CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021394
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 644 
Protein Synonyms/Alias
 Zinc finger motif enhancer-binding protein 2; Zep-2 
Gene Name
 ZNF644 
Gene Synonyms/Alias
 KIAA1221; ZEP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
319NCVPNKSKMQEVDFLubiquitination[1]
485MEEIRELKELQDEGRubiquitination[2]
553IAHGAVVKCPMVTSDubiquitination[1]
589KSATYICKMCPFTTSubiquitination[1]
645DSTKTLTKQQSTTFPubiquitination[1]
720SSVDQKPKYFHQAAKubiquitination[2]
817RVIKESKKESSVGGEubiquitination[1, 2]
843MTVVVLQKLNSAEKKubiquitination[3, 4]
963TDLSLEKKSCPYCPAubiquitination[1, 2]
1009EQIATSDKMQHFKRTubiquitination[1, 2]
1094EKYEKILKALNSRRIubiquitination[1, 2]
1110PRPFVAQKLASSDDFubiquitination[1, 2, 5]
1165PELPSGKKNQSLTLIubiquitination[1, 2]
1176LTLIELLKNKRMGEEubiquitination[1, 3, 4]
1178LIELLKNKRMGEERNubiquitination[1]
1205ARKRFVQKCVLPLNEubiquitination[1]
1234MHSALDCKQKKSRSRubiquitination[2]
1237ALDCKQKKSRSRSGSubiquitination[1]
1282SVQEDWIKHLQRHIVubiquitination[1]
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] 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] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 ZN_FING 410 432 C2H2-type 1.
 ZN_FING 448 470 C2H2-type 2.
 ZN_FING 496 518 C2H2-type 3.
 ZN_FING 525 548 C2H2-type 4.
 ZN_FING 586 609 C2H2-type 5.
 ZN_FING 963 987 C2H2-type 6.
 ZN_FING 1038 1060 C2H2-type 7.
 MOD_RES 309 309 Phosphoserine.
 MOD_RES 1000 1000 Phosphoserine.
 MOD_RES 1189 1189 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; 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
 1327 AA 
Protein Sequence
MRSFLQQDVN KTKSRLNVLN GLANNMDDLK INTDITGAKE ELLDDNNFIS DKESGVHKPK 60
DCQTSFQKNN TLTLPEELSK DKSENALSGG QSSLFIHAGA PTVSSENFIL PKGAAVNGPV 120
SHSSLTKTSN MNKGSVSLTT GQPVDQPTTE SCSTLKVAAD LQLSTPQKAS QHQVLFLLSD 180
VAHAKNPTHS NKKLPTSASV GCDIQNSVGS NIKSDGTLIN QVEVGEDGED LLVKDDCVNT 240
VTGISSGTDG FRSENDTNWD PQKEFIQFLM TNEETVDKAP PHSKIGLEKK RKRKMDVSKI 300
TRYTEDCFSD SNCVPNKSKM QEVDFLEQNE ELQAVDSQKY ALSKVKPEST DEDLESVDAF 360
QHLIYNPDKC GEESSPVHTS TFLSNTLKKK CEESDSESPA TFSTEEPSFY PCTKCNVNFR 420
EKKHLHRHMM YHLDGNSHFR HLNVPRPYAC RECGRTFRDR NSLLKHMIIH QERRQKLMEE 480
IRELKELQDE GRSARLQCPQ CVFGTNCPKT FVQHAKTHEK DKRYYCCEEC NFMAVTENEL 540
ECHRGIAHGA VVKCPMVTSD IAQRKTQKKT FMKDSVVGSS KKSATYICKM CPFTTSAKSV 600
LKKHTEYLHS SSCVDSFGSP LGLDKRKNDI LEEPVDSDST KTLTKQQSTT FPKNSALKQD 660
VKRTFGSTSQ SSSFSKIHKR PHRIQKARKS IAQSGVNMCN QNSSPHKNVT IKSSVDQKPK 720
YFHQAAKEKS NAKANSHYLY RHKYENYRMI KKSGESYPVH FKKEEASSLN SLHLFSSSSN 780
SHNNFISDPH KPDAKRPESF KDHRRVAVKR VIKESKKESS VGGEDLDSYP DFLHKMTVVV 840
LQKLNSAEKK DSYETEDESS WDNVELGDYT TQAIEDETYS DINQEHVNLF PLFKSKVEGQ 900
EPGENATLSY DQNDGFYFEY YEDTGSNNFL HEIHDPQHLE TADASLSKHS SVFHWTDLSL 960
EKKSCPYCPA TFETGVGLSN HVRGHLHRAG LSYEARHVVS PEQIATSDKM QHFKRTGTGT 1020
PVKRVRKAIE KSETTSEHTC QLCGGWFDTK IGLSNHVRGH LKRLGKTKWD AHKSPICVLN 1080
EMMQNEEKYE KILKALNSRR IIPRPFVAQK LASSDDFISQ NVIPLEAYRN GLKTEALSVS 1140
ASEEEGLNFL NEYDETKPEL PSGKKNQSLT LIELLKNKRM GEERNSAISP QKIHNQTARK 1200
RFVQKCVLPL NEDSPLMYQP QKMDLTMHSA LDCKQKKSRS RSGSKKKMLT LPHGADEVYI 1260
LRCRFCGLVF RGPLSVQEDW IKHLQRHIVN ANLPRTGAGM VEVTSLLKKP ASITETSFSL 1320
LMAEAAS 1327 
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
 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