CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019464
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RING finger protein 145 
Protein Synonyms/Alias
  
Gene Name
 RNF145 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
507LRAQLGWKSFLLRRDubiquitination[1, 2, 3, 4]
520RDAVNKIKSLPIATKubiquitination[2, 4]
527KSLPIATKEQLEKHNubiquitination[2, 4]
545AICYQDMKSAVITPCubiquitination[4]
562FFHAGCLKKWLYVQEubiquitination[4]
563FHAGCLKKWLYVQETubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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 537 575 RING-type; atypical.  
Keyword
 Alternative splicing; Complete proteome; Membrane; Metal-binding; Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 663 AA 
Protein Sequence
MAAKEKLEAV LNVALRVPSI MLLDVLYRWD VSSFFQQIQR SSLSNNPLFQ YKYLALNMHY 60
VGYILSVVLL TLPRQHLVQL YLYFLTALLL YAGHQISRDY VRSELEFAYE GPMYLEPLSM 120
NRFTTALIGQ LVVCTLCSCV MKTKQIWLFS AHMLPLLARL CLVPLETIVI INKFAMIFTG 180
LEVLYFLGSN LLVPYNLAKS AYRELVQVVE VYGLLALGMS LWNQLVVPVL FMVFWLVLFA 240
LQIYSYFSTR DQPASRERLL FLFLTSIAEC CSTPYSLLGL VFTVSFVALG VLTLCKFYLQ 300
GYRAFMNDPA MNRGMTEGVT LLILAVQTGL IELQVVHRAF LLSIILFIVV ASILQSMLEI 360
ADPIVLALGA SRDKSLWKHF RAVSLCLFLL VFPAYMAYMI CQFFHMDFWL LIIISSSILT 420
SLQVLGTLFI YVLFMVEEFR KEPVENMDDV IYYVNGTYRL LEFLVALCVV AYGVSETIFG 480
EWTVMGSMII FIHSYYNVWL RAQLGWKSFL LRRDAVNKIK SLPIATKEQL EKHNDICAIC 540
YQDMKSAVIT PCSHFFHAGC LKKWLYVQET CPLCHCHLKN SSQLPGLGTE PVLQPHAGAE 600
QNVMFQEGTE PPGQEHTPGT RIQEGSRDNN EYIARRPDNQ EGAFDPKEYP HSAKDEAHPV 660
ESA 663 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR025754; TRC8_N_dom.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13705; TRC8_N
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS