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Q6IBS0 (TWF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twinfilin-2
Alternative name(s):
A6-related protein
Short name=hA6RP
Protein tyrosine kinase 9-like
Twinfilin-1-like protein
Gene names
Name:TWF2
Synonyms:PTK9L
ORF Names:MSTP011
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May play a role in regulating the mature length of the middle and short rows of stereocilia By similarity.

Subunit structure

Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF1 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts with MYO7A By similarity.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell projectionstereocilium By similarity. Note: Perinuclear and G-actin-rich cortical actin structure sublocalization. Ref.1

Tissue specificity

Ubiquitously expressed (at protein level). Ref.1

Post-translational modification

In vitro, phosphorylated by PRKCZ, CK2 and SRC. Ref.1

Sequence similarities

Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.

Contains 2 ADF-H domains.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbarbed-end actin filament capping

Inferred from sequence or structural similarity PubMed 18837697. Source: BHF-UCL

cell projection organization

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to growth factor stimulus

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

cellular response to retinoic acid

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

negative regulation of actin filament polymerization

Inferred from sequence or structural similarity PubMed 12807912. Source: BHF-UCL

positive regulation of axon extension

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

positive regulation of lamellipodium assembly

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

regulation of microvillus length

Inferred by curator PubMed 19955359. Source: BHF-UCL

sequestering of actin monomers

Inferred from sequence or structural similarity PubMed 18837697. Source: BHF-UCL

   Cellular_componentcytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

filopodium

Inferred from sequence or structural similarity PubMed 12807912. Source: BHF-UCL

growth cone

Inferred from direct assay PubMed 17910947. Source: BHF-UCL

lamellipodium

Inferred from sequence or structural similarity PubMed 12807912. Source: BHF-UCL

myofibril

Inferred from sequence or structural similarity PubMed 18837697. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from sequence or structural similarity PubMed 12807912. Source: BHF-UCL

stereocilium

Inferred from sequence or structural similarity PubMed 19955359. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

actin monomer binding

Inferred from sequence or structural similarity PubMed 12807912PubMed 18837697. Source: BHF-UCL

phosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence or structural similarity PubMed 12807912. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein kinase C binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 349348Twinfilin-2
PRO_0000233136

Regions

Domain4 – 139136ADF-H 1
Domain177 – 313137ADF-H 2

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.9 Ref.11
Modified residue141N6-acetyllysine Ref.11
Modified residue3091Phosphotyrosine Ref.7 Ref.10
Modified residue3491Phosphoserine Ref.10 Ref.13

Natural variations

Natural variant721R → C. Ref.14
Corresponds to variant rs35114109 [ dbSNP | Ensembl ].
VAR_042407
Natural variant761Q → R. Ref.14
Corresponds to variant rs35711542 [ dbSNP | Ensembl ].
VAR_042408
Natural variant1031A → T in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.14
VAR_042409

Experimental info

Sequence conflict1101K → R in CAG33013. Ref.4

Secondary structure

.............................................. 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6IBS0 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 635EF8C04EFCE92B

FASTA34939,548
        10         20         30         40         50         60 
MAHQTGIHAT EELKEFFAKA RAGSVRLIKV VIEDEQLVLG ASQEPVGRWD QDYDRAVLPL 

        70         80         90        100        110        120 
LDAQQPCYLL YRLDSQNAQG FEWLFLAWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE 

       130        140        150        160        170        180 
LFGTVKDDLS FAGYQKHLSS CAAPAPLTSA ERELQQIRIN EVKTEISVES KHQTLQGLAF 

       190        200        210        220        230        240 
PLQPEAQRAL QQLKQKMVNY IQMKLDLERE TIELVHTEPT DVAQLPSRVP RDAARYHFFL 

       250        260        270        280        290        300 
YKHTHEGDPL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFHLE IAKKIEIGDG 

       310        320        330        340 
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGDDS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and characterization of an A6 related protein."
Rohwer A., Kittstein W., Marks F., Gschwendt M.
Eur. J. Biochem. 263:518-525(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Tissue: Keratinocyte.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y., Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J., Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L. expand/collapse author list , Jiang Y.X., Zhao X.W., Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Aorta.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney, Lung and Placenta.
[6]Bienvenut W.V., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19 AND 279-293, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-72; ARG-76 AND THR-103.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17169 mRNA. Translation: CAB38055.1.
AL136773 mRNA. Translation: CAB66707.1.
AF109365 mRNA. Translation: AAQ13513.1.
CR456732 mRNA. Translation: CAG33013.1.
CR533520 mRNA. Translation: CAG38551.1.
BC000327 mRNA. Translation: AAH00327.1.
BC003161 mRNA. Translation: AAH03161.1.
BC016452 mRNA. Translation: AAH16452.1.
PIRT46362.
RefSeqNP_009215.1. NM_007284.3.
UniGeneHs.436439.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VACX-ray1.70A6-137[»]
2W0IX-ray1.80A181-313[»]
ProteinModelPortalQ6IBS0.
SMRQ6IBS0. Positions 6-137, 181-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116472. 49 interactions.
IntActQ6IBS0. 6 interactions.
MINTMINT-1414584.
STRING9606.ENSP00000303908.

PTM databases

PhosphoSiteQ6IBS0.

Polymorphism databases

DMDM94730596.

2D gel databases

OGPQ9Y3F5.

Proteomic databases

PaxDbQ6IBS0.
PeptideAtlasQ6IBS0.
PRIDEQ6IBS0.

Protocols and materials databases

DNASU11344.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305533; ENSP00000303908; ENSG00000247596.
GeneID11344.
KEGGhsa:11344.
UCSCuc003ddd.3. human.

Organism-specific databases

CTD11344.
GeneCardsGC03M052262.
HGNCHGNC:9621. TWF2.
HPAHPA053874.
MIM607433. gene.
neXtProtNX_Q6IBS0.
PharmGKBPA162407429.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263290.
HOGENOMHOG000168296.
HOVERGENHBG000848.
InParanoidQ6IBS0.
KOK08870.
OMAHATPELK.
OrthoDBEOG79GT6W.
PhylomeDBQ6IBS0.
TreeFamTF352598.

Gene expression databases

ArrayExpressQ6IBS0.
BgeeQ6IBS0.
CleanExHS_TWF2.
GenevestigatorQ6IBS0.

Family and domain databases

InterProIPR002108. ADF-H.
IPR028458. Twinfilin.
[Graphical view]
PANTHERPTHR13759. PTHR13759. 1 hit.
PfamPF00241. Cofilin_ADF. 2 hits.
[Graphical view]
SMARTSM00102. ADF. 2 hits.
[Graphical view]
PROSITEPS51263. ADF_H. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ6IBS0.
GeneWikiTWF2.
GenomeRNAi11344.
NextBio43112.
PROQ6IBS0.
SOURCESearch...

Entry information

Entry nameTWF2_HUMAN
AccessionPrimary (citable) accession number: Q6IBS0
Secondary accession number(s): Q9Y3F5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM