CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000364
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Synemin 
Protein Synonyms/Alias
 Desmuslin 
Gene Name
 SYNM 
Gene Synonyms/Alias
 DMN; KIAA0353; SYN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1546RSVISDEKKVALLYLubiquitination[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
Functional Description
 Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells. 
Sequence Annotation
 REGION 1 10 Head.
 REGION 11 320 Interaction with DMD and UTRN.
 REGION 11 300 Rod.
 REGION 11 49 Coil 1A.
 REGION 50 58 Linker 1.
 REGION 59 163 Coil 1B.
 REGION 164 186 Linker 12.
 REGION 187 300 Coil 2.
 REGION 301 1565 Tail.
 REGION 1152 1463 Interaction with TLN1 and VCL.
 REGION 1244 1563 Interaction with DMD and UTRN.
 MOD_RES 429 429 Phosphoserine.
 MOD_RES 598 598 Phosphothreonine.
 MOD_RES 1044 1044 Phosphoserine.
 MOD_RES 1049 1049 Phosphoserine.
 MOD_RES 1181 1181 Phosphoserine.
 MOD_RES 1184 1184 Phosphoserine.
 MOD_RES 1435 1435 Phosphoserine.  
Keyword
 Alternative splicing; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Intermediate filament; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1565 AA 
Protein Sequence
MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE GLWAEGQARC 60
AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA EERAARGRLD AELGAQQREL 120
QEALGARAAL EALLGRLQAE RRGLDAAHER DVRELRARAA SLTMHFRARA TGPAAPPPRL 180
REVHDSYALL VAESWRETVQ LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE 240
ALGLEQLRAR LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV 300
KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ RENERNLFSR 360
QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG SGYSSSATTQ QENSYGKAVS 420
SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK AGDTREVPVY IGEDSTIARE SYRDRRDKVA 480
AGASESTRSN ERTVILGKKT EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE 540
ELTKLDKEAR QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV 600
KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF TQSPETEASA 660
DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD EAGLDYLLSK DIKEVGLKGK 720
SAEQMIGDII NLGLKGREGR AKVVNVEIVE EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP 780
WGLVKEEEGY GESDVTFSVN QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG 840
GHDRDDGSVY GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG 900
DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV EVIGQLEETL 960
PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV AEVNVSQTVD ADRLDLEELS 1020
KDEASEMEKA VESVVRESLS RQRSPAPGSP DEEGGAEAPA AGIRFRRWAT RELYIPSGES 1080
EVAGGASHSS GQRTPQGPVS ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM 1140
SYEGPTAEVV EVSAGGDLSQ AASPTGASRS VRHVTLGPGQ SPLSREVIFL GPAPACPEAW 1200
GSPEPGPAES SADMDGSGRH STFGCRQFHA EKEIIFQGPI SAAGKVGDYF ATEESVGTQT 1260
SVRQLQLGPK EGFSGQIQFT APLSDKVELG VIGDSVHMEG LPGSSTSIRH ISIGPQRHQT 1320
TQQIVYHGLV PQLGESGDSE STVHGEGSAD VHQATHSHTS GRQTVMTEKS TFQSVVSESP 1380
QEDSAGDTSG AEMTSGVSRS FRHIRLGPTE TETSEHIAIR GPVSRTFVLA GSADSPELGK 1440
LADSSRTLRH IAPGPKETSF TFQMDVSNVE AIRSRTQEAG ALGVSDRGSW RDADSRNDQA 1500
VGVSFKASAG EGDQAHREQG KEQAMFDKKV QLQRMVDQRS VISDEKKVAL LYLDNEEEEN 1560
DGHWF 1565 
Gene Ontology
 GO:0005912; C:adherens junction; IDA:UniProtKB.
 GO:0043034; C:costamere; IDA:UniProtKB.
 GO:0005882; C:intermediate filament; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0060053; C:neurofilament cytoskeleton; TAS:UniProtKB.
 GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
 GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
 GO:0017166; F:vinculin binding; IDA:UniProtKB.
 GO:0045104; P:intermediate filament cytoskeleton organization; TAS:UniProtKB. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS. 
Pfam
 PF00038; Filament 
SMART
  
PROSITE
 PS00226; IF 
PRINTS