CPLM-015118

Genbank Nucleotide ID

Polymerase I and transcript release factor

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
60	LVLSLLDKIIGAVDQ	ubiquitination	[1, 2]
95	SIQGELSKLGKAHAT	ubiquitination	[3, 4, 5, 6, 7]
98	GELSKLGKAHATTSN	ubiquitination	[3, 4, 5, 7]
109	TTSNTVSKLLEKVRK	acetylation	[8, 9]
109	TTSNTVSKLLEKVRK	ubiquitination	[1, 2, 3, 4, 6, 7, 10]
113	TVSKLLEKVRKVSVN	ubiquitination	[1, 2, 3, 7]
122	RKVSVNVKTVRGSLE	ubiquitination	[3, 4, 6, 7]
137	RQAGQIKKLEVNEAE	ubiquitination	[3, 6]
152	LLRRRNFKVMIYQDE	ubiquitination	[2, 3, 6, 7, 10]
161	MIYQDEVKLPAKLSI	sumoylation	[11]
161	MIYQDEVKLPAKLSI	ubiquitination	[3, 4, 6, 7]
165	DEVKLPAKLSISKSL	ubiquitination	[3, 6, 7]
170	PAKLSISKSLKESEA	ubiquitination	[3, 6, 7]
173	LSISKSLKESEALPE	ubiquitination	[3, 7]
299	TSRDKLRKSFTPDHV	ubiquitination	[1, 2, 6, 10]
317	RSKTAVYKVPPFTFH	ubiquitination	[2, 6, 10]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[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] 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]
[11] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]

Functional Description

Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex.

MOD_RES 1 1 N-acetylmethionine.
MOD_RES 36 36 Phosphoserine.
MOD_RES 40 40 Phosphoserine.
MOD_RES 167 167 Phosphoserine.
MOD_RES 175 175 Phosphoserine (By similarity).
MOD_RES 202 202 Phosphoserine.
MOD_RES 203 203 Phosphoserine.
MOD_RES 300 300 Phosphoserine.
MOD_RES 302 302 Phosphothreonine.
MOD_RES 365 365 Phosphoserine.
MOD_RES 366 366 Phosphoserine.
MOD_RES 387 387 Phosphoserine.
MOD_RES 389 389 Phosphoserine.

Acetylation; Alternative splicing; Cell membrane; Coiled coil; Complete proteome; Congenital generalized lipodystrophy; Cytoplasm; Diabetes mellitus; Direct protein sequencing; Endoplasmic reticulum; Membrane; Microsome; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; rRNA-binding; Transcription; Transcription regulation; Transcription termination.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005901; C:caveola; IDA:UniProtKB.
GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0042134; F:rRNA primary transcript binding; IDA:UniProtKB.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006363; P:termination of RNA polymerase I transcription; IDA:UniProtKB.
GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:UniProtKB.

IPR026752; Cavin_fam.