CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019974
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RING finger protein 17 
Protein Synonyms/Alias
 Mad member-interacting protein 2; Mmip-2 
Gene Name
 Rnf17 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
229KSYIEEKKSDLDAAMacetylation[1]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753
Functional Description
 Seems to be involved in regulation of transcriptional activity of MYC. In vitro, inhibits DNA-binding activity of Mad- MAX heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis. 
Sequence Annotation
 DOMAIN 751 809 Tudor 1.
 DOMAIN 985 1044 Tudor 2.
 DOMAIN 1246 1303 Tudor 3.
 DOMAIN 1496 1556 Tudor 4.
 ZN_FING 30 73 RING-type.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Metal-binding; Nucleus; Reference proteome; Repeat; Spermatogenesis; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1640 AA 
Protein Sequence
MAAEASSTGL ASCHLVESKS GAQGASGCQC TRCGRKVSVA SGDHHKFPCG HAFCELCLLA 60
PQEYTTSKCT DCEVHTTVSM NQGHYPVDGF IEEDSSLEAL PPKMVNNCSS DLEKTVDQLI 120
NDLEHSSSIH RNVSNPSAVM SETEEIDEAL KIAGCNFEQL SNAIKMLDST QDQTRQETHS 180
LTEAVEKQFD TLLASLDSRK KSLCEELIRR TDDYLSKLVT VKSYIEEKKS DLDAAMKIAK 240
ELRSAPSLRT YCDLTQIIRT LKLTFESELS QVSSIIPRNT PRLDINCSEA ICMFSSMGKI 300
EFEDSTKCYP QENEDGQNVQ KKFNNRKELC CDVYSSLEKK KVDAAVLTDE TPEPPLQAEA 360
PDRHLEGKKK QPTKEMVVVT SPKTIAVLPQ LGSSPDVIIE EIIEENLESC FTDDPIETSG 420
YPKKPPQKEQ SAPVGSKAGC PELVFVSHVI HPCHFYVRKY SQIKDATILE KKMKQVCNRS 480
LHLDPSDILE LGARIFVNSI KNRMWCRGII TEIIPSKTKN IRKPCSPTKF SVCEISLIQI 540
FMVDFGNSEV LIITGVGDTH EGPEHDGEQH ITLSDFCLLL MKSEPYSEEL LKDIPHLAHL 600
CSLKDIVPYN STEGWEKEAK VEFLKMVNKK AVLMKVFGEE DDVLIVDLQK PPTNKISSDM 660
PVSLRDALVF MELARFRSQS PRSHSEKNTT LCYHPPILPE EMTEVSVMVC HINSPTDFYL 720
QLMENLDFLS LLKTIEEFYK GEDGENLEIL CPLQNQACVA KFEDGIWYRA KVIGLPGHRE 780
VEVKYVDFGN TAKITLKDMR KIKDEFLEPP EKAIKCKLAY VEPSKKSQWS KKAKEKFEEK 840
TQDKFVTCSV IKILENNVLL VELFDSRAPG KSAVSINDQL VKEGLASYEA GYTLKDNSKK 900
HLEVWDPSPE EIITSEINNL SPLSVKSLPN ENFQSLYNKE LPVNICNVIS PEKIYVQWLL 960
TENLLNSLEE KMVAAYEHSE WKPVKWECDM HCAVKVPAKN QWRRGQILRM VTDKLVEVLL 1020
YDVGVELVVN IHCLRELQEN LKTMGRLSLE CSLVDIRPTG GSDKWTATAC DCLSLHLTGA 1080
IATIILQESN TTWPLPVKIF CRDEKGERVD VSKYLIKKGL ALRERRVSKS SNSHSPEKSL 1140
EIPLEQGDSV VTKCFKINFD TNKKIADKVN EHKVPDSKGK KSESRSTGCY RPPAVPNTSS 1200
FEAIVTCIGD DGTIFVVPKL SEFELIKMMD EIQSNLKCLG LLEPYSWKKG EPCAVRGSDT 1260
LWYRGKVMEV VGGTIRVQYL DHGFTEKIPQ CHLYPILLYP DTPQFCIPCQ LYQTLPVGNT 1320
WQPDAIELLQ ELLSKREVDI HIMELPNNSW GKLSVHLYFD GMSLSHFMAH HKYCIFEHTE 1380
EIFKEKPRGQ NKKYEDENWK IRFEDLLLPE MEAPVLPPYL SSLLPPPEEL FAVQVKHIVS 1440
PDEMYICLDS EDSYTQFNHH GDTDDSGVSW ESESENLEEA LQRFNKNVET FPPLTDFSSE 1500
MPCLAEYADG LWYRAKIISI KEFNPLSVLV LFVDYGCTEK LTINRLRQIP VQLMQYPAQA 1560
IKVLLAGFKP PLSDSGKTRI PYCPKWSMEA LWTMIDCLQG KQLYASSVAQ APEQIVTLYE 1620
DEQYPVHMSL VEMGLADKDE 1640 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0007286; P:spermatid development; IMP:MGI. 
Interpro
 IPR016071; Staphylococal_nuclease_OB-fold.
 IPR006021; Staphylococcal_nuclease.
 IPR002999; Tudor.
 IPR001841; Znf_RING.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00567; TUDOR 
SMART
 SM00333; TUDOR 
PROSITE
 PS50304; TUDOR
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS