CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015913
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pogo transposable element with ZNF domain 
Protein Synonyms/Alias
 Suppressor of hairy wing homolog 5; Zinc finger protein 280E; Zinc finger protein 635 
Gene Name
 POGZ 
Gene Synonyms/Alias
 KIAA0461; SUHW5; ZNF280E; ZNF635; Nbla00003 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
489AQLTNFPKVATSFRCubiquitination[1]
801HVPRKSPKYLALFKNacetylation[2]
801HVPRKSPKYLALFKNubiquitination[3, 4]
883PPSFPTNKAATVKSAacetylation[5]
1053NEETLFQKATKIGRSubiquitination[6]
1056TLFQKATKIGRSLEGubiquitination[6]
1223HTACQRSKGMLVMDCubiquitination[6]
1269QPLDVCIKRTVKNFLubiquitination[6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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] 
Functional Description
 Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. 
Sequence Annotation
 DOMAIN 1015 1085 HTH CENPB-type.
 DOMAIN 1117 1323 DDE.
 ZN_FING 375 397 C2H2-type 1; atypical.
 ZN_FING 494 516 C2H2-type 2.
 ZN_FING 530 553 C2H2-type 3.
 ZN_FING 560 583 C2H2-type 4.
 ZN_FING 590 613 C2H2-type 5.
 ZN_FING 619 641 C2H2-type 6.
 ZN_FING 647 670 C2H2-type 7.
 ZN_FING 771 794 C2H2-type 8.
 ZN_FING 815 840 C2H2-type 9.
 REGION 810 850 Required for interaction with CBX5.
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 425 425 Phosphoserine.
 MOD_RES 439 439 Phosphothreonine.
 MOD_RES 445 445 Phosphoserine.
 MOD_RES 1338 1338 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1410 AA 
Protein Sequence
MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT TVSVSQQPVS APVPIAAHAS 60
VAGHLSTSTT VSSSGAQNSD STKKTLVTLI ANNNAGNPLV QQGGQPLILT QNPAPGLGTM 120
VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ 180
TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST 240
VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AVQSPGQSNQ TTNPKLAPSF PSPPAVSIAS 300
FVTVKRPGVT GENSNEVAKL VNTLNTIPSL GQSPGPVVVS NNSSAHGSQR TSGPESSMKV 360
TSSIPVFDLQ DGGRKICPRC NAQFRVTEAL RGHMCYCCPE MVEYQKKGKS LDSEPSVPSA 420
AKPPSPEKTA PVASTPSSTP IPALSPPTKV PEPNENVGDA VQTKLIMLVD DFYYGRDGGK 480
VAQLTNFPKV ATSFRCPHCT KRLKNNIRFM NHMKHHVELD QQNGEVDGHT ICQHCYRQFS 540
TPFQLQCHLE NVHSPYESTT KCKICEWAFE SEPLFLQHMK DTHKPGEMPY VCQVCQYRSS 600
LYSEVDVHFR MIHEDTRHLL CPYCLKVFKN GNAFQQHYMR HQKRNVYHCN KCRLQFLFAK 660
DKIEHKLQHH KTFRKPKQLE GLKPGTKVTI RASRGQPRTV PVSSNDTPPS ALQEAAPLTS 720
SMDPLPVFLY PPVQRSIQKR AVRKMSVMGR QTCLECSFEI PDFPNHFPTY VHCSLCRYST 780
CCSRAYANHM INNHVPRKSP KYLALFKNSV SGIKLACTSC TFVTSVGDAM AKHLVFNPSH 840
RSSSILPRGL TWIAHSRHGQ TRDRVHDRNV KNMYPPPSFP TNKAATVKSA GATPAEPEEL 900
LTPLAPALPS PASTATPPPT PTHPQALALP PLATEGAECL NVDDQDEGSP VTQEPELASG 960
GGGSGGVGKK EQLSVKKLRV VLFALCCNTE QAAEHFRNPQ RRIRRWLRRF QASQGENLEG 1020
KYLSFEAEEK LAEWVLTQRE QQLPVNEETL FQKATKIGRS LEGGFKISYE WAVRFMLRHH 1080
LTPHARRAVA HTLPKDVAEN AGLFIDFVQR QIHNQDLPLS MIVAIDEISL FLDTEVLSSD 1140
DRKENALQTV GTGEPWCDVV LAILADGTVL PTLVFYRGQM DQPANMPDSI LLEAKESGYS 1200
DDEIMELWST RVWQKHTACQ RSKGMLVMDC HRTHLSEEVL AMLSASSTLP AVVPAGCSSK 1260
IQPLDVCIKR TVKNFLHKKW KEQAREMADT ACDSDVLLQL VLVWLGEVLG VIGDCPELVQ 1320
RSFLVASVLP GPDGNINSPT RNADMQEELI ASLEEQLKLS GEHSESSTPR PRSSPEETIE 1380
PESLHQLFEG ESETESFYGF EEADLDLMEI 1410 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051382; P:kinetochore assembly; IMP:UniProtKB.
 GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB. 
Interpro
 IPR004875; DDE_SF_endonuclease_CENPB-like.
 IPR009057; Homeodomain-like.
 IPR006600; HTH_CenpB_DNA-bd_dom.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF03184; DDE_1
 PF03221; HTH_Tnp_Tc5 
SMART
 SM00674; CENPB
 SM00355; ZnF_C2H2 
PROSITE
 PS51253; HTH_CENPB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS