Overview
| Uniprot ID | Q15014 |
|---|
| Protein Name | Mortality factor 4-like protein 2 |
|---|
| Gene Name | MORF4L2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 22 |
SAEEENFKKPTRSNM |
| 49 |
KTAGPQQKNLEPALP |
Function
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone 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 a component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones
Protein Sequence
10
MSSRKQGSQP
20
RGQQSAEEEN
30
FKKPTRSNMQ
40
RSKMRGASSG
50
KKTAGPQQKN
60
LEPALPGRWG
70
GRSAENPPSG
80
SVRKTRKNKQ
90
KTPGNGDGGS
100
TSEAPQPPRK
110
KRARADPTVE
120
SEEAFKNRME
130
VKVKIPEELK
140
PWLVEDWDLV
150
TRQKQLFQLP
160
AKKNVDAILE
170
EYANCKKSQG
180
NVDNKEYAVN
190
EVVAGIKEYF
200
NVMLGTQLLY
210
KFERPQYAEI
220
LLAHPDAPMS
230
QVYGAPHLLR
240
LFVRIGAMLA
250
YTPLDEKSLA
260
LLLGYLHDFL
270
KYLAKNSASL
280
FTASDYKVAS
AEYHRKAL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0035267 |
NuA4 histone acetyltransferase complex |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0000786 |
nucleosome |
| Biological Process |
GO:0006325 |
chromatin organization |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0045893 |
positive regulation of DNA-templated transcription |
| Biological Process |
GO:1905168 |
positive regulation of double-strand break repair via homologous recombination |
| Biological Process |
GO:0042981 |
regulation of apoptotic process |
| Biological Process |
GO:0051726 |
regulation of cell cycle |
| Biological Process |
GO:2000779 |
regulation of double-strand break repair |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.