CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 M-phase phosphoprotein 8 
Protein Synonyms/Alias
 Two hybrid-associated protein 3 with RanBPM; Twa3 
Gene Name
 MPHOSPH8 
Gene Synonyms/Alias
 MPP8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73DMKTEGGKVLYKVRWacetylation[1]
172PDDLKKKKAKAGKLKacetylation[2]
177KKKAKAGKLKDKSKPacetylation[2]
458FKLTPEEKNDVSENNubiquitination[1, 3]
550MKLEDFQKHLDGKDEubiquitination[3]
555FQKHLDGKDENFAATubiquitination[3]
575NVLRDAVKNGDYITVubiquitination[1, 3]
623LLRLLITKGAKVNGRubiquitination[1, 3]
708NSALHFAKQSNNVLVubiquitination[3, 4, 5]
720VLVYDLLKNHLETLSubiquitination[3]
735RVAEETIKDYFEARLubiquitination[1, 3]
847LTEAPSAKVKLLIGAubiquitination[3]
849EAPSAKVKLLIGAYRubiquitination[4, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Involved in transcriptional regulation. Specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression. 
Sequence Annotation
 DOMAIN 59 118 Chromo.
 REPEAT 600 629 ANK 1.
 REPEAT 633 662 ANK 2.
 REPEAT 666 695 ANK 3.
 REPEAT 699 728 ANK 4.
 REGION 80 87 Histone H3K9me3 binding.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 85 85 Phosphoserine (By similarity).
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 138 138 Phosphoserine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 189 189 Phosphoserine.
 MOD_RES 192 192 Phosphoserine.
 MOD_RES 272 272 Phosphoserine (Potential).
 MOD_RES 319 319 Phosphoserine.
 MOD_RES 334 334 Phosphothreonine (Potential).
 MOD_RES 385 385 Phosphothreonine (Potential).
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 403 403 Phosphoserine.
 MOD_RES 454 454 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ANK repeat; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 860 AA 
Protein Sequence
MEQVAEGARV TAVPVSAADS TEELAEVEEG VGVVGEDNDA AARGAEAFGD SEEDGEDVFE 60
VEKILDMKTE GGKVLYKVRW KGYTSDDDTW EPEIHLEDCK EVLLEFRKKI AENKAKAVRK 120
DIQRLSLNND IFEANSDSDQ QSETKEDTSP KKKKKKLRQR EEKSPDDLKK KKAKAGKLKD 180
KSKPDLESSL ESLVFDLRTK KRISEAKEEL KESKKPKKDE VKETKELKKV KKGEIRDLKT 240
KTREDPKENR KTKKEKFVES QVESESSVLN DSPFPEDDSE GLHSDSREEK QNTKSARERA 300
GQDMGLEHGF EKPLDSAMSA EEDTDVRGRR KKKTPRKAED TRENRKLENK NAFLEKKTVP 360
KKQRNQDRSK SAAELEKLMP VSAQTPKGRR LSGEERGLWS TDSAEEDKET KRNESKEKYQ 420
KRHDSDKEEK GRKEPKGLKT LKEIRNAFDL FKLTPEEKND VSENNRKREE IPLDFKTIDD 480
HKTKENKQSL KERRNTRDET DTWAYIAAEG DQEVLDSVCQ ADENSDGRQQ ILSLGMDLQL 540
EWMKLEDFQK HLDGKDENFA ATDAIPSNVL RDAVKNGDYI TVKVALNSNE EYNLDQEDSS 600
GMTLVMLAAA GGQDDLLRLL ITKGAKVNGR QKNGTTALIH AAEKNFLTTV AILLEAGAFV 660
NVQQSNGETA LMKACKRGNS DIVRLVIECG ADCNILSKHQ NSALHFAKQS NNVLVYDLLK 720
NHLETLSRVA EETIKDYFEA RLALLEPVFP IACHRLCEGP DFSTDFNYKP PQNIPEGSGI 780
LLFIFHANFL GKEVIARLCG PCSVQAVVLN DKFQLPVFLD SHFVYSFSPV AGPNKLFIRL 840
TEAPSAKVKL LIGAYRVQLQ 860 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
 GO:0000788; C:nuclear nucleosome; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; NAS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0044030; P:regulation of DNA methylation; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS. 
Pfam
 PF00023; Ank
 PF12796; Ank_2
 PF00385; Chromo 
SMART
 SM00248; ANK
 SM00298; CHROMO 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS00598; CHROMO_1
 PS50013; CHROMO_2 
PRINTS