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Protein

Tropomyosin beta chain

Gene

TPM2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: -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

GO - Molecular functioni

Keywordsi

Molecular functionActin-binding, Muscle protein

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin beta chain
Alternative name(s):
Beta-tropomyosin
Tropomyosin-2
Gene namesi
Name:TPM2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002056301 – 284Tropomyosin beta chainAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei53PhosphothreonineBy similarity1
Modified residuei61Phosphoserine; by PIK3CGBy similarity1
Modified residuei79PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei158PhosphoserineBy similarity1
Modified residuei206PhosphoserineBy similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei252PhosphothreonineBy similarity1
Modified residuei261PhosphotyrosineBy similarity1
Modified residuei271PhosphoserineBy similarity1
Modified residuei282PhosphothreonineBy similarity1
Modified residuei283PhosphoserineBy similarity1

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

PRIDEiP58776

PTM databases

iPTMnetiP58776

Expressioni

Gene expression databases

BgeeiENSOCUG00000010198

Interactioni

Subunit structurei

Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP58776, 1 interactor
MINTiP58776
STRINGi9986.ENSOCUP00000008788

Structurei

3D structure databases

ProteinModelPortaliP58776
SMRiP58776
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1 – 284By similarityAdd BLAST284

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

eggNOGiKOG1003 Eukaryota
ENOG410XR5K LUCA
GeneTreeiENSGT00550000074494
HOGENOMiHOG000231521
HOVERGENiHBG107404
InParanoidiP58776
OMAiAVLESKF
OrthoDBiEOG091G0UO7

Family and domain databases

InterProiView protein in InterPro
IPR000533 Tropomyosin
PfamiView protein in Pfam
PF00261 Tropomyosin, 1 hit
PRINTSiPR00194 TROPOMYOSIN
PROSITEiView protein in PROSITE
PS00326 TROPOMYOSIN, 1 hit

Sequencei

Sequence statusi: Complete.

P58776-1 [UniParc]FASTAAdd to basket

« 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

Sequence databases

PIRiA02980 TMRBB
RefSeqiXP_017194790.1, XM_017339301.1
UniGeneiOcu.3371

Genome annotation databases

EnsembliENSOCUT00000022879; ENSOCUP00000022333; ENSOCUG00000010198
GeneIDi100125984

Similar proteinsi

Entry informationi

Entry nameiTPM2_RABIT
AccessioniPrimary (citable) accession number: P58776
Secondary accession number(s): P02560
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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