CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Zinc finger protein 292 
Protein Synonyms/Alias
  
Gene Name
 ZNF292 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
208SQATALAKLCSDHPEubiquitination[1]
1112NSSQSIGKHMKTAHPacetylation[2]
2037NVAVIPEKQLVEKKSacetylation[2, 3, 4]
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] 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]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2718 AA 
Protein Sequence
MADEEAEQER LSCGEGGCVA ELQRLGERLQ ELELQLRESR VPAVEAATDY CQQLCQTLLE 60
YAEKWKTSED PLPLLEVYTV AIQSYVKARP YLTSECENVA LVLERLALSC VELLLCLPVE 120
LSDKQWEQFQ TLVQVAHEKL MENGSCELHF LATLAQETGV WKNPVLCTIL SQEPLDKDKA 180
FEGPILLDMR IKHLIKTNQL SQATALAKLC SDHPEIGIKG SFKQTYLVCL CTSSPNGKLI 240
EEISEVDCKD ALEMICNLES EGDEKSALVL CTAFLSRQLQ QGDMYCAWEL TLFWSKLQQR 300
VEPSIQVYLE RCRQLSLLTK TVYHIFFLIK VINSETEGAG LATCIELCVK ALRLESTENT 360
EVKISICKTI SCLLPDDLEV KRACQLSEFL IEPTVDAYYA VEMLYNQPDQ KYDEENLPIP 420
NSLRCELLLV LKTQWPFDPE FWDWKTLKRQ CLALMGEEAS IVSSIDELND SEVYEKVVDY 480
QEESKETSMN GLSGGVGANS GLLKDIGDEK QKKREIKQLR ERGFISARFR NWQAYMQYCV 540
LCDKEFLGHR IVRHAQKHYK DGIYSCPICA KNFNSKETFV PHVTLHVKQS SKERLAAMKP 600
LRRLGRPPKI TTTNENQKTN TVAKQEQRPI KKNSLYSTDF IVFNDNDGSD DENDDKDKSY 660
EPEVIPVQKP VPVNEFNCPV TFCKKGFKYF KNLIAHVKGH KDNEDAKRFL EMQSKKVICQ 720
YCRRHFVSVT HLNDHLQMHC GSKPYICIQM KCKAGFNSYA ELLTHRKEHQ VFRAKCMFPK 780
CGRIFSEAYL LYDHEAQHYN TYTCKFTGCG KVYRSQGELE KHLDDHSTPP EKVLPPEAQL 840
NSSGDSIQPS EVNQNTAENI EKERSMLPSE NNIENSLLAD RSDAWDKSKA ESAVTKQDQI 900
SASELRQANG PLSNGLENPA TTPLLQSSEV AVSIKVSLNQ GIEDNFGKQE NSTVEGSGEA 960
LVTDLHTPVE DTCNDLCHPG FQERKEQDCF NDAHVTQNSL VNSETLKIGD LTPQNLERQV 1020
NNLMTFSVQN QAAFQNNLPT SKFECGDNVK TSSNLYNLPL KTLESIAFVP PQSDLSNSLG 1080
TPSVPPKAPV QKFSCQVEGC TRTYNSSQSI GKHMKTAHPD QYAAFKMQRK SKKGQKANNL 1140
NTPNNGKFVY FLPSPVNSSN PFFTSQTKAN GNPACSAQLQ HVSPPIFPAH LASVSTPLLS 1200
SMESVINPNI TSQDKNEQGG MLCSQMENLP STALPAQMED LTKTVLPLNI DSGSDPFLPL 1260
PAESSSMSLF PSPADSGTNS VFSQLENNTN HYSSQIEGNT NSSFLKGGNG ENAVFPSQVN 1320
VANNFSSTNA QQSAPEKVKK DRGRGPNGKE RKPKHNKRAK WPAIIRDGKF ICSRCYRAFT 1380
NPRSLGGHLS KRSYCKPLDG AEIAQELLQS NGQPSLLASM ILSTNAVNLQ QPQQSTFNPE 1440
ACFKDPSFLQ LLAENRSPAF LPNTFPRSGV TNFNTSVSQE GSEIIKQALE TAGIPSTFEG 1500
AEMLSHVSTG CVSDASQVNA TVMPNPTVPP LLHTVCHPNT LLTNQNRTSN SKTSSIEECS 1560
SLPVFPTNDL LLKTVENGLC SSSFPNSGGP SQNFTSNSSR VSVISGPQNT RSSHLNKKGN 1620
SASKRRKKVA PPLIAPNASQ NLVTSDLTTM GLIAKSVEIP TTNLHSNVIP TCEPQSLVEN 1680
LTQKLNNVNN QLFMTDVKEN FKTSLESHTV LAPLTLKTEN GDSQMMALNS CTTSINSDLQ 1740
ISEDNVIQNF EKTLEIIKTA MNSQILEVKS GSQGAGETSQ NAQINYNIQL PSVNTVQNNK 1800
LPDSSPFSSF ISVMPTKSNI PQSEVSHKED QIQEILEGLQ KLKLENDLST PASQCVLINT 1860
SVTLTPTPVK STADITVIQP VSEMINIQFN DKVNKPFVCQ NQGCNYSAMT KDALFKHYGK 1920
IHQYTPEMIL EIKKNQLKFA PFKCVVPTCT KTFTRNSNLR AHCQLVHHFT TEEMVKLKIK 1980
RPYGRKSQSE NVPASRSTQV KKQLAMTEEN KKESQPALEL RAETQNTHSN VAVIPEKQLV 2040
EKKSPDKTES SLQVITVTSE QCNTNALTNT QTKGRKIRRH KKEKEEKKRK KPVSQSLEFP 2100
TRYSPYRPYR CVHQGCFAAF TIQQNLILHY QAVHKSDLPA FSAEVEEESE AGKESEETET 2160
KQTLKEFRCQ VSDCSRIFQA ITGLIQHYMK LHEMTPEEIE SMTASVDVGK FPCDQLECKS 2220
SFTTYLNYVV HLEADHGIGL RASKTEEDGV YKCDCEGCDR IYATRSNLLR HIFNKHNDKH 2280
KAHLIRPRRL TPGQENMSSK ANQEKSKSKH RGTKHSRCGK EGIKMPKTKR KKKNNLENKN 2340
AKIVQIEENK PYSLKRGKHV YSIKARNDAL SECTSRFVTQ YPCMIKGCTS VVTSESNIIR 2400
HYKCHKLSKA FTSQHRNLLI VFKRCCNSQV KETSEQEGAK NDVKDSDTCV SESNDNSRTT 2460
ATVSQKEVEK NEKDEMDELT ELFITKLINE DSTSVETQAN TSSNVSNDFQ EDNLCQSERQ 2520
KASNLKRVNK EKNVSQNKKR KVEKAEPASA AELSSVRKEE ETAVAIQTIE EHPASFDWSS 2580
FKPMGFEVSF LKFLEESAVK QKKNTDKDHP NTGNKKGSHS NSRKNIDKTA VTSGNHVCPC 2640
KESETFVQFA NPSQLQCSDN VKIVLDKNLK DCTELVLKQL QEMKPTVSLK KLEVHSNDPD 2700
MSVMKDISIG KATGRGQY 2718 
Gene Ontology
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 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