MO4L1_HUMAN - dbPTM
MO4L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MO4L1_HUMAN
UniProt AC Q9UBU8
Protein Name Mortality factor 4-like protein 1
Gene Name MORF4L1
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Nucleus.
Protein 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..
Protein Sequence MAPKQDPKPKFQEGERVLCFHGPLLYEAKCVKVAIKDKQVKYFIHYSGWNKKSAVRPRRSEKSLKTHEDIVALFPVPEGAPSVHHPLLTSSWDEWVPESRVLKYVDTNLQKQRELQKANQEQYAEGKMRGAAPGKKTSGLQQKNVEVKTKKNKQKTPGNGDGGSTSETPQPPRKKRARVDPTVENEETFMNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGNTDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRLFVRIGAMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9UbiquitinationAPKQDPKPKFQEGER
CCCCCCCCCCCCCCE
48.3527667366
10UbiquitinationPKQDPKPKFQEGERV
CCCCCCCCCCCCCEE
66.8533845483
16AcetylationPKFQEGERVLCFHGP
CCCCCCCEEEEECCC
37.2519608861
16UbiquitinationPKFQEGERVLCFHGP
CCCCCCCEEEEECCC
37.2523000965
21UbiquitinationGERVLCFHGPLLYEA
CCEEEEECCCEEEEE
35.6423000965
28UbiquitinationHGPLLYEAKCVKVAI
CCCEEEEEEEEEEEE
9.2933845483
29AcetylationGPLLYEAKCVKVAIK
CCEEEEEEEEEEEEC
27.8526051181
29UbiquitinationGPLLYEAKCVKVAIK
CCEEEEEEEEEEEEC
27.8532015554
32UbiquitinationLYEAKCVKVAIKDKQ
EEEEEEEEEEECCCE
35.1033845483
36UbiquitinationKCVKVAIKDKQVKYF
EEEEEEECCCEEEEE
49.4927667366
38UbiquitinationVKVAIKDKQVKYFIH
EEEEECCCEEEEEEE
52.57-
42PhosphorylationIKDKQVKYFIHYSGW
ECCCEEEEEEEECCC
14.6526074081
46PhosphorylationQVKYFIHYSGWNKKS
EEEEEEEECCCCCCC
12.2226074081
47PhosphorylationVKYFIHYSGWNKKSA
EEEEEEECCCCCCCC
24.1426074081
47UbiquitinationVKYFIHYSGWNKKSA
EEEEEEECCCCCCCC
24.1429967540
47 (in isoform 2)Phosphorylation-24.1425159151
48UbiquitinationKYFIHYSGWNKKSAV
EEEEEECCCCCCCCC
25.4729967540
51UbiquitinationIHYSGWNKKSAVRPR
EEECCCCCCCCCCCC
41.4129967540
53PhosphorylationYSGWNKKSAVRPRRS
ECCCCCCCCCCCCCC
33.3426074081
60PhosphorylationSAVRPRRSEKSLKTH
CCCCCCCCHHHCCCC
51.1326074081
64UbiquitinationPRRSEKSLKTHEDIV
CCCCHHHCCCCHHEE
12.5821890473
64 (in isoform 2)Ubiquitination-12.5821890473
69UbiquitinationKSLKTHEDIVALFPV
HHCCCCHHEEEHEEC
32.8129967540
71UbiquitinationLKTHEDIVALFPVPE
CCCCHHEEEHEECCC
6.1533845483
72UbiquitinationKTHEDIVALFPVPEG
CCCHHEEEHEECCCC
12.1023000965
72 (in isoform 2)Ubiquitination-12.1021890473
77UbiquitinationIVALFPVPEGAPSVH
EEEHEECCCCCCCCC
34.2423503661
78UbiquitinationVALFPVPEGAPSVHH
EEHEECCCCCCCCCC
69.1223000965
78 (in isoform 2)Ubiquitination-69.1221890473
88UbiquitinationPSVHHPLLTSSWDEW
CCCCCCCCCCCHHHC
5.2722817900
88 (in isoform 2)Ubiquitination-5.2721890473
91UbiquitinationHHPLLTSSWDEWVPE
CCCCCCCCHHHCCCH
33.0533845483
97UbiquitinationSSWDEWVPESRVLKY
CCHHHCCCHHHHHHH
34.6133845483
99UbiquitinationWDEWVPESRVLKYVD
HHHCCCHHHHHHHHH
22.9421890473
99UbiquitinationWDEWVPESRVLKYVD
HHHCCCHHHHHHHHH
22.9427667366
100UbiquitinationDEWVPESRVLKYVDT
HHCCCHHHHHHHHHH
35.8033845483
103AcetylationVPESRVLKYVDTNLQ
CCHHHHHHHHHHHHH
40.1326051181
103UbiquitinationVPESRVLKYVDTNLQ
CCHHHHHHHHHHHHH
40.1322817900
103 (in isoform 1)Ubiquitination-40.1321890473
104AcetylationPESRVLKYVDTNLQK
CHHHHHHHHHHHHHH
10.2119608861
104UbiquitinationPESRVLKYVDTNLQK
CHHHHHHHHHHHHHH
10.2123000965
104 (in isoform 2)Ubiquitination-10.2121890473
109UbiquitinationLKYVDTNLQKQRELQ
HHHHHHHHHHHHHHH
7.9523000965
111UbiquitinationYVDTNLQKQRELQKA
HHHHHHHHHHHHHHH
55.2623000965
111 (in isoform 1)Ubiquitination-55.2621890473
113UbiquitinationDTNLQKQRELQKANQ
HHHHHHHHHHHHHHH
54.3421890473
113UbiquitinationDTNLQKQRELQKANQ
HHHHHHHHHHHHHHH
54.3422817900
114UbiquitinationTNLQKQRELQKANQE
HHHHHHHHHHHHHHH
53.7321890473
114UbiquitinationTNLQKQRELQKANQE
HHHHHHHHHHHHHHH
53.7321890473
116UbiquitinationLQKQRELQKANQEQY
HHHHHHHHHHHHHHH
37.7533845483
117UbiquitinationQKQRELQKANQEQYA
HHHHHHHHHHHHHHH
63.0323000965
117 (in isoform 1)Ubiquitination-63.0321890473
122UbiquitinationLQKANQEQYAEGKMR
HHHHHHHHHHHHHCC
32.7321890473
122UbiquitinationLQKANQEQYAEGKMR
HHHHHHHHHHHHHCC
32.7323000965
123PhosphorylationQKANQEQYAEGKMRG
HHHHHHHHHHHHCCC
13.08-
127AcetylationQEQYAEGKMRGAAPG
HHHHHHHHCCCCCCC
19.5425953088
127UbiquitinationQEQYAEGKMRGAAPG
HHHHHHHHCCCCCCC
19.5421906983
127 (in isoform 1)Ubiquitination-19.5421890473
135UbiquitinationMRGAAPGKKTSGLQQ
CCCCCCCCCCCCCHH
52.3929967540
136UbiquitinationRGAAPGKKTSGLQQK
CCCCCCCCCCCCHHC
54.5633845483
143AcetylationKTSGLQQKNVEVKTK
CCCCCHHCCCEEEEC
50.4219608861
143UbiquitinationKTSGLQQKNVEVKTK
CCCCCHHCCCEEEEC
50.4223000965
143 (in isoform 1)Ubiquitination-50.4221890473
148UbiquitinationQQKNVEVKTKKNKQK
HHCCCEEEECCCCCC
40.9123000965
155UbiquitinationKTKKNKQKTPGNGDG
EECCCCCCCCCCCCC
59.2933845483
156PhosphorylationTKKNKQKTPGNGDGG
ECCCCCCCCCCCCCC
33.6521815630
157UbiquitinationKKNKQKTPGNGDGGS
CCCCCCCCCCCCCCC
41.0929967540
159UbiquitinationNKQKTPGNGDGGSTS
CCCCCCCCCCCCCCC
46.7333845483
164PhosphorylationPGNGDGGSTSETPQP
CCCCCCCCCCCCCCC
34.0021712546
165UbiquitinationGNGDGGSTSETPQPP
CCCCCCCCCCCCCCC
33.5823503661
165 (in isoform 2)Ubiquitination-33.58-
166PhosphorylationNGDGGSTSETPQPPR
CCCCCCCCCCCCCCC
40.9625159151
168PhosphorylationDGGSTSETPQPPRKK
CCCCCCCCCCCCCCC
27.3021815630
174UbiquitinationETPQPPRKKRARVDP
CCCCCCCCCCCCCCC
53.0029967540
175UbiquitinationTPQPPRKKRARVDPT
CCCCCCCCCCCCCCC
53.2029967540
179UbiquitinationPRKKRARVDPTVENE
CCCCCCCCCCCCCCH
11.4533845483
187UbiquitinationDPTVENEETFMNRVE
CCCCCCHHHHHHCEE
59.9527667366
187 (in isoform 2)Ubiquitination-59.9521890473
188UbiquitinationPTVENEETFMNRVEV
CCCCCHHHHHHCEEE
23.2333845483
190SulfoxidationVENEETFMNRVEVKV
CCCHHHHHHCEEEEE
4.0121406390
196UbiquitinationFMNRVEVKVKIPEEL
HHHCEEEEEECCHHH
25.0629967540
198UbiquitinationNRVEVKVKIPEELKP
HCEEEEEECCHHHCC
46.9933845483
201UbiquitinationEVKVKIPEELKPWLV
EEEEECCHHHCCHHC
78.4422817900
201 (in isoform 2)Ubiquitination-78.4421890473
202UbiquitinationVKVKIPEELKPWLVD
EEEECCHHHCCHHCC
57.6621890473
202 (in isoform 2)Ubiquitination-57.6621890473
204UbiquitinationVKIPEELKPWLVDDW
EECCHHHCCHHCCCH
37.1123503661
208UbiquitinationEELKPWLVDDWDLIT
HHHCCHHCCCHHHHH
5.7623000965
210UbiquitinationLKPWLVDDWDLITRQ
HCCHHCCCHHHHHHH
33.0523000965
210 (in isoform 2)Ubiquitination-33.0521890473
212UbiquitinationPWLVDDWDLITRQKQ
CHHCCCHHHHHHHHH
34.8823000965
218UbiquitinationWDLITRQKQLFYLPA
HHHHHHHHHHEECCC
45.7533845483
226AcetylationQLFYLPAKKNVDSIL
HHEECCCCCCHHHHH
42.8325953088
226UbiquitinationQLFYLPAKKNVDSIL
HHEECCCCCCHHHHH
42.8327667366
226 (in isoform 1)Ubiquitination-42.8321890473
227UbiquitinationLFYLPAKKNVDSILE
HEECCCCCCHHHHHH
65.3922817900
236PhosphorylationVDSILEDYANYKKSR
HHHHHHHHHHHHHHC
6.33-
239PhosphorylationILEDYANYKKSRGNT
HHHHHHHHHHHCCCC
16.18-
240AcetylationLEDYANYKKSRGNTD
HHHHHHHHHHCCCCC
44.0425953088
240UbiquitinationLEDYANYKKSRGNTD
HHHHHHHHHHCCCCC
44.0422817900
240 (in isoform 1)Ubiquitination-44.0421890473
241UbiquitinationEDYANYKKSRGNTDN
HHHHHHHHHCCCCCC
34.7222817900
241 (in isoform 1)Ubiquitination-34.7221890473
249UbiquitinationSRGNTDNKEYAVNEV
HCCCCCCHHHHHHHH
55.7123000965
249 (in isoform 1)Ubiquitination-55.7121890473
296UbiquitinationPDAPMSQVYGAPHLL
CCCCHHHHHCHHHHH
3.5923000965
300UbiquitinationMSQVYGAPHLLRLFV
HHHHHCHHHHHHHHH
17.8123000965
300 (in isoform 2)Ubiquitination-17.81-
312SulfoxidationLFVRIGAMLAYTPLD
HHHHHHCHHHCCCCC
1.5328183972
315PhosphorylationRIGAMLAYTPLDEKS
HHHCHHHCCCCCHHH
12.6219835603
316PhosphorylationIGAMLAYTPLDEKSL
HHCHHHCCCCCHHHH
16.2719835603
335UbiquitinationNYLHDFLKYLAKNSA
HHHHHHHHHHHHCCC
37.9123000965
339UbiquitinationDFLKYLAKNSATLFS
HHHHHHHHCCCCCCC
49.1723000965
348PhosphorylationSATLFSASDYEVAPP
CCCCCCCCCCCCCCH
39.26-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MO4L1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MO4L1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MO4L1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MR1L1_HUMANMRFAP1L1physical
16189514
MOFA1_HUMANMRFAP1physical
11500496
RB_HUMANRB1physical
11500496
RB_HUMANRB1physical
12397079
KAT8_HUMANKAT8physical
12397079
H33_BOVINH3F3Aphysical
17135209
MOFA1_HUMANMRFAP1physical
17008723
MOFA1_HUMANMRFAP1physical
16407074
MRGBP_HUMANMRGBPphysical
16407074
MRGBP_HUMANMRGBPphysical
18218781
PHF12_HUMANPHF12physical
21440557
SRCAP_HUMANSRCAPphysical
17573780
KDM5A_HUMANKDM5Aphysical
17573780
BRD8_HUMANBRD8physical
17573780
SIN3B_HUMANSIN3Bphysical
17573780
PHF12_HUMANPHF12physical
17573780
EPC1_HUMANEPC1physical
17573780
EPC2_HUMANEPC2physical
17573780
IMB1_HUMANKPNB1physical
17573780
HNRPU_HUMANHNRNPUphysical
17573780
ZN131_HUMANZNF131physical
17573780
MBTD1_HUMANMBTD1physical
17573780
HSP74_HUMANHSPA4physical
17573780
HNRPM_HUMANHNRNPMphysical
17573780
LMNA_HUMANLMNAphysical
17573780
HDAC1_HUMANHDAC1physical
17573780
HDAC2_HUMANHDAC2physical
17573780
DMAP1_HUMANDMAP1physical
17573780
HNRPK_HUMANHNRNPKphysical
17573780
TBB2A_HUMANTUBB2Aphysical
17573780
TBA1A_HUMANTUBA1Aphysical
17573780
KAT5_HUMANKAT5physical
17573780
RBBP7_HUMANRBBP7physical
17573780
RUVB1_HUMANRUVBL1physical
17573780
RUVB2_HUMANRUVBL2physical
17573780
ACL6A_HUMANACTL6Aphysical
17573780
ACTS_HUMANACTA1physical
17573780
ACTB_HUMANACTBphysical
17573780
ACTG_HUMANACTG1physical
17573780
MO4L1_HUMANMORF4L1physical
17573780
MRGBP_HUMANMRGBPphysical
17573780
MOFA1_HUMANMRFAP1physical
17573780
H2AV_HUMANH2AFVphysical
17573780
H2B2E_HUMANHIST2H2BEphysical
17573780
PALB2_HUMANPALB2physical
20332121
BRCA2_HUMANBRCA2physical
20332121
RAD51_HUMANRAD51physical
20332121
BRCA1_HUMANBRCA1physical
20332121
TRRAP_HUMANTRRAPphysical
20332121
EP400_HUMANEP400physical
20332121
RET2_HUMANRBP2physical
20332121
BRD8_HUMANBRD8physical
20332121
SIN3B_HUMANSIN3Bphysical
20332121
PHF12_HUMANPHF12physical
20332121
EPC1_HUMANEPC1physical
20332121
EPC2_HUMANEPC2physical
20332121
HDAC1_HUMANHDAC1physical
20332121
HDAC2_HUMANHDAC2physical
20332121
KAT5_HUMANKAT5physical
20332121
RBBP7_HUMANRBBP7physical
20332121
RUVB1_HUMANRUVBL1physical
20332121
RUVB2_HUMANRUVBL2physical
20332121
MRGBP_HUMANMRGBPphysical
20332121
H2A2C_HUMANHIST2H2ACphysical
20332121
H2B2E_HUMANHIST2H2BEphysical
20332121
BRD8_HUMANBRD8physical
19553677
EP400_HUMANEP400physical
19553677
PHF12_HUMANPHF12physical
19553677
MSH6_HUMANMSH6physical
19553677
PALB2_HUMANPALB2physical
19553677
MRGBP_HUMANMRGBPphysical
19553677
SIN3B_HUMANSIN3Bphysical
19553677
MO4L2_HUMANMORF4L2physical
19553677
TRRAP_HUMANTRRAPphysical
19553677
TRRAP_HUMANTRRAPphysical
14966270
EPC1_HUMANEPC1physical
14966270
RUVB1_HUMANRUVBL1physical
14966270
ACL6A_HUMANACTL6Aphysical
14966270
SIN3A_HUMANSIN3Aphysical
14966270
HDAC2_HUMANHDAC2physical
14966270
A4_HUMANAPPphysical
21832049
RUVB2_HUMANRUVBL2physical
22939629
MO4L1_HUMANMORF4L1physical
25416956
RGAP1_HUMANRACGAP1physical
25416956
THAP1_HUMANTHAP1physical
25416956
MRGBP_HUMANMRGBPphysical
25416956
PBIP1_HUMANPBXIP1physical
25416956
ARRD3_HUMANARRDC3physical
25416956
PHF12_HUMANPHF12physical
25416956
GMCL1_HUMANGMCL1physical
25416956
ZBT10_HUMANZBTB10physical
25416956
HMBX1_HUMANHMBOX1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
NAV2_HUMANNAV2physical
25416956
TRI41_HUMANTRIM41physical
25416956
MOFA1_HUMANMRFAP1physical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
ZBTB9_HUMANZBTB9physical
25416956
BEND7_HUMANBEND7physical
25416956
CE57L_HUMANCEP57L1physical
25416956
MRGBP_HUMANMRGBPphysical
26186194
EP400_HUMANEP400physical
26186194
KDM5A_HUMANKDM5Aphysical
26186194
EAF6_HUMANMEAF6physical
26186194
PHF12_HUMANPHF12physical
26186194
EPC1_HUMANEPC1physical
26186194
EPC2_HUMANEPC2physical
26186194
DMAP1_HUMANDMAP1physical
26186194
TRRAP_HUMANTRRAPphysical
26186194
RBBP7_HUMANRBBP7physical
26186194
BRD8_HUMANBRD8physical
26186194
EMSY_HUMANC11orf30physical
26186194
VPS72_HUMANVPS72physical
26186194
MO4L2_HUMANMORF4L2physical
26186194
SIN3B_HUMANSIN3Bphysical
26186194
GATD1_HUMANGATAD1physical
26186194
PALB2_HUMANPALB2physical
26186194
KAT5_HUMANKAT5physical
26186194
BRCA2_HUMANBRCA2physical
26186194
MBTD1_HUMANMBTD1physical
26186194
YETS4_HUMANYEATS4physical
26186194
ASH1L_HUMANASH1Lphysical
26186194
MOFA1_HUMANMRFAP1physical
26186194
MR1L1_HUMANMRFAP1L1physical
26186194
ING3_HUMANING3physical
26186194
BRD8_HUMANBRD8physical
26344197
HDAC2_HUMANHDAC2physical
26344197
MRGBP_HUMANMRGBPphysical
26344197
TRRAP_HUMANTRRAPphysical
26344197
VAPA_HUMANVAPAphysical
26344197
VAPB_HUMANVAPBphysical
26344197
MR1L1_HUMANMRFAP1L1physical
21516116
MO4L2_HUMANMORF4L2physical
28514442
PHF12_HUMANPHF12physical
28514442
KDM5A_HUMANKDM5Aphysical
28514442
MR1L1_HUMANMRFAP1L1physical
28514442
EMSY_HUMANC11orf30physical
28514442
BRD8_HUMANBRD8physical
28514442
KAT5_HUMANKAT5physical
28514442
PALB2_HUMANPALB2physical
28514442
GATD1_HUMANGATAD1physical
28514442
EPC1_HUMANEPC1physical
28514442
EPC2_HUMANEPC2physical
28514442
EP400_HUMANEP400physical
28514442
SIN3B_HUMANSIN3Bphysical
28514442
MBTD1_HUMANMBTD1physical
28514442
ING3_HUMANING3physical
28514442
MOFA1_HUMANMRFAP1physical
28514442
TRRAP_HUMANTRRAPphysical
28514442
VPS72_HUMANVPS72physical
28514442
YETS4_HUMANYEATS4physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
DMAP1_HUMANDMAP1physical
28514442
ASH1L_HUMANASH1Lphysical
28514442
RBBP7_HUMANRBBP7physical
28514442
HDAC1_HUMANHDAC1physical
28514442
RUVB2_HUMANRUVBL2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MO4L1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND MASS SPECTROMETRY.

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