MSL1_HUMAN - dbPTM
MSL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSL1_HUMAN
UniProt AC Q68DK7
Protein Name Male-specific lethal 1 homolog
Gene Name MSL1
Organism Homo sapiens (Human).
Sequence Length 614
Subcellular Localization Nucleus .
Protein Description Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation..
Protein Sequence MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDEPGAAEAHFLPRHRKLKEPGPPLASSQGGSPAPSPAGCGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPAAAGAGCSPRPKYQAVLPIQTGSLVAAAKEPTPWAGDKGGAASPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSMRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKKDNEKERHKLFQGYETEEREETELSEKIKLECQPELSETSQTLPPKPFSCGRSGKGHKRKSPFGSTERKTPVKKLAPEFSKVKTKTPKHSPIKEEPCGSLSETVCKRELRSQETPEKPRSSVDTPPRLSTPQKGPSTHPKEKAFSSEIEDLPYLSTTEMYLCRWHQPPPSPLPLRESSPKKEETVARCLMPSSVAGETSVLAVPSWRDHSVEPLRDPNPSDLLENLDDSVFSKRHAKLELDEKRRKRWDIQRIREQRILQRLQLRMYKKKGIQESEPEVTSFFPEPDDVESLMITPFLPVVAFGRPLPKLTPQNFELPWLDERSRCRLEIQKKQTPHRTCRK
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
4 (in isoform 2)Phosphorylation-16.5829743597
9AcetylationTMRSAVFKAAAAPAG
CHHHHHHHHHHCCCC		30.4325953088
9MethylationTMRSAVFKAAAAPAG
CHHHHHHHHHHCCCC		30.43115973307
25PhosphorylationNPEQRLDYERAAALG
CHHHHCCHHHHHHHC		16.3527251275
61PhosphorylationEPGPPLASSQGGSPA
CCCCCCCCCCCCCCC		30.7730266825
62PhosphorylationPGPPLASSQGGSPAP
CCCCCCCCCCCCCCC		27.5130266825
66PhosphorylationLASSQGGSPAPSPAG
CCCCCCCCCCCCCCC		25.3923401153
70PhosphorylationQGGSPAPSPAGCGGK
CCCCCCCCCCCCCCC		29.5030266825
77AcetylationSPAGCGGKGRGLLLP
CCCCCCCCCCCEEEC		30.6226051181
79MethylationAGCGGKGRGLLLPAG
CCCCCCCCCEEECCC		35.7582955111
90AcetylationLPAGAAPGQQEESWG
ECCCCCCCCCCCCCC		36.7619608861
99PhosphorylationQEESWGGSVPLPCPP
CCCCCCCCCCCCCCC		19.3426074081
109PhosphorylationLPCPPPATKQAGIGG
CCCCCCCCCCCCCCC		29.4826074081
123PhosphorylationGEPAAAGAGCSPRPK
CCCCCCCCCCCCCCC		15.8727251275
126PhosphorylationAAAGAGCSPRPKYQA
CCCCCCCCCCCCEEE		24.0329255136
130AcetylationAGCSPRPKYQAVLPI
CCCCCCCCEEEEEEE		51.8025953088
131PhosphorylationGCSPRPKYQAVLPIQ
CCCCCCCEEEEEEEC		12.3726074081
133PhosphorylationSPRPKYQAVLPIQTG
CCCCCEEEEEEECCC		11.1727251275
139PhosphorylationQAVLPIQTGSLVAAA
EEEEEECCCCEEEEC		29.4728464451
150PhosphorylationVAAAKEPTPWAGDKG
EEECCCCCCCCCCCC		32.3326714015
161PhosphorylationGDKGGAASPAATASD
CCCCCCCCCCCCCCC		17.9729255136
165PhosphorylationGAASPAATASDPAGP
CCCCCCCCCCCCCCC		28.8828464451
167PhosphorylationASPAATASDPAGPPP
CCCCCCCCCCCCCCC		39.5128464451
179PhosphorylationPPPLPLPGPPPLAPT
CCCCCCCCCCCCCCC		55.8427251275
186PhosphorylationGPPPLAPTATAGTLA
CCCCCCCCCCHHHHH		30.9126074081
188PhosphorylationPPLAPTATAGTLAAS
CCCCCCCCHHHHHHC		28.2626074081
191PhosphorylationAPTATAGTLAASEGR
CCCCCHHHHHHCCCC		15.6826074081
195PhosphorylationTAGTLAASEGRWKSM
CHHHHHHCCCCCCCC		34.6726074081
201PhosphorylationASEGRWKSMRKSPLG
HCCCCCCCCCCCCCC		19.5026074081
204UbiquitinationGRWKSMRKSPLGGGG
CCCCCCCCCCCCCCC		48.02-
205PhosphorylationRWKSMRKSPLGGGGG
CCCCCCCCCCCCCCC		18.2623927012
205O-linked_GlycosylationRWKSMRKSPLGGGGG
CCCCCCCCCCCCCCC		18.2630379171
213PhosphorylationPLGGGGGSGASSQAA
CCCCCCCCCHHHHHH		34.1730266825
216PhosphorylationGGGGSGASSQAACLK
CCCCCCHHHHHHHHH		26.8930266825
217PhosphorylationGGGSGASSQAACLKQ
CCCCCHHHHHHHHHH		24.2530266825
245UbiquitinationQQLQAKEKEIEELKS
HHHHHHHHHHHHHHH		64.38-
251UbiquitinationEKEIEELKSERDTLL
HHHHHHHHHHHHHHH		54.25-
252O-linked_GlycosylationKEIEELKSERDTLLA
HHHHHHHHHHHHHHH		50.9530379171
272AcetylationERRMQLVKKDNEKER
HHHHHHHHCCCHHHH		64.107682095
273MethylationRRMQLVKKDNEKERH
HHHHHHHCCCHHHHH		59.3019822423
273AcetylationRRMQLVKKDNEKERH
HHHHHHHCCCHHHHH		59.3019822423
286PhosphorylationRHKLFQGYETEEREE
HHHHHCCCCCCHHHH		14.6428450419
288PhosphorylationKLFQGYETEEREETE
HHHCCCCCCHHHHHH		34.3623898821
294PhosphorylationETEEREETELSEKIK
CCCHHHHHHHHHHHC		37.1628450419
297PhosphorylationEREETELSEKIKLEC
HHHHHHHHHHHCEEE		30.5228450419
301SumoylationTELSEKIKLECQPEL
HHHHHHHCEEECCCC		49.6728112733
318AcetylationTSQTLPPKPFSCGRS
CCCCCCCCCCCCCCC		57.6726051181
321PhosphorylationTLPPKPFSCGRSGKG
CCCCCCCCCCCCCCC		24.9628555341
333PhosphorylationGKGHKRKSPFGSTER
CCCCCCCCCCCCCCC		29.5125159151
337PhosphorylationKRKSPFGSTERKTPV
CCCCCCCCCCCCCCH		27.7223401153
338PhosphorylationRKSPFGSTERKTPVK
CCCCCCCCCCCCCHH		39.9421406692
342PhosphorylationFGSTERKTPVKKLAP
CCCCCCCCCHHHHCC		39.2629214152
352PhosphorylationKKLAPEFSKVKTKTP
HHHCCCHHCCCCCCC		34.5726074081
353AcetylationKLAPEFSKVKTKTPK
HHCCCHHCCCCCCCC		53.7419608861
356PhosphorylationPEFSKVKTKTPKHSP
CCHHCCCCCCCCCCC		43.0426074081
358PhosphorylationFSKVKTKTPKHSPIK
HHCCCCCCCCCCCCC		42.6829496963
362PhosphorylationKTKTPKHSPIKEEPC
CCCCCCCCCCCCCCC		34.1523401153
365SumoylationTPKHSPIKEEPCGSL
CCCCCCCCCCCCCCC		60.4528112733
365AcetylationTPKHSPIKEEPCGSL
CCCCCCCCCCCCCCC		60.4526051181
371PhosphorylationIKEEPCGSLSETVCK
CCCCCCCCCCHHHHH		35.1228387310
373PhosphorylationEEPCGSLSETVCKRE
CCCCCCCCHHHHHHH		32.6828387310
375PhosphorylationPCGSLSETVCKRELR
CCCCCCHHHHHHHHH		28.0323927012
378SumoylationSLSETVCKRELRSQE
CCCHHHHHHHHHCCC		44.5728112733
383PhosphorylationVCKRELRSQETPEKP
HHHHHHHCCCCCCCC		45.0229396449
386PhosphorylationRELRSQETPEKPRSS
HHHHCCCCCCCCCCC		29.1628176443
389AcetylationRSQETPEKPRSSVDT
HCCCCCCCCCCCCCC		47.1125953088
392PhosphorylationETPEKPRSSVDTPPR
CCCCCCCCCCCCCCC		43.1525159151
393PhosphorylationTPEKPRSSVDTPPRL
CCCCCCCCCCCCCCC		25.8725159151
396PhosphorylationKPRSSVDTPPRLSTP
CCCCCCCCCCCCCCC		32.7923401153
401PhosphorylationVDTPPRLSTPQKGPS
CCCCCCCCCCCCCCC		39.0423401153
402PhosphorylationDTPPRLSTPQKGPST
CCCCCCCCCCCCCCC		34.0425159151
405AcetylationPRLSTPQKGPSTHPK
CCCCCCCCCCCCCCC		74.1925953088
408PhosphorylationSTPQKGPSTHPKEKA
CCCCCCCCCCCCHHH		48.2826074081
409PhosphorylationTPQKGPSTHPKEKAF
CCCCCCCCCCCHHHC		45.3830576142
417PhosphorylationHPKEKAFSSEIEDLP
CCCHHHCCCCCCCCC		31.7426074081
418PhosphorylationPKEKAFSSEIEDLPY
CCHHHCCCCCCCCCC		35.8226074081
442PhosphorylationRWHQPPPSPLPLRES
CCCCCCCCCCCCCCC		44.8630266825
449PhosphorylationSPLPLRESSPKKEET
CCCCCCCCCCCHHHH		45.5723401153
450PhosphorylationPLPLRESSPKKEETV
CCCCCCCCCCHHHHH		35.6723401153
456PhosphorylationSSPKKEETVARCLMP
CCCCHHHHHHHHHCC		22.1323403867
471PhosphorylationSSVAGETSVLAVPSW
HHHCCCCEEEECCCC		15.7230387612
477PhosphorylationTSVLAVPSWRDHSVE
CEEEECCCCCCCCCC		28.3026091039
509AcetylationVFSKRHAKLELDEKR
HHHHHHHCCCCHHHH		36.0523749302
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 MSL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSL1_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 MSL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSL2_HUMANMSL2physical
16227571
MSL2_HUMANMSL2physical
23084835
H2B2E_HUMANHIST2H2BEphysical
24837678
UB2D3_HUMANUBE2D3physical
24837678
BRE1A_HUMANRNF20physical
24837678
BRE1B_HUMANRNF40physical
24837678
PAF1_HUMANPAF1physical
24837678
CDK9_HUMANCDK9physical
24837678
NUPR1_HUMANNUPR1physical
19650074
TP53B_HUMANTP53BP1physical
19650074
MO4L1_HUMANMORF4L1physical
19650074
RAN_HUMANRANphysical
19650074
IMB1_HUMANKPNB1physical
19650074
SNW1_HUMANSNW1physical
19650074
MRGBP_HUMANMRGBPphysical
19650074
PPM1G_HUMANPPM1Gphysical
19650074
HORM1_HUMANHORMAD1physical
19650074
SMRC1_HUMANSMARCC1physical
19650074
MS3L1_HUMANMSL3physical
26186194
TOPK_HUMANPBKphysical
26186194
KAT8_HUMANKAT8physical
26186194
SAHH3_HUMANAHCYL2physical
26186194
KAT8_HUMANKAT8physical
28514442
MS3L1_HUMANMSL3physical
28514442
TOPK_HUMANPBKphysical
28514442
SAHH3_HUMANAHCYL2physical
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 MSL1_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-353, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-205, AND MASSSPECTROMETRY.

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