubules towards the spindle equator and by aiding the establishment and maintenance of connections between kinetochores and spindle microtubules. The transport of pole-proximal chromosomes towards the spindle equator is favored by microtubule tracks that are detyrosinated. Acts as a processive bi-directional tracker of dynamic microtubule tips; after chromosomes have congressed, continues to play an active role at kinetochores, enhancing their links with dynamic microtubule ends. Suppresses chromosome congression in NDC80-depleted cells and contributes positively to congression only when microtubules are stabilized (By similarity). Plays an important role in the formation of stable attachments between kinetochores and spindle microtubules. [PubMed: 12925705 The stabilization of kinetochore-microtubule attachment also requires CENPE-dependent localization of other proteins to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in spindle assembly checkpoint activation (SAC) via its interaction with BUB1B resulting in the activation of its kinase activity, which is important for activating SAC]
Protein Sequence MAEEASVAVCVRVRPLNSREEELGEATHIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCNAQKMKPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDGSVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPASLDETLTTLQFASTAKYMKNTPYVNEVSNDEALLKRYRREIADLRKQLEEVNTKTRAQEMEKDQLAQLLDEKDLLQKVQDEKINNLKRMLVTSSSIALQQELEIKRKRRVTWCYGKMKDSNYEKEFKVPTSITTRKRKTSVTSLRENSLMKFGESAASSEFEMLNNTLESLAEVEWSSATTLLSEENVESELNSLNAQYNDLVLDYEQLRRENEDLKLKLKEKNELEEFELLEQKEERDQEMQLMHEVSNLKNLIKHAEEYNQDLENDLSSKVKLLKEKEEQIKNLQEYIDAQKSEKMKIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRSENLELKEKINELSDSRKQMESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVDGKGLLSNLELEKRITDLQKELNKEAEEKQTLQEEVNLLSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQLSRRGSDGEWQALESLHAELEHRHAGVLEERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLRSDIQDTVNMNIDTQEQLLNALESLKQHQETINMLKMKAAEELSDNLHVKDRGGARDEAQQKMDGIDEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAEGLQAKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKSAPELQGEVPELLEQELLPVVKEARHSAEKVNGLEPVGAHSRTVHSMTMEGIEIGNLRLTKKLEESQMEISCLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETELSSVRGQLALTTAELERKVQELCEKQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEESQEEMKTLREEREELRRMQEALHVESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSVRKERDDLKKLEEILRMERDQLKDNLREAMLKAHQNHEETMKCGKGLLCAGEYCTGRLREKCFRIEKLLKRYSEMANDYECLNKVSLDLERETKTQKELSVTVRTKLSLPHTQTKEMEKLLTANQRCSLEFHRALKRLKYVLSSIARIKEEQHESINKREMAFIQEVEKQNELQIQIQSLSQTYRIPARDLQIKLSQEMDLHIEEMLKDFSENDFLTIKTEVQQVLNNRKEITEFLGKWLNTLFDTENLKSTIQKENKSIGLVNNFYHSRITAMINESTEFEERSATRSKDLDQYLKSLKETTEQLSEVYQTLTASQSVVHLHPTVQPSTRDSERPQAASGAEQLTSKNKIALGAVPYKEEIEDLKMQLVKSDLEKKATAKEFDKKILSLKATVEHQEEMIRLLRENLRGHQQAQDTSMISEQDSQLLSKPLTCGGGSGIVQSTKALILKSEYKRMGSEISKLKQQNEQLRKQNNQLLSDNSQLSNEVKTWEERTLKRDSYRETTCENSPKSPKVTRTDSKRRQNTTSQCRAQNLQDPVPKDSPKSWFFDNRSKSLPAPHPIRYFDNSSLGLCPEPDDVENVEPKTDLCQASLEKDVSQCKTQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
229PhosphorylationCDGSVKVSHLNLVDL
CCCCEEEEEEEEEEC		19.2822871156
245PhosphorylationGSERAAQTGAEGVRL
CCHHHHHHCCCCCCC		33.3622871156
404PhosphorylationLKRMLVTSSSIALQQ
HHHHHHHCHHHHHHH		18.0125338131
405PhosphorylationKRMLVTSSSIALQQE
HHHHHHCHHHHHHHH		19.1925338131
422PhosphorylationIKRKRRVTWCYGKMK
HHHHHCEEEEECCCC		14.1727600695
450PhosphorylationITTRKRKTSVTSLRE
CCCCCCCCCCCCHHH		32.2528066266
451PhosphorylationTTRKRKTSVTSLREN
CCCCCCCCCCCHHHC		26.8326824392
453PhosphorylationRKRKTSVTSLRENSL
CCCCCCCCCHHHCCC		23.0828066266
590AcetylationKVKLLKEKEEQIKNL
HHHHHHHHHHHHHHH		66.0323806337
614PhosphorylationEKMKIDLSYTSDATE
CCCCCCCCCCCCCHH		23.7128066266
615PhosphorylationKMKIDLSYTSDATED
CCCCCCCCCCCCHHH		19.9828066266
616PhosphorylationMKIDLSYTSDATEDL
CCCCCCCCCCCHHHH		19.4328066266
617PhosphorylationKIDLSYTSDATEDLK
CCCCCCCCCCHHHHH		19.6028066266
620PhosphorylationLSYTSDATEDLKQAM
CCCCCCCHHHHHHHH		34.7128066266
751PhosphorylationNLLSELKSLPSEVET
HHHHHHHCCCHHHHH		59.1320139300
758PhosphorylationSLPSEVETLRRELYE
CCCHHHHHHHHHHHH		30.6420139300
807PhosphorylationNTRDDLATSQLSRRG
CCHHHHHHHHHHHCC		25.0528066266
808PhosphorylationTRDDLATSQLSRRGS
CHHHHHHHHHHHCCC		24.4224719451
811PhosphorylationDLATSQLSRRGSDGE
HHHHHHHHHCCCCHH		16.5828066266
815PhosphorylationSQLSRRGSDGEWQAL
HHHHHCCCCHHHHHH		40.4025266776
824PhosphorylationGEWQALESLHAELEH
HHHHHHHHHHHHHHH		26.7225266776
844AcetylationLEERERLKQEIGALS
HHHHHHHHHHHHHHH		52.7022902405
979PhosphorylationSLKQHQETINMLKMK
HHHHHHHHHHHHHHH		15.87-
1020PhosphorylationGIDEQNESAHTLLGG
CCCCCCHHHHHHCCC		32.6625266776
1023PhosphorylationEQNESAHTLLGGGKD
CCCHHHHHHCCCCCC		24.3228066266
1034PhosphorylationGGKDNEVTEEQRKID
CCCCCCCCHHHHHHH		27.8527180971
1186PhosphorylationLAQRLHESYEEVKSI
HHHHHHHHHHHHHHH		27.3927149854
1449PhosphorylationSEAQGKMSELEQLRE
HHHHCCCHHHHHHHH		42.3822817900
1730PhosphorylationNENLKKITLVTKEND
HHHHHHEEEEECCCC		24.85-
1913AcetylationQNHEETMKCGKGLLC
HCHHHHHCCCCCEEH		47.4519861565
1938AcetylationEKCFRIEKLLKRYSE
HHHHHHHHHHHHHHH		57.6721728379
1938MalonylationEKCFRIEKLLKRYSE
HHHHHHHHHHHHHHH		57.6726073543
1941AcetylationFRIEKLLKRYSEMAN
HHHHHHHHHHHHHCC		60.7821728379
1973PhosphorylationTQKELSVTVRTKLSL
CHHHEEEEEEHHCCC		10.8220139300
2104PhosphorylationLNNRKEITEFLGKWL
HHCHHHHHHHHHHHH		23.0627180971
2257PhosphorylationTAKEFDKKILSLKAT
CHHHHHHHHHHHHHH		51.2024719451
2350PhosphorylationKQNNQLLSDNSQLSN
HHHHHHCCCCHHHHH		43.2530635358
2353PhosphorylationNQLLSDNSQLSNEVK
HHHCCCCHHHHHHHH		37.1730635358
2356PhosphorylationLSDNSQLSNEVKTWE
CCCCHHHHHHHHHHH		24.2530635358
2361PhosphorylationQLSNEVKTWEERTLK
HHHHHHHHHHHHHHC		43.1930635358
2376PhosphorylationRDSYRETTCENSPKS
CCCCCCCCCCCCCCC		17.0525266776
2380PhosphorylationRETTCENSPKSPKVT
CCCCCCCCCCCCCCC		16.0625263469
2383PhosphorylationTCENSPKSPKVTRTD
CCCCCCCCCCCCCCC		33.0824453211
2414PhosphorylationQDPVPKDSPKSWFFD
CCCCCCCCCCCCCCC		40.1125619855
2424PhosphorylationSWFFDNRSKSLPAPH
CCCCCCCCCCCCCCC		32.6225266776
2426PhosphorylationFFDNRSKSLPAPHPI
CCCCCCCCCCCCCCC		40.6126824392
2436PhosphorylationAPHPIRYFDNSSLGL
CCCCCEECCCCCCCC		5.2824719451
2437PhosphorylationPHPIRYFDNSSLGLC
CCCCEECCCCCCCCC		45.2124719451
2471MethylationLEKDVSQCKTQ----
HHHHHHHHCCC----		3.92-
2471FarnesylationLEKDVSQCKTQ----
HHHHHHHHCCC----		3.92-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CENPE_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPE_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CENPE_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLAP1_HUMANCLASP1physical
20360068
CENPE_HUMANCENPEphysical
20360068
CLAP2_HUMANCLASP2physical
20360068
C4BPA_HUMANC4BPAphysical
26496610
CALU_HUMANCALUphysical
26496610
CENPB_HUMANCENPBphysical
26496610
CLCA_HUMANCLTAphysical
26496610
DCTN1_HUMANDCTN1physical
26496610
DYHC1_HUMANDYNC1H1physical
26496610
DC1L2_HUMANDYNC1LI2physical
26496610
EF1D_HUMANEEF1Dphysical
26496610
EMD_HUMANEMDphysical
26496610
MARK2_HUMANMARK2physical
26496610
GOGA4_HUMANGOLGA4physical
26496610
HD_HUMANHTTphysical
26496610
LAMA5_HUMANLAMA5physical
26496610
LMNA_HUMANLMNAphysical
26496610
MTRR_HUMANMTRRphysical
26496610
NEK1_HUMANNEK1physical
26496610
PCM1_HUMANPCM1physical
26496610
PDE3A_HUMANPDE3Aphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
RCN1_HUMANRCN1physical
26496610
S12A2_HUMANSLC12A2physical
26496610
SYUG_HUMANSNCGphysical
26496610
PHLA2_HUMANPHLDA2physical
26496610
1433B_HUMANYWHABphysical
26496610
1433G_HUMANYWHAGphysical
26496610
1433F_HUMANYWHAHphysical
26496610
1433Z_HUMANYWHAZphysical
26496610
EVI5_HUMANEVI5physical
26496610
OFD1_HUMANOFD1physical
26496610
TAXB1_HUMANTAX1BP1physical
26496610
MAP7_HUMANMAP7physical
26496610
COX5A_HUMANCOX5Aphysical
26496610
SC24C_HUMANSEC24Cphysical
26496610
MATR3_HUMANMATR3physical
26496610
CE170_HUMANCEP170physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
ARC1B_HUMANARPC1Bphysical
26496610
DCTN2_HUMANDCTN2physical
26496610
SDCG3_HUMANSDCCAG3physical
26496610
IASPP_HUMANPPP1R13Lphysical
26496610
AFG32_HUMANAFG3L2physical
26496610
CLP1_HUMANCLP1physical
26496610
AKP13_HUMANAKAP13physical
26496610
SCMH1_HUMANSCMH1physical
26496610
CP131_HUMANCEP131physical
26496610
CLAP2_HUMANCLASP2physical
26496610
N4BP3_HUMANN4BP3physical
26496610
LAR4B_HUMANLARP4Bphysical
26496610
MTCL1_HUMANMTCL1physical
26496610
CLAP1_HUMANCLASP1physical
26496610
COR1C_HUMANCORO1Cphysical
26496610
TRI29_HUMANTRIM29physical
26496610
PTN23_HUMANPTPN23physical
26496610
SENP1_HUMANSENP1physical
26496610
RM04_HUMANMRPL4physical
26496610
DC1L1_HUMANDYNC1LI1physical
26496610
EGFL7_HUMANEGFL7physical
26496610
5NT3A_HUMANNT5C3Aphysical
26496610
UBR5_HUMANUBR5physical
26496610
TPPC4_HUMANTRAPPC4physical
26496610
STX18_HUMANSTX18physical
26496610
DJC10_HUMANDNAJC10physical
26496610
MACOI_HUMANTMEM57physical
26496610
CEP72_HUMANCEP72physical
26496610
BBX_HUMANBBXphysical
26496610
RHG21_HUMANARHGAP21physical
26496610
WIZ_HUMANWIZphysical
26496610
RM38_HUMANMRPL38physical
26496610
TPC6A_HUMANTRAPPC6Aphysical
26496610
GT251_HUMANCOLGALT1physical
26496610
IPO4_HUMANIPO4physical
26496610
SLIRP_HUMANSLIRPphysical
26496610
SEH1_HUMANSEH1Lphysical
26496610
DLRB1_HUMANDYNLRB1physical
26496610
CCD77_HUMANCCDC77physical
26496610
NAV1_HUMANNAV1physical
26496610
TRI41_HUMANTRIM41physical
26496610
TOP1M_HUMANTOP1MTphysical
26496610
CE128_HUMANCEP128physical
26496610
F122B_HUMANFAM122Bphysical
26496610
PATL1_HUMANPATL1physical
26496610
CCD18_HUMANCCDC18physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CENPE_MOUSE

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Related Literatures of Post-Translational Modification

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