CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012631
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein with KRAB and SCAN domains 8 
Protein Synonyms/Alias
 LD5-1; Zinc finger protein 192 
Gene Name
 ZKSCAN8 
Gene Synonyms/Alias
 ZNF192 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
272ENRELASKQVISTGIubiquitination[1]
519HTGERPYKCKECGKAacetylation[2]
521GERPYKCKECGKAFNacetylation[2]
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] 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] 
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 DOMAIN 51 133 SCAN box.
 DOMAIN 220 316 KRAB.
 ZN_FING 322 344 C2H2-type 1.
 ZN_FING 350 372 C2H2-type 2.
 ZN_FING 378 400 C2H2-type 3.
 ZN_FING 406 428 C2H2-type 4.
 ZN_FING 434 456 C2H2-type 5.
 ZN_FING 462 484 C2H2-type 6.
 ZN_FING 490 512 C2H2-type 7.
 ZN_FING 518 540 C2H2-type 8.
 ZN_FING 546 568 C2H2-type 9.
 MOD_RES 12 12 Phosphoserine.  
Keyword
 Complete proteome; 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
 578 AA 
Protein Sequence
MAEESRKPSA PSPPDQTPEE DLVIVKVEED HGWDQESSLH ESNPLGQEVF RLRFRQLRYQ 60
ETLGPREALI QLRALCHQWL RPDLNTKEQI LELLVLEQFL TILPEELQTL VKEHQLENGE 120
EVVTLLEDLE RQIDILGRPV SARVHGHRVL WEEVVHSASA PEPPNTQLQS EATQHKSPVP 180
QESQERAMST SQSPTRSQKG SSGDQEMTAT LLTAGFQTLE KIEDMAVSLI REEWLLDPSQ 240
KDLCRDNRPE NFRNMFSLGG ETRSENRELA SKQVISTGIQ PHGETAAKCN GDVIRGLEHE 300
EARDLLGRLE RQRGNPTQER RHKCDECGKS FAQSSGLVRH WRIHTGEKPY QCNVCGKAFS 360
YRSALLSHQD IHNKVKRYHC KECGKAFSQN TGLILHQRIH TGEKPYQCNQ CGKAFSQSAG 420
LILHQRIHSG ERPYECNECG KAFSHSSHLI GHQRIHTGEK PYECDECGKT FRRSSHLIGH 480
QRSHTGEKPY KCNECGRAFS QKSGLIEHQR IHTGERPYKC KECGKAFNGN TGLIQHLRIH 540
TGEKPYQCNE CGKAFIQRSS LIRHQRIHSG EKSESISV 578 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0016032; P:viral reproduction; IEA:InterPro. 
Interpro
 IPR001909; Krueppel-associated_box.
 IPR008916; Retrov_capsid_C.
 IPR003309; Tscrpt_reg_SCAN.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF01352; KRAB
 PF02023; SCAN 
SMART
 SM00349; KRAB
 SM00431; SCAN
 SM00355; ZnF_C2H2 
PROSITE
 PS50805; KRAB
 PS50804; SCAN_BOX
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS