TPM4_HUMAN
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 03-AUG-2022, entry version 173.
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;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P67936-2, P07226-2;
CC 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="http://atlasgeneticsoncology.org/Genes/TPM4ID359.html";
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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; 221.
DR IntAct; P67936; 99.
DR MINT; P67936; -.
DR STRING; 9606.ENSP00000345230; -.
DR ChEMBL; CHEMBL4295789; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
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 PeptideAtlas; P67936; -.
DR PRIDE; P67936; -.
DR ProteomicsDB; 57525; -.
DR ProteomicsDB; 57526; -. [P67936-2]
DR Antibodypedia; 27276; 172 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 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; EDKCKQM; -.
DR OrthoDB; 1576041at2759; -.
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 BioGRID-ORCS; 7171; 42 hits in 1070 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 193 other tissues.
DR ExpressionAtlas; P67936; baseline and differential.
DR Genevisible; P67936; HS.
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; 1.20.5.370; -; 1.
DR InterPro; IPR000533; Tropomyosin.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
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
