CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011939
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripartite motif-containing protein 26 
Protein Synonyms/Alias
 Acid finger protein; AFP; RING finger protein 95; Zinc finger protein 173 
Gene Name
 TRIM26 
Gene Synonyms/Alias
 RNF95; ZNF173 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85IERLKVDKGRQPGEVubiquitination[1]
148AAQPHREKILNHLSTubiquitination[1]
162TLRRDRDKIQGFQAKubiquitination[1]
179ADILAALKKLQDQRQubiquitination[2, 3, 4]
180DILAALKKLQDQRQYubiquitination[1]
245VISELEGKAQQPAAEubiquitination[1, 5]
273RKKFWVGKPIARVVKubiquitination[1]
289KTGEFSDKLLSLQRGubiquitination[1]
303GLREFQGKLLRDLEYacetylation[6]
342VTYTSLYKSAYLHPQubiquitination[1, 7]
361EPGVLGSKGFTWGKVubiquitination[1, 7]
449ARDSVKRKGDLSLRPubiquitination[1]
529LVPFLWLKWPGTRLLubiquitination[8]
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] 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]
 [4] 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]
 [5] 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]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
  
Sequence Annotation
 DOMAIN 295 539 B30.2/SPRY.
 ZN_FING 16 57 RING-type.
 ZN_FING 97 138 B box-type.  
Keyword
 Coiled coil; Complete proteome; Metal-binding; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 539 AA 
Protein Sequence
MATSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT TDVRPISGSR PVCPLCKKPF 60
KKENIRPVWQ LASLVENIER LKVDKGRQPG EVTREQQDAK LCERHREKLH YYCEDDGKLL 120
CVMCRESREH RPHTAVLMEK AAQPHREKIL NHLSTLRRDR DKIQGFQAKG EADILAALKK 180
LQDQRQYIVA EFEQGHQFLR EREEHLLEQL AKLEQELTEG REKFKSRGVG ELARLALVIS 240
ELEGKAQQPA AELMQDTRDF LNRYPRKKFW VGKPIARVVK KKTGEFSDKL LSLQRGLREF 300
QGKLLRDLEY KTVSVTLDPQ SASGYLQLSE DWKCVTYTSL YKSAYLHPQQ FDCEPGVLGS 360
KGFTWGKVYW EVEVEREGWS EDEEEGDEEE EGEEEEEEEE AGYGDGYDDW ETDEDEESLG 420
DEEEEEEEEE EEVLESCMVG VARDSVKRKG DLSLRPEDGV WALRLSSSGI WANTSPEAEL 480
FPALRPRRVG IALDYEGGTV TFTNAESQEL IYTFTATFTR RLVPFLWLKW PGTRLLLRP 539 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR006574; PRY.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box 
SMART
 SM00336; BBOX
 SM00589; PRY
 SM00184; RING
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.