ID SYNCI_HUMAN Reviewed; 482 AA. AC Q9H7C4; B4DNK8; B4DY58; C9IY41; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 3. DT 24-JAN-2024, entry version 146. DE RecName: Full=Syncoilin; DE AltName: Full=Syncoilin intermediate filament 1; DE AltName: Full=Syncoilin-1; GN Name=SYNC; Synonyms=SYNC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000312|EMBL:BAB14970.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] {ECO:0000312|EMBL:AAI19702.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-482 (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] {ECO:0000305} RP INDUCTION. RX PubMed=16124004; DOI=10.1002/mus.20431; RA Brown S.C., Torelli S., Ugo I., De Biasia F., Howman E.V., Poon E., RA Britton J., Davies K.E., Muntoni F.; RT "Syncoilin upregulation in muscle of patients with neuromuscular disease."; RL Muscle Nerve 32:715-725(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-325, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Atypical type III intermediate filament (IF) protein that may CC play a supportive role in the efficient coupling of mechanical stress CC between the myofibril and fiber exterior. May facilitate lateral force CC transmission during skeletal muscle contraction. Does not form CC homofilaments nor heterofilaments with other IF proteins. CC {ECO:0000250|UniProtKB:Q9EPM5}. CC -!- SUBUNIT: May link the dystrophin-associated glycoprotein complex (DAPC) CC to intracellular desmin (DES) filaments. Interacts with DES and DTNA. CC {ECO:0000250|UniProtKB:Q9EPM5}. CC -!- INTERACTION: CC Q9H7C4; P68133: ACTA1; NbExp=3; IntAct=EBI-11285923, EBI-367510; CC Q9H7C4; P13637: ATP1A3; NbExp=3; IntAct=EBI-11285923, EBI-948169; CC Q9H7C4; P14136: GFAP; NbExp=3; IntAct=EBI-11285923, EBI-744302; CC Q9H7C4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-11285923, EBI-10975473; CC Q9H7C4; P07196: NEFL; NbExp=3; IntAct=EBI-11285923, EBI-475646; CC Q9H7C4; P16284: PECAM1; NbExp=3; IntAct=EBI-11285923, EBI-716404; CC Q9H7C4; Q13393: PLD1; NbExp=3; IntAct=EBI-11285923, EBI-2827556; CC Q9H7C4; P20339: RAB5A; NbExp=3; IntAct=EBI-11285923, EBI-399437; CC Q9H7C4; P08670: VIM; NbExp=3; IntAct=EBI-11285923, EBI-353844; CC Q9H7C4; O76024: WFS1; NbExp=3; IntAct=EBI-11285923, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:Q9EPM5}. Note=In skeletal muscle, colocalizes CC with DES and DTNA, and is localized at the myotendinous and CC neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected CC in a punctate cytoplasmic pattern (By similarity). CC {ECO:0000250|UniProtKB:Q9EPM5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H7C4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H7C4-2; Sequence=VSP_039404; CC -!- INDUCTION: Up-regulated at the sarcolemma in individuals with various CC forms of neuromuscular disease. {ECO:0000269|PubMed:16124004}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI19701.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI19702.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK024707; BAB14970.1; ALT_INIT; mRNA. DR EMBL; AK297958; BAG60270.1; -; mRNA. DR EMBL; AK302275; BAG63620.1; -; mRNA. DR EMBL; AC114489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC119700; AAI19701.1; ALT_INIT; mRNA. DR EMBL; BC119701; AAI19702.1; ALT_INIT; mRNA. DR CCDS; CCDS367.2; -. [Q9H7C4-1] DR CCDS; CCDS53294.1; -. [Q9H7C4-2] DR RefSeq; NP_001155180.1; NM_001161708.1. [Q9H7C4-2] DR RefSeq; NP_110413.2; NM_030786.2. [Q9H7C4-1] DR AlphaFoldDB; Q9H7C4; -. DR SMR; Q9H7C4; -. DR BioGRID; 123502; 64. DR IntAct; Q9H7C4; 51. DR STRING; 9606.ENSP00000386439; -. DR iPTMnet; Q9H7C4; -. DR PhosphoSitePlus; Q9H7C4; -. DR BioMuta; SYNC; -. DR DMDM; 300669677; -. DR EPD; Q9H7C4; -. DR jPOST; Q9H7C4; -. DR MassIVE; Q9H7C4; -. DR MaxQB; Q9H7C4; -. DR PaxDb; 9606-ENSP00000386439; -. DR PeptideAtlas; Q9H7C4; -. DR ProteomicsDB; 81100; -. [Q9H7C4-1] DR ProteomicsDB; 81101; -. [Q9H7C4-2] DR Pumba; Q9H7C4; -. DR Antibodypedia; 54803; 189 antibodies from 20 providers. DR DNASU; 81493; -. DR Ensembl; ENST00000373484.4; ENSP00000362583.3; ENSG00000162520.15. [Q9H7C4-2] DR Ensembl; ENST00000409190.8; ENSP00000386439.3; ENSG00000162520.15. [Q9H7C4-1] DR GeneID; 81493; -. DR KEGG; hsa:81493; -. DR MANE-Select; ENST00000409190.8; ENSP00000386439.3; NM_030786.3; NP_110413.3. DR UCSC; uc001bvt.3; human. [Q9H7C4-1] DR AGR; HGNC:28897; -. DR CTD; 81493; -. DR DisGeNET; 81493; -. DR GeneCards; SYNC; -. DR HGNC; HGNC:28897; SYNC. DR HPA; ENSG00000162520; Group enriched (skeletal muscle, smooth muscle, tongue). DR MIM; 611750; gene. DR neXtProt; NX_Q9H7C4; -. DR OpenTargets; ENSG00000162520; -. DR PharmGKB; PA164726395; -. DR VEuPathDB; HostDB:ENSG00000162520; -. DR eggNOG; ENOG502RKZJ; Eukaryota. DR GeneTree; ENSGT00390000018108; -. DR HOGENOM; CLU_562526_0_0_1; -. DR InParanoid; Q9H7C4; -. DR OMA; GGMETKS; -. DR OrthoDB; 5319272at2759; -. DR PhylomeDB; Q9H7C4; -. DR PathwayCommons; Q9H7C4; -. DR SignaLink; Q9H7C4; -. DR BioGRID-ORCS; 81493; 16 hits in 1150 CRISPR screens. DR ChiTaRS; SYNC; human. DR GenomeRNAi; 81493; -. DR Pharos; Q9H7C4; Tbio. DR PRO; PR:Q9H7C4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H7C4; Protein. DR Bgee; ENSG00000162520; Expressed in biceps brachii and 182 other cell types or tissues. DR ExpressionAtlas; Q9H7C4; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW. DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central. DR GO; GO:0030018; C:Z disc; IBA:GO_Central. DR GO; GO:0045103; P:intermediate filament-based process; IBA:GO_Central. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR027702; Syncoilin. DR PANTHER; PTHR47147; SYNCOILIN; 1. DR PANTHER; PTHR47147:SF1; SYNCOILIN; 1. DR Pfam; PF00038; Filament; 1. DR SMART; SM01391; Filament; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR Genevisible; Q9H7C4; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Intermediate filament; KW Phosphoprotein; Reference proteome. FT CHAIN 1..482 FT /note="Syncoilin" FT /id="PRO_0000306180" FT DOMAIN 168..463 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..161 FT /note="Head" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 144..165 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..204 FT /note="Coil 1A" FT REGION 205..231 FT /note="Linker 1" FT REGION 232..309 FT /note="Coil 1b" FT REGION 310..349 FT /note="Linker 2" FT REGION 350..458 FT /note="Coil 2" FT REGION 459..482 FT /note="Tail" FT REGION 460..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 463..482 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EPM5" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 454..482 FT /note="AMLLPKSLEQADAPTSQAGGMETQSQGAV -> GCLEIYGQICNPETAKNFL FT AKDH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039404" FT CONFLICT 58 FT /note="I -> T (in Ref. 1; BAG60270)" FT /evidence="ECO:0000305" FT CONFLICT 163 FT /note="M -> V (in Ref. 1; BAG63620/BAG60270)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="R -> Q (in Ref. 1; BAG63620/BAG60270)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="F -> S (in Ref. 1; BAG60270)" FT /evidence="ECO:0000305" SQ SEQUENCE 482 AA; 55299 MW; 969F2DA9C48C858B CRC64; MASPEPRRGG DGAAQAARKT RVEANSPLPK NSGSLNEAEA LNPEVTLSSE GSLNLEDILY LEDTGDLDET LYVQETEKAE EALYIEEAMQ PDEALHVEEP GNPEETVCVE ETTEPDRIQF VEGPVEPGKP TSPEHVVYEG ETVTRAEKSN PEESLRAEQS PSMEENLSIE DLELLEGRFQ QCVQAVAQLE EERDQLIHEL VLLREPALQE VQQVHQDILA AYKLHAQAEL ERDGLREEIR LVKQKLFKVT KECVAYQYQL ECRQQDVAQF ADFREVLTTR ATQLSEELAQ LRDAYQKQKE QLRQQLEAPP SQRDGHFLQE SRRLSAQFEN LMAESRQDLE EEYEPQFLRL LERKEAGTKA LQRTQAEIQE MKEALRPLQA EARQLRLQNR NLEDQIALVR QKRDEEVQQY REQLEEMEER QRQLRNGVQL QQQKNKEMEQ LRLSLAEELS TYKAMLLPKS LEQADAPTSQ AGGMETQSQG AV //