CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 148 
Protein Synonyms/Alias
 Transcription factor ZBP-89; Zinc finger DNA-binding protein 89 
Gene Name
 ZNF148 
Gene Synonyms/Alias
 ZBP89 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115LNVPISVKQEITFTDsumoylation[1]
153RKQRSPAKILTINEDubiquitination[2, 3]
166EDGSLGLKTPKSHVCubiquitination[4]
197VFIHTGEKPFQCSQCubiquitination[5]
356YSSSTKVKDEYMVAEsumoylation[1]
402INSKRSLKQPLEQNQubiquitination[4, 5]
424YEESKVSKYAFELVDubiquitination[5]
607NMLQEYSKFLQQALDacetylation[6]
607NMLQEYSKFLQQALDubiquitination[5]
Reference
 [1] Sumoylation-dependent control of homotypic and heterotypic synergy by the Kruppel-type zinc finger protein ZBP-89.
 Chupreta S, Brevig H, Bai L, Merchant JL, Iñiguez-Lluhí JA.
 J Biol Chem. 2007 Dec 14;282(50):36155-66. [PMID: 17940278]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes. 
Sequence Annotation
 ZN_FING 171 193 C2H2-type 1.
 ZN_FING 199 221 C2H2-type 2.
 ZN_FING 227 249 C2H2-type 3.
 ZN_FING 255 278 C2H2-type 4.
 MOD_RES 194 194 Phosphothreonine.
 MOD_RES 250 250 Phosphoserine.
 MOD_RES 305 305 Phosphothreonine (By similarity).
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 412 412 Phosphoserine.
 MOD_RES 607 607 N6-acetyllysine.
 MOD_RES 665 665 Phosphoserine.
 MOD_RES 784 784 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 794 AA 
Protein Sequence
MNIDDKLEGL FLKCGGIDEM QSSRTMVVMG GVSGQSTVSG ELQDSVLQDR SMPHQEILAA 60
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMETHERL PQGLQYALNV PISVKQEITF 120
TDVSEQLMRD KKQIREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF 180
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY 240
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED 300
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SALDKSDLKK DKNDYLPLYS SSTKVKDEYM 360
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQNQT ISPLSTYEES 420
KVSKYAFELV DKQALLDSEG NADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA 480
SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILES QALNVEIKSN HDKNVIPDEV 540
LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSEVPE VTPSENVGSS SQASSSDKAN 600
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSIDKQV YATMPINSFR 660
SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT STQDFLDQVT SQKKAEAQPV 720
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG 780
MTSSPDATTG QTFG 794 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003690; F:double-stranded DNA binding; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006968; P:cellular defense response; TAS:ProtInc.
 GO:0007276; P:gamete generation; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006461; P:protein complex assembly; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
  
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS