CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015122
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger CCHC domain-containing protein 8 
Protein Synonyms/Alias
  
Gene Name
 ZCCHC8 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
128KRFEEQQKNDVEKTSubiquitination[1]
363SVTYDLSKLVNYPGFubiquitination[1, 2, 3]
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] 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] 
Functional Description
 May be involved in pre-mRNA splicing. 
Sequence Annotation
 ZN_FING 227 244 CCHC-type.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 479 479 Phosphothreonine.
 MOD_RES 485 485 Phosphothreonine.
 MOD_RES 598 598 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Metal-binding; mRNA processing; mRNA splicing; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 707 AA 
Protein Sequence
MAAEVYFGDL ELFEPFDHPE ESIPKPVHTR FKDDDGDEED ENGVGDAELR ERLRQCEETI 60
EQLRAENQEL KRKLNILTRP SGILVNDTKL DGPILQILFM NNAISKQYHQ EIEEFVSNLV 120
KRFEEQQKND VEKTSFNLLP QPSSIVLEED HKVEESCAIK NNKEAFSVVG SVLYFTNFCL 180
DKLGQPLLNE NPQLSEGWEI PKYHQVFSHI VSLEGQEIQV KAKRPKPHCF NCGSEEHQMK 240
DCPMPRNAAR ISEKRKEYMD ACGEANNQNF QQRYHAEEVE ERFGRFKPGV ISEELQDALG 300
VTDKSLPPFI YRMRQLGYPP GWLKEAELEN SGLALYDGKD GTDGETEVGE IQQNKSVTYD 360
LSKLVNYPGF NISTPRGIPD EWRIFGSIPM QACQQKDVFA NYLTSNFQAP GVKSGNKRSS 420
SHSSPGSPKK QKNESNSAGS PADMELDSDM EVPHGSQSSE SFQFQPPLPP DTPPLPRGTP 480
PPVFTPPLPK GTPPLTPSDS PQTRTASGAV DEDALTLEEL EEQQRRIWAA LEQAESVNSD 540
SDVPVDTPLT GNSVASSPCP NELDLPVPEG KTSEKQTLDE PEVPEIFTKK SEAGHASSPD 600
SEVTSLCQKE KAELAPVNTE GALLDNGSVV PNCDISNGGS QKLFPADTSP STATKIHSPI 660
PDMSKFATGI TPFEFENMAE STGMYLRIRS LLKNSPRNQQ KNKKASE 707 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 
Interpro
 IPR006568; PSP.
 IPR001878; Znf_CCHC. 
Pfam
 PF04046; PSP
 PF00098; zf-CCHC 
SMART
 SM00581; PSP
 SM00343; ZnF_C2HC 
PROSITE
 PS50158; ZF_CCHC 
PRINTS