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Protein

Tropomyosin beta chain

Gene

TPM2

Organism
Oryctolagus cuniculus (Rabbit)
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

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

GO - Cellular componenti

Complete GO annotation...

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
Cross-linki77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
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, Isopeptide bond, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP58776.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

IntActiP58776. 1 interactor.
MINTiMINT-7966042.
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.
OMAiTEPTHEC.
OrthoDBiEOG091G0UO7.

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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP58776.
SMRiP58776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP58776. 1 interactor.
MINTiMINT-7966042.
STRINGi9986.ENSOCUP00000008788.

PTM databases

iPTMnetiP58776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000022879; ENSOCUP00000022333; ENSOCUG00000010198.
GeneIDi100125984.

Phylogenomic databases

eggNOGiKOG1003. Eukaryota.
ENOG410XR5K. LUCA.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58776.
OMAiTEPTHEC.
OrthoDBiEOG091G0UO7.

Family and domain databases

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

Entry informationi

Entry nameiTPM2_RABIT
AccessioniPrimary (citable) accession number: P58776
Secondary accession number(s): P02560
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
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, Direct protein sequencing, 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.