CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018017
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 675 
Protein Synonyms/Alias
 TRAF6-binding zinc finger protein; TRAF6-inhibitory zinc finger protein 
Gene Name
 ZNF675 
Gene Synonyms/Alias
 TIZ 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30TAQRNLYKNVILENYubiquitination[1]
66EKEPLTVKRHEMVNEubiquitination[1]
105VTLRRYEKCGNDNFQubiquitination[1]
155KYVKVFNKFSHSDRHubiquitination[1]
201YTKVNFCKCEECEKAubiquitination[1]
226KRIYTCEKLYKCQECubiquitination[1]
369HTGEQPYKCEECGKAubiquitination[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] 
Functional Description
 May be involved in transcriptional regulation. May play a role during osteoclast differentiation by modulating TRAF6 signaling activity. 
Sequence Annotation
 DOMAIN 4 75 KRAB.
 ZN_FING 144 166 C2H2-type 1; degenerate.
 ZN_FING 172 194 C2H2-type 2; degenerate.
 ZN_FING 200 222 C2H2-type 3; degenerate.
 ZN_FING 228 250 C2H2-type 4; degenerate.
 ZN_FING 256 278 C2H2-type 5.
 ZN_FING 284 306 C2H2-type 6.
 ZN_FING 312 334 C2H2-type 7.
 ZN_FING 340 362 C2H2-type 8.
 ZN_FING 368 390 C2H2-type 9.
 ZN_FING 396 418 C2H2-type 10.
 ZN_FING 424 446 C2H2-type 11.
 ZN_FING 452 474 C2H2-type 12.
 ZN_FING 480 502 C2H2-type 13.
 ZN_FING 508 530 C2H2-type 14.
 ZN_FING 536 558 C2H2-type 15.  
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
 568 AA 
Protein Sequence
MGLLTFRDVA IEFSLEEWQC LDTAQRNLYK NVILENYRNL VFLGIAVSKQ DLITCLEQEK 60
EPLTVKRHEM VNEPPVMCSH FAQEFWPEQN IKDSFEKVTL RRYEKCGNDN FQLKGCKSVD 120
ECKLHKGGYN GLNQCLPTMQ SKMFQCDKYV KVFNKFSHSD RHKIKHMENK PFKCKECGRS 180
FCMLSHLTRH ERNYTKVNFC KCEECEKAVN QSSKLTKHKR IYTCEKLYKC QECDRTFNQF 240
SNLTEYKKDY AREKPYKCEE CGKAFNQSSH LTTHKIIHTG EKPYKCEECG KAFNQFSNLT 300
THKKIHTGEQ PYICEECGKA FTQSSTLTTH KRIHTGEKPY KCEECGKAFN RSSKLTEHKN 360
IHTGEQPYKC EECGKAFNRS SNLTEHRKIH TEEKPYKCKE CGKAFKHSSA LTTHKRIHTG 420
EKPYKCEECG KAFNRSSKLT EHKKLHTGKK PYKCEECGKA FIQSSKLTEH KKIHSGEIPY 480
KCEECGKAFK HSSSLTTHKR IHTGEKPYKC EECGKAFSRS SKLTEHKIIH TGEKPYKCER 540
CDKAFNQSAN LTKHKKIHTG EKLQNWNV 568 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0045453; P:bone resorption; TAS:UniProtKB.
 GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
 GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
 GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
 GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
 GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
 GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
 GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
 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