MS3L1_HUMAN - dbPTM
MS3L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MS3L1_HUMAN
UniProt AC Q8N5Y2
Protein Name Male-specific lethal 3 homolog
Gene Name MSL3
Organism Homo sapiens (Human).
Sequence Length 521
Subcellular Localization Nucleus .
Protein Description May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex..
Protein Sequence MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAKIVDVIVGKDEKGRKIPEYLIHFNGWNRSWDRWAAEDHVLRDTDENRRLQRKLARKAVARLRSTGRKKKRCRLPGVDSVLKGLPTEEKDENDENSLSSSSDCSENKDEEISEESDIEEKTEVKEEPELQTRREMEERTITIEIPEVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHVMPHANMNVHYIPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQAQYKKVTSSKFFLPIKESATSTNRSQEELSPSPPLLNPSTPQSTESQPTTGEPATPKRRKAEPEALQSLRRSTRHSANCDRLSESSASPQPKRRQQDTSASMPKLFLHLEKKTPVHSRSSSPIPLTPSKEGSAVFAGFEGRRTNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY
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
2Phosphorylation------MSASEGMKF
------CCCCCCCEE		40.2729083192
4Phosphorylation----MSASEGMKFKF
----CCCCCCCEEEE		27.6329083192
16UbiquitinationFKFHSGEKVLCFEPD
EEECCCCEEEEECCC		43.9929967540
17 (in isoform 2)Phosphorylation-4.98-
33UbiquitinationKARVLYDAKIVDVIV
CEEEEEEEEEEEEEE		7.0129967540
42AcetylationIVDVIVGKDEKGRKI
EEEEEECCCCCCCCC		52.3925953088
45AcetylationVIVGKDEKGRKIPEY
EEECCCCCCCCCCCE		74.3225953088
76PhosphorylationEDHVLRDTDENRRLQ
HCCCCCCCHHHHHHH		38.4924275569
85AcetylationENRRLQRKLARKAVA
HHHHHHHHHHHHHHH		33.2769317
111PhosphorylationCRLPGVDSVLKGLPT
CCCCCHHHHHCCCCC		27.2628555341
118UbiquitinationSVLKGLPTEEKDEND
HHHCCCCCCCCCCCC		62.9222817900
123UbiquitinationLPTEEKDENDENSLS
CCCCCCCCCCCCCCC		77.1021890473
123UbiquitinationLPTEEKDENDENSLS
CCCCCCCCCCCCCCC		77.1021890473
129UbiquitinationDENDENSLSSSSDCS
CCCCCCCCCCCCCCC		9.6823000965
135UbiquitinationSLSSSSDCSENKDEE
CCCCCCCCCCCCCHH		6.2522817900
140UbiquitinationSDCSENKDEEISEES
CCCCCCCCHHHHCCC		71.0521890473
143PhosphorylationSENKDEEISEESDIE
CCCCCHHHHCCCCCH		6.2133259812
144PhosphorylationENKDEEISEESDIEE
CCCCHHHHCCCCCHH		38.2920363803
146UbiquitinationKDEEISEESDIEEKT
CCHHHHCCCCCHHHH		47.0923000965
147PhosphorylationDEEISEESDIEEKTE
CHHHHCCCCCHHHHC		39.5820363803
160PhosphorylationTEVKEEPELQTRREM
HCCCCCHHHHCHHHH		57.7133259812
170UbiquitinationTRREMEERTITIEIP
CHHHHHHCEEEEEHH		20.3729967540
182UbiquitinationEIPEVLKKQLEDDCY
EHHHHHHHHHHCCCE		56.8229967540
189PhosphorylationKQLEDDCYYINRRKR
HHHHCCCEEEHHHHC		17.8625147952
201 (in isoform 4)Phosphorylation-11.49-
217UbiquitinationLESYVKHFAINAAFS
HHHHHHHHHHHHHCC		6.3929967540
224PhosphorylationFAINAAFSANERPRH
HHHHHHCCCCCCCCC		26.0028842319
230UbiquitinationFSANERPRHHHVMPH
CCCCCCCCCCCCCCC		48.2521890473
230 (in isoform 2)Ubiquitination-48.2521890473
232PhosphorylationANERPRHHHVMPHAN
CCCCCCCCCCCCCCC		19.2732142685
232 (in isoform 4)Phosphorylation-19.27-
233 (in isoform 4)Phosphorylation-16.08-
234AcetylationERPRHHHVMPHANMN
CCCCCCCCCCCCCCC		5.76-
234 (in isoform 4)Phosphorylation-5.76-
234PhosphorylationERPRHHHVMPHANMN
CCCCCCCCCCCCCCC		5.7632645325
234UbiquitinationERPRHHHVMPHANMN
CCCCCCCCCCCCCCC		5.7629967540
239 (in isoform 4)Phosphorylation-21.37-
241UbiquitinationVMPHANMNVHYIPAE
CCCCCCCCEEEECCH		19.74-
241 (in isoform 4)Phosphorylation-19.74-
245 (in isoform 4)Phosphorylation-1.25-
249PhosphorylationVHYIPAEKNVDLCKE
EEEECCHHCHHHHHH		65.4632142685
251PhosphorylationYIPAEKNVDLCKEMV
EECCHHCHHHHHHHC		9.8432645325
272UbiquitinationFDYTLPLVLLYPYEQ
EECCCEEEEEEEHHH		3.0622817900
277UbiquitinationPLVLLYPYEQAQYKK
EEEEEEEHHHHHHEE		13.7121890473
283UbiquitinationPYEQAQYKKVTSSKF
EHHHHHHEECCCCCC		28.7823000965
284UbiquitinationYEQAQYKKVTSSKFF
HHHHHHEECCCCCCE		45.9022817900
289 (in isoform 1)Ubiquitination-39.6421890473
289UbiquitinationYKKVTSSKFFLPIKE
HEECCCCCCEEEECC		39.6423000965
289UbiquitinationYKKVTSSKFFLPIKE
HEECCCCCCEEEECC		39.6421890473
289UbiquitinationYKKVTSSKFFLPIKE
HEECCCCCCEEEECC		39.6421890473
289UbiquitinationYKKVTSSKFFLPIKE
HEECCCCCCEEEECC		39.6421890473
295UbiquitinationSKFFLPIKESATSTN
CCCEEEECCCCCCCC		43.6123000965
297PhosphorylationFFLPIKESATSTNRS
CEEEECCCCCCCCCC		31.6733259812
304PhosphorylationSATSTNRSQEELSPS
CCCCCCCCHHHHCCC		43.9730108239
308 (in isoform 2)Phosphorylation-10.05-
309PhosphorylationNRSQEELSPSPPLLN
CCCHHHHCCCCCCCC		26.9822115753
311PhosphorylationSQEELSPSPPLLNPS
CHHHHCCCCCCCCCC		35.4628355574
318PhosphorylationSPPLLNPSTPQSTES
CCCCCCCCCCCCCCC		52.2022115753
319PhosphorylationPPLLNPSTPQSTESQ
CCCCCCCCCCCCCCC		26.9722115753
322PhosphorylationLNPSTPQSTESQPTT
CCCCCCCCCCCCCCC		35.0328450419
323PhosphorylationNPSTPQSTESQPTTG
CCCCCCCCCCCCCCC		34.1128450419
325PhosphorylationSTPQSTESQPTTGEP
CCCCCCCCCCCCCCC		41.3628450419
328PhosphorylationQSTESQPTTGEPATP
CCCCCCCCCCCCCCC		39.5328450419
329PhosphorylationSTESQPTTGEPATPK
CCCCCCCCCCCCCCC		46.3530576142
334PhosphorylationPTTGEPATPKRRKAE
CCCCCCCCCCHHHCC		39.8122115753
339 (in isoform 2)Phosphorylation-62.22-
341 (in isoform 2)Phosphorylation-46.86-
346 (in isoform 2)Phosphorylation-47.68-
347PhosphorylationAEPEALQSLRRSTRH
CCHHHHHHHHHHHHH		25.3721815630
348 (in isoform 2)Phosphorylation-3.21-
352 (in isoform 2)Phosphorylation-30.50-
362PhosphorylationSANCDRLSESSASPQ
HCHHHHHCCCCCCCC		36.0030266825
364PhosphorylationNCDRLSESSASPQPK
HHHHHCCCCCCCCCC		28.0330266825
365PhosphorylationCDRLSESSASPQPKR
HHHHCCCCCCCCCCC		28.8130266825
367PhosphorylationRLSESSASPQPKRRQ
HHCCCCCCCCCCCCC		26.4730266825
367 (in isoform 5)Phosphorylation-26.47-
371UbiquitinationSSASPQPKRRQQDTS
CCCCCCCCCCCCCCC		55.7729967540
377PhosphorylationPKRRQQDTSASMPKL
CCCCCCCCCCCHHHH		23.1229978859
378PhosphorylationKRRQQDTSASMPKLF
CCCCCCCCCCHHHHH		27.0029978859
380PhosphorylationRQQDTSASMPKLFLH
CCCCCCCCHHHHHHE		35.0729978859
383UbiquitinationDTSASMPKLFLHLEK
CCCCCHHHHHHEECC		43.1429967540
383AcetylationDTSASMPKLFLHLEK
CCCCCHHHHHHEECC		43.1423749302
386PhosphorylationASMPKLFLHLEKKTP
CCHHHHHHEECCCCC		6.9832142685
388PhosphorylationMPKLFLHLEKKTPVH
HHHHHHEECCCCCCC		12.8832645325
390UbiquitinationKLFLHLEKKTPVHSR
HHHHEECCCCCCCCC		69.20-
392PhosphorylationFLHLEKKTPVHSRSS
HHEECCCCCCCCCCC		41.4323401153
396PhosphorylationEKKTPVHSRSSSPIP
CCCCCCCCCCCCCCC		33.8123401153
398PhosphorylationKTPVHSRSSSPIPLT
CCCCCCCCCCCCCCC		37.8830266825
399PhosphorylationTPVHSRSSSPIPLTP
CCCCCCCCCCCCCCC		38.7422167270
400PhosphorylationPVHSRSSSPIPLTPS
CCCCCCCCCCCCCCC		28.2623927012
405PhosphorylationSSSPIPLTPSKEGSA
CCCCCCCCCCCCCCE		21.8422167270
407PhosphorylationSPIPLTPSKEGSAVF
CCCCCCCCCCCCEEE		37.8030266825
408AcetylationPIPLTPSKEGSAVFA
CCCCCCCCCCCEEEE		68.2625953088
411PhosphorylationLTPSKEGSAVFAGFE
CCCCCCCCEEEEECC		23.5020657587
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 MS3L1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MS3L1_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 MS3L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSL1_HUMANMSL1physical
16227571
MSL2_HUMANMSL2physical
16227571
H31_HUMANHIST1H3Aphysical
16227571
PRKDC_HUMANPRKDCphysical
20479123
MSL1_HUMANMSL1physical
20479123
MSL1_HUMANMSL1physical
21217699
KAT8_HUMANKAT8physical
21217699
H31T_HUMANHIST3H3physical
20943666
A4_HUMANAPPphysical
21832049
PAF1_HUMANPAF1physical
24837678
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 MS3L1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-400; THR-405AND SER-407, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-407 ANDSER-411, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory