CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023832
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 451 
Protein Synonyms/Alias
 Coactivator for steroid receptors 
Gene Name
 ZNF451 
Gene Synonyms/Alias
 COASTER; KIAA0576; KIAA1702 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75KDHIDYQKDKVALTLubiquitination[1, 2]
77HIDYQKDKVALTLARubiquitination[2]
106KNRAFREKIDFQHAHubiquitination[1, 2, 3, 4, 5, 6]
139LCVDQWLKMPGLKTGubiquitination[2, 4]
144WLKMPGLKTGTINCGubiquitination[2, 4]
153GTINCGTKSSFRRGGubiquitination[2, 7]
191HLLLGHLKRFDHSPCubiquitination[2]
220ACVVCYKKFVTQQQYubiquitination[2]
275CSKHMSGKNHFHQSFubiquitination[2]
283NHFHQSFKLGDNKGIubiquitination[2]
288SFKLGDNKGIAHPISubiquitination[1, 2]
302SFPSFAKKLLISLCKubiquitination[2]
309KLLISLCKDVPFQVKubiquitination[2]
316KDVPFQVKCVACHKTubiquitination[2, 3, 6]
349GPVAVAEKSITQVAEubiquitination[1]
357SITQVAEKFILRGYCubiquitination[2, 3, 6]
381ETSTQNHKQNSGHKVubiquitination[2]
387HKQNSGHKVRVINSVubiquitination[2]
409CHSSEGNKDPSSDLHubiquitination[2]
423HLLLDQSKFSSLKRTubiquitination[1, 3, 6]
434LKRTMSIKESSSLECubiquitination[2]
448CIAIPKKKMNLKDKSubiquitination[2]
452PKKKMNLKDKSHEGVubiquitination[2]
454KKMNLKDKSHEGVACubiquitination[1, 2]
464EGVACVQKEKSVVKTubiquitination[1, 2]
505YKCVVCGKVCDDSGVubiquitination[2]
585LDNLTANKPSSAITVubiquitination[1, 2]
647HCRKPFHKIETLYRHubiquitination[2]
664DEHDNEIKIKYFCGLubiquitination[2, 4]
706EKTETSIKTEDDFPVsumoylation[8]
706EKTETSIKTEDDFPVubiquitination[1, 2, 7]
731CRESYICKVNRKEDYubiquitination[2, 4, 7]
735YICKVNRKEDYSRCLubiquitination[2]
748CLQIMLDKGKLWFRCubiquitination[2]
750QIMLDKGKLWFRCSLubiquitination[2]
779IHQVHKEKSDEEEQQubiquitination[1, 2]
790EEQQYVIKCGTCTKAubiquitination[2, 4]
817RKHCFLQKPSVAHFGubiquitination[2, 4]
827VAHFGSEKSNLYKFTubiquitination[2, 3, 5, 6]
832SEKSNLYKFTASASHubiquitination[1, 2, 3, 4, 6]
843SASHTERKLKQAINYubiquitination[2]
845SHTERKLKQAINYSKubiquitination[1, 2, 7]
852KQAINYSKSLDMEKGubiquitination[1, 2, 3, 5, 6, 7]
951HPRCSKRKDAADFAIubiquitination[2, 4]
992LELENQFKKTQRPAHubiquitination[1, 2, 7]
993ELENQFKKTQRPAHIubiquitination[2]
1034SDDNMGAKNTSIGEEubiquitination[9]
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] 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]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [9] 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. Coactivator for steroid receptors. 
Sequence Annotation
 ZN_FING 169 195 C2H2-type 1.
 ZN_FING 253 277 C2H2-type 2.
 ZN_FING 315 337 C2H2-type 3.
 ZN_FING 362 386 C2H2-type 4.
 ZN_FING 498 521 C2H2-type 5.
 ZN_FING 531 554 C2H2-type 6.
 ZN_FING 606 631 C2H2-type 7; atypical.
 ZN_FING 636 659 C2H2-type 8.
 ZN_FING 667 690 C2H2-type 9.
 ZN_FING 753 776 C2H2-type 10.
 ZN_FING 789 812 C2H2-type 11.  
Keyword
 Alternative splicing; Complete proteome; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1061 AA 
Protein Sequence
MGDPGSEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS SDDEEPSTSY 60
TDENIKRKDH IDYQKDKVAL TLARLARHVE VEKQQKEEKN RAFREKIDFQ HAHGLQELEF 120
IRGHSDTEAA RLCVDQWLKM PGLKTGTINC GTKSSFRRGG HTWVSGKPIL CPIMHCNKEF 180
DNGHLLLGHL KRFDHSPCDP TITLHGPFFS SFACVVCYKK FVTQQQYRDH LFDKEATDDG 240
HNNNLLPQII QCFACPNCFL LFSRKEECSK HMSGKNHFHQ SFKLGDNKGI AHPISFPSFA 300
KKLLISLCKD VPFQVKCVAC HKTLRSHMEL TAHFRVHCRN AGPVAVAEKS ITQVAEKFIL 360
RGYCPDCNQV FVDETSTQNH KQNSGHKVRV INSVEESVLL YCHSSEGNKD PSSDLHLLLD 420
QSKFSSLKRT MSIKESSSLE CIAIPKKKMN LKDKSHEGVA CVQKEKSVVK TWFCECNQRF 480
PSEDAVEKHV FSANTMGYKC VVCGKVCDDS GVIRLHMSRI HGGAHLNNFL FWCRTCKKEL 540
TRKDTIMAHV TEFHNGHRYF YEMDEVEGET LPSSSTTLDN LTANKPSSAI TVIDHSPANS 600
SPRGKWQCRI CEDMFDSQEY VKQHCMSLAS HKFHRYSCAH CRKPFHKIET LYRHCQDEHD 660
NEIKIKYFCG LCDLIFNVEE AFLSHYEEHH SIDYVFVSEK TETSIKTEDD FPVIETSNQL 720
TCGCRESYIC KVNRKEDYSR CLQIMLDKGK LWFRCSLCSA TAQNLTDMNT HIHQVHKEKS 780
DEEEQQYVIK CGTCTKAFHD PESAQQHFHR KHCFLQKPSV AHFGSEKSNL YKFTASASHT 840
ERKLKQAINY SKSLDMEKGV ENDLSYQNIE EEIVELPDLD YLRTMTHIVF VDFDNWSNFF 900
GHLPGHLNQG TFIWGFQGGN TNWKPPLNCK IYNYLNRIGC FFLHPRCSKR KDAADFAICM 960
HAGRLDEQLP KQIPFTILSG DQGFLELENQ FKKTQRPAHI LNPHHLEGDM MCALLNSISD 1020
TTKECDSDDN MGAKNTSIGE EFISTEDVEL EEAIRRSLEE M 1061 
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. 
Pfam
  
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS