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P09493

- TPM1_HUMAN

UniProt

P09493 - TPM1_HUMAN

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Protein

Tropomyosin alpha-1 chain

Gene
TPM1, C15orf13, TMSA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. actin binding Source: BHF-UCL
  2. cytoskeletal protein binding Source: UniProtKB
  3. structural constituent of cytoskeleton Source: BHF-UCL
  4. structural constituent of muscle Source: ProtInc

GO - Biological processi

  1. cardiac muscle contraction Source: BHF-UCL
  2. cellular component movement Source: UniProtKB
  3. cellular response to reactive oxygen species Source: BHF-UCL
  4. cytoskeleton organization Source: BHF-UCL
  5. in utero embryonic development Source: Ensembl
  6. muscle contraction Source: Reactome
  7. muscle filament sliding Source: BHF-UCL
  8. negative regulation of cell migration Source: BHF-UCL
  9. positive regulation of ATPase activity Source: BHF-UCL
  10. positive regulation of cell adhesion Source: BHF-UCL
  11. positive regulation of heart rate by epinephrine Source: BHF-UCL
  12. positive regulation of stress fiber assembly Source: BHF-UCL
  13. regulation of heart contraction Source: ProtInc
  14. regulation of muscle contraction Source: ProtInc
  15. ruffle organization Source: BHF-UCL
  16. sarcomere organization Source: BHF-UCL
  17. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
  18. wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
Synonyms:C15orf13, TMSA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:12010. TPM1.

Subcellular locationi

GO - Cellular componenti

  1. bleb Source: BHF-UCL
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: Reactome
  4. filamentous actin Source: Ensembl
  5. muscle thin filament tropomyosin Source: ProtInc
  6. ruffle membrane Source: BHF-UCL
  7. sarcomere Source: BHF-UCL
  8. stress fiber Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631A → V in CMH3. 1 Publication
VAR_013135
Natural varianti175 – 1751D → N in CMH3. 4 Publications
Corresponds to variant rs28934270 [ dbSNP | Ensembl ].
VAR_007601
Natural varianti180 – 1801E → G in CMH3. 1 Publication
Corresponds to variant rs28934269 [ dbSNP | Ensembl ].
VAR_007602
Natural varianti180 – 1801E → V in CMH3. 1 Publication
VAR_029452
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401E → K in CMD1Y. 1 Publication
VAR_043986
Natural varianti54 – 541E → K in CMD1Y. 1 Publication
VAR_043987
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti192 – 1921E → K in LVNC9. 1 Publication
VAR_070121
Natural varianti248 – 2481K → E in LVNC9. 1 Publication
VAR_070122

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi283 – 2831S → A: Loss of phosphorylation and decreased formation of actin stress fibers. 1 Publication
Mutagenesisi283 – 2831S → E: Increased formation of actin stress fibers. 1 Publication

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi115196. phenotype.
611878. phenotype.
Orphaneti154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
54260. Left ventricular noncompaction.
PharmGKBiPA36690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei283 – 2831Phosphoserine; by DAPK11 Publication

Post-translational modificationi

Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP09493.
PaxDbiP09493.
PRIDEiP09493.

2D gel databases

UCD-2DPAGEP09493.

PTM databases

PhosphoSiteiP09493.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiP09493.
BgeeiP09493.
GenevestigatoriP09493.

Organism-specific databases

HPAiCAB017698.
HPA000261.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi113021. 60 interactions.
IntActiP09493. 14 interactions.
MINTiMINT-1458755.

Structurei

3D structure databases

ProteinModelPortaliP09493.
SMRiP09493. Positions 1-284.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284 By similarityAdd
BLAST

Domaini

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Sequence similaritiesi

Belongs to the tropomyosin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
KOiK10373.
OMAiRDICNTI.
OrthoDBiEOG7673C8.
PhylomeDBiP09493.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P09493-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL    50
KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
Length:284
Mass (Da):32,709
Last modified:November 1, 1990 - v2
Checksum:iF57139E2B0972F4D
GO
Isoform 2 (identifier: P09493-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:228
Mass (Da):26,680
Checksum:iA6770D102A359A7B
GO
Isoform 3 (identifier: P09493-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:284
Mass (Da):32,876
Checksum:iFDBEEFE342C4ACE3
GO
Isoform 4 (identifier: P09493-4) [UniParc]FASTAAdd to Basket

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

Note: Contains a N6-acetyllysine at position 213.

Show »
Length:284
Mass (Da):32,848
Checksum:iD29DBCA97BC3C6EE
GO
Isoform 5 (identifier: P09493-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:245
Mass (Da):28,385
Checksum:i1255A14D9F26E29F
GO
Isoform 6 (identifier: P09493-6) [UniParc]FASTAAdd to Basket

Also known as: 10, TPM1kappa

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

Show »
Length:284
Mass (Da):32,649
Checksum:i1610BB50FB8EB0F5
GO
Isoform 7 (identifier: P09493-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:284
Mass (Da):32,678
Checksum:i3933E81AC289DAF8
GO
Isoform 8 (identifier: P09493-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:284
Mass (Da):32,817
Checksum:i1EDF6D5109DD335B
GO
Isoform 9 (identifier: P09493-9) [UniParc]FASTAAdd to Basket

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

Note: Gene prediction based on EST data.

Show »
Length:284
Mass (Da):32,737
Checksum:iDA526AA889904540
GO
Isoform 10 (identifier: P09493-10) [UniParc]FASTAAdd to Basket

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.

Show »
Length:284
Mass (Da):32,866
Checksum:iD45DBCA97BC3C6EE
GO

Mass spectrometryi

Isoform 3 : Molecular mass is 32875.93 Da from positions 1 - 284. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401E → K in CMD1Y. 1 Publication
VAR_043986
Natural varianti54 – 541E → K in CMD1Y. 1 Publication
VAR_043987
Natural varianti63 – 631A → V in CMH3. 1 Publication
VAR_013135
Natural varianti175 – 1751D → N in CMH3. 4 Publications
Corresponds to variant rs28934270 [ dbSNP | Ensembl ].
VAR_007601
Natural varianti180 – 1801E → G in CMH3. 1 Publication
Corresponds to variant rs28934269 [ dbSNP | Ensembl ].
VAR_007602
Natural varianti180 – 1801E → V in CMH3. 1 Publication
VAR_029452
Natural varianti192 – 1921E → K in LVNC9. 1 Publication
VAR_070121
Natural varianti248 – 2481K → E in LVNC9. 1 Publication
VAR_070122

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080MDAIK…KKATD → MCRLRIFLRTASSEHLHERK LRET in isoform 2. VSP_006576Add
BLAST
Alternative sequencei1 – 8080MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGTLQRELDHERK LRET in isoform 5. VSP_017498Add
BLAST
Alternative sequencei41 – 8040DELVS…KKATD → EDIAAKEKLLRVSEDERDRV LEELHKAEDSLLAAEEAAAK in isoform 6 and isoform 7. VSP_036064Add
BLAST
Alternative sequencei41 – 5313DELVS…KLKGT → EDIAAKEKLLRVS in isoform 8. VSP_047297Add
BLAST
Alternative sequencei57 – 8024LDKYS…KKATD → RDRVLEELHKAEDSLLAAEE AAAK in isoform 8. VSP_047298Add
BLAST
Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDSDLESIN AAED in isoform 2. VSP_006578Add
BLAST
Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 3 and isoform 4. VSP_006577Add
BLAST
Alternative sequencei189 – 1924KCAE → QVRQ in isoform 8 and isoform 10. VSP_047299
Alternative sequencei196 – 21217ELKTV…EAQAE → QLRIMDQTLKALMAAED in isoform 8 and isoform 10. VSP_047300Add
BLAST
Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2, isoform 3, isoform 7, isoform 8 and isoform 9. VSP_006579Add
BLAST
Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYQQLEQNRRLTNELKLAL NED in isoform 5. VSP_017499Add
BLAST
Alternative sequencei284 – 2841I → M in isoform 10. VSP_047301

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091A → V in CAA30930. 1 Publication
Sequence conflicti203 – 2031N → D in AAT68294. 1 Publication
Sequence conflicti203 – 2031N → D in AAT68295. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10181.1. [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]
PIRiA27674.
A27678. A25825.
S05585.
RefSeqiNP_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]
UniGeneiHs.133892.
Hs.602995.

Genome annotation databases

EnsembliENST00000267996; 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]
GeneIDi7168.
KEGGihsa:7168.
UCSCiuc002alg.3. human. [P09493-1]
uc002alh.3. human.
uc002ali.3. human.
uc002alj.3. human. [P09493-7]
uc002all.3. human.
uc010uie.2. human. [P09493-6]

Polymorphism databases

DMDMi136092.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10181.1. [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 ]
PIRi A27674.
A27678. A25825.
S05585.
RefSeqi NP_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 ]
UniGenei Hs.133892.
Hs.602995.

3D structure databases

ProteinModelPortali P09493.
SMRi P09493. Positions 1-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113021. 60 interactions.
IntActi P09493. 14 interactions.
MINTi MINT-1458755.

PTM databases

PhosphoSitei P09493.

Polymorphism databases

DMDMi 136092.

2D gel databases

UCD-2DPAGE P09493.

Proteomic databases

MaxQBi P09493.
PaxDbi P09493.
PRIDEi P09493.

Protocols and materials databases

DNASUi 7168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000267996 ; 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 ]
GeneIDi 7168.
KEGGi hsa:7168.
UCSCi uc002alg.3. human. [P09493-1 ]
uc002alh.3. human.
uc002ali.3. human.
uc002alj.3. human. [P09493-7 ]
uc002all.3. human.
uc010uie.2. human. [P09493-6 ]

Organism-specific databases

CTDi 7168.
GeneCardsi GC15P063334.
GeneReviewsi TPM1.
HGNCi HGNC:12010. TPM1.
HPAi CAB017698.
HPA000261.
MIMi 115196. phenotype.
191010. gene.
611878. phenotype.
neXtProti NX_P09493.
Orphaneti 154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
54260. Left ventricular noncompaction.
PharmGKBi PA36690.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304012.
HOGENOMi HOG000231521.
HOVERGENi HBG107404.
KOi K10373.
OMAi RDICNTI.
OrthoDBi EOG7673C8.
PhylomeDBi P09493.
TreeFami TF351519.

Enzyme and pathway databases

Reactomei REACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSi TPM1. human.
GeneWikii TPM1.
GenomeRNAii 7168.
NextBioi 28070.
PROi P09493.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09493.
Bgeei P09493.
Genevestigatori P09493.

Family and domain databases

InterProi IPR000533. Tropomyosin.
[Graphical view ]
Pfami PF00261. Tropomyosin. 1 hit.
[Graphical view ]
PRINTSi PR00194. TROPOMYOSIN.
PROSITEi PS00326. TROPOMYOSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiTPM1_HUMAN
AccessioniPrimary (citable) accession number: P09493
Secondary accession number(s): B7Z5T7
, D9YZV2, D9YZV3, D9YZV8, P09494, P10469, Q6DV89, Q6DV90, Q7Z6L8, Q86W64, Q96IK2, Q9UCI1, Q9UCI2, Q9UCY9, Q9Y427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: September 3, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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