CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021628
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transmembrane protein 165 
Protein Synonyms/Alias
 Transmembrane protein PT27; Transmembrane protein TPARL 
Gene Name
 TMEM165 
Gene Synonyms/Alias
 TPARL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
180RMLREGLKMSPDEGQubiquitination[1, 2]
198EEVQAELKKKDEEFQubiquitination[1, 2]
208DEEFQRTKLLNGPGDubiquitination[1, 2, 3, 4, 5, 6]
227TSITVPQKKWLHFISubiquitination[1, 2, 3, 6]
228SITVPQKKWLHFISPubiquitination[5]
294GGRMIAQKISVRTVTubiquitination[1, 3, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation. 
Sequence Annotation
  
Keyword
 Coiled coil; Complete proteome; Congenital disorder of glycosylation; Disease mutation; Endosome; Golgi apparatus; Lysosome; Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 324 AA 
Protein Sequence
MAAAAPGNGR ASAPRLLLLF LVPLLWAPAA VRAGPDEDLS HRNKEPPAPA QQLQPQPVAV 60
QGPEPARVEK IFTPAAPVHT NKEDPATQTN LGFIHAFVAA ISVIIVSELG DKTFFIAAIM 120
AMRYNRLTVL AGAMLALGLM TCLSVLFGYA TTVIPRVYTY YVSTVLFAIF GIRMLREGLK 180
MSPDEGQEEL EEVQAELKKK DEEFQRTKLL NGPGDVETGT SITVPQKKWL HFISPIFVQA 240
LTLTFLAEWG DRSQLTTIVL AAREDPYGVA VGGTVGHCLC TGLAVIGGRM IAQKISVRTV 300
TIIGGIVFLA FAFSALFISP DSGF 324 
Gene Ontology
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0010008; C:endosome membrane; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
 GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
 GO:0006874; P:cellular calcium ion homeostasis; IGI:UniProtKB.
 GO:0032472; P:Golgi calcium ion transport; IDA:UniProtKB.
 GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
 GO:0035751; P:regulation of lysosomal lumen pH; IMP:UniProtKB. 
Interpro
 IPR001727; UPF0016. 
Pfam
 PF01169; UPF0016 
SMART
  
PROSITE
 PS01214; UPF0016 
PRINTS