TAGL_HUMAN
ID TAGL_HUMAN Reviewed; 201 AA.
AC Q01995; O15542;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Transgelin;
DE AltName: Full=22 kDa actin-binding protein;
DE AltName: Full=Protein WS3-10;
DE AltName: Full=Smooth muscle protein 22-alpha;
DE Short=SM22-alpha;
GN Name=TAGLN; Synonyms=SM22, WS3-10;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=1520290; DOI=10.1016/s0006-291x(05)81449-4;
RA Thweatt R., Lumpkin C.K. Jr., Goldstein S.;
RT "A novel gene encoding a smooth muscle protein is overexpressed in
RT senescent human fibroblasts.";
RL Biochem. Biophys. Res. Commun. 187:1-7(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1872880;
RA Nishida W., Kitami Y., Abe M., Kiwada K.;
RT "Gene cloning and nucleotide sequence of SM22 alpha from the chicken
RT gizzard smooth muscle.";
RL Biochem. Int. 23:663-668(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9615232; DOI=10.1006/geno.1998.5267;
RA Camoretti-Mercado B., Forsythe S.M., Lebeau M.M., Espinosa R.D. III,
RA Vieira J.E., Halayko A.J., Willadsen S., Kurtz B., Ober C., Evans G.A.,
RA Thweatt R., Shapiro S., Niu Q., Qin Y., Padrid P.A., Solway J.;
RT "Expression and cytogenetic localization of the human SM22 gene (TAGLN).";
RL Genomics 49:452-457(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Aorta, and Peripheral blood;
RX PubMed=9276683; DOI=10.1093/oxfordjournals.jbchem.a021722;
RA Yamamura H., Masuda H., Ikeda W., Tokuyama T., Takagi M., Shibata N.,
RA Tatsuta M., Takahashi K.;
RT "Structure and expression of the human SM22alpha gene, assignment of the
RT gene to chromosome 11, and repression of the promoter activity by cytosine
RT DNA methylation.";
RL J. Biochem. 122:157-167(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-183, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Actin cross-linking/gelling protein (By similarity). Involved
CC in calcium interactions and contractile properties of the cell that may
CC contribute to replicative senescence. {ECO:0000250}.
CC -!- INTERACTION:
CC Q01995; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-1054248, EBI-739467;
CC Q01995; P08069: IGF1R; NbExp=2; IntAct=EBI-1054248, EBI-475981;
CC Q01995; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1054248, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Overexpressed in senescent human fibroblasts.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TAGLNID46168ch11q23.html";
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; M95787; AAA58351.1; -; mRNA.
DR EMBL; M83106; AAA58375.1; -; mRNA.
DR EMBL; AF013711; AAC21582.1; -; Genomic_DNA.
DR EMBL; D17409; BAA21811.1; -; mRNA.
DR EMBL; D84342; BAA21839.1; -; Genomic_DNA.
DR EMBL; BC004927; AAH04927.1; -; mRNA.
DR EMBL; BC065829; AAH65829.1; -; mRNA.
DR CCDS; CCDS8381.1; -.
DR PIR; JC5577; JS0774.
DR RefSeq; NP_001001522.1; NM_001001522.1.
DR RefSeq; NP_003177.2; NM_003186.3.
DR AlphaFoldDB; Q01995; -.
DR BMRB; Q01995; -.
DR SMR; Q01995; -.
DR BioGRID; 112739; 56.
DR IntAct; Q01995; 291.
DR MINT; Q01995; -.
DR STRING; 9606.ENSP00000432282; -.
DR DrugBank; DB11638; Artenimol.
DR iPTMnet; Q01995; -.
DR MetOSite; Q01995; -.
DR PhosphoSitePlus; Q01995; -.
DR SwissPalm; Q01995; -.
DR BioMuta; TAGLN; -.
DR DMDM; 3123283; -.
DR REPRODUCTION-2DPAGE; IPI00216138; -.
DR UCD-2DPAGE; Q01995; -.
DR CPTAC; CPTAC-443; -.
DR CPTAC; CPTAC-726; -.
DR EPD; Q01995; -.
DR jPOST; Q01995; -.
DR MassIVE; Q01995; -.
DR PaxDb; Q01995; -.
DR PeptideAtlas; Q01995; -.
DR PRIDE; Q01995; -.
DR ProteomicsDB; 58029; -.
DR ABCD; Q01995; 1 sequenced antibody.
DR Antibodypedia; 3666; 718 antibodies from 40 providers.
DR CPTC; Q01995; 1 antibody.
DR DNASU; 6876; -.
DR Ensembl; ENST00000278968.10; ENSP00000278968.6; ENSG00000149591.17.
DR Ensembl; ENST00000392951.9; ENSP00000376678.4; ENSG00000149591.17.
DR Ensembl; ENST00000525531.5; ENSP00000432054.1; ENSG00000149591.17.
DR Ensembl; ENST00000530649.5; ENSP00000431941.1; ENSG00000149591.17.
DR Ensembl; ENST00000532870.5; ENSP00000432282.1; ENSG00000149591.17.
DR GeneID; 6876; -.
DR KEGG; hsa:6876; -.
DR MANE-Select; ENST00000392951.9; ENSP00000376678.4; NM_003186.5; NP_003177.2.
DR CTD; 6876; -.
DR DisGeNET; 6876; -.
DR GeneCards; TAGLN; -.
DR HGNC; HGNC:11553; TAGLN.
DR HPA; ENSG00000149591; Tissue enhanced (endometrium, intestine).
DR MIM; 600818; gene.
DR neXtProt; NX_Q01995; -.
DR OpenTargets; ENSG00000149591; -.
DR PharmGKB; PA36324; -.
DR VEuPathDB; HostDB:ENSG00000149591; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000155162; -.
DR HOGENOM; CLU_055232_1_0_1; -.
DR InParanoid; Q01995; -.
DR OMA; AYKHPEW; -.
DR PhylomeDB; Q01995; -.
DR TreeFam; TF313921; -.
DR PathwayCommons; Q01995; -.
DR SignaLink; Q01995; -.
DR SIGNOR; Q01995; -.
DR BioGRID-ORCS; 6876; 6 hits in 1077 CRISPR screens.
DR ChiTaRS; TAGLN; human.
DR GeneWiki; TAGLN; -.
DR GenomeRNAi; 6876; -.
DR Pharos; Q01995; Tbio.
DR PRO; PR:Q01995; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q01995; protein.
DR Bgee; ENSG00000149591; Expressed in saphenous vein and 200 other tissues.
DR ExpressionAtlas; Q01995; baseline and differential.
DR Genevisible; Q01995; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR029976; TAGLN.
DR PANTHER; PTHR18959:SF40; PTHR18959:SF40; 1.
DR Pfam; PF00402; Calponin; 1.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS01052; CALPONIN_1; 1.
DR PROSITE; PS51122; CALPONIN_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Methylation; Muscle protein;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..201
FT /note="Transgelin"
FT /id="PRO_0000204781"
FT DOMAIN 24..137
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 175..200
FT /note="Calponin-like"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37804"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 183
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 182
FT /note="N -> S (in dbSNP:rs12284316)"
FT /id="VAR_048670"
FT CONFLICT 49
FT /note="R -> P (in Ref. 1; AAA58351)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> E (in Ref. 2; AAA58375)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Y -> C (in Ref. 2; AAA58375)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Y -> S (in Ref. 1; AAA58351)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="M -> V (in Ref. 2; AAA58375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22611 MW; 7AE9E7A9A45602C3 CRC64;
MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV
ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG
KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG
SNRGASQAGM TGYGRPRQII S
