CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023705
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inner nuclear membrane protein Man1 
Protein Synonyms/Alias
 LEM domain-containing protein 3 
Gene Name
 LEMD3 
Gene Synonyms/Alias
 MAN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
458EELLQQFKREEVSPTubiquitination[1, 2]
524GKIQESEKTLMMNTLubiquitination[1, 2, 3]
533LMMNTLYKLHDRLAQubiquitination[2]
756QPSASCDKILVIPSKubiquitination[2]
763KILVIPSKVWQGQAFubiquitination[2]
787NSLTPCLKIRNMFDPubiquitination[2, 4]
827IVHIAVDKNSREGCVubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional 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. 
Sequence Annotation
 DOMAIN 6 50 LEM.
 DNA_BIND 707 726
 REGION 699 911 Interaction with SMAD1, SMAD2, SMAD3 and
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 144 144 Phosphoserine.
 MOD_RES 185 185 Phosphoserine.
 MOD_RES 187 187 Phosphoserine.
 MOD_RES 258 258 Phosphotyrosine (By similarity).
 MOD_RES 259 259 Phosphoserine.
 MOD_RES 261 261 Phosphoserine.
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.
 MOD_RES 365 365 Phosphothreonine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 777 777 Phosphoserine.
 MOD_RES 883 883 Phosphothreonine.
 MOD_RES 911 911 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; DNA-binding; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 911 AA 
Protein Sequence
MAAAAASAPQ QLSDEELFSQ LRRYGLSPGP VTESTRPVYL KKLKKLREEE QQQHRSGGRG 60
NKTRNSNNNN TAAATVAAAG PAAAAAAGMG VRPVSGDLSY LRTPGGLCRI SASGPESLLG 120
GPGGASAAPA AGSKVLLGFS SDESDVEASP RDQAGGGGRK DRASLQYRGL KAPPAPLAAS 180
EVTNSNSAER RKPHSWWGAR RPAGPELQTP PGKDGAVEDE EGEGEDGEER DPETEEPLWA 240
SRTVNGSRLV PYSCRENYSD SEEEDDDDVA SSRQVLKDDS LSRHRPRRTH SKPLPPLTAK 300
SAGGRLETSV QGGGGLAMND RAAAAGSLDR SRNLEEAAAA EQGGGCDQVD SSPVPRYRVN 360
AKKLTPLLPP PLTDMDSTLD SSTGSLLKTN NHIGGGAFSV DSPRIYSNSL PPSAAVAASS 420
SLRINHANHT GSNHTYLKNT YNKPKLSEPE EELLQQFKRE EVSPTGSFSA HYLSMFLLTA 480
ACLFFLILGL TYLGMRGTGV SEDGELSIEN PFGETFGKIQ ESEKTLMMNT LYKLHDRLAQ 540
LAGDHECGSS SQRTLSVQEA AAYLKDLGPE YEGIFNTSLQ WILENGKDVG IRCVGFGPEE 600
ELTNITDVQF LQSTRPLMSF WCRFRRAFVT VTHRLLLLCL GVVMVCVVLR YMKYRWTKEE 660
EETRQMYDMV VKIIDVLRSH NEACQENKDL QPYMPIPHVR DSLIQPHDRK KMKKVWDRAV 720
DFLAANESRV RTETRRIGGA DFLVWRWIQP SASCDKILVI PSKVWQGQAF HLDRRNSPPN 780
SLTPCLKIRN MFDPVMEIGD QWHLAIQEAI LEKCSDNDGI VHIAVDKNSR EGCVYVKCLS 840
PEYAGKAFKA LHGSWFDGKL VTVKYLRLDR YHHRFPQALT SNTPLKPSNK HMNSMSHLRL 900
RTGLTNSQGS S 911 
Gene Ontology
 GO:0005639; C:integral to nuclear inner membrane; TAS:ProtInc.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
 GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IEA:Compara.
 GO:0035914; P:skeletal muscle cell differentiation; IEA:Compara. 
Interpro
 IPR018996; Inner-Nucl-membr_MAN1.
 IPR011015; LEM/LEM-like_dom.
 IPR003887; LEM_dom.
 IPR012677; Nucleotide-bd_a/b_plait. 
Pfam
 PF03020; LEM
 PF09402; MSC 
SMART
 SM00540; LEM 
PROSITE
 PS50954; LEM 
PRINTS