CPLM-022861

Genbank Nucleotide ID

Mortality factor 4-like protein 1

Protein Synonyms/Alias

MORF-related gene 15 protein; Protein MSL3-1; Transcription factor-like protein MRG15

MRG15; FWP006; HSPC008; HSPC061; PP368

Homo sapiens (Human)

Position	Peptide	Type	References
103	VPESRVLKYVDTNLQ	ubiquitination	[1, 2]
111	YVDTNLQKQRELQKA	ubiquitination	[1, 2, 3, 4, 5, 6]
117	QKQRELQKANQEQYA	ubiquitination	[3, 4, 6]
127	QEQYAEGKMRGAAPG	ubiquitination	[3, 6]
143	KTSGLQQKNVEVKTK	acetylation	[7]
143	KTSGLQQKNVEVKTK	ubiquitination	[3, 5, 6]
148	QQKNVEVKTKKNKQK	ubiquitination	[6]
218	WDLITRQKQLFYLPA	ubiquitination	[6]
226	QLFYLPAKKNVDSIL	ubiquitination	[1, 2, 3, 6, 8]
227	LFYLPAKKNVDSILE	ubiquitination	[6]
240	LEDYANYKKSRGNTD	ubiquitination	[1, 2, 3, 4]
241	EDYANYKKSRGNTDN	ubiquitination	[1, 2, 6]
249	SRGNTDNKEYAVNEV	ubiquitination	[1, 2, 3, 5]
339	DFLKYLAKNSATLFS	ubiquitination	[5, 8]

[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] 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] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]

Functional Description

Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the mSin3A complex which acts to repress transcription by deacetylation of nucleosomal histones. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci.

DOMAIN 191 362 MRG.
REGION 26 62 Interaction with KAT8.
REGION 133 266 Sufficient for interaction with SIN3A.
REGION 164 230 Interaction with RB1-1.
REGION 188 342 Sufficient for interaction with PHF12.
REGION 323 344 Interaction with RB1-2.
MOTIF 135 146 Nuclear localization signal (Potential).
MOD_RES 143 143 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; Growth regulation; Nucleus; Reference proteome; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO:0016580; C:Sin3 complex; IDA:UniProtKB.
GO:0003682; F:chromatin binding; IEA:Compara.
GO:0008283; P:cell proliferation; IEA:Compara.
GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO:0016575; P:histone deacetylation; IDA:UniProtKB.
GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR016197; Chromodomain-like.
IPR017398; EAF3/MRG15.
IPR008676; MRG.
IPR026541; MRG_dom.
IPR025995; Tudor-knot.

PF05712; MRG
PF11717; Tudor-knot