Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Inner nuclear membrane protein Man1  

UniProtKB / Swiss-Prot ID :  MAN1_HUMAN

Gene Name (Synonyms) : 
LEMD3, MAN1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus inner membrane; Multi-pass membrane protein. 

Protein Function :  Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. 

Transmembrane Topology (topPTM) : MAN1_HUMAN 

Protein Sequence MAAAAASAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQHRSGGRGNKTRNSNNNN...
Predicted Secondary Structure CCCCCCCCCHHCCHHHHHHHHHHCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
260D -> Y (in dbSNP:rs7487311). VAR_034605
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
27PhosphoserineRYGLSPGPV
HCCCCCCCC
24.37HPRD
Link-
27PhosphoserineRYGLSPGPV
HCCCCCCCC
24.37PhosphoELM
Link-
27PhosphoserineRYGLSPGPV
HCCCCCCCC
24.37Phosphositeplus
Link-
32PhosphothreoninePGPVTESTR
CCCCCCCCC
27.61HPRD
Link-
32PhosphothreoninePGPVTESTR
CCCCCCCCC
27.61PhosphoELM
Link-
32PhosphothreoninePGPVTESTR
CCCCCCCCC
27.61Phosphositeplus
Link-
140PhosphoserineLLGFSSDES
EEEECCCCC
34.77HPRD
Link-
140PhosphoserineLLGFSSDES
EEEECCCCC
34.77PhosphoELM
Link-
140PhosphoserineLLGFSSDES
EEEECCCCC
34.77Phosphositeplus
Link-
140Phosphoserine.LLGFSSDES
EEEECCCCC
34.77UniProtKB
Link-
141PhosphoserineLGFSSDESD
EEECCCCCC
43.04HPRD
Link-
141PhosphoserineLGFSSDESD
EEECCCCCC
43.04PhosphoELM
Link-
141PhosphoserineLGFSSDESD
EEECCCCCC
43.04Phosphositeplus
Link-
141PhosphoserineLGFSSDESD
EEECCCCCC
43.04SysPTM
Link-
141Phosphoserine.LGFSSDESD
EEECCCCCC
43.04UniProtKB
Link-
144PhosphoserineSSDESDVEA
CCCCCCCCC
52.53HPRD
Link-
144PhosphoserineSSDESDVEA
CCCCCCCCC
52.53PhosphoELM
Link-
144PhosphoserineSSDESDVEA
CCCCCCCCC
52.53Phosphositeplus
Link-
144PhosphoserineSSDESDVEA
CCCCCCCCC
52.53SysPTM
Link-
144Phosphoserine.SSDESDVEA
CCCCCCCCC
52.53UniProtKB
Link-
149PhosphoserineDVEASPRDQ
CCCCCCCHH
13.63PhosphoELM
Link-
164PhosphoserineKDRASLQYR
CCCCEEEEC
19.52Phosphositeplus
Link-
185PhosphoserineEVTNSNSAE
CCCCCCCCC
23.85HPRD
Link-
185PhosphoserineEVTNSNSAE
CCCCCCCCC
23.85PhosphoELM
Link-
185PhosphoserineEVTNSNSAE
CCCCCCCCC
23.85Phosphositeplus
Link-
185PhosphoserineEVTNSNSAE
CCCCCCCCC
23.85SysPTM
Link-
185Phosphoserine.EVTNSNSAE
CCCCCCCCC
23.85UniProtKB
Link-
187PhosphoserineTNSNSAERR
CCCCCCCCC
31.18HPRD
Link-
187PhosphoserineTNSNSAERR
CCCCCCCCC
31.18PhosphoELM
Link-
187PhosphoserineTNSNSAERR
CCCCCCCCC
31.18Phosphositeplus
Link-
187PhosphoserineTNSNSAERR
CCCCCCCCC
31.18SysPTM
Link-
187Phosphoserine.TNSNSAERR
CCCCCCCCC
31.18UniProtKB
Link-
209PhosphothreoninePELQTPPGK
CCCCCCCCC
44.04HPRD
Link-
209PhosphothreoninePELQTPPGK
CCCCCCCCC
44.04Phosphositeplus
Link-
252PhosphotyrosineRLVPYSCRE
EECCCHHHC
16.96Phosphositeplus
Link-
258PhosphotyrosineCRENYSDSE
HHCCCCCCC
14.76HPRD
Link-
258PhosphotyrosineCRENYSDSE
HHCCCCCCC
14.76PhosphoELM
Link-
258PhosphotyrosineCRENYSDSE
HHCCCCCCC
14.76Phosphositeplus
Link-
259PhosphoserineRENYSDSEE
HCCCCCCCC
46.36HPRD
Link-
259PhosphoserineRENYSDSEE
HCCCCCCCC
46.36PhosphoELM
Link-
259PhosphoserineRENYSDSEE
HCCCCCCCC
46.36Phosphositeplus
Link-
259PhosphoserineRENYSDSEE
HCCCCCCCC
46.36SysPTM
Link-
259Phosphoserine.RENYSDSEE
HCCCCCCCC
46.36UniProtKB
Link-
261PhosphoserineNYSDSEEED
CCCCCCCCC
40.75HPRD
Link-
261PhosphoserineNYSDSEEED
CCCCCCCCC
40.75PhosphoELM
Link-
261PhosphoserineNYSDSEEED
CCCCCCCCC
40.75Phosphositeplus
Link-
261PhosphoserineNYSDSEEED
CCCCCCCCC
40.75SysPTM
Link-
261Phosphoserine.NYSDSEEED
CCCCCCCCC
40.75UniProtKB
Link-
280PhosphoserineLKDDSLSRH
HHCCCHHHC
38.08HPRD
Link-
280PhosphoserineLKDDSLSRH
HHCCCHHHC
38.08PhosphoELM
Link-
280PhosphoserineLKDDSLSRH
HHCCCHHHC
38.08Phosphositeplus
Link-
280PhosphoserineLKDDSLSRH
HHCCCHHHC
38.08SysPTM
Link-
280Phosphoserine.LKDDSLSRH
HHCCCHHHC
38.08UniProtKB
Link-
331PhosphoserineSLDRSRNLE
CCHHHCCHH
25.78HPRD
Link-
331PhosphoserineSLDRSRNLE
CCHHHCCHH
25.78Phosphositeplus
Link-
331Phosphoserine.SLDRSRNLE
CCHHHCCHH
25.78UniProtKB
Link-
351PhosphoserineDQVDSSPVP
CCCCCCCCC
37.37HPRD
Link-
351PhosphoserineDQVDSSPVP
CCCCCCCCC
37.37PhosphoELM
Link-
352PhosphoserineQVDSSPVPR
CCCCCCCCC
26.00HPRD
Link-
352PhosphoserineQVDSSPVPR
CCCCCCCCC
26.00PhosphoELM
Link-
352PhosphoserineQVDSSPVPR
CCCCCCCCC
26.00Phosphositeplus
Link-
352PhosphoserineQVDSSPVPR
CCCCCCCCC
26.00SysPTM
Link-
352Phosphoserine.QVDSSPVPR
CCCCCCCCC
26.00UniProtKB
Link-
365PhosphothreonineAKKLTPLLP
HHHCCCCCC
22.29HPRD
Link-
365PhosphothreonineAKKLTPLLP
HHHCCCCCC
22.29PhosphoELM
Link-
365PhosphothreonineAKKLTPLLP
HHHCCCCCC
22.29Phosphositeplus
Link-
365PhosphothreonineAKKLTPLLP
HHHCCCCCC
22.29SysPTM
Link-
365Phosphothreonine.AKKLTPLLP
HHHCCCCCC
22.29UniProtKB
Link-
377PhosphoserineTDMDSTLDS
CCCCCCCCC
25.00HPRD
Link-
377PhosphoserineTDMDSTLDS
CCCCCCCCC
25.00PhosphoELM
Link-
377PhosphoserineTDMDSTLDS
CCCCCCCCC
25.00SysPTM
Link-
377Phosphoserine.TDMDSTLDS
CCCCCCCCC
25.00UniProtKB
Link-
381PhosphoserineSTLDSSTGS
CCCCCCCCC
32.67HPRD
Link-
382PhosphoserineTLDSSTGSL
CCCCCCCCC
36.13HPRD
Link-
382PhosphoserineTLDSSTGSL
CCCCCCCCC
36.13PhosphoELM
Link-
402PhosphoserineFSVDSPRIY
CCCCCCCCC
17.58HPRD
Link-
402PhosphoserineFSVDSPRIY
CCCCCCCCC
17.58PhosphoELM
Link-
402PhosphoserineFSVDSPRIY
CCCCCCCCC
17.58Phosphositeplus
Link-
402PhosphoserineFSVDSPRIY
CCCCCCCCC
17.58SysPTM
Link-
402Phosphoserine.FSVDSPRIY
CCCCCCCCC
17.58UniProtKB
Link-
458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LQQFKREEV
HHHHHHHHC
55.34Phosphositeplus
Link-
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QESEKTLMM
HHHHHHHHH
57.12Phosphositeplus
Link-
777PhosphoserineDRRNSPPNS
HHCCCCCCH
39.66HPRD
Link-
777PhosphoserineDRRNSPPNS
HHCCCCCCH
39.66PhosphoELM
Link-
777PhosphoserineDRRNSPPNS
HHCCCCCCH
39.66Phosphositeplus
Link-
777PhosphoserineDRRNSPPNS
HHCCCCCCH
39.66SysPTM
Link-
777Phosphoserine.DRRNSPPNS
HHCCCCCCH
39.66UniProtKB
Link-
827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IAVDKNSRE
EECCCCCCC
50.66Phosphositeplus
Link-
883PhosphothreonineLTSNTPLKP
CCCCCCCCC
29.75HPRD
Link-
883PhosphothreonineLTSNTPLKP
CCCCCCCCC
29.75PhosphoELM
Link-
883PhosphothreonineLTSNTPLKP
CCCCCCCCC
29.75Phosphositeplus
Link-
907PhosphoserineGLTNSQGSS
CCCCCCCCC
30.59HPRD
Link-
907PhosphoserineGLTNSQGSS
CCCCCCCCC
30.59PhosphoELM
Link-
910PhosphoserineNSQGSS
CCCCCC
25.82HPRD
Link-
910PhosphoserineNSQGSS
CCCCCC
25.82PhosphoELM
Link-
911PhosphoserineSQGSS
CCCCC
51.57HPRD
Link
911PhosphoserineSQGSS
CCCCC
51.57PhosphoELM
Link
911PhosphoserineSQGSS
CCCCC
51.57Phosphositeplus
Link
911PhosphoserineSQGSS
CCCCC
51.57SysPTM
Link
911Phosphoserine.SQGSS
CCCCC
51.57UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD9_HUMANphysical interactionMINT-62084MINT15231748
SMAD1_HUMANphysical interactionMINT-61999MINT15231748
SMAD2_HUMANyeast 2-hybridHPRD:09704HPRD15489854
SMAD1_HUMANyeast 2-hybridHPRD:09704HPRD15489854
15231748
SMAD9_HUMANyeast 2-hybridHPRD:09704HPRD15231748
SMAD3_HUMANENSP00000308369STRING
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Disease Reference
Kegg disease
H00452 Disorders caused by loss-of-function of LEMD3, including: Osteopoikilosis; Buschke-Ollendorff syndro
OMIM disease
166700Buschke-Ollendorff syndrome (BOS)
155950Melorheostosis (MEL)
Drug Reference
There are no disease associations of PTM sites.
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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-140; SER-141; SER-144AND SER-261, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-402, ANDMASS SPECTROMETRY.
"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-185; SER-187; SER-259;SER-261; SER-280; SER-352; THR-365; SER-377; SER-402; SER-777 ANDSER-911, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures