Search Results
Overview
| Uniprot ID | P58771 |
|---|---|
| Protein Name | Tropomyosin alpha-1 chain |
| Gene Name | Tpm1 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 112 | RLATALQKLEEAEKA |
| 118 | QKLEEAEKAADESER |
| 12 | KKKMQMLKLDKENAL |
| 128 | DESERGMKVIESRAQ |
| 140 | RAQKDEEKMEIQEIQ |
| 152 | EIQLKEAKHIAEDAD |
| 161 | IAEDADRKYEEVARK |
| 168 | KYEEVARKLVIIESD |
| 189 | RAELSEGKCAELEEE |
| 205 | KTVTNNLKSLEAQAE |
| 213 | SLEAQAEKYSQKEDK |
| 217 | QAEKYSQKEDKYEEE |
| 220 | KYSQKEDKYEEEIKV |
| 226 | DKYEEEIKVLSDKLK |
| 251 | RSVTKLEKSIDDLED |
| 264 | EDELYAQKLKYKAIS |
| 37 | KAAEDRSKQLEDELV |
| 48 | DELVSLQKKLKGTED |
| 51 | VSLQKKLKGTEDELD |
| 59 | GTEDELDKYSEALKD |
| 65 | DKYSEALKDAQEKLE |
| 70 | ALKDAQEKLELAEKK |
| 76 | EKLELAEKKATDAEA |
| 77 | KLELAEKKATDAEAD |
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
Protein Sequence
10
MDAIKKKMQM
20
LKLDKENALD
30
RAEQAEADKK
40
AAEDRSKQLE
50
DELVSLQKKL
60
KGTEDELDKY
70
SEALKDAQEK
80
LELAEKKATD
90
AEADVASLNR
100
RIQLVEEELD
110
RAQERLATAL
120
QKLEEAEKAA
130
DESERGMKVI
140
ESRAQKDEEK
150
MEIQEIQLKE
160
AKHIAEDADR
170
KYEEVARKLV
180
IIESDLERAE
190
ERAELSEGKC
200
AELEEELKTV
210
TNNLKSLEAQ
220
AEKYSQKEDK
230
YEEEIKVLSD
240
KLKEAETRAE
250
FAERSVTKLE
260
KSIDDLEDEL
270
YAQKLKYKAI
280
SEELDHALND
MTSI
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0005884 | actin filament |
| Cellular Component | GO:0032059 | bleb |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005862 | muscle thin filament tropomyosin |
| Cellular Component | GO:0030016 | myofibril |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0032587 | ruffle membrane |
| Cellular Component | GO:0001725 | stress fiber |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0008092 | cytoskeletal protein binding |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Biological Process | GO:0051693 | actin filament capping |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0060048 | cardiac muscle contraction |
| Biological Process | GO:0001701 | in utero embryonic development |
| Biological Process | GO:0030049 | muscle filament sliding |
| Biological Process | GO:0030336 | negative regulation of cell migration |
| Biological Process | GO:1904753 | negative regulation of vascular associated smooth muscle cell migration |
| Biological Process | GO:1904706 | negative regulation of vascular associated smooth muscle cell proliferation |
| Biological Process | GO:0032781 | positive regulation of ATP-dependent activity |
| Biological Process | GO:0045785 | positive regulation of cell adhesion |
| Biological Process | GO:0003065 | positive regulation of heart rate by epinephrine |
| Biological Process | GO:0051496 | positive regulation of stress fiber assembly |
| Biological Process | GO:0043462 | regulation of ATP-dependent activity |
| Biological Process | GO:0008360 | regulation of cell shape |
| Biological Process | GO:0031529 | ruffle organization |
| Biological Process | GO:0045214 | sarcomere organization |
| Biological Process | GO:0055010 | ventricular cardiac muscle tissue morphogenesis |
| Biological Process | GO:0042060 | wound healing |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.