Full text data of TPM4
TPM4
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tropomyosin alpha-4 chain (TM30p1; Tropomyosin-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tropomyosin alpha-4 chain (TM30p1; Tropomyosin-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00010779
IPI00010779 Splice isoform 1 of P07226 Tropomyosin alpha 4 chain Splice isoform 1 of P07226 Tropomyosin alpha 4 chain membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a 7 n/a n/a cytoskeleton n/a found at its expected molecular weight found at molecular weight
IPI00010779 Splice isoform 1 of P07226 Tropomyosin alpha 4 chain Splice isoform 1 of P07226 Tropomyosin alpha 4 chain membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a 7 n/a n/a cytoskeleton n/a found at its expected molecular weight found at molecular weight
UniProt
P67936
ID TPM4_HUMAN Reviewed; 248 AA.
AC P67936; P07226; Q15659; Q5U0D9; Q9BU85; Q9H8Q3; Q9UCS1; Q9UCS2;
read moreAC Q9UCS3; Q9UCS4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 103.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS
RP 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
RP 1), 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.,
RA Erne P.;
RT "The calcium binding protein tropomyosin in human platelets and
RT cardiac 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 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.,
RA Modi G., Walsh F.S.;
RT "A muscle-type tropomyosin in human fibroblasts: evidence for
RT expression by 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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
CC the calcium dependent regulation of vertebrate striated muscle
CC contraction. Smooth muscle contraction is regulated by interaction
CC with caldesmon. In non-muscle cells is implicated in stabilizing
CC cytoskeleton actin filaments. Binds calcium.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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
CC form found in cardiac tissue is a higher molecular weight than the
CC form found in platelets. Expressed at higher levels in the
CC platelets of hypertensive patients with cardiac hypertrophy than
CC in the platelets of hypertensive patients without cardiac
CC hypertrophy (at protein level).
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed
CC by 2 polypeptide chains. The sequence exhibits a prominent seven-
CC residues periodicity.
CC -!- SIMILARITY: Belongs to the tropomyosin family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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 PIR; S07282; S07282.
DR RefSeq; NP_001138632.1; NM_001145160.1.
DR RefSeq; NP_003281.1; NM_003290.2.
DR UniGene; Hs.631618; -.
DR ProteinModelPortal; P67936; -.
DR SMR; P67936; 5-248.
DR IntAct; P67936; 6.
DR MINT; MINT-4138291; -.
DR PhosphoSite; P67936; -.
DR DMDM; 54039751; -.
DR DOSAC-COBS-2DPAGE; P67936; -.
DR OGP; P07226; -.
DR PaxDb; P67936; -.
DR PeptideAtlas; P67936; -.
DR PRIDE; P67936; -.
DR DNASU; 7171; -.
DR Ensembl; ENST00000300933; ENSP00000300933; ENSG00000167460.
DR Ensembl; ENST00000344824; ENSP00000345230; ENSG00000167460.
DR Ensembl; ENST00000538887; ENSP00000439135; ENSG00000167460.
DR GeneID; 7171; -.
DR KEGG; hsa:7171; -.
DR UCSC; uc002ndj.2; human.
DR CTD; 7171; -.
DR GeneCards; GC19P017322; -.
DR H-InvDB; HIX0022609; -.
DR HGNC; HGNC:12013; TPM4.
DR HPA; CAB004685; -.
DR MIM; 600317; gene.
DR neXtProt; NX_P67936; -.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR PharmGKB; PA36693; -.
DR eggNOG; NOG304012; -.
DR HOVERGEN; HBG107404; -.
DR KO; K10375; -.
DR OMA; EKCKQVE; -.
DR Reactome; REACT_17044; Muscle contraction.
DR ChiTaRS; TPM4; human.
DR GeneWiki; TPM4; -.
DR GenomeRNAi; 7171; -.
DR NextBio; 28104; -.
DR PRO; PR:P67936; -.
DR ArrayExpress; P67936; -.
DR Bgee; P67936; -.
DR CleanEx; HS_TPM4; -.
DR Genevestigator; P67936; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
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:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR InterPro; IPR000533; Tropomyosin.
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;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Metal-binding; Muscle protein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 248 Tropomyosin alpha-4 chain.
FT /FTId=PRO_0000205635.
FT COILED 2 248 By similarity.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 177 177 N6-acetyllysine.
FT MOD_RES 215 215 N6-acetyllysine.
FT VAR_SEQ 1 44 MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERER
FT REK -> MEAIKKKMQMLKLDKENAIDRAEQAEADKKAAED
FT KCKQVEEELTHLQKKLKGTEDELDKYSEDLKDAQEKLELTE
FT KKASD (in isoform 2).
FT /FTId=VSP_006611.
FT VARIANT 204 204 E -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036535.
FT CONFLICT 59 59 V -> F (in Ref. 5; AAH02827).
FT CONFLICT 152 152 L -> S (in Ref. 10; AAA36774).
FT CONFLICT 162 163 KN -> RT (in Ref. 10; AAA36774).
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
//
ID TPM4_HUMAN Reviewed; 248 AA.
AC P67936; P07226; Q15659; Q5U0D9; Q9BU85; Q9H8Q3; Q9UCS1; Q9UCS2;
read moreAC Q9UCS3; Q9UCS4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 103.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS
RP 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
RP 1), 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.,
RA Erne P.;
RT "The calcium binding protein tropomyosin in human platelets and
RT cardiac 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 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.,
RA Modi G., Walsh F.S.;
RT "A muscle-type tropomyosin in human fibroblasts: evidence for
RT expression by 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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
CC the calcium dependent regulation of vertebrate striated muscle
CC contraction. Smooth muscle contraction is regulated by interaction
CC with caldesmon. In non-muscle cells is implicated in stabilizing
CC cytoskeleton actin filaments. Binds calcium.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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
CC form found in cardiac tissue is a higher molecular weight than the
CC form found in platelets. Expressed at higher levels in the
CC platelets of hypertensive patients with cardiac hypertrophy than
CC in the platelets of hypertensive patients without cardiac
CC hypertrophy (at protein level).
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed
CC by 2 polypeptide chains. The sequence exhibits a prominent seven-
CC residues periodicity.
CC -!- SIMILARITY: Belongs to the tropomyosin family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TPM4ID359.html";
CC -----------------------------------------------------------------------
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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 PIR; S07282; S07282.
DR RefSeq; NP_001138632.1; NM_001145160.1.
DR RefSeq; NP_003281.1; NM_003290.2.
DR UniGene; Hs.631618; -.
DR ProteinModelPortal; P67936; -.
DR SMR; P67936; 5-248.
DR IntAct; P67936; 6.
DR MINT; MINT-4138291; -.
DR PhosphoSite; P67936; -.
DR DMDM; 54039751; -.
DR DOSAC-COBS-2DPAGE; P67936; -.
DR OGP; P07226; -.
DR PaxDb; P67936; -.
DR PeptideAtlas; P67936; -.
DR PRIDE; P67936; -.
DR DNASU; 7171; -.
DR Ensembl; ENST00000300933; ENSP00000300933; ENSG00000167460.
DR Ensembl; ENST00000344824; ENSP00000345230; ENSG00000167460.
DR Ensembl; ENST00000538887; ENSP00000439135; ENSG00000167460.
DR GeneID; 7171; -.
DR KEGG; hsa:7171; -.
DR UCSC; uc002ndj.2; human.
DR CTD; 7171; -.
DR GeneCards; GC19P017322; -.
DR H-InvDB; HIX0022609; -.
DR HGNC; HGNC:12013; TPM4.
DR HPA; CAB004685; -.
DR MIM; 600317; gene.
DR neXtProt; NX_P67936; -.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR PharmGKB; PA36693; -.
DR eggNOG; NOG304012; -.
DR HOVERGEN; HBG107404; -.
DR KO; K10375; -.
DR OMA; EKCKQVE; -.
DR Reactome; REACT_17044; Muscle contraction.
DR ChiTaRS; TPM4; human.
DR GeneWiki; TPM4; -.
DR GenomeRNAi; 7171; -.
DR NextBio; 28104; -.
DR PRO; PR:P67936; -.
DR ArrayExpress; P67936; -.
DR Bgee; P67936; -.
DR CleanEx; HS_TPM4; -.
DR Genevestigator; P67936; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
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:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR InterPro; IPR000533; Tropomyosin.
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;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Metal-binding; Muscle protein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 248 Tropomyosin alpha-4 chain.
FT /FTId=PRO_0000205635.
FT COILED 2 248 By similarity.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 177 177 N6-acetyllysine.
FT MOD_RES 215 215 N6-acetyllysine.
FT VAR_SEQ 1 44 MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERER
FT REK -> MEAIKKKMQMLKLDKENAIDRAEQAEADKKAAED
FT KCKQVEEELTHLQKKLKGTEDELDKYSEDLKDAQEKLELTE
FT KKASD (in isoform 2).
FT /FTId=VSP_006611.
FT VARIANT 204 204 E -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036535.
FT CONFLICT 59 59 V -> F (in Ref. 5; AAH02827).
FT CONFLICT 152 152 L -> S (in Ref. 10; AAA36774).
FT CONFLICT 162 163 KN -> RT (in Ref. 10; AAA36774).
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
//
MIM
600317
*RECORD*
*FIELD* NO
600317
*FIELD* TI
*600317 TROPOMYOSIN 4; TPM4
*FIELD* TX
Vertebrates have at least 4 different tropomyosin genes; in humans, they
read moreare named TPM1 (191010), TPM2 (190990), TPM3 (191030), and TPM4. Both
the muscle and nonmuscle isoforms of the tropomyosins are expressed
through alternative splicing of each of the 4 genes. Laing et al. (1995)
referred to unpublished observations indicating that the TPM4 gene maps
to human chromosome 19. Wilton et al. (1996) developed sequence tagged
sites (STS) for the TPM4 gene. One STS was used to amplify DNA from
somatic cell hybrids to localize TPM4 to chromosome 19. The other, a
product from a long-range PCR, was used directly as a probe to refine
the localization of TPM4 to 19p13.1 by fluorescence in situ
hybridization to metaphase chromosome spreads.
*FIELD* RF
1. Laing, N. G.; Wilton, S. D.; Akkari, P. A.; Dorosz, S.; Boundy,
K.; Kneebone, C.; Blumbergs, P.; White, S.; Watkins, H.; Love, D.
R.; Haan, E.: A mutation in the alpha tropomyosin gene TPM3 associated
with autosomal dominant nemaline myopathy. Nature Genet. 9: 75-79,
1995. Note: Erratum: Nature Genet. 10: 249 only, 1995.
2. Wilton, S. D.; Lim, L.; Dorosz, S. D.; Gunn, H. C.; Eyre, H. J.;
Callen, D. F.; Laing, N. G.: Assignment of the human alpha-tropomyosin
gene TPM4 to band 19p13.1 by fluorescence in situ hybridization. Cytogenet.
Cell Genet. 72: 294-296, 1996.
*FIELD* CD
Victor A. McKusick: 1/20/1995
*FIELD* ED
terry: 05/16/2012
mgross: 4/8/1999
alopez: 7/30/1997
terry: 6/6/1996
carol: 1/20/1995
*RECORD*
*FIELD* NO
600317
*FIELD* TI
*600317 TROPOMYOSIN 4; TPM4
*FIELD* TX
Vertebrates have at least 4 different tropomyosin genes; in humans, they
read moreare named TPM1 (191010), TPM2 (190990), TPM3 (191030), and TPM4. Both
the muscle and nonmuscle isoforms of the tropomyosins are expressed
through alternative splicing of each of the 4 genes. Laing et al. (1995)
referred to unpublished observations indicating that the TPM4 gene maps
to human chromosome 19. Wilton et al. (1996) developed sequence tagged
sites (STS) for the TPM4 gene. One STS was used to amplify DNA from
somatic cell hybrids to localize TPM4 to chromosome 19. The other, a
product from a long-range PCR, was used directly as a probe to refine
the localization of TPM4 to 19p13.1 by fluorescence in situ
hybridization to metaphase chromosome spreads.
*FIELD* RF
1. Laing, N. G.; Wilton, S. D.; Akkari, P. A.; Dorosz, S.; Boundy,
K.; Kneebone, C.; Blumbergs, P.; White, S.; Watkins, H.; Love, D.
R.; Haan, E.: A mutation in the alpha tropomyosin gene TPM3 associated
with autosomal dominant nemaline myopathy. Nature Genet. 9: 75-79,
1995. Note: Erratum: Nature Genet. 10: 249 only, 1995.
2. Wilton, S. D.; Lim, L.; Dorosz, S. D.; Gunn, H. C.; Eyre, H. J.;
Callen, D. F.; Laing, N. G.: Assignment of the human alpha-tropomyosin
gene TPM4 to band 19p13.1 by fluorescence in situ hybridization. Cytogenet.
Cell Genet. 72: 294-296, 1996.
*FIELD* CD
Victor A. McKusick: 1/20/1995
*FIELD* ED
terry: 05/16/2012
mgross: 4/8/1999
alopez: 7/30/1997
terry: 6/6/1996
carol: 1/20/1995