P09493 (TPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tropomyosin alpha-1 chain

Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1

Gene names

Name:	TPM1
Synonyms:	C15orf13, TMSA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subunit structure	Heterodimer of an alpha and a beta chain By similarity. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Detected in primary breast cancer tissues but undetectable in normal breast tissues in Sudanese patients. Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues. Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle. Ref.4 Ref.12
Domain	The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Post-translational modification	Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells. Ref.11
Involvement in disease	Defects in TPM1 are the cause of familial hypertrophic cardiomyopathy type 3 (CMH3) [MIM:115196]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Defects in TPM1 are the cause of cardiomyopathy dilated type 1Y (CMD1Y) [MIM:611878]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.18
Sequence similarities	Belongs to the tropomyosin family.
Mass spectrometry	Isoform 3: Molecular mass is 32875.93 Da from positions 1 - 284. Determined by MALDI. Ref.10

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Disease	Cardiomyopathy Disease mutation
Domain	Coiled coil
Ligand	Actin-binding
Molecular function	Muscle protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cardiac muscle contraction Inferred from mutant phenotype. Source: BHF-UCL cellular response to reactive oxygen species Inferred from expression pattern. Source: BHF-UCL muscle filament sliding Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cell migration Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of ATPase activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of heart rate by epinephrine Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of stress fiber assembly Inferred from sequence or structural similarity. Source: BHF-UCL regulation of muscle contraction Traceable author statement. Source: ProtInc ruffle organization Inferred from sequence or structural similarity. Source: BHF-UCL sarcomere organization Inferred from mutant phenotype Ref.18. Source: BHF-UCL ventricular cardiac muscle tissue morphogenesis Inferred from mutant phenotype. Source: BHF-UCL wound healing Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	bleb Inferred from mutant phenotype. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome muscle thin filament tropomyosin Traceable author statement. Source: ProtInc ruffle membrane Inferred from direct assay. Source: BHF-UCL stress fiber Inferred from direct assay. Source: BHF-UCL
Molecular function	actin binding Traceable author statement. Source: BHF-UCL structural constituent of cytoskeleton Traceable author statement. Source: BHF-UCL structural constituent of muscle Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P09493-1)

Also known as: Skeletal muscle; TPM1alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P09493-2)

Also known as: Smooth muscle;

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MCRLRIFLRTASSEHLHERKLRET
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDSDLESINAAED
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

Note: Incomplete sequence.

Isoform 3 (identifier: P09493-3)

Also known as: Fibroblast; TM3;

The sequence of this isoform differs from the canonical sequence as follows:
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

Isoform 4 (identifier: P09493-4)

The sequence of this isoform differs from the canonical sequence as follows:
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED

Isoform 5 (identifier: P09493-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDHERKLRET
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYQQLEQNRRLTNELKLALNED

Isoform 6 (identifier: P09493-6)

Also known as: 10; TPM1kappa;

The sequence of this isoform differs from the canonical sequence as follows:
     41-80: DELVSLQKKL...LELAEKKATD → EDIAAKEKLL...LLAAEEAAAK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 284	284	Tropomyosin alpha-1 chain		PRO_0000205620
Regions
	Coiled coil	1 – 284	284	By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine
	Modified residue	283	1	Phosphoserine; by DAPK1 Ref.11
	Cross-link	77		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	1 – 80	80	MDAIK…KKATD → MCRLRIFLRTASSEHLHERK LRET in isoform 2.		VSP_006576
	Alternative sequence	1 – 80	80	MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGTLQRELDHERK LRET in isoform 5.		VSP_017498
	Alternative sequence	41 – 80	40	DELVS…KKATD → EDIAAKEKLLRVSEDERDRV LEELHKAEDSLLAAEEAAAK in isoform 6.		VSP_036064
	Alternative sequence	189 – 212	24	KCAEL…EAQAE → QVRQLEEQLRIMDSDLESIN AAED in isoform 2.		VSP_006578
	Alternative sequence	189 – 212	24	KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 3 and isoform 4.		VSP_006577
	Alternative sequence	258 – 284	27	DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2 and isoform 3.		VSP_006579
	Alternative sequence	259 – 284	26	ELYAQ…DMTSI → QLYQQLEQNRRLTNELKLAL NED in isoform 5.		VSP_017499
	Natural variant	40	1	E → K in CMD1Y. Ref.18		VAR_043986
	Natural variant	54	1	E → K in CMD1Y. Ref.18		VAR_043987
	Natural variant	63	1	A → V in CMH3. Ref.15		VAR_013135
	Natural variant	175	1	D → N in CMH3. Ref.14 Ref.15 Ref.16 Ref.17 Corresponds to variant rs28934270 [ dbSNP | Ensembl ].		VAR_007601
	Natural variant	180	1	E → G in CMH3. Ref.14 Corresponds to variant rs28934269 [ dbSNP | Ensembl ].		VAR_007602
	Natural variant	180	1	E → V in CMH3. Ref.19		VAR_029452
Experimental info
	Mutagenesis	283	1	S → A: Loss of phosphorylation and decreased formation of actin stress fibers. Ref.11
	Mutagenesis	283	1	S → E: Increased formation of actin stress fibers. Ref.11
	Sequence conflict	109	1	A → V in CAA30930. Ref.8
	Sequence conflict	203	1	N → D in AAT68294. Ref.4
	Sequence conflict	203	1	N → D in AAT68295. Ref.4
	Sequence conflict	284	1	I → M in AAA61226. Ref.3
	Sequence conflict	284	1	I → M in AAH07433. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Skeletal muscle) (TPM1alpha) [UniParc]. Last modified November 1, 1990. Version 2. Checksum: F57139E2B0972F4D	FASTA	284	32,709
	10 20 30 40 50 60 MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 70 80 90 100 110 120 SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 190 200 210 220 230 240 ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE 250 260 270 280 FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
	Isoform 2 (Smooth muscle) [UniParc]. Checksum: A6770D102A359A7B	FASTA	228	26,680
	10 20 30 40 50 60 MCRLRIFLRT ASSEHLHERK LRETAEADVA SLNRRIQLVE EELDRAQERL ATALQKLEEA 70 80 90 100 110 120 EKAADESERG MKVIESRAQK DEEKMEIQEI QLKEAKHIAE DADRKYEEVA RKLVIIESDL 130 140 150 160 170 180 ERAEERAELS EGQVRQLEEQ LRIMDSDLES INAAEDKYSQ KEDRYEEEIK VLSDKLKEAE 190 200 210 220 TRAEFAERSV TKLEKSIDDL EEKVAHAKEE NLSMHQMLDQ TLLELNNM
	Isoform 3 (Fibroblast) (TM3) [UniParc]. Checksum: FDBEEFE342C4ACE3	FASTA	284	32,876
	10 20 30 40 50 60 MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 70 80 90 100 110 120 SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 190 200 210 220 230 240 ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE 250 260 270 280 FAERSVTKLE KSIDDLEEKV AHAKEENLSM HQMLDQTLLE LNNM
	Isoform 4 [UniParc]. Checksum: D29DBCA97BC3C6EE	FASTA	284	32,848
	10 20 30 40 50 60 MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 70 80 90 100 110 120 SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 190 200 210 220 230 240 ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE 250 260 270 280 FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
	Isoform 5 [UniParc]. Checksum: 1255A14D9F26E29F	FASTA	245	28,385
	10 20 30 40 50 60 MAGSSSLEAV RRKIRSLQEQ ADAAEERAGT LQRELDHERK LRETAEADVA SLNRRIQLVE 70 80 90 100 110 120 EELDRAQERL ATALQKLEEA EKAADESERG MKVIESRAQK DEEKMEIQEI QLKEAKHIAE 130 140 150 160 170 180 DADRKYEEVA RKLVIIESDL ERAEERAELS EGKCAELEEE LKTVTNNLKS LEAQAEKYSQ 190 200 210 220 230 240 KEDRYEEEIK VLSDKLKEAE TRAEFAERSV TKLEKSIDDL EDQLYQQLEQ NRRLTNELKL ALNED
	Isoform 6 (10) (TPM1kappa) [UniParc]. Checksum: 1610BB50FB8EB0F5	FASTA	284	32,649
	10 20 30 40 50 60 MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE EDIAAKEKLL RVSEDERDRV 70 80 90 100 110 120 LEELHKAEDS LLAAEEAAAK AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 190 200 210 220 230 240 ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE 250 260 270 280 FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Relation of streptococcal M protein with human and rabbit tropomyosin: the complete amino acid sequence of human cardiac alpha tropomyosin, a highly conserved contractile protein." Mische S.M., Manjula B.N., Fischetti V.A. Biochem. Biophys. Res. Commun. 142:813-818(1987) [PubMed: 3548719] [Abstract] Cited for: PROTEIN SEQUENCE (ISOFORM 1).
[2]	"Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts." Lin C.-S., Leavitt J. Mol. Cell. Biol. 8:160-168(1988) [PubMed: 3336357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Fibroblast.
[3]	"Human hTM alpha gene: expression in muscle and nonmuscle tissue." McLeod A.R., Gooding C. Mol. Cell. Biol. 8:433-440(1988) [PubMed: 3336363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[4]	"Expression of a novel cardiac-specific tropomyosin isoform in humans." Denz C.R., Narshi A., Zajdel R.W., Dube D.K. Biochem. Biophys. Res. Commun. 320:1291-1297(2004) [PubMed: 15249230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), TISSUE SPECIFICITY. Tissue: Heart.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Tongue.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). Tissue: Brain, Hippocampus and Placenta.
[8]	"Evolution of tropomyosin functional domains: differential splicing and genomic constraints." Colote S., Widada J.S., Ferraz C., Bonhomme F., Marti J., Liautard J.-P. J. Mol. Evol. 27:228-235(1988) [PubMed: 3138425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2). Tissue: Liver.
[9]	"Autoimmunity to cytoskeletal protein tropomyosin. A clue to the pathogenetic mechanism for ulcerative colitis." Das K.M., Dasgupta A., Mandal A., Geng X. J. Immunol. 150:2487-2493(1993) [PubMed: 8450225] [Abstract] Cited for: PROTEIN SEQUENCE OF 134-149 AND 153-167. Tissue: Colon.
[10]	"Cluster analysis of an extensive human breast cancer cell line protein expression map database." Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J. Proteomics 2:212-223(2002) [PubMed: 11840567] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Mammary cancer.
[11]	"DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress." Houle F., Poirier A., Dumaresq J., Huot J. J. Cell Sci. 120:3666-3677(2007) [PubMed: 17895359] [Abstract] Cited for: PHOSPHORYLATION AT SER-283, MUTAGENESIS OF SER-283.
[12]	Ahamed M.E. Submitted (APR-2007) to UniProtKB Cited for: TISSUE SPECIFICITY, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere." Thierfelder L., Watkins H., Macrae C., Lamas R., McKenna W.J., Vosberg H.-P., Seidman J.G., Seidman C.E. Cell 77:701-712(1994) [PubMed: 8205619] [Abstract] Cited for: VARIANTS CMH3 ASN-175 AND GLY-180.
[15]	"Novel missense mutation in alpha-tropomyosin gene found in Japanese patients with hypertrophic cardiomyopathy." Nakajima-Taniguchi C., Matsui H., Nagata S., Kishimoto T., Yamauchi-Takihara K. J. Mol. Cell. Cardiol. 27:2053-2058(1995) [PubMed: 8523464] [Abstract] Cited for: VARIANTS CMH3 VAL-63 AND ASN-175.
[16]	"Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy." Watkins H., McKenna W.J., Thierfelder L., Suk H.J., Anan R., O'Donoghue A., Spirito P., Matsumori A., Moravec C.S., Seidman J.G., Seidman C.E. N. Engl. J. Med. 332:1058-1064(1995) [PubMed: 7898523] [Abstract] Cited for: VARIANT CMH3 ASN-175.
[17]	"The cardiac beta-myosin heavy chain gene is not the predominant gene for hypertrophic cardiomyopathy in the Finnish population." Jaeaeskelaeinen P., Soranta M., Miettinen R., Saarinen L., Pihlajamaeki J., Silvennoinen K., Tikanoja T., Laakso M., Kuusisto J. J. Am. Coll. Cardiol. 32:1709-1716(1998) [PubMed: 9822100] [Abstract] Cited for: VARIANT CMH3 ASN-175.
[18]	"Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy." Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V. J. Mol. Cell. Cardiol. 33:723-732(2001) [PubMed: 11273725] [Abstract] Cited for: VARIANTS CMD1Y LYS-40 AND LYS-54.
[19]	"Mutation spectrum in a large cohort of unrelated consecutive patients with hypertrophic cardiomyopathy." Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J., Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V. Clin. Genet. 64:339-349(2003) [PubMed: 12974739] [Abstract] Cited for: VARIANT CMH3 VAL-180.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19267 mRNA. Translation: AAA36771.1. M19713 mRNA. Translation: AAA61225.1. M19714 mRNA. Translation: AAA61226.1. M19715 mRNA. Translation: AAA61227.1. AY640414 mRNA. Translation: AAT68294.1. AY640415 mRNA. Translation: AAT68295.1. AK299387 mRNA. Translation: BAH13023.1. CH471082 Genomic DNA. Translation: EAW77623.1. BC007433 mRNA. Translation: AAH07433.1. BC050473 mRNA. Translation: AAH50473.1. BC053545 mRNA. Translation: AAH53545.1. X12369 mRNA. Translation: CAA30930.1.
IPI	IPI00014581. IPI00216135. IPI00296039. IPI00745267. IPI00915324. IPI01012191.
PIR	A27674. A25825. A27678. S05585.
RefSeq	NP_000357.3. NM_000366.5. NP_001018005.1. NM_001018005.1. NP_001018006.1. NM_001018006.1. NP_001018008.1. NM_001018008.1.
UniGene	Hs.133892.
3D structure databases
ProteinModelPortal	P09493.
SMR	P09493. Positions 1-284.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09493. 5 interactions.
MINT	MINT-1150102.
STRING	P09493.
PTM databases
PhosphoSite	P09493.
Polymorphism databases
DMDM	136092.
2D gel databases
UCD-2DPAGE	P09493.
Proteomic databases
PRIDE	P09493.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000403994; ENSP00000385107; ENSG00000140416.
GeneID	7168.
KEGG	hsa:7168.
UCSC	uc002alg.1. human. uc002alh.1. human. uc002alk.1. human.
Organism-specific databases
CTD	7168.
GeneCards	GC15P063334.
HGNC	HGNC:12010. TPM1.
HPA	CAB017698. HPA000261.
MIM	115196. phenotype. 191010. gene. 611878. phenotype.
neXtProt	NX_P09493.
Orphanet	154. Familial isolated dilated cardiomyopathy. 155. Familial isolated hypertrophic cardiomyopathy. 54260. Left ventricular noncompaction.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074494.
HOVERGEN	HBG107404.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P09493.
Bgee	P09493.
Genevestigator	P09493.
GermOnline	ENSG00000140416. Homo sapiens.
Family and domain databases
InterPro	IPR000533. Tropomyosin. [Graphical view]
KO	K10373.
Pfam	PF00261. Tropomyosin. 1 hit. [Graphical view]
PRINTS	PR00194. TROPOMYOSIN.
PROSITE	PS00326. TROPOMYOSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	28070.
SOURCE	Search...

Entry information

Entry name

TPM1_HUMAN

Accession

Primary (citable) accession number: P09493
Secondary accession number(s): B7Z5T7 , P09494, P10469, Q6DV89, Q6DV90, Q7Z6L8, Q86W64, Q96IK2, Q9UCI1, Q9UCI2, Q9UCY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.