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P09493 (TPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene names
Name:TPM1
Synonyms:C15orf13, TMSA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeleton.

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.15

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.14

Involvement in disease

Cardiomyopathy, familial hypertrophic 3 (CMH3) [MIM:115196]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.21 Ref.22 Ref.24

Cardiomyopathy, dilated 1Y (CMD1Y) [MIM:611878]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25

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.13

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DiseaseCardiomyopathy
Disease mutation
   DomainCoiled coil
   LigandActin-binding
   Molecular functionMuscle protein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle contraction

Inferred from mutant phenotype PubMed 11136687. Source: BHF-UCL

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from expression pattern PubMed 12686598. Source: BHF-UCL

cytoskeleton organization

Traceable author statement PubMed 12686598. Source: BHF-UCL

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Traceable author statement. Source: Reactome

muscle filament sliding

Inferred from sequence or structural similarity PubMed 11136687. Source: BHF-UCL

negative regulation of cell migration

Inferred from sequence or structural similarity PubMed 15897890. Source: BHF-UCL

positive regulation of ATPase activity

Inferred from sequence or structural similarity PubMed 11136687. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from sequence or structural similarity PubMed 17721995. Source: BHF-UCL

positive regulation of heart rate by epinephrine

Inferred from sequence or structural similarity PubMed 17556658. Source: BHF-UCL

positive regulation of stress fiber assembly

Inferred from sequence or structural similarity PubMed 15897890. Source: BHF-UCL

regulation of heart contraction

Traceable author statement Ref.19. Source: ProtInc

regulation of muscle contraction

Traceable author statement Ref.3. Source: ProtInc

ruffle organization

Inferred from sequence or structural similarity PubMed 15897890. Source: BHF-UCL

sarcomere organization

Inferred from mutant phenotype Ref.23. Source: BHF-UCL

ventricular cardiac muscle tissue morphogenesis

Inferred from mutant phenotype PubMed 11136687. Source: BHF-UCL

wound healing

Inferred from sequence or structural similarity PubMed 17721995. Source: BHF-UCL

   Cellular_componentbleb

Inferred from mutant phenotype PubMed 12686598. Source: BHF-UCL

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

filamentous actin

Inferred from electronic annotation. Source: Ensembl

muscle thin filament tropomyosin

Traceable author statement Ref.19. Source: ProtInc

ruffle membrane

Inferred from direct assay PubMed 12686598. Source: BHF-UCL

sarcomere

Traceable author statement PubMed 16754800. Source: BHF-UCL

stress fiber

Inferred from direct assay PubMed 12686598. Source: BHF-UCL

   Molecular_functionactin binding

Traceable author statement PubMed 12686598. Source: BHF-UCL

cytoskeletal protein binding

Inferred from physical interaction PubMed 17987659. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement PubMed 12686598. Source: BHF-UCL

structural constituent of muscle

Traceable author statement Ref.19. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 10 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
Note: Contains a N6-acetyllysine at position 213.
Isoform 4 (identifier: P09493-4)

The sequence of this isoform differs from the canonical sequence as follows:
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
Note: Contains a N6-acetyllysine at position 213.
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
Isoform 7 (identifier: P09493-7)

The sequence of this isoform differs from the canonical sequence as follows:
     41-80: DELVSLQKKL...LELAEKKATD → EDIAAKEKLL...LLAAEEAAAK
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM
Note: No experimental confirmation available.
Isoform 8 (identifier: P09493-8)

The sequence of this isoform differs from the canonical sequence as follows:
     41-53: DELVSLQKKLKGT → EDIAAKEKLLRVS
     57-80: LDKYSEALKDAQEKLELAEKKATD → RDRVLEELHKAEDSLLAAEEAAAK
     189-192: KCAE → QVRQ
     196-212: ELKTVTNNLKSLEAQAE → QLRIMDQTLKALMAAED
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM
Note: Gene prediction based on EST data. Contains a N6-acetyllysine at position 213.
Isoform 9 (identifier: P09493-9)

The sequence of this isoform differs from the canonical sequence as follows:
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM
Note: Gene prediction based on EST data.
Isoform 10 (identifier: P09493-10)

The sequence of this isoform differs from the canonical sequence as follows:
     189-192: KCAE → QVRQ
     196-212: ELKTVTNNLKSLEAQAE → QLRIMDQTLKALMAAED
     284-284: I → M
Note: No experimental confirmation available. Contains a N6-acetyllysine at position 213.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin alpha-1 chain
PRO_0000205620

Regions

Coiled coil1 – 284284 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1
Modified residue2831Phosphoserine; by DAPK1 Ref.14
Cross-link77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1 – 8080MDAIK…KKATD → MCRLRIFLRTASSEHLHERK LRET in isoform 2.
VSP_006576
Alternative sequence1 – 8080MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGTLQRELDHERK LRET in isoform 5.
VSP_017498
Alternative sequence41 – 8040DELVS…KKATD → EDIAAKEKLLRVSEDERDRV LEELHKAEDSLLAAEEAAAK in isoform 6 and isoform 7.
VSP_036064
Alternative sequence41 – 5313DELVS…KLKGT → EDIAAKEKLLRVS in isoform 8.
VSP_047297
Alternative sequence57 – 8024LDKYS…KKATD → RDRVLEELHKAEDSLLAAEE AAAK in isoform 8.
VSP_047298
Alternative sequence189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDSDLESIN AAED in isoform 2.
VSP_006578
Alternative sequence189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 3 and isoform 4.
VSP_006577
Alternative sequence189 – 1924KCAE → QVRQ in isoform 8 and isoform 10.
VSP_047299
Alternative sequence196 – 21217ELKTV…EAQAE → QLRIMDQTLKALMAAED in isoform 8 and isoform 10.
VSP_047300
Alternative sequence258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2, isoform 3, isoform 7, isoform 8 and isoform 9.
VSP_006579
Alternative sequence259 – 28426ELYAQ…DMTSI → QLYQQLEQNRRLTNELKLAL NED in isoform 5.
VSP_017499
Alternative sequence2841I → M in isoform 10.
VSP_047301
Natural variant401E → K in CMD1Y. Ref.23
VAR_043986
Natural variant541E → K in CMD1Y. Ref.23
VAR_043987
Natural variant631A → V in CMH3. Ref.20
VAR_013135
Natural variant1751D → N in CMH3. Ref.19 Ref.20 Ref.21 Ref.22
Corresponds to variant rs28934270 [ dbSNP | Ensembl ].
VAR_007601
Natural variant1801E → G in CMH3. Ref.19
Corresponds to variant rs28934269 [ dbSNP | Ensembl ].
VAR_007602
Natural variant1801E → V in CMH3. Ref.24
VAR_029452
Natural variant1921E → K in LVNC9. Ref.25
VAR_070121
Natural variant2481K → E in LVNC9. Ref.25
VAR_070122

Experimental info

Mutagenesis2831S → A: Loss of phosphorylation and decreased formation of actin stress fibers. Ref.14
Mutagenesis2831S → E: Increased formation of actin stress fibers. Ref.14
Sequence conflict1091A → V in CAA30930. Ref.11
Sequence conflict2031N → D in AAT68294. Ref.4
Sequence conflict2031N → D in AAT68295. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Skeletal muscle) (TPM1alpha) [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: F57139E2B0972F4D

FASTA28432,709
        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 

« Hide

Isoform 2 (Smooth muscle) [UniParc].

Checksum: A6770D102A359A7B
Show »

FASTA22826,680
Isoform 3 (Fibroblast) (TM3) [UniParc].

Checksum: FDBEEFE342C4ACE3
Show »

FASTA28432,876
Isoform 4 [UniParc].

Checksum: D29DBCA97BC3C6EE
Show »

FASTA28432,848
Isoform 5 [UniParc].

Checksum: 1255A14D9F26E29F
Show »

FASTA24528,385
Isoform 6 (10) (TPM1kappa) [UniParc].

Checksum: 1610BB50FB8EB0F5
Show »

FASTA28432,649
Isoform 7 [UniParc].

Checksum: 3933E81AC289DAF8
Show »

FASTA28432,678
Isoform 8 [UniParc].

Checksum: 1EDF6D5109DD335B
Show »

FASTA28432,817
Isoform 9 [UniParc].

Checksum: DA526AA889904540
Show »

FASTA28432,737
Isoform 10 [UniParc].

Checksum: D45DBCA97BC3C6EE
Show »

FASTA28432,866

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT MET-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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Tongue.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Uterus.
[7]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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. expand/collapse author list , 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].
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
Tissue: Brain, Hippocampus and Placenta.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2).
Tissue: Liver.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 134-149 AND 153-167.
Tissue: Colon.
[13]"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] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-283, MUTAGENESIS OF SER-283.
[15]Ahamed M.E.
Submitted (APR-2007) to UniProtKB
Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213 (ISOFORMS 10; 3; 4 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CMH3 ASN-175 AND GLY-180.
[20]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CMH3 VAL-63 AND ASN-175.
[21]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CMH3 ASN-175.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CMH3 ASN-175.
[23]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1Y LYS-40 AND LYS-54.
[24]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CMH3 VAL-180.
[25]"Sarcomere gene mutations in isolated left ventricular noncompaction cardiomyopathy do not predict clinical phenotype."
Probst S., Oechslin E., Schuler P., Greutmann M., Boye P., Knirsch W., Berger F., Thierfelder L., Jenni R., Klaassen S.
Circ. Cardiovasc. Genet. 4:367-374(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LVNC9 LYS-192 AND GLU-248.
+Additional computationally mapped references.

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.
AL050179 mRNA. Translation: CAB43309.2.
GU324929 Genomic DNA. Translation: ADL14500.1.
GU324930 Genomic DNA. Translation: ADL14501.1.
GU324933 Genomic DNA. Translation: ADL14504.1.
GU324935 Genomic DNA. Translation: ADL14506.1.
AC079328 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77619.1.
CH471082 Genomic DNA. Translation: EAW77622.1.
CH471082 Genomic DNA. Translation: EAW77623.1.
CH471082 Genomic DNA. Translation: EAW77627.1.
CH471082 Genomic DNA. Translation: EAW77628.1.
BC007433 mRNA. Translation: AAH07433.1.
BC050473 mRNA. Translation: AAH50473.1.
BC053545 mRNA. Translation: AAH53545.1.
X12369 mRNA. Translation: CAA30930.1.
CCDSCCDS10181.1. [P09493-10]
CCDS32262.1. [P09493-7]
CCDS32263.1. [P09493-3]
CCDS32264.1. [P09493-5]
CCDS45273.1. [P09493-1]
CCDS58368.1. [P09493-8]
CCDS58369.1. [P09493-9]
PIRA27674.
A25825. A27678.
S05585.
RefSeqNP_000357.3. NM_000366.5. [P09493-10]
NP_001018004.1. NM_001018004.1. [P09493-9]
NP_001018005.1. NM_001018005.1. [P09493-1]
NP_001018006.1. NM_001018006.1. [P09493-3]
NP_001018007.1. NM_001018007.1. [P09493-7]
NP_001018008.1. NM_001018008.1. [P09493-5]
NP_001018020.1. NM_001018020.1. [P09493-8]
XP_005254700.1. XM_005254643.1. [P09493-6]
XP_006720730.1. XM_006720667.1. [P09493-4]
XP_006720731.1. XM_006720668.1. [P09493-10]
UniGeneHs.133892.
Hs.602995.

3D structure databases

ProteinModelPortalP09493.
SMRP09493. Positions 1-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113021. 59 interactions.
IntActP09493. 14 interactions.
MINTMINT-1458755.

PTM databases

PhosphoSiteP09493.

Polymorphism databases

DMDM136092.

2D gel databases

UCD-2DPAGEP09493.

Proteomic databases

MaxQBP09493.
PaxDbP09493.
PRIDEP09493.

Protocols and materials databases

DNASU7168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267996; ENSP00000267996; ENSG00000140416. [P09493-7]
ENST00000288398; ENSP00000288398; ENSG00000140416. [P09493-10]
ENST00000334895; ENSP00000334624; ENSG00000140416. [P09493-5]
ENST00000358278; ENSP00000351022; ENSG00000140416. [P09493-3]
ENST00000403994; ENSP00000385107; ENSG00000140416. [P09493-1]
ENST00000559397; ENSP00000452879; ENSG00000140416. [P09493-8]
ENST00000559556; ENSP00000453941; ENSG00000140416. [P09493-9]
GeneID7168.
KEGGhsa:7168.
UCSCuc002alg.3. human. [P09493-1]
uc002alh.3. human.
uc002alj.3. human. [P09493-7]
uc010uie.2. human. [P09493-6]

Organism-specific databases

CTD7168.
GeneCardsGC15P063334.
GeneReviewsTPM1.
HGNCHGNC:12010. TPM1.
HPACAB017698.
HPA000261.
MIM115196. phenotype.
191010. gene.
611878. phenotype.
neXtProtNX_P09493.
Orphanet154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
54260. Left ventricular noncompaction.
PharmGKBPA36690.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304012.
HOGENOMHOG000231521.
HOVERGENHBG107404.
KOK10373.
OMARDICNTI.
OrthoDBEOG7673C8.
PhylomeDBP09493.
TreeFamTF351519.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP09493.
BgeeP09493.
GenevestigatorP09493.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPM1. human.
GeneWikiTPM1.
GenomeRNAi7168.
NextBio28070.
PROP09493.
SOURCESearch...

Entry information

Entry nameTPM1_HUMAN
AccessionPrimary (citable) accession number: P09493
Secondary accession number(s): B7Z5T7 expand/collapse secondary AC list , D9YZV2, D9YZV3, D9YZV8, P09494, P10469, Q6DV89, Q6DV90, Q7Z6L8, Q86W64, Q96IK2, Q9UCI1, Q9UCI2, Q9UCY9, Q9Y427
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM