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Protein

Tropomyosin beta chain

Gene

Tpm2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.
R-RNO-445355. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin beta chain
Alternative name(s):
Beta-tropomyosin
Tropomyosin-2
Gene namesi
Name:Tpm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1559479. Tpm2.

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 beta chainPRO_0000205629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei53 – 531PhosphothreonineBy similarity
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei252 – 2521PhosphothreonineCombined sources
Modified residuei261 – 2611PhosphotyrosineCombined sources
Modified residuei271 – 2711PhosphoserineCombined sources
Modified residuei282 – 2821PhosphothreonineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Isoform 2 (identifier: P58775-2)
Modified residuei210 – 2101PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is required for ADRB2 internalization (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP58775.

PTM databases

iPTMnetiP58775.

Expressioni

Gene expression databases

ExpressionAtlasiP58775. baseline and differential.
GenevisibleiP58775. RN.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

BioGridi271758. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP58775.
SMRiP58775. 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

GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58775.
KOiK10374.
OMAiKCKAISE.
OrthoDBiEOG7673C8.
PhylomeDBiP58775.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P58775-1) [UniParc]FASTAAdd to basket

Also known as: Skeletal muscle

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

        10         20         30         40         50
MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL
60 70 80 90 100
KGTEDEVEKY SESVKDAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD
110 120 130 140 150
RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE
160 170 180 190 200
AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESKC GDLEEELKIV
210 220 230 240 250
TNNLKSLEAQ ADKYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE
260 270 280
KTIDDLEDEV YAQKMKYKAI SEELDNALND ITSL
Length:284
Mass (Da):32,837
Last modified:July 21, 1986 - v1
Checksum:iF95D2BF6250F40AE
GO
Isoform 2 (identifier: P58775-2) [UniParc]FASTAAdd to basket

Also known as: non-muscle, Fibroblast, Embryonic fibroblast TM-1

The sequence of this isoform differs from the canonical sequence as follows:
     189-213: KCGDLEEELKIVTNNLKSLEAQADK → RARQLEEELRTMDQALKSLIASEEE
     258-284: DEVYAQKMKYKAISEELDNALNDITSL → ETLASAKEENVEIHQTLDQTLLELNNL

Show »
Length:284
Mass (Da):32,958
Checksum:iA35EBB080ADC5DDF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei189 – 21325KCGDL…AQADK → RARQLEEELRTMDQALKSLI ASEEE in isoform 2. CuratedVSP_006599Add
BLAST
Alternative sequencei258 – 28427DEVYA…DITSL → ETLASAKEENVEIHQTLDQT LLELNNL in isoform 2. CuratedVSP_006600Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00381
, L00372, L00373, L00374, L00375, L00376, L00378, L00379, L00380 Genomic DNA. Translation: AAA42288.1.
L00382
, L00372, L00373, L00374, L00375, L00376, L00377, L00379, L00380 Genomic DNA. Translation: AAA42289.1.
PIRiA02981. TMRTF1.
B25073.
RefSeqiNP_001019516.1. NM_001024345.2. [P58775-2]
NP_001288164.1. NM_001301235.1. [P58775-1]
UniGeneiRn.17580.

Genome annotation databases

EnsembliENSRNOT00000022801; ENSRNOP00000022801; ENSRNOG00000016731. [P58775-1]
ENSRNOT00000049000; ENSRNOP00000044473; ENSRNOG00000016731. [P58775-2]
GeneIDi500450.
KEGGirno:500450.
UCSCiRGD:1559479. rat. [P58775-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00381
, L00372, L00373, L00374, L00375, L00376, L00378, L00379, L00380 Genomic DNA. Translation: AAA42288.1.
L00382
, L00372, L00373, L00374, L00375, L00376, L00377, L00379, L00380 Genomic DNA. Translation: AAA42289.1.
PIRiA02981. TMRTF1.
B25073.
RefSeqiNP_001019516.1. NM_001024345.2. [P58775-2]
NP_001288164.1. NM_001301235.1. [P58775-1]
UniGeneiRn.17580.

3D structure databases

ProteinModelPortaliP58775.
SMRiP58775. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi271758. 1 interaction.

PTM databases

iPTMnetiP58775.

Proteomic databases

PRIDEiP58775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022801; ENSRNOP00000022801; ENSRNOG00000016731. [P58775-1]
ENSRNOT00000049000; ENSRNOP00000044473; ENSRNOG00000016731. [P58775-2]
GeneIDi500450.
KEGGirno:500450.
UCSCiRGD:1559479. rat. [P58775-1]

Organism-specific databases

CTDi7169.
RGDi1559479. Tpm2.

Phylogenomic databases

GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58775.
KOiK10374.
OMAiKCKAISE.
OrthoDBiEOG7673C8.
PhylomeDBiP58775.

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.
R-RNO-445355. Smooth Muscle Contraction.

Miscellaneous databases

NextBioi706240.
PROiP58775.

Gene expression databases

ExpressionAtlasiP58775. baseline and differential.
GenevisibleiP58775. RN.

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. "Rat embryonic fibroblast tropomyosin 1. cDNA and complete primary amino acid sequence."
    Yamawaki-Kataoka Y., Helfman D.M.
    J. Biol. Chem. 260:14440-14445(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
  2. "Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation."
    Helfman D.M., Cheley S., Kuismanen E., Finn L.A., Yamawaki-Kataoka Y.
    Mol. Cell. Biol. 6:3582-3595(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-206; SER-215; THR-252; TYR-261 AND SER-271, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPM2_RAT
AccessioniPrimary (citable) accession number: P58775
Secondary accession number(s): P02560, P06395
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 17, 2016
This is version 98 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.