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RAT:TPM1

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Species (Taxon ID) Rattus norvegicus (Rat). (10116)
Gene Name(s) Tpm1 (synonyms: Alpha-tm, Tpma)
Protein Name(s) Tropomyosin alpha-1 chain

Alpha-tropomyosin Tropomyosin-1

External Links
UniProt P04692
EMBL M15474
M15472
M15473
M16432
M16433
M18135
M16432
M15472
M16433
M15473
M18135
M16432
M16433
M18135
M16432
M15472
M16433
X02411
M34135
M34134
M34136
M34137
M34138
M60666
M60668
M60669
X02412
PIR A34787
A39816
B27407
B34787
C34787
C39816
D39816
RefSeq NP_001029241.1
NP_001029244.1
NP_001029245.1
NP_001029246.1
NP_001029247.1
NP_001288265.1
NP_001288665.1
NP_062004.1
UniGene Rn.87540
PDB 1IHQ
1MV4
1TMZ
2B9C
2G9J
3AZD
PDBsum 1IHQ
1MV4
1TMZ
2B9C
2G9J
3AZD
ProteinModelPortal P04692
SMR P04692
BioGrid 246968
DIP DIP-29020N
IntAct P04692
PhosphoSite P04692
PaxDb P04692
PRIDE P04692
Ensembl ENSRNOT00000024575
ENSRNOT00000024617
ENSRNOT00000048044
GeneID 24851
KEGG rno:24851
CTD 7168
RGD 3898
eggNOG NOG304012
GeneTree ENSGT00550000074494
HOVERGEN HBG107404
InParanoid P04692
KO K10373
PhylomeDB P04692
TreeFam TF351519
Reactome REACT_224772
REACT_234304
EvolutionaryTrace P04692
NextBio 604620
Proteomes UP000002494
ExpressionAtlas P04692
Genevestigator P04692
GO GO:0005737
GO:0005856
GO:0043234
GO:0003779
GO:0051015
GO:0042803
GO:0047485
GO:0051693
GO:0060048
GO:0006936
GO:0030049
GO:0030336
GO:0032781
GO:0045785
GO:0051496
GO:0043462
GO:0031529
GO:0042060
InterPro IPR000533
Pfam PF00261
PRINTS PR00194
PROSITE PS00326

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0042802

identical protein binding

PMID:22812662[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:22812662[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046982

protein heterodimerization activity

PMID:22812662[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:22812662[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

PMID:15475586[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9DEA6

F

Seeded From UniProt

complete

part_of

GO:0015629

actin cytoskeleton

PMID:7568216[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:7568216[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046982

protein heterodimerization activity

PMID:7568216[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:7568216[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:7568216[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051496

positive regulation of stress fiber assembly

PMID:15897890[4]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0045785

positive regulation of cell adhesion

PMID:17721995[5]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0042060

wound healing

PMID:17721995[5]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0032781

positive regulation of ATPase activity

PMID:11136687[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031529

ruffle organization

PMID:15897890[4]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0030336

negative regulation of cell migration

PMID:15897890[4]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0030049

muscle filament sliding

PMID:11136687[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0060048

cardiac muscle contraction

PMID:14551059[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051693

actin filament capping

PMID:15779917[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:11329279[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0047485

protein N-terminus binding

PMID:15779917[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043462

regulation of ATPase activity

PMID:19041430[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:16420482[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:15823548[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0032781

positive regulation of ATPase activity

PMID:11329279[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003779

actin binding

PMID:14640678[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003779

actin binding

PMID:19041430[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0060048

cardiac muscle contraction

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:98809
PANTHER:PTN000751039
RGD:3898
UniProtKB:P09493

P

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0003721
MGI:MGI:1890149
MGI:MGI:2449202
MGI:MGI:98809
PANTHER:PTN000443979
PomBase:SPAC27F1.02c
RGD:1559479
RGD:3898
RGD:3899
WB:WBGene00002978

F

Seeded From UniProt

complete

involved_in

GO:0007015

actin filament organization

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000443979
WB:WBGene00002978

P

Seeded From UniProt

complete

part_of

GO:0005884

actin filament

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000443979
PomBase:SPAC27F1.02c

C

Seeded From UniProt

complete

involved_in

GO:0006936

muscle contraction

PMID:2022655[15]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003779

actin binding

PMID:2022655[15]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206
UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Kalyva, A et al. (2012) In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers. Biochemistry 51 6388-99 PubMed GONUTS page
  2. Greenfield, NJ et al. (2005) Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. Biophys. J. 88 372-83 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Gimona, M et al. (1995) Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Natl. Acad. Sci. U.S.A. 92 9776-80 PubMed GONUTS page
  4. 4.0 4.1 4.2 Varga, AE et al. (2005) Silencing of the Tropomyosin-1 gene by DNA methylation alters tumor suppressor function of TGF-beta. Oncogene 24 5043-52 PubMed GONUTS page
  5. 5.0 5.1 Zheng, Q et al. (2008) Role of high-molecular weight tropomyosins in TGF-beta-mediated control of cell motility. Int. J. Cancer 122 78-90 PubMed GONUTS page
  6. 6.0 6.1 Karibe, A et al. (2001) Hypertrophic cardiomyopathy caused by a novel alpha-tropomyosin mutation (V95A) is associated with mild cardiac phenotype, abnormal calcium binding to troponin, abnormal myosin cycling, and poor prognosis. Circulation 103 65-71 PubMed GONUTS page
  7. Radisic, M et al. (2004) Medium perfusion enables engineering of compact and contractile cardiac tissue. Am. J. Physiol. Heart Circ. Physiol. 286 H507-16 PubMed GONUTS page
  8. 8.0 8.1 Kostyukova, AS et al. (2005) Structural requirements of tropomodulin for tropomyosin binding and actin filament capping. Biochemistry 44 4905-10 PubMed GONUTS page
  9. 9.0 9.1 Hitchcock-DeGregori, SE et al. (2001) Importance of internal regions and the overall length of tropomyosin for actin binding and regulatory function. Biochemistry 40 2104-12 PubMed GONUTS page
  10. 10.0 10.1 Skórzewski, R et al. (2009) Effect of actin C-terminal modification on tropomyosin isoforms binding and thin filament regulation. Biochim. Biophys. Acta 1794 237-43 PubMed GONUTS page
  11. Kremneva, E et al. (2006) Thermal unfolding of smooth muscle and nonmuscle tropomyosin alpha-homodimers with alternatively spliced exons. FEBS J. 273 588-600 PubMed GONUTS page
  12. Noda, Y et al. (2005) Identification of a multiprotein "motor" complex binding to water channel aquaporin-2. Biochem. Biophys. Res. Commun. 330 1041-7 PubMed GONUTS page
  13. Singh, A & Hitchcock-DeGregori, SE (2003) Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 42 14114-21 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  15. 15.0 15.1 Goodwin, LO et al. (1991) Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters. J. Biol. Chem. 266 8408-15 PubMed GONUTS page