CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012873
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 284 
Protein Synonyms/Alias
  
Gene Name
 ZNF284 
Gene Synonyms/Alias
 ZNF284L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
64FHFQREEKFWIMETAacetylation[1]
481KRLHTGEKPFKCEECubiquitination[2]
484HTGEKPFKCEECGKRubiquitination[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 DOMAIN 8 78 KRAB.
 ZN_FING 145 169 C2H2-type 1; degenerate.
 ZN_FING 175 197 C2H2-type 2; degenerate.
 ZN_FING 203 225 C2H2-type 3.
 ZN_FING 231 253 C2H2-type 4.
 ZN_FING 259 281 C2H2-type 5.
 ZN_FING 287 309 C2H2-type 6.
 ZN_FING 315 337 C2H2-type 7.
 ZN_FING 343 365 C2H2-type 8.
 ZN_FING 371 393 C2H2-type 9.
 ZN_FING 399 421 C2H2-type 10; degenerate.
 ZN_FING 427 449 C2H2-type 11.
 ZN_FING 455 477 C2H2-type 12.
 ZN_FING 483 505 C2H2-type 13.
 ZN_FING 511 533 C2H2-type 14.
 ZN_FING 539 561 C2H2-type 15; degenerate.  
Keyword
 Complete proteome; DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 593 AA 
Protein Sequence
MTMFKEAVTF KDVAVVFTEE ELGLLDVSQR KLYRDVMLEN FRNLLSVGHQ LSHRDTFHFQ 60
REEKFWIMET ATQREGNSGG KIQTELESVP ETGPHEEWSC QQIWEQTASE LTRPQDSISS 120
SQFSTQGDVP SQVDAGLSII HIGETPSEHG KCKKFFSDVS ILDLHQQLHS GKISHTCNEY 180
RKRFCYSSAL CLHQKVHMGE KRYKCDVCSK AFSQNSQLQT HQRIHTGEKP FKCEQCGKSF 240
SRRSGMYVHC KLHTGEKPHI CEECGKAFIH NSQLREHQRI HTGEKPFKCY ICGKSFHSRS 300
NLNRHSMVHM QEKSFRCDTC SNSFGQRSAL NSHCMDHTKE KLYKCEECGR SFTCRQDLCK 360
HQMDHTGDKP YNCNVCGKGF RWSSCLSRHQ RVHNGETTFK CDGCGKRFYM NSQGHSHQRA 420
YREEELYKCQ KCGKGYISKF NLDLHQRVHT GERPYNCKEC GKSFRWASGI LRHKRLHTGE 480
KPFKCEECGK RFTENSKLRF HQRIHTGEKP YKCEECGKGF RWASTHLTHQ RLHSREKLFQ 540
CEDCGKSSEH SSCLQDQQSD HSGEKTSKCE DCGKRYERRL NLDMILSLFL NDI 593 
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
 IPR001909; Krueppel-associated_box.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF01352; KRAB 
SMART
 SM00349; KRAB
 SM00355; ZnF_C2H2 
PROSITE
 PS50805; KRAB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS