CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023868
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RING finger protein 114 
Protein Synonyms/Alias
 Zinc finger protein 228; Zinc finger protein 313 
Gene Name
 RNF114 
Gene Synonyms/Alias
 ZNF228; ZNF313 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38VCLEVYEKPVQVPCGubiquitination[1, 2, 3]
58ACLQECLKPKKPVCGubiquitination[2]
61QECLKPKKPVCGVCRubiquitination[2]
96TSCHGCRKNFFLSKIubiquitination[1, 2, 4, 5]
102RKNFFLSKIRSHVATacetylation[6, 7]
102RKNFFLSKIRSHVATubiquitination[2, 4, 5, 8]
112SHVATCSKYQNYIMEacetylation[3, 6, 7, 9]
112SHVATCSKYQNYIMEubiquitination[1, 2, 3, 4, 10]
122NYIMEGVKATIKDASubiquitination[1, 2, 3, 4, 5, 8, 10, 11, 12]
126EGVKATIKDASLQPRubiquitination[1, 2, 3, 4, 5, 8, 10, 11, 12]
149PCPYCPEKNFDQEGLubiquitination[2]
161EGLVEHCKLFHSTDTubiquitination[1, 2, 3, 4, 5, 10]
169LFHSTDTKSVVCPICubiquitination[1, 2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 May play a role in spermatogenesis. 
Sequence Annotation
 ZN_FING 29 68 RING-type.
 MOD_RES 102 102 N6-acetyllysine.
 MOD_RES 112 112 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Developmental protein; Differentiation; Metal-binding; Reference proteome; Spermatogenesis; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 228 AA 
Protein Sequence
MAAQQRDCGG AAQLAGPAAE ADPLGRFTCP VCLEVYEKPV QVPCGHVFCS ACLQECLKPK 60
KPVCGVCRSA LAPGVRAVEL ERQIESTETS CHGCRKNFFL SKIRSHVATC SKYQNYIMEG 120
VKATIKDASL QPRNVPNRYT FPCPYCPEKN FDQEGLVEHC KLFHSTDTKS VVCPICASMP 180
WGDPNYRSAN FREHIQRRHR FSYDTFVDYD VDEEDMMNQV LQRSIIDQ 228 
Gene Ontology
 GO:0005622; C:intracellular; IDA:LIFEdb.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. 
Interpro
 IPR008598; Di19_RING_finger_144.
 IPR015880; Znf_C2H2-like.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF05605; Di19 
SMART
 SM00184; RING
 SM00355; ZnF_C2H2 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS