CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015327
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger CCCH domain-containing protein 14 
Protein Synonyms/Alias
 Mammalian suppressor of tau pathology-2; MSUT-2; Renal carcinoma antigen NY-REN-37 
Gene Name
 ZC3H14 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
84TTEPSSLKSSDTNIFubiquitination[1, 2]
99DSNVPSNKSNFSRGDubiquitination[2]
126IPSARPEKRDSRVSTubiquitination[1]
139STSSQESKTTNVRQTubiquitination[2]
160TRLMSTVKPLREPAPubiquitination[1]
175SEDVIDIKPEPDDLIubiquitination[1]
245QNSIHAAKQLDMQSSubiquitination[1, 2, 3, 4]
283FFRNNSEKMSMEDENubiquitination[1, 2]
295DENFRKRKLPVVSSVubiquitination[2]
306VSSVVKVKKFNHDGEubiquitination[2]
307SSVVKVKKFNHDGEEubiquitination[1, 2]
337SSVSVPAKPERRPSLubiquitination[1, 2]
348RPSLPPSKQANKNLIubiquitination[5]
352PPSKQANKNLILKAIubiquitination[2]
357ANKNLILKAISEAQEacetylation[6]
357ANKNLILKAISEAQEubiquitination[1, 2]
368EAQESVTKTTNYSTVubiquitination[1, 2, 3]
378NYSTVPQKQTLPVAPubiquitination[1, 2, 3, 5]
413PRISPPIKEEETKGDubiquitination[1, 2]
418PIKEEETKGDSVEKNubiquitination[2]
424TKGDSVEKNQGTQQRubiquitination[1]
470DTRSFILKKPKLSEEubiquitination[2]
471TRSFILKKPKLSEEVubiquitination[1, 2]
473SFILKKPKLSEEVVVubiquitination[1, 2]
489PNQESGMKTADSLRVubiquitination[1, 2, 4, 5]
512RDLVQPDKPASPKFIubiquitination[1, 2]
555NQTAASNKGLRGLLHubiquitination[5]
593SELSVAQKPEKLLERubiquitination[1, 2]
623HHPISPCKAFPNCKFubiquitination[2]
646PNCKYDAKCTKPDCPubiquitination[2]
Reference
 [1] 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]
 [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] 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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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
 Binds the polyadenosine RNA oligonucleotides. 
Sequence Annotation
 ZN_FING 595 620 C3H1-type 1.
 ZN_FING 621 640 C3H1-type 2.
 ZN_FING 641 656 C3H1-type 3.
 ZN_FING 682 699 C3H1-type 4.
 ZN_FING 701 719 C3H1-type 5.
 MOD_RES 357 357 N6-acetyllysine.
 MOD_RES 515 515 Phosphoserine.
 MOD_RES 620 620 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 736 AA 
Protein Sequence
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI 60
RFTVWLHGVL DKLRSVTTEP SSLKSSDTNI FDSNVPSNKS NFSRGDERRH EAAVPPLAIP 120
SARPEKRDSR VSTSSQESKT TNVRQTYDDG AATRLMSTVK PLREPAPSED VIDIKPEPDD 180
LIDEDLNFVQ ENPLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADSGVHLN RLQFQQQQNS 240
IHAAKQLDMQ SSWVYETGRL CEPEVLNSLE ETYSPFFRNN SEKMSMEDEN FRKRKLPVVS 300
SVVKVKKFNH DGEEEEEDDD YGSRTGSISS SVSVPAKPER RPSLPPSKQA NKNLILKAIS 360
EAQESVTKTT NYSTVPQKQT LPVAPRTRTS QEELLAEVVQ GQSRTPRISP PIKEEETKGD 420
SVEKNQGTQQ RQLLSRLQID PVMAETLQMS QDYYDMESMV HADTRSFILK KPKLSEEVVV 480
APNQESGMKT ADSLRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC 540
FEGMKPVNQT AASNKGLRGL LHPQQLHLLS RQLEDPNGSF SNAEMSELSV AQKPEKLLER 600
CKYWPACKNG DECAYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP DCPFTHVSRR 660
IPVLSPKPAV APPAPPSSSQ LCRYFPACKK MECPFYHPKH CRFNTQCTRP DCTFYHPTIN 720
VPPRHALKWI RPQTSE 736 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR000571; Znf_CCCH. 
Pfam
  
SMART
 SM00356; ZnF_C3H1 
PROSITE
 PS50103; ZF_C3H1 
PRINTS