MAN1_HUMAN - dbPTM
MAN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAN1_HUMAN
UniProt AC Q9Y2U8
Protein Name Inner nuclear membrane protein Man1
Gene Name LEMD3
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Nucleus inner membrane
Multi-pass membrane protein .
Protein Description 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..
Protein Sequence MAAAAASAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQHRSGGRGNKTRNSNNNNTAAATVAAAGPAAAAAAGMGVRPVSGDLSYLRTPGGLCRISASGPESLLGGPGGASAAPAAGSKVLLGFSSDESDVEASPRDQAGGGGRKDRASLQYRGLKAPPAPLAASEVTNSNSAERRKPHSWWGARRPAGPELQTPPGKDGAVEDEEGEGEDGEERDPETEEPLWASRTVNGSRLVPYSCRENYSDSEEEDDDDVASSRQVLKDDSLSRHRPRRTHSKPLPPLTAKSAGGRLETSVQGGGGLAMNDRAAAAGSLDRSRNLEEAAAAEQGGGCDQVDSSPVPRYRVNAKKLTPLLPPPLTDMDSTLDSSTGSLLKTNNHIGGGAFSVDSPRIYSNSLPPSAAVAASSSLRINHANHTGSNHTYLKNTYNKPKLSEPEEELLQQFKREEVSPTGSFSAHYLSMFLLTAACLFFLILGLTYLGMRGTGVSEDGELSIENPFGETFGKIQESEKTLMMNTLYKLHDRLAQLAGDHECGSSSQRTLSVQEAAAYLKDLGPEYEGIFNTSLQWILENGKDVGIRCVGFGPEEELTNITDVQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCLGVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQENKDLQPYMPIPHVRDSLIQPHDRKKMKKVWDRAVDFLAANESRVRTETRRIGGADFLVWRWIQPSASCDKILVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQALTSNTPLKPSNKHMNSMSHLRLRTGLTNSQGSS
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
2Acetylation------MAAAAASAP
------CCHHHCCCC
13.0522814378
7Phosphorylation-MAAAAASAPQQLSD
-CCHHHCCCCCCCCH
35.4422199227
13PhosphorylationASAPQQLSDEELFSQ
CCCCCCCCHHHHHHH
38.3422199227
19PhosphorylationLSDEELFSQLRRYGL
CCHHHHHHHHHHHCC
40.7128464451
24PhosphorylationLFSQLRRYGLSPGPV
HHHHHHHHCCCCCCC
18.9121712546
27PhosphorylationQLRRYGLSPGPVTES
HHHHHCCCCCCCCCC
24.3725159151
32PhosphorylationGLSPGPVTESTRPVY
CCCCCCCCCCCCHHH
27.6125159151
34PhosphorylationSPGPVTESTRPVYLK
CCCCCCCCCCHHHHH
21.9822199227
35PhosphorylationPGPVTESTRPVYLKK
CCCCCCCCCHHHHHH
32.5322199227
39PhosphorylationTESTRPVYLKKLKKL
CCCCCHHHHHHHHHH
18.5829396449
41MalonylationSTRPVYLKKLKKLRE
CCCHHHHHHHHHHHH
38.0726320211
41UbiquitinationSTRPVYLKKLKKLRE
CCCHHHHHHHHHHHH
38.07-
56O-linked_GlycosylationEEQQQHRSGGRGNKT
HHHHHHHCCCCCCCC
43.4030379171
95PhosphorylationGMGVRPVSGDLSYLR
CCCCEECCCCCCCCC
29.3121712546
99PhosphorylationRPVSGDLSYLRTPGG
EECCCCCCCCCCCCC
27.1924719451
103PhosphorylationGDLSYLRTPGGLCRI
CCCCCCCCCCCEEEE
24.5621815630
111PhosphorylationPGGLCRISASGPESL
CCCEEEEECCCCHHH
9.3125850435
113PhosphorylationGLCRISASGPESLLG
CEEEEECCCCHHHCC
48.3525850435
117PhosphorylationISASGPESLLGGPGG
EECCCCHHHCCCCCC
31.8425850435
126PhosphorylationLGGPGGASAAPAAGS
CCCCCCHHCCCCCCC
28.3928857561
133PhosphorylationSAAPAAGSKVLLGFS
HCCCCCCCEEEEECC
18.1828857561
140PhosphorylationSKVLLGFSSDESDVE
CEEEEECCCCHHHCC
34.7729255136
141PhosphorylationKVLLGFSSDESDVEA
EEEEECCCCHHHCCC
43.0429255136
144PhosphorylationLGFSSDESDVEASPR
EECCCCHHHCCCCCC
52.5319664994
149PhosphorylationDESDVEASPRDQAGG
CHHHCCCCCCCCCCC
13.6330266825
164PhosphorylationGGRKDRASLQYRGLK
CCCCCCHHHEECCCC
19.5223401153
167PhosphorylationKDRASLQYRGLKAPP
CCCHHHEECCCCCCC
16.37-
180PhosphorylationPPAPLAASEVTNSNS
CCCCCCCHHCCCCCC
27.3029978859
183PhosphorylationPLAASEVTNSNSAER
CCCCHHCCCCCCCHH
28.9530266825
185PhosphorylationAASEVTNSNSAERRK
CCHHCCCCCCCHHCC
23.8530266825
187PhosphorylationSEVTNSNSAERRKPH
HHCCCCCCCHHCCCC
31.1829255136
209PhosphorylationPAGPELQTPPGKDGA
CCCCCCCCCCCCCCC
44.0425159151
213UbiquitinationELQTPPGKDGAVEDE
CCCCCCCCCCCCCCC
59.78-
243PhosphorylationEPLWASRTVNGSRLV
CCCEEECCCCCCCCE
18.8128555341
247PhosphorylationASRTVNGSRLVPYSC
EECCCCCCCCEEEEC
19.7623898821
252PhosphorylationNGSRLVPYSCRENYS
CCCCCEEEECCCCCC
16.9622115753
253PhosphorylationGSRLVPYSCRENYSD
CCCCEEEECCCCCCC
10.7128450419
258PhosphorylationPYSCRENYSDSEEED
EEECCCCCCCCCCCC
14.7622167270
259PhosphorylationYSCRENYSDSEEEDD
EECCCCCCCCCCCCC
46.3622167270
261PhosphorylationCRENYSDSEEEDDDD
CCCCCCCCCCCCCCC
40.7522167270
271PhosphorylationEDDDDVASSRQVLKD
CCCCCHHHHHHHHHC
26.3823927012
272PhosphorylationDDDDVASSRQVLKDD
CCCCHHHHHHHHHCC
19.5923927012
277UbiquitinationASSRQVLKDDSLSRH
HHHHHHHHCCCHHCC
61.71-
280PhosphorylationRQVLKDDSLSRHRPR
HHHHHCCCHHCCCCC
38.0823401153
282PhosphorylationVLKDDSLSRHRPRRT
HHHCCCHHCCCCCCC
29.9630266825
289PhosphorylationSRHRPRRTHSKPLPP
HCCCCCCCCCCCCCC
31.6127732954
291PhosphorylationHRPRRTHSKPLPPLT
CCCCCCCCCCCCCCC
35.0427732954
298PhosphorylationSKPLPPLTAKSAGGR
CCCCCCCCCCCCCCC
37.5023186163
300UbiquitinationPLPPLTAKSAGGRLE
CCCCCCCCCCCCCEE
35.29-
301PhosphorylationLPPLTAKSAGGRLET
CCCCCCCCCCCCEEE
29.6728555341
308PhosphorylationSAGGRLETSVQGGGG
CCCCCEEEEEECCCC
38.5023186163
309PhosphorylationAGGRLETSVQGGGGL
CCCCEEEEEECCCCC
11.7621815630
327PhosphorylationDRAAAAGSLDRSRNL
HHHHHHCCCCCCCCH
23.5225159151
331PhosphorylationAAGSLDRSRNLEEAA
HHCCCCCCCCHHHHH
25.7825159151
351PhosphorylationGGCDQVDSSPVPRYR
CCCCCCCCCCCCCCE
37.3730278072
352PhosphorylationGCDQVDSSPVPRYRV
CCCCCCCCCCCCCEE
26.0030278072
365PhosphorylationRVNAKKLTPLLPPPL
EECCCCCCCCCCCCC
22.2929255136
373PhosphorylationPLLPPPLTDMDSTLD
CCCCCCCCCCCCCCC
34.7420068231
377PhosphorylationPPLTDMDSTLDSSTG
CCCCCCCCCCCCCCC
25.0021712546
378PhosphorylationPLTDMDSTLDSSTGS
CCCCCCCCCCCCCCC
30.2520068231
381PhosphorylationDMDSTLDSSTGSLLK
CCCCCCCCCCCCEEE
32.6720068231
382PhosphorylationMDSTLDSSTGSLLKT
CCCCCCCCCCCEEEC
36.1325159151
383PhosphorylationDSTLDSSTGSLLKTN
CCCCCCCCCCEEECC
34.4420068231
385PhosphorylationTLDSSTGSLLKTNNH
CCCCCCCCEEECCCC
30.5320068231
389PhosphorylationSTGSLLKTNNHIGGG
CCCCEEECCCCCCCC
41.0220068231
399PhosphorylationHIGGGAFSVDSPRIY
CCCCCCEECCCCCEE
25.2025159151
402PhosphorylationGGAFSVDSPRIYSNS
CCCEECCCCCEECCC
17.5825159151
406PhosphorylationSVDSPRIYSNSLPPS
ECCCCCEECCCCCHH
11.7722210691
407PhosphorylationVDSPRIYSNSLPPSA
CCCCCEECCCCCHHH
19.9925159151
409PhosphorylationSPRIYSNSLPPSAAV
CCCEECCCCCHHHHH
35.9925627689
413PhosphorylationYSNSLPPSAAVAASS
ECCCCCHHHHHHHCC
27.2425627689
419PhosphorylationPSAAVAASSSLRINH
HHHHHHHCCCCEEEC
15.6628555341
420PhosphorylationSAAVAASSSLRINHA
HHHHHHCCCCEEECC
28.7625159151
421PhosphorylationAAVAASSSLRINHAN
HHHHHCCCCEEECCC
21.1225627689
430PhosphorylationRINHANHTGSNHTYL
EEECCCCCCCCCCEE
41.9529214152
432PhosphorylationNHANHTGSNHTYLKN
ECCCCCCCCCCEEEC
26.9622210691
436PhosphorylationHTGSNHTYLKNTYNK
CCCCCCCEEECCCCC
14.2328555341
438UbiquitinationGSNHTYLKNTYNKPK
CCCCCEEECCCCCCC
36.51-
441PhosphorylationHTYLKNTYNKPKLSE
CCEEECCCCCCCCCC
30.4921712546
443AcetylationYLKNTYNKPKLSEPE
EEECCCCCCCCCCCH
32.8730590259
445AcetylationKNTYNKPKLSEPEEE
ECCCCCCCCCCCHHH
67.2730590265
445UbiquitinationKNTYNKPKLSEPEEE
ECCCCCCCCCCCHHH
67.27-
447PhosphorylationTYNKPKLSEPEEELL
CCCCCCCCCCHHHHH
58.1825159151
458UbiquitinationEELLQQFKREEVSPT
HHHHHHHHHHCCCCC
55.3421906983
463PhosphorylationQFKREEVSPTGSFSA
HHHHHCCCCCCCHHH
21.7422817900
472PhosphorylationTGSFSAHYLSMFLLT
CCCHHHHHHHHHHHH
10.5330387612
491PhosphorylationFFLILGLTYLGMRGT
HHHHHHHHHHCCCCC
18.2030387612
524UbiquitinationGKIQESEKTLMMNTL
CHHHHHHHHHHHHHH
57.1221906983
533UbiquitinationLMMNTLYKLHDRLAQ
HHHHHHHHHHHHHHH
42.32-
537MethylationTLYKLHDRLAQLAGD
HHHHHHHHHHHHHCC
22.60115482519
630PhosphorylationRFRRAFVTVTHRLLL
HHHHHHHHHHHHHHH
17.15-
632PhosphorylationRRAFVTVTHRLLLLC
HHHHHHHHHHHHHHH
7.60-
651PhosphorylationMVCVVLRYMKYRWTK
HHHHHHHHHHHCCCC
8.19-
679PhosphorylationKIIDVLRSHNEACQE
HHHHHHHHCHHHHHH
26.89-
688AcetylationNEACQENKDLQPYMP
HHHHHHCCCCCCCCC
60.0926051181
688UbiquitinationNEACQENKDLQPYMP
HHHHHHCCCCCCCCC
60.09-
728PhosphorylationDFLAANESRVRTETR
HHHHHCHHHCHHCCC
35.5623312004
751PhosphorylationVWRWIQPSASCDKIL
EEEECCCCCCCCEEE
19.2121815630
753PhosphorylationRWIQPSASCDKILVI
EECCCCCCCCEEEEE
27.4721815630
756AcetylationQPSASCDKILVIPSK
CCCCCCCEEEEEECH
42.1226051181
756UbiquitinationQPSASCDKILVIPSK
CCCCCCCEEEEEECH
42.12-
762PhosphorylationDKILVIPSKVWQGQA
CEEEEEECHHHCCCC
28.8124719451
763UbiquitinationKILVIPSKVWQGQAF
EEEEEECHHHCCCCC
41.98-
776PhosphorylationAFHLDRRNSPPNSLT
CCCCCCCCCCCCCCC
60.8124719451
777PhosphorylationFHLDRRNSPPNSLTP
CCCCCCCCCCCCCCH
39.6630266825
781PhosphorylationRRNSPPNSLTPCLKI
CCCCCCCCCCHHHHH
39.1230266825
783PhosphorylationNSPPNSLTPCLKIRN
CCCCCCCCHHHHHHH
16.2730266825
787AcetylationNSLTPCLKIRNMFDP
CCCCHHHHHHHHCCC
46.4626051181
787MalonylationNSLTPCLKIRNMFDP
CCCCHHHHHHHHCCC
46.4626320211
787UbiquitinationNSLTPCLKIRNMFDP
CCCCHHHHHHHHCCC
46.46-
827UbiquitinationIVHIAVDKNSREGCV
EEEEEECCCCCCCEE
50.6621906983
837AcetylationREGCVYVKCLSPEYA
CCCEEEEEECCHHHC
16.2726051181
837UbiquitinationREGCVYVKCLSPEYA
CCCEEEEEECCHHHC
16.27-
840PhosphorylationCVYVKCLSPEYAGKA
EEEEEECCHHHCHHH
25.7522199227
843PhosphorylationVKCLSPEYAGKAFKA
EEECCHHHCHHHHHH
24.8429759185
849MalonylationEYAGKAFKALHGSWF
HHCHHHHHHHHCCEE
55.7026320211
849UbiquitinationEYAGKAFKALHGSWF
HHCHHHHHHHHCCEE
55.70-
864AcetylationDGKLVTVKYLRLDRY
CCEEEEEEEEEECCC
29.2426051181
864MalonylationDGKLVTVKYLRLDRY
CCEEEEEEEEEECCC
29.2426320211
880PhosphorylationHRFPQALTSNTPLKP
HHCCHHHHCCCCCCC
23.9730266825
881PhosphorylationRFPQALTSNTPLKPS
HCCHHHHCCCCCCCC
39.2930266825
882PhosphorylationFPQALTSNTPLKPSN
CCHHHHCCCCCCCCC
40.2424719451
883PhosphorylationPQALTSNTPLKPSNK
CHHHHCCCCCCCCCC
29.7530266825
888PhosphorylationSNTPLKPSNKHMNSM
CCCCCCCCCCCCCCC
57.8530266825
894PhosphorylationPSNKHMNSMSHLRLR
CCCCCCCCCCCHHHH
17.68-
895PhosphorylationSNKHMNSMSHLRLRT
CCCCCCCCCCHHHHH
2.1924719451
896PhosphorylationNKHMNSMSHLRLRTG
CCCCCCCCCHHHHHC
21.1321857030
902PhosphorylationMSHLRLRTGLTNSQG
CCCHHHHHCCCCCCC
40.9322199227
905PhosphorylationLRLRTGLTNSQGSS-
HHHHHCCCCCCCCC-
33.8822199227
907PhosphorylationLRTGLTNSQGSS---
HHHCCCCCCCCC---
30.5926055452
910PhosphorylationGLTNSQGSS------
CCCCCCCCC------
25.8222199227
911PhosphorylationLTNSQGSS-------
CCCCCCCC-------
51.5725159151

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 MAN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAN1_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 MAN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MAN1_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00452 Disorders caused by loss-of-function of LEMD3, including: Osteopoikilosis; Buschke-Ollendorff syndro
OMIM Disease
166700Buschke-Ollendorff syndrome (BOS)
155950Melorheostosis (MEL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAN1_HUMAN

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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.
"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.
"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.
"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.
"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.

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