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P58776

- TPM2_RABIT

UniProt

P58776 - TPM2_RABIT

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Protein

Tropomyosin beta chain

Gene

TPM2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

  1. regulation of ATPase activity Source: Ensembl
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
ProteomesiUP000001811: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin beta chainPRO_0000205630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei53 – 531PhosphothreonineBy similarity
Modified residuei61 – 611Phosphoserine; by PIK3CGBy similarity
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei252 – 2521PhosphothreonineBy similarity
Modified residuei282 – 2821PhosphothreonineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity

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.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP58776.
SMRiP58776. 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

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58776.
OMAiFLEVIIE.

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.

Genome annotation databases

EnsembliENSOCUT00000022879; ENSOCUP00000022333; ENSOCUG00000010198.

Cross-referencesi

Sequence databases

PIRi A02980. TMRBB.

3D structure databases

ProteinModelPortali P58776.
SMRi P58776. Positions 1-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P58776. 1 interaction.
MINTi MINT-7966042.
STRINGi 9986.ENSOCUP00000008788.

Proteomic databases

PRIDEi P58776.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOCUT00000022879 ; ENSOCUP00000022333 ; ENSOCUG00000010198 .

Phylogenomic databases

eggNOGi NOG304012.
GeneTreei ENSGT00550000074494.
HOGENOMi HOG000231521.
HOVERGENi HBG107404.
InParanoidi P58776.
OMAi FLEVIIE.

Family and domain databases

InterProi IPR000533. Tropomyosin.
[Graphical view ]
Pfami PF00261. Tropomyosin. 1 hit.
[Graphical view ]
PRINTSi PR00194. TROPOMYOSIN.
PROSITEi PS00326. TROPOMYOSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A comparison of the amino acid sequences of rabbit skeletal muscle alpha- and beta-tropomyosins."
    Mak A.S., Smillie L.B., Steward G.R.
    J. Biol. Chem. 255:3647-3655(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

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: October 29, 2014
This is version 58 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

External Data

Dasty 3