Tag | Content |
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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 |
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1546 | RSVISDEKKVALLYL | ubiquitination | [1] |
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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. |
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