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Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000283716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei261 – 2611PhosphotyrosineBy similarity
Modified residuei271 – 2711PhosphoserineBy similarity
Modified residuei283 – 2831Phosphoserine; by DAPK1By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ5KR49.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain. 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

IntActiQ5KR49. 3 interactions.
MINTiMINT-8189950.

Structurei

3D structure databases

ProteinModelPortaliQ5KR49.
SMRiQ5KR49. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284By 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.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiQ5KR49.
KOiK10373.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q5KR49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL
60 70 80 90 100
KATEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD
110 120 130 140 150
RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE
160 170 180 190 200
AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV
210 220 230 240 250
TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE
260 270 280
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
Length:284
Mass (Da):32,695
Last modified:February 15, 2005 - v1
Checksum:i18DBC129191DC4E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB198070 mRNA. Translation: BAD86590.1.
BC102909 mRNA. Translation: AAI02910.1.
RefSeqiNP_001013608.1. NM_001013590.2.
UniGeneiBt.109484.

Genome annotation databases

GeneIDi281544.
KEGGibta:281544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB198070 mRNA. Translation: BAD86590.1.
BC102909 mRNA. Translation: AAI02910.1.
RefSeqiNP_001013608.1. NM_001013590.2.
UniGeneiBt.109484.

3D structure databases

ProteinModelPortaliQ5KR49.
SMRiQ5KR49. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5KR49. 3 interactions.
MINTiMINT-8189950.

Proteomic databases

PRIDEiQ5KR49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281544.
KEGGibta:281544.

Organism-specific databases

CTDi7168.

Phylogenomic databases

HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiQ5KR49.
KOiK10373.

Miscellaneous databases

NextBioi20805496.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Bovine tropomyosin isoforms."
    Oe M., Nakajima I., Muroya S., Chikuni K.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Heart ventricle.

Entry informationi

Entry nameiTPM1_BOVIN
AccessioniPrimary (citable) accession number: Q5KR49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 15, 2005
Last modified: November 11, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.