CPLM-012445

Genbank Nucleotide ID

PCNA-associated factor

Protein Synonyms/Alias

Hepatitis C virus NS5A-transactivated protein 9; HCV NS5A-transactivated protein 9; Overexpressed in anaplastic thyroid carcinoma 1; OEATC-1; PCNA-associated factor of 15 kDa; PAF15; p15PAF

Homo sapiens (Human)

Position	Peptide	Type	References
15	SVPGTYRKVVAARAP	ubiquitination	[1]
24	VAARAPRKVLGSSTS	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
63	RPTPKWQKGIGEFFR	ubiquitination	[4]
95	SSGLGKAKRKACPLQ	acetylation	[8]

[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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[3] 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]
[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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[6] 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]
[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] 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]

Functional Description

PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number.

MOTIF 23 34 D-box.
MOTIF 62 72 PIP-box.
MOTIF 78 80 KEN box.
MOTIF 85 97 Initiation motif.
MOD_RES 31 31 Phosphoserine.
MOD_RES 72 72 Phosphoserine.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 24 24 Glycyl lysine isopeptide (Lys-Gly)

Alternative splicing; Complete proteome; Cytoplasm; DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO:0051297; P:centrosome organization; IMP:UniProtKB.
GO:0006260; P:DNA replication; IDA:UniProtKB.
GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
GO:0009411; P:response to UV; IDA:UniProtKB.
GO:0019985; P:translesion synthesis; IMP:UniProtKB.