CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007588
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable helicase with zinc finger domain 
Protein Synonyms/Alias
 Down-regulated in human cancers protein 
Gene Name
 HELZ 
Gene Synonyms/Alias
 DRHC; KIAA0054 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56PLEIERIKIESLLYRubiquitination[1, 2]
90VLGEGLAKGEDAFRAubiquitination[2]
107CCMQLKGKLQPVSTIubiquitination[2]
117PVSTILAKSLTGESLubiquitination[2]
130SLNGMVTKDLTRLKTubiquitination[2]
185SEEYTLCKRFLEQGIubiquitination[2]
213EELAEWQKRYASRLIubiquitination[2]
396LEYLMHAKQQLVTTAubiquitination[2]
411KRWDSSSKTIIDFEPubiquitination[2]
426NETTDLEKSLLIRYQubiquitination[2]
449FTQSVLDKSLTKSNYubiquitination[1, 2]
453VLDKSLTKSNYQSRLubiquitination[2]
543LLPVPKQKLVQTQGTubiquitination[2]
553QTQGTKEKVYEATIEubiquitination[2]
564ATIEEKTKEYIFLRLubiquitination[2]
611HYALDRIKDNGVLFPubiquitination[2]
895SGKQPAHKDFYPLTFubiquitination[2]
913RGEDVQEKNSTAFYNubiquitination[3]
986RVLNVQGKQFRVLFLubiquitination[2]
1095QLEALELKKTYVLNPubiquitination[2]
1096LEALELKKTYVLNPLubiquitination[2, 3]
1281HEQNRNGKSDTNNSGubiquitination[2]
1293NSGPEINKIRTPEKKubiquitination[2]
1560PPVRADWKLTSSAEDubiquitination[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] 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]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo. 
Sequence Annotation
 ZN_FING 178 206 C3H1-type.
 NP_BIND 668 675 ATP (Potential).
 MOTIF 794 797 DEAA box.
 MOD_RES 1614 1614 Phosphoserine.
 MOD_RES 1738 1738 Phosphoserine.
 MOD_RES 1766 1766 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1942 AA 
Protein Sequence
MEDRRAEKSC EQACESLKRQ DYEMALKHCT EALLSLGQYS MADFTGPCPL EIERIKIESL 60
LYRIASFLQL KNYVQADEDC RHVLGEGLAK GEDAFRAVLC CMQLKGKLQP VSTILAKSLT 120
GESLNGMVTK DLTRLKTLLS ETETATSNAL SGYHVEDLDE GSCNGWHFRP PPRGITSSEE 180
YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQNENKQ LSGSYMETLI 240
EKWMNSLSPE KVLSECIEGV KVEHNPDLSV TVSTKKSHQT WTFALTCKPA RMLYRVALLY 300
DAHRPHFSII AISAGDSTTQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT 360
FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKQQLV TTAKRWDSSS KTIIDFEPNE 420
TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKSNYQSRL HDLLYIEEIA QYKEISKFNL 480
KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLTETLSED TLAGRLVMTK VNAVYLLPVP 540
KQKLVQTQGT KEKVYEATIE EKTKEYIFLR LSRECCEELN LRPDCDTQVE LQFQLNRLPL 600
CEMHYALDRI KDNGVLFPDI SMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAITTPLAIQ 660
LPPVLIIGPY GTGKTFTLAQ AVKHILQQQE TRILICTHSN SAADLYIKDY LHPYVEAGNP 720
QARPLRVYFR NRWVKTVHPV VHQYCLISSA HSTFQMPQKE DILKHRVVVV TLNTSQYLCQ 780
LDLEPGFFTH ILLDEAAQAM ECETIMPLAL ATQNTRIVLA GDHMQLSPFV YSEFARERNL 840
HVSLLDRLYE HYPAEFPCRI LLCENYRSHE AIINYTSELF YEGKLMASGK QPAHKDFYPL 900
TFFTARGEDV QEKNSTAFYN NAEVFEVVER VEELRRKWPV AWGKLDDGSI GVVTPYADQV 960
FRIRAELRKK RLSDVNVERV LNVQGKQFRV LFLSTVRTRH TCKHKQTPIK KKEQLLEDST 1020
EDLDYGFLSN YKLLNTAITR AQSLVAVVGD PIALCSIGRC RKFWERFIAL CHENSSLHGI 1080
TFEQIKAQLE ALELKKTYVL NPLAPEFIPR ALRLQHSGST NKQQQSPPKG KSLHHTQNDH 1140
FQNDGIVQPN PSVLIGNPIR AYTPPPPLGP HPNLGKSPSP VQRIDPHTGT SILYVPAVYG 1200
GNVVMSVPLP VPWTGYQGRF AVDPRIITHQ AAMAYNMNLL QTHGRGSPIP YGLGHHPPVT 1260
IGQPQNQHQE KDQHEQNRNG KSDTNNSGPE INKIRTPEKK PTEPKQVDLE SNPQNRSPES 1320
RPSVVYPSTK FPRKDNLNPR HINLPLPAPH AQYAIPNRHF HPLPQLPRPP FPIPQQHTLL 1380
NQQQNNLPEQ PNQIPPQPNQ VVQQQSQLNQ QPQQPPPQLS PAYQAGPNNA FFNSAVAHRP 1440
QSPPAEAVIP EQQPPPMLQE GHSPLRAIAQ PGPILPSHLN SFIDENPSGL PIGEALDRIH 1500
GSVALETLRQ QQARFQQWSE HHAFLSQGSA PYPHHHHPHL QHLPQPPLGL HQPPVRADWK 1560
LTSSAEDEVE TTYSRFQDLI RELSHRDQSE TRELAEMPPP QSRLLQYRQV QSRSPPAVPS 1620
PPSSTDHSSH FSNFNDNSRD IEVASNPAFP QRLPPQIFNS PFSLPSEHLA PPPLKYLAPD 1680
GAWTFANLQQ NHLMGPGFPY GLPPLPHRPP QNPFVQIQNH QHAIGQEPFH PLSSRTVSSS 1740
SLPSLEEYEP RGPGRPLYQR RISSSSVQPC SEEVSTPQDS LAQCKELQDH SNQSSFNFSS 1800
PESWVNTTSS TPYQNIPCNG SSRTAQPREL IAPPKTVKPP EDQLKSENLE VSSSFNYSVL 1860
QHLGQFPPLM PNKQIAESAN SSSPQSSAGG KPAMSYASAL RAPPKPRPPP EQAKKSSDPL 1920
SLFQELSLGS SSGSNGFYSY FK 1942 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR000571; Znf_CCCH. 
Pfam
 PF00642; zf-CCCH 
SMART
 SM00356; ZnF_C3H1 
PROSITE
 PS50103; ZF_C3H1 
PRINTS