CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000901
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 292 
Protein Synonyms/Alias
  
Gene Name
 ZNF292 
Gene Synonyms/Alias
 KIAA0530 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
213SQATALAKLCSDHPEubiquitination[1]
1117NSSQSIGKHMKTAHPacetylation[2]
Reference
 [1] 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]
 [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] 
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 ZN_FING 569 591 C2H2-type 1.
 ZN_FING 681 705 C2H2-type 2.
 ZN_FING 722 744 C2H2-type 3.
 ZN_FING 750 774 C2H2-type 4.
 ZN_FING 779 803 C2H2-type 5.
 ZN_FING 807 831 C2H2-type 6.
 ZN_FING 1098 1123 C2H2-type 7.
 ZN_FING 1375 1397 C2H2-type 8; degenerate.
 ZN_FING 1902 1927 C2H2-type 9.
 ZN_FING 1947 1972 C2H2-type 10.
 ZN_FING 2114 2139 C2H2-type 11.
 ZN_FING 2172 2197 C2H2-type 12.
 ZN_FING 2216 2241 C2H2-type 13.
 ZN_FING 2256 2281 C2H2-type 14.
 ZN_FING 2386 2410 C2H2-type 15.
 MOD_RES 1159 1159 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; 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
 2723 AA 
Protein Sequence
MADEEAEQER LSCGEGGCVA ELQRLGERLQ ELELQLRESR VPAVEAATDY CQQLCQTLLE 60
YAEKWKTSED PLPLLEVYTV AIQSYVKARP YLTSECENVA LVLERLALSC VELLLCLPVE 120
LSDKQWEQFQ TLVQVAHEKL MENGSCELHF LATLAQETGV WKNPVLCTIL SQEPLDKDKV 180
NEFLAFEGPI LLDMRIKHLI KTNQLSQATA LAKLCSDHPE IGIKGSFKQT YLVCLCTSSP 240
NGKLIEEISE VDCKDALEMI CNLESEGDEK SALVLCTAFL SRQLQQGDMY CAWELTLFWS 300
KLQQRVEPSI QVYLERCRQL SLLTKTVYHI FFLIKVINSE TEGAGLATCI ELCVKALRLE 360
STENTEVKIS ICKTISCLLP DDLEVKRACQ LSEFLIEPTV DAYYAVEMLY NQPDQKYDEE 420
NLPIPNSLRC ELLLVLKTQW PFDPEFWDWK TLKRQCLALM GEEASIVSSI DELNDSEVYE 480
KVVDYQEESK ETSMNGLSGG VGANSGLLKD IGDEKQKKRE IKQLRERGFI SARFRNWQAY 540
MQYCVLCDKE FLGHRIVRHA QKHYKDGIYS CPICAKNFNS KETFVPHVTL HVKQSSKERL 600
AAMKPLRRLG RPPKITTTNE NQKTNTVAKQ EQRPIKKNSL YSTDFIVFND NDGSDDENDD 660
KDKSYEPEVI PVQKPVPVNE FNCPVTFCKK GFKYFKNLIA HVKGHKDNED AKRFLEMQSK 720
KVICQYCRRH FVSVTHLNDH LQMHCGSKPY ICIQMKCKAG FNSYAELLTH RKEHQVFRAK 780
CMFPKCGRIF SEAYLLYDHE AQHYNTYTCK FTGCGKVYRS QGELEKHLDD HSTPPEKVLP 840
PEAQLNSSGD SIQPSEVNQN TAENIEKERS MLPSENNIEN SLLADRSDAW DKSKAESAVT 900
KQDQISASEL RQANGPLSNG LENPATTPLL QSSEVAVSIK VSLNQGIEDN FGKQENSTVE 960
GSGEALVTDL HTPVEDTCND LCHPGFQERK EQDCFNDAHV TQNSLVNSET LKIGDLTPQN 1020
LERQVNNLMT FSVQNQAAFQ NNLPTSKFEC GDNVKTSSNL YNLPLKTLES IAFVPPQSDL 1080
SNSLGTPSVP PKAPVQKFSC QVEGCTRTYN SSQSIGKHMK TAHPDQYAAF KMQRKSKKGQ 1140
KANNLNTPNN GKFVYFLPSP VNSSNPFFTS QTKANGNPAC SAQLQHVSPP IFPAHLASVS 1200
TPLLSSMESV INPNITSQDK NEQGGMLCSQ MENLPSTALP AQMEDLTKTV LPLNIDSGSD 1260
PFLPLPAESS SMSLFPSPAD SGTNSVFSQL ENNTNHYSSQ IEGNTNSSFL KGGNGENAVF 1320
PSQVNVANNF SSTNAQQSAP EKVKKDRGRG PNGKERKPKH NKRAKWPAII RDGKFICSRC 1380
YRAFTNPRSL GGHLSKRSYC KPLDGAEIAQ ELLQSNGQPS LLASMILSTN AVNLQQPQQS 1440
TFNPEACFKD PSFLQLLAEN RSPAFLPNTF PRSGVTNFNT SVSQEGSEII KQALETAGIP 1500
STFEGAEMLS HVSTGCVSDA SQVNATVMPN PTVPPLLHTV CHPNTLLTNQ NRTSNSKTSS 1560
IEECSSLPVF PTNDLLLKTV ENGLCSSSFP NSGGPSQNFT SNSSRVSVIS GPQNTRSSHL 1620
NKKGNSASKR RKKVAPPLIA PNASQNLVTS DLTTMGLIAK SVEIPTTNLH SNVIPTCEPQ 1680
SLVENLTQKL NNVNNQLFMT DVKENFKTSL ESHTVLAPLT LKTENGDSQM MALNSCTTSI 1740
NSDLQISEDN VIQNFEKTLE IIKTAMNSQI LEVKSGSQGA GETSQNAQIN YNIQLPSVNT 1800
VQNNKLPDSS PFSSFISVMP TKSNIPQSEV SHKEDQIQEI LEGLQKLKLE NDLSTPASQC 1860
VLINTSVTLT PTPVKSTADI TVIQPVSEMI NIQFNDKVNK PFVCQNQGCN YSAMTKDALF 1920
KHYGKIHQYT PEMILEIKKN QLKFAPFKCV VPTCTKTFTR NSNLRAHCQL VHHFTTEEMV 1980
KLKIKRPYGR KSQSENVPAS RSTQVKKQLA MTEENKKESQ PALELRAETQ NTHSNVAVIP 2040
EKQLVEKKSP DKTESSLQVI TVTSEQCNTN ALTNTQTKGR KIRRHKKEKE EKKRKKPVSQ 2100
SLEFPTRYSP YRPYRCVHQG CFAAFTIQQN LILHYQAVHK SDLPAFSAEV EEESEAGKES 2160
EETETKQTLK EFRCQVSDCS RIFQAITGLI QHYMKLHEMT PEEIESMTAS VDVGKFPCDQ 2220
LECKSSFTTY LNYVVHLEAD HGIGLRASKT EEDGVYKCDC EGCDRIYATR SNLLRHIFNK 2280
HNDKHKAHLI RPRRLTPGQE NMSSKANQEK SKSKHRGTKH SRCGKEGIKM PKTKRKKKNN 2340
LENKNAKIVQ IEENKPYSLK RGKHVYSIKA RNDALSECTS RFVTQYPCMI KGCTSVVTSE 2400
SNIIRHYKCH KLSKAFTSQH RNLLIVFKRC CNSQVKETSE QEGAKNDVKD SDTCVSESND 2460
NSRTTATVSQ KEVEKNEKDE MDELTELFIT KLINEDSTSV ETQANTSSNV SNDFQEDNLC 2520
QSERQKASNL KRVNKEKNVS QNKKRKVEKA EPASAAELSS VRKEEETAVA IQTIEEHPAS 2580
FDWSSFKPMG FEVSFLKFLE ESAVKQKKNT DKDHPNTGNK KGSHSNSRKN IDKTAVTSGN 2640
HVCPCKESET FVQFANPSQL QCSDNVKIVL DKNLKDCTEL VLKQLQEMKP TVSLKKLEVH 2700
SNDPDMSVMK DISIGKATGR GQY 2723 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00096; zf-C2H2 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS