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Q5R7N2

- TWF1_PONAB

UniProt

Q5R7N2 - TWF1_PONAB

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Protein
Twinfilin-1
Gene
TWF1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles By similarity.

GO - Biological processi

  1. negative regulation of actin filament polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Twinfilin-1
Gene namesi
Name:TWF1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton By similarity
Note: Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts By similarity.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 350349Twinfilin-1
PRO_0000232405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei143 – 1431Phosphoserine By similarity
Modified residuei309 – 3091Phosphotyrosine By similarity
Modified residuei349 – 3491Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated on serine and threonine residues By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5R7N2.

Interactioni

Subunit structurei

Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF2 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R7N2.
SMRiQ5R7N2. Positions 7-139, 161-313.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 139138ADF-H 1
Add
BLAST
Domaini175 – 313139ADF-H 2
Add
BLAST

Sequence similaritiesi

Contains 2 ADF-H domains.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000848.
InParanoidiQ5R7N2.
KOiK08870.

Family and domain databases

Gene3Di3.40.20.10. 2 hits.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028458. Twinfilin.
[Graphical view]
PANTHERiPTHR13759. PTHR13759. 1 hit.
PfamiPF00241. Cofilin_ADF. 2 hits.
[Graphical view]
SMARTiSM00102. ADF. 2 hits.
[Graphical view]
PROSITEiPS51263. ADF_H. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R7N2-1 [UniParc]FASTAAdd to Basket

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MSHRTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD    50
KDYDSFVLPL LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML 100
YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA 150
EEELRQIKIN EVQTDVGVDT KHQTLQGVAF PISREAFQAL EKLNNRQLNY 200
VQLEIDIKNE IIILANTTDT ELKDLPKRIP KDSARYHFFL YKHSHEGDYL 250
ESIVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMG VIRKIEIDNG 300
DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD 350
Length:350
Mass (Da):40,195
Last modified:December 21, 2004 - v1
Checksum:i47C2FEBD973D8770
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860082 mRNA. Translation: CAH92228.1.
RefSeqiNP_001126303.1. NM_001132831.1.

Genome annotation databases

GeneIDi100173282.
KEGGipon:100173282.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860082 mRNA. Translation: CAH92228.1 .
RefSeqi NP_001126303.1. NM_001132831.1.

3D structure databases

ProteinModelPortali Q5R7N2.
SMRi Q5R7N2. Positions 7-139, 161-313.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R7N2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173282.
KEGGi pon:100173282.

Organism-specific databases

CTDi 5756.

Phylogenomic databases

HOVERGENi HBG000848.
InParanoidi Q5R7N2.
KOi K08870.

Family and domain databases

Gene3Di 3.40.20.10. 2 hits.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028458. Twinfilin.
[Graphical view ]
PANTHERi PTHR13759. PTHR13759. 1 hit.
Pfami PF00241. Cofilin_ADF. 2 hits.
[Graphical view ]
SMARTi SM00102. ADF. 2 hits.
[Graphical view ]
PROSITEi PS51263. ADF_H. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiTWF1_PONAB
AccessioniPrimary (citable) accession number: Q5R7N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 55 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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