SYNCI_HUMAN
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 03-AUG-2022, entry version 139.
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};
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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; 50.
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; Q9H7C4; -.
DR PeptideAtlas; Q9H7C4; -.
DR PRIDE; Q9H7C4; -.
DR ProteomicsDB; 81100; -. [Q9H7C4-1]
DR ProteomicsDB; 81101; -. [Q9H7C4-2]
DR Antibodypedia; 54803; 169 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 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; FKVTREC; -.
DR OrthoDB; 906986at2759; -.
DR PhylomeDB; Q9H7C4; -.
DR PathwayCommons; Q9H7C4; -.
DR SignaLink; Q9H7C4; -.
DR BioGRID-ORCS; 81493; 11 hits in 1071 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 181 other tissues.
DR ExpressionAtlas; Q9H7C4; baseline and differential.
DR Genevisible; Q9H7C4; HS.
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 InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR027702; Syncoilin.
DR PANTHER; PTHR47147; PTHR47147; 1.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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
