CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019164
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger and BTB domain-containing protein 10 
Protein Synonyms/Alias
 Zinc finger protein RIN ZF 
Gene Name
 ZBTB10 
Gene Synonyms/Alias
 RINZF; RINZFC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
460QTCRNFIKDALNISIubiquitination[1, 2, 3]
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] 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]
 [3] 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
 May be involved in transcriptional regulation. 
Sequence Annotation
 DOMAIN 364 433 BTB.
 ZN_FING 722 744 C2H2-type 1.
 ZN_FING 750 772 C2H2-type 2.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 565 565 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 871 AA 
Protein Sequence
MSFSEMNRRT LAFRGGGLVT ASGGGSTNNN AGGEASAWPP QPQPRQPPPP APPALQPPNG 60
RGADEEVELE GLEPQDLEAS AGPAAGAAEE AKELLLPQDA GGPTSLGGGA GGPLLAERNR 120
RTLAFRGGGG GGLGNNGSSR GRPETSVWPL RHFNGRGPAT VDLELDALEG KELMQDGASL 180
SDSTEDEEEG ASLGDGSGAE GGSCSSSRRS GGDGGDEVEG SGVGAGEGET VQHFPLARPK 240
SLMQKLQCSF QTSWLKDFPW LRYSKDTGLM SCGWCQKTPA DGGSVDLPPV GHDELSRGTR 300
NYKKTLLLRH HVSTEHKLHE ANAQESEIPS EEGYCDFNSR PNENSYCYQL LRQLNEQRKK 360
GILCDVSIVV SGKIFKAHKN ILVAGSRFFK TLYCFSNKES PNQNNTTHLD IAAVQGFSVI 420
LDFLYSGNLV LTSQNAIEVM TVASYLQMSE VVQTCRNFIK DALNISIKSE APESVVVDYN 480
NRKPVNRDGL SSSRDQKIAS FWATRNLTNL ASNVKIENDG CNVDEGQIEN YQMNDSSWVQ 540
DGSPEMAENE SEGQTKVFIW NNMGSQGIQE TGKTRRKNQT TKRFIYNIPP NNETNLEDCS 600
VMQPPVAYPE ENTLLIKEEP DLDGALLSGP DGDRNVNANL LAEAGTSQDG GDAGTSHDFK 660
YGLMPGPSND FKYGLIPGTS NDFKYGLIPG ASNDFKYGLL PESWPKQETW ENGESSLIMN 720
KLKCPHCSYV AKYRRTLKRH LLIHTGVRSF SCDICGKLFT RREHVKRHSL VHKKDKKYKC 780
MVCKKIFMLA ASVGIRHGSR RYGVCVDCAD KSQPGGQEGV DQGQDTEFPR DEEYEENEVG 840
EADEELVDDG EDQNDPSRWD ESGEVCMSLD D 871 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00651; BTB 
SMART
 SM00225; BTB
 SM00355; ZnF_C2H2 
PROSITE
 PS50097; BTB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS