dbPTM

MAN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MAN1_MOUSE
UniProt AC	Q9WU40
Protein Name	Inner nuclear membrane protein Man1
Gene Name	Lemd3
Organism	Mus musculus (Mouse).
Sequence Length	921
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 (By similarity)..
Protein Sequence	MAAATAAAAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQQQQQQQQQHRAGGRGNKTRNSNNNNTATAMGGRPGSGDLAYLRSPAGLGRLSASAAESPVAGGSGGAAAVPAAGSKVLLGFSSDESDVEASPREQAGGGGGGGARRDRAALQYRGLRAPPAPPAAGEVTGGHPGERRKPHSWWGARRPAGPEPQPPAAGSDGAAEDADEELADGEDRDPEAEEPLWASRAVNGSRLLPYSSCREHYSDSEEEEEEGEEDGDVAPARQVLKDDSLARHRPRRSHSKPFSALTAKSGGSRQETSVQGGGALAMNDRAAAAGSLDRSRNLEEAAAEPGGGGGGGCGCDPVDSIPRYRAGAKKLAPLLSPPSPDGDSTLESPTGPLLKTNNHIGGGAFGVDSPGLYANSLPPGATAAAAPGTLRINHANHTGSNHTYLKTAYGKPKLCEPEEELLQQFKREEVSPTGSFSAHYLSMFLLTAACLFFLILGLTYLGMRGTGVPEDGGLIKNPFDETFGKIQESEKNLLMSTLYKLHDRLAQIAGDHECGSSSQRMLSVQEAAAYLKNLGPEYEDVFNTSLLWIFKNGKDVGIRCVGYGPEEDLTNITDVQFLQSTRPQMPFWCRFRRAFITVTHRLLLLCLGVVLVCVALRYMRYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQETKDLQPYMPLPHVRDSLIQPQDRKKMKKVWDRAVDFLAANESRVRTETRRVGGADFLVWRWIQPSASCDKTLVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGDHWHLAIQEAILEKCSDNDGIVHIAVDRNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQALTCNTPLKPANKHMNSLSHLRLRTGLANSQGSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	AAAPQQLSDEELFSQ HCCCHHCCHHHHHHH	38.34	28066266
20	Phosphorylation	LSDEELFSQLRRYGL CCHHHHHHHHHHHCC	40.71	29472430
25	Phosphorylation	LFSQLRRYGLSPGPV HHHHHHHHCCCCCCC	18.91	23984901
28	Phosphorylation	QLRRYGLSPGPVTES HHHHHCCCCCCCCCC	24.37	23984901
80	Phosphorylation	RNSNNNNTATAMGGR CCCCCCCCCCCCCCC	27.75	29472430
82	Phosphorylation	SNNNNTATAMGGRPG CCCCCCCCCCCCCCC	18.35	29472430
90	Phosphorylation	AMGGRPGSGDLAYLR CCCCCCCCCCCEECC	31.64	29472430
95	Phosphorylation	PGSGDLAYLRSPAGL CCCCCCEECCCCCCC	15.22	29472430
98	Phosphorylation	GDLAYLRSPAGLGRL CCCEECCCCCCCCCC	19.26	28066266
106	Phosphorylation	PAGLGRLSASAAESP CCCCCCCCCHHHCCC	20.86	25619855
108	Phosphorylation	GLGRLSASAAESPVA CCCCCCCHHHCCCCC	25.33	25619855
112	Phosphorylation	LSASAAESPVAGGSG CCCHHHCCCCCCCCC	21.68	25619855
118	Phosphorylation	ESPVAGGSGGAAAVP CCCCCCCCCCCCCCC	32.89	25619855
129	Phosphorylation	AAVPAAGSKVLLGFS CCCCCCCCEEEEECC	18.18	25619855
136	Phosphorylation	SKVLLGFSSDESDVE CEEEEECCCCHHHCC	34.77	26824392
137	Phosphorylation	KVLLGFSSDESDVEA EEEEECCCCHHHCCC	43.04	24723360
140	Phosphorylation	LGFSSDESDVEASPR EECCCCHHHCCCCHH	52.53	27087446
145	Phosphorylation	DESDVEASPREQAGG CHHHCCCCHHHHCCC	15.81	25619855
214	Phosphorylation	PQPPAAGSDGAAEDA CCCCCCCCCCCCCCH	28.30	25338131
260	Phosphorylation	YSSCREHYSDSEEEE CHHHHHHCCCCHHHH	14.93	23684622
261	Phosphorylation	SSCREHYSDSEEEEE HHHHHHCCCCHHHHH	36.25	25521595
263	Phosphorylation	CREHYSDSEEEEEEG HHHHCCCCHHHHHCC	40.75	25521595
287	Phosphorylation	RQVLKDDSLARHRPR HHHHCCCHHHHCCCC	33.78	28066266
296	Phosphorylation	ARHRPRRSHSKPFSA HHCCCCCCCCCCCCE	33.13	28066266
298	Phosphorylation	HRPRRSHSKPFSALT CCCCCCCCCCCCEEE	43.18	25266776
316	Phosphorylation	GGSRQETSVQGGGAL CCCCCEEEECCCCCE	16.22	28059163
338	Phosphorylation	AAGSLDRSRNLEEAA HHCCCCCCCCHHHHH	25.78	26824392
363	Phosphorylation	CGCDPVDSIPRYRAG CCCCCCCCCCCCCCC	34.42	25619855
379	Phosphorylation	KKLAPLLSPPSPDGD HHHHCCCCCCCCCCC	42.31	23984901
382	Phosphorylation	APLLSPPSPDGDSTL HCCCCCCCCCCCCCC	38.72	23984901
387	Phosphorylation	PPSPDGDSTLESPTG CCCCCCCCCCCCCCC	40.18	23984901
388	Phosphorylation	PSPDGDSTLESPTGP CCCCCCCCCCCCCCC	39.01	23984901
391	Phosphorylation	DGDSTLESPTGPLLK CCCCCCCCCCCCCCC	30.76	29514104
412	Phosphorylation	GGAFGVDSPGLYANS CCCCCCCCCCCCCCC	20.61	-
540	Phosphorylation	EKNLLMSTLYKLHDR HHHHHHHHHHHHHHH	21.82	19655815
542	Phosphorylation	NLLMSTLYKLHDRLA HHHHHHHHHHHHHHH	16.16	19655815
761	Phosphorylation	VWRWIQPSASCDKTL EEEECCCCCCCCCEE	19.21	28066266
763	Phosphorylation	RWIQPSASCDKTLVI EECCCCCCCCCEEEE	27.47	28066266
787	Phosphorylation	FHLDRRNSPPNSLTP CCCCCCCCCCCCCCH	39.66	-
893	Phosphorylation	PQALTCNTPLKPANK CCCEECCCCCCCCHH	31.95	-
917	Phosphorylation	LRTGLANSQGSS--- HHHHHCCCCCCC---	30.25	29514104
920	Phosphorylation	GLANSQGSS------ HHCCCCCCC------	25.82	23984901
921	Phosphorylation	LANSQGSS------- HCCCCCCC-------	51.57	23984901

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MAN1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MAN1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MAN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	16452087 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASSSPECTROMETRY.	17242355 [Abstract]