CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021607
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RING finger and CCCH-type zinc finger domain-containing protein 2 
Protein Synonyms/Alias
 Membrane-associated nucleic acid-binding protein; RING finger protein 164 
Gene Name
 RC3H2 
Gene Synonyms/Alias
 MNAB; RNF164 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1031LTLNLLSKEIELRNGubiquitination[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
  
Sequence Annotation
 ZN_FING 14 54 RING-type; degenerate.
 ZN_FING 410 438 C3H1-type.
 MOD_RES 549 549 Phosphoserine.
 MOD_RES 808 808 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1191 AA 
Protein Sequence
MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD 60
IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS 120
LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL 180
WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG 240
HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW 300
SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI 360
DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR 420
QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI NATVRTFPLL NKVGVNNTVT TTAGNVISVI 480
GSTETTGKIV PSTNGISNAE NSVSQLISRS TDSTLRALET VKKVGKVGAN GQNAAGPSAD 540
SVTENKIGSP PKTPVSNVAA TSAGPSNVGT ELNSVPQKSS PFLTRVPVYP PHSENIQYFQ 600
DPRTQIPFEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA SMPYADHYST 660
FSPRDRMNSS PYQPPPPQPY GPVPPVPSGM YAPVYDSRRI WRPPMYQRDD IIRSNSLPPM 720
DVMHSSVYQT SLRERYNSLD GYYSVACQPP SEPRTTVPLP REPCGHLKTS CEEQIRRKPD 780
QWAQYHTQKA PLVSSTLPVA TQSPTPPSPL FSVDFRADFS ESVSGTKFEE DHLSHYSPWS 840
CGTIGSCINA IDSEPKDVIA NSNAVLMDLD SGDVKRRVHL FETQRRTKEE DPIIPFSDGP 900
IISKWGAISR SSRTGYHTTD PVQATASQGS ATKPISVSDY VPYVNAVDSR WSSYGNEATS 960
SAHYVERDRF IVTDLSGHRK HSSTGDLLSL ELQQAKSNSL LLQREANALA MQQKWNSLDE 1020
GRHLTLNLLS KEIELRNGEL QSDYTEDATD TKPDRDIELE LSALDTDEPD GQSEPIEEIL 1080
DIQLGISSQN DQLLNGMAVE NGHPVQQHQK EPPKQKKQSL GEDHVILEEQ KTILPVTSCF 1140
SQPLPVSISN ASCLPITTSV SAGNLILKTH VMSEDKNDFL KPVANGKMVN S 1191 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR000571; Znf_CCCH.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00642; zf-CCCH 
SMART
 SM00184; RING
 SM00356; ZnF_C3H1 
PROSITE
 PS50103; ZF_C3H1
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS