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Q12792 (TWF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twinfilin-1
Alternative name(s):
Protein A6
Protein tyrosine kinase 9
Gene names
Name:TWF1
Synonyms:PTK9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 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 By similarity.

Subunit structure

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.

Subcellular location

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.

Tissue specificity

Expressed at high levels in the colon, testis, ovary, prostate and lung. Expressed at lower levels in the brain, bladder and heart. Not detected in liver. Ref.1

Post-translational modification

Phosphorylated on serine and threonine residues. Ref.1

Sequence similarities

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

Contains 2 ADF-H domains.

Caution

Was originally (Ref.1) thought to have protein tyrosine kinase activity.

Sequence caution

The sequence AAH43148.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH68548.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD92539.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbarbed-end actin filament capping

Inferred from electronic annotation. Source: Ensembl

negative regulation of actin filament polymerization

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

regulation of actin phosphorylation

Inferred from direct assay PubMed 10406962. Source: BHF-UCL

sequestering of actin monomers

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

   Cellular_componentactin cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

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

cytoplasm

Inferred from direct assay. Source: HPA

filopodium

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

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay PubMed 10406962. Source: BHF-UCL

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

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12792-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 3 (identifier: Q12792-3)

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: E → ESPEDHIG
Isoform 4 (identifier: Q12792-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 350349Twinfilin-1
PRO_0000214950

Regions

Domain2 – 139138ADF-H 1
Domain175 – 313139ADF-H 2

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue1431Phosphoserine Ref.11
Modified residue3091Phosphotyrosine Ref.8 Ref.10
Modified residue3491Phosphothreonine Ref.9

Natural variations

Alternative sequence1 – 9898Missing in isoform 4.
VSP_038075
Alternative sequence1611E → ESPEDHIG in isoform 3.
VSP_017899

Experimental info

Sequence conflict121D → Y in CAG46561. Ref.3
Sequence conflict2461E → V in BAG54588. Ref.2
Sequence conflict2691R → W in CAG46536. Ref.3
Sequence conflict3021E → G in BAF83912. Ref.2
Sequence conflict3291P → H in BAG59691. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: 5F68A6946E969A80

FASTA35040,283
        10         20         30         40         50         60 
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD KDYDSFVLPL 

        70         80         90        100        110        120 
LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE 

       130        140        150        160        170        180 
VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVGVDT KHQTLQGVAF 

       190        200        210        220        230        240 
PISREAFQAL EKLNNRQLNY VQLEIDIKNE IIILANTTNT ELKDLPKRIP KDSARYHFFL 

       250        260        270        280        290        300 
YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSRLL EIVERQLQMD VIRKIEIDNG 

       310        320        330        340        350 
DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD 

« Hide

Isoform 3 [UniParc].

Checksum: 826E95A7D995033B
Show »

FASTA35741,018
Isoform 4 [UniParc].

Checksum: CCE0A5A82BBE109D
Show »

FASTA25228,823

References

« Hide 'large scale' references
[1]"Prokaryotic expression cloning of a novel human tyrosine kinase."
Beeler J.F., LaRochelle W.J., Chedid M., Tronick S.R., Aaronson S.A.
Mol. Cell. Biol. 14:982-988(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, TISSUE SPECIFICITY, PHOSPHORYLATION.
Tissue: Lung fibroblast.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Tissue: Brain, Placenta and Teratocarcinoma.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[6]"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] (ISOFORMS 1 AND 4).
Tissue: Prostate and Testis.
[7]Bienvenut W.V., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-37 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 65-72; 99-105; 111-155; 172-192; 236-242 AND 279-285 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 159-171 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"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].
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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].

Web resources

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02680 mRNA. Translation: AAC50062.1.
AK127868 mRNA. Translation: BAG54588.1.
AK291223 mRNA. Translation: BAF83912.1.
AK297206 mRNA. Translation: BAG59691.1.
CR541736 mRNA. Translation: CAG46536.1.
CR541761 mRNA. Translation: CAG46561.1.
BT019691 mRNA. Translation: AAV38497.1.
AB209302 mRNA. Translation: BAD92539.1. Different initiation.
BC022344 mRNA. Translation: AAH22344.1.
BC043148 mRNA. Translation: AAH43148.2. Different initiation.
BC068548 mRNA. Translation: AAH68548.1. Different initiation.
PIRA55922.
RefSeqNP_001229326.1. NM_001242397.1.
NP_002813.3. NM_002822.4.
UniGeneHs.189075.
Hs.313056.

3D structure databases

ProteinModelPortalQ12792.
SMRQ12792. Positions 7-139, 176-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111723. 23 interactions.
IntActQ12792. 3 interactions.
MINTMINT-3026525.

PTM databases

PhosphoSiteQ12792.

Polymorphism databases

DMDM259016376.

2D gel databases

OGPQ12792.

Proteomic databases

PaxDbQ12792.
PRIDEQ12792.

Protocols and materials databases

DNASU5756.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325127; ENSP00000321058; ENSG00000151239.
ENST00000395510; ENSP00000378886; ENSG00000151239. [Q12792-2]
ENST00000548315; ENSP00000449428; ENSG00000151239. [Q12792-3]
ENST00000552521; ENSP00000448750; ENSG00000151239. [Q12792-4]
GeneID5756.
KEGGhsa:5756.
UCSCuc001roa.4. human. [Q12792-2]
uc001rob.3. human. [Q12792-3]

Organism-specific databases

CTD5756.
GeneCardsGC12M044187.
HGNCHGNC:9620. TWF1.
HPAHPA018116.
MIM610932. gene.
neXtProtNX_Q12792.
PharmGKBPA162407406.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263290.
HOVERGENHBG000848.
KOK08870.
OrthoDBEOG79GT6W.
PhylomeDBQ12792.
TreeFamTF352598.

Gene expression databases

ArrayExpressQ12792.
BgeeQ12792.
GenevestigatorQ12792.

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

GeneWikiTWF1.
GenomeRNAi5756.
NextBio22400.
PROQ12792.
SOURCESearch...

Entry information

Entry nameTWF1_HUMAN
AccessionPrimary (citable) accession number: Q12792
Secondary accession number(s): A8K5A8 expand/collapse secondary AC list , B3KXS6, B4DLX9, Q59G07, Q5U0B1, Q6FHJ1, Q6FHL6, Q6NUK9, Q86XL6, Q8TCD3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 128 of the entry and version 3 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM