ID TPM4_HUMAN Reviewed; 248 AA. AC P67936; P07226; Q15659; Q5U0D9; Q9BU85; Q9H8Q3; Q9UCS1; Q9UCS2; Q9UCS3; AC Q9UCS4; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 182. DE RecName: Full=Tropomyosin alpha-4 chain; DE AltName: Full=TM30p1; DE AltName: Full=Tropomyosin-4; GN Name=TPM4; 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] (ISOFORM 1). RC TISSUE=Fibroblast; RX PubMed=3612796; DOI=10.1016/0022-2836(87)90710-8; RA McLeod A.R., Talbot K., Smillie L.B., Houlker C.; RT "Characterization of a cDNA defining a gene family encoding TM30p1, a human RT fibroblast tropomyosin."; RL J. Mol. Biol. 194:1-10(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Ovarian carcinoma, and Tongue; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, Placenta, and Testis; 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 PROTEIN SEQUENCE OF 2-12. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 2-11; 45-54; 56-69; 77-89; 133-146 AND 216-223, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 9-31; 44-61; 89-95; 205-214 AND 231-243 (ISOFORM 1), RP FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Platelet; RX PubMed=1836432; DOI=10.1111/j.1365-2362.1991.tb01397.x; RA Crabos M., Yamakado T., Heizmann C.W., Cerletti N., Buehler F.R., Erne P.; RT "The calcium binding protein tropomyosin in human platelets and cardiac RT tissue: elevation in hypertensive cardiac hypertrophy."; RL Eur. J. Clin. Invest. 21:472-478(1991). RN [9] RP PROTEIN SEQUENCE OF 13-27; 45-82; 132-142; 154-169 AND 216-228, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 118-248. RC TISSUE=Fibroblast; RX PubMed=3865200; DOI=10.1073/pnas.82.23.7835; RA MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., RA Walsh F.S.; RT "A muscle-type tropomyosin in human fibroblasts: evidence for expression by RT an alternative RNA splicing mechanism."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985). RN [11] RP PROTEIN SEQUENCE OF 177-189 AND 228-247. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [12] 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=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 AND LYS-215, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] 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 [15] 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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND IDENTIFICATION BY RP 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). RN [18] RP IDENTIFICATION BY 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 [19] RP VARIANT [LARGE SCALE ANALYSIS] GLN-204. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells. CC Plays a central role, in association with the troponin complex, in the CC calcium dependent regulation of vertebrate striated muscle contraction. CC Smooth muscle contraction is regulated by interaction with caldesmon. CC In non-muscle cells is implicated in stabilizing cytoskeleton actin CC filaments (By similarity). Binds calcium (PubMed:1836432). CC {ECO:0000250|UniProtKB:P09495, ECO:0000269|PubMed:1836432}. CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a CC beta (TPM2) chain. {ECO:0000250|UniProtKB:P04692}. CC -!- INTERACTION: CC P67936; O75564-2: JRK; NbExp=3; IntAct=EBI-1642100, EBI-17181882; CC P67936; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1642100, EBI-79165; CC P67936; O95295: SNAPIN; NbExp=3; IntAct=EBI-1642100, EBI-296723; CC P67936; P06753: TPM3; NbExp=3; IntAct=EBI-1642100, EBI-355607; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress CC fibers. {ECO:0000250|UniProtKB:P09495}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P67936-1, P07226-1; Sequence=Displayed; CC Name=2; CC IsoId=P67936-2, P07226-2; Sequence=VSP_006611; CC -!- TISSUE SPECIFICITY: Detected in cardiac tissue and platelets, the form CC found in cardiac tissue is a higher molecular weight than the form CC found in platelets. Expressed at higher levels in the platelets of CC hypertensive patients with cardiac hypertrophy than in the platelets of CC hypertensive patients without cardiac hypertrophy (at protein level). CC {ECO:0000269|PubMed:1836432}. CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2 CC polypeptide chains. The sequence exhibits a prominent seven-residues CC periodicity. CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/359/TPM4"; 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; X05276; CAA28888.1; -; mRNA. DR EMBL; AK023385; BAB14554.1; -; mRNA. DR EMBL; AK315076; BAG37545.1; -; mRNA. DR EMBL; BT019634; AAV38440.1; -; mRNA. DR EMBL; CH471106; EAW84521.1; -; Genomic_DNA. DR EMBL; BC002827; AAH02827.1; -; mRNA. DR EMBL; BC037576; AAH37576.1; -; mRNA. DR EMBL; BC067225; AAH67225.1; -; mRNA. DR EMBL; M12127; AAA36774.1; -; mRNA. DR CCDS; CCDS12338.1; -. DR CCDS; CCDS46007.1; -. [P67936-2] DR PIR; S07282; S07282. DR RefSeq; NP_001138632.1; NM_001145160.1. [P67936-2] DR RefSeq; NP_003281.1; NM_003290.2. [P67936-1] DR AlphaFoldDB; P67936; -. DR SMR; P67936; -. DR BioGRID; 113024; 251. DR IntAct; P67936; 107. DR MINT; P67936; -. DR STRING; 9606.ENSP00000494125; -. DR ChEMBL; CHEMBL4295789; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyGen; P67936; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P67936; -. DR MetOSite; P67936; -. DR PhosphoSitePlus; P67936; -. DR SwissPalm; P67936; -. DR BioMuta; TPM4; -. DR DMDM; 54039751; -. DR DOSAC-COBS-2DPAGE; P67936; -. DR OGP; P07226; -. DR CPTAC; CPTAC-154; -. DR CPTAC; CPTAC-155; -. DR CPTAC; CPTAC-156; -. DR EPD; P67936; -. DR jPOST; P67936; -. DR MassIVE; P67936; -. DR MaxQB; P67936; -. DR PaxDb; 9606-ENSP00000345230; -. DR PeptideAtlas; P67936; -. DR ProteomicsDB; 57525; -. DR ProteomicsDB; 57526; -. [P67936-2] DR Antibodypedia; 27276; 202 antibodies from 28 providers. DR DNASU; 7171; -. DR Ensembl; ENST00000643579.2; ENSP00000495347.1; ENSG00000167460.17. [P67936-1] DR Ensembl; ENST00000646974.2; ENSP00000494125.1; ENSG00000167460.17. [P67936-2] DR GeneID; 7171; -. DR KEGG; hsa:7171; -. DR MANE-Select; ENST00000643579.2; ENSP00000495347.1; NM_003290.3; NP_003281.1. DR UCSC; uc002ndi.3; human. DR AGR; HGNC:12013; -. DR CTD; 7171; -. DR DisGeNET; 7171; -. DR GeneCards; TPM4; -. DR HGNC; HGNC:12013; TPM4. DR HPA; ENSG00000167460; Low tissue specificity. DR MalaCards; TPM4; -. DR MIM; 600317; gene. DR neXtProt; NX_P67936; -. DR OpenTargets; ENSG00000167460; -. DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia. DR Orphanet; 178342; Inflammatory myofibroblastic tumor. DR PharmGKB; PA36693; -. DR VEuPathDB; HostDB:ENSG00000167460; -. DR GeneTree; ENSGT01030000234542; -. DR HOGENOM; CLU_055027_0_0_1; -. DR InParanoid; P67936; -. DR OMA; QMEDELM; -. DR OrthoDB; 5398117at2759; -. DR PhylomeDB; P67936; -. DR TreeFam; TF351519; -. DR PathwayCommons; P67936; -. DR Reactome; R-HSA-390522; Striated Muscle Contraction. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-9013424; RHOV GTPase cycle. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR SignaLink; P67936; -. DR SIGNOR; P67936; -. DR BioGRID-ORCS; 7171; 42 hits in 1148 CRISPR screens. DR ChiTaRS; TPM4; human. DR GeneWiki; TPM4; -. DR GenomeRNAi; 7171; -. DR Pharos; P67936; Tbio. DR PRO; PR:P67936; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P67936; Protein. DR Bgee; ENSG00000167460; Expressed in tendon of biceps brachii and 195 other cell types or tissues. DR ExpressionAtlas; P67936; baseline and differential. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl. DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc. DR GO; GO:0002102; C:podosome; IEA:Ensembl. DR GO; GO:0001725; C:stress fiber; IDA:MGI. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.370; -; 1. DR InterPro; IPR000533; Tropomyosin. DR InterPro; IPR014751; XRCC4-like_C. DR PANTHER; PTHR19269; TROPOMYOSIN; 1. DR PANTHER; PTHR19269:SF70; TROPOMYOSIN ALPHA-4 CHAIN; 1. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS00326; TROPOMYOSIN; 1. DR Genevisible; P67936; HS. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Alternative splicing; Calcium; Coiled coil; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Metal-binding; KW Muscle protein; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..248 FT /note="Tropomyosin alpha-4 chain" FT /id="PRO_0000205635" FT REGION 15..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 2..248 FT /evidence="ECO:0000250" FT COMPBIAS 26..47 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09495" FT MOD_RES 177 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 215 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 216 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..44 FT /note="MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERERREK -> MEAI FT KKKMQMLKLDKENAIDRAEQAEADKKAAEDKCKQVEEELTHLQKKLKGTEDELDKYSED FT LKDAQEKLELTEKKASD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_006611" FT VARIANT 204 FT /note="E -> Q (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036535" FT CONFLICT 59 FT /note="V -> F (in Ref. 5; AAH02827)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="L -> S (in Ref. 10; AAA36774)" FT /evidence="ECO:0000305" FT CONFLICT 162..163 FT /note="KN -> RT (in Ref. 10; AAA36774)" FT /evidence="ECO:0000305" SQ SEQUENCE 248 AA; 28522 MW; 5D5CDF6BF76552A8 CRC64; MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI //