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Q12792

- TWF1_HUMAN

UniProt

Q12792 - TWF1_HUMAN

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Protein

Twinfilin-1

Gene

TWF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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).By similarity

GO - Molecular functioni

  1. actin monomer binding Source: BHF-UCL
  2. ATP binding Source: BHF-UCL
  3. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL

GO - Biological processi

  1. barbed-end actin filament capping Source: Ensembl
  2. negative regulation of actin filament polymerization Source: BHF-UCL
  3. peptidyl-tyrosine phosphorylation Source: Ensembl
  4. regulation of actin phosphorylation Source: BHF-UCL
  5. sequestering of actin monomers Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Twinfilin-1
Alternative name(s):
Protein A6
Protein tyrosine kinase 9
Gene namesi
Name:TWF1
Synonyms:PTK9
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9620. TWF1.

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).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cell-cell junction Source: BHF-UCL
  3. cytoplasm Source: HPA
  4. filopodium Source: BHF-UCL
  5. focal adhesion Source: UniProtKB
  6. myofibril Source: BHF-UCL
  7. perinuclear region of cytoplasm Source: BHF-UCL
  8. ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 350349Twinfilin-1PRO_0000214950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei309 – 3091Phosphotyrosine2 Publications
Modified residuei349 – 3491Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12792.
PaxDbiQ12792.
PRIDEiQ12792.

2D gel databases

OGPiQ12792.

PTM databases

PhosphoSiteiQ12792.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ12792.
ExpressionAtlasiQ12792. baseline and differential.
GenevestigatoriQ12792.

Organism-specific databases

HPAiHPA018116.

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).By similarity

Protein-protein interaction databases

BioGridi111723. 23 interactions.
IntActiQ12792. 3 interactions.
MINTiMINT-3026525.

Structurei

3D structure databases

ProteinModelPortaliQ12792.
SMRiQ12792. Positions 7-139, 176-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 ADF-H domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG263290.
GeneTreeiENSGT00530000063868.
HOVERGENiHBG000848.
InParanoidiQ12792.
KOiK08870.
OrthoDBiEOG79GT6W.
PhylomeDBiQ12792.
TreeFamiTF352598.

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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1Curated (identifier: Q12792-2) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD
60 70 80 90 100
KDYDSFVLPL LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML
110 120 130 140 150
YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA
160 170 180 190 200
EEELRQIKIN EVQTDVGVDT KHQTLQGVAF PISREAFQAL EKLNNRQLNY
210 220 230 240 250
VQLEIDIKNE IIILANTTNT ELKDLPKRIP KDSARYHFFL YKHSHEGDYL
260 270 280 290 300
ESIVFIYSMP GYTCSIRERM LYSSCKSRLL EIVERQLQMD VIRKIEIDNG
310 320 330 340 350
DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD
Length:350
Mass (Da):40,283
Last modified:September 22, 2009 - v3
Checksum:i5F68A6946E969A80
GO
Isoform 3 (identifier: Q12792-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: E → ESPEDHIG

Show »
Length:357
Mass (Da):41,018
Checksum:i826E95A7D995033B
GO
Isoform 4 (identifier: Q12792-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:252
Mass (Da):28,823
Checksum:iCCE0A5A82BBE109D
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121D → Y in CAG46561. 1 PublicationCurated
Sequence conflicti246 – 2461E → V in BAG54588. (PubMed:14702039)Curated
Sequence conflicti269 – 2691R → W in CAG46536. 1 PublicationCurated
Sequence conflicti302 – 3021E → G in BAF83912. (PubMed:14702039)Curated
Sequence conflicti329 – 3291P → H in BAG59691. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9898Missing in isoform 4. 2 PublicationsVSP_038075Add
BLAST
Alternative sequencei161 – 1611E → ESPEDHIG in isoform 3. 1 PublicationVSP_017899

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31780.2. [Q12792-2]
CCDS55818.1. [Q12792-3]
PIRiA55922.
RefSeqiNP_001229326.1. NM_001242397.1. [Q12792-3]
NP_002813.3. NM_002822.4. [Q12792-2]
UniGeneiHs.189075.
Hs.313056.

Genome annotation databases

GeneIDi5756.
KEGGihsa:5756.
UCSCiuc001roa.4. human. [Q12792-2]
uc001rob.3. human. [Q12792-3]

Polymorphism databases

DMDMi259016376.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS31780.2. [Q12792-2 ]
CCDS55818.1. [Q12792-3 ]
PIRi A55922.
RefSeqi NP_001229326.1. NM_001242397.1. [Q12792-3 ]
NP_002813.3. NM_002822.4. [Q12792-2 ]
UniGenei Hs.189075.
Hs.313056.

3D structure databases

ProteinModelPortali Q12792.
SMRi Q12792. Positions 7-139, 176-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111723. 23 interactions.
IntActi Q12792. 3 interactions.
MINTi MINT-3026525.

PTM databases

PhosphoSitei Q12792.

Polymorphism databases

DMDMi 259016376.

2D gel databases

OGPi Q12792.

Proteomic databases

MaxQBi Q12792.
PaxDbi Q12792.
PRIDEi Q12792.

Protocols and materials databases

DNASUi 5756.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5756.
KEGGi hsa:5756.
UCSCi uc001roa.4. human. [Q12792-2 ]
uc001rob.3. human. [Q12792-3 ]

Organism-specific databases

CTDi 5756.
GeneCardsi GC12M044187.
HGNCi HGNC:9620. TWF1.
HPAi HPA018116.
MIMi 610932. gene.
neXtProti NX_Q12792.
PharmGKBi PA162407406.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263290.
GeneTreei ENSGT00530000063868.
HOVERGENi HBG000848.
InParanoidi Q12792.
KOi K08870.
OrthoDBi EOG79GT6W.
PhylomeDBi Q12792.
TreeFami TF352598.

Miscellaneous databases

GeneWikii TWF1.
GenomeRNAii 5756.
NextBioi 22400.
PROi Q12792.
SOURCEi Search...

Gene expression databases

Bgeei Q12792.
ExpressionAtlasi Q12792. baseline and differential.
Genevestigatori Q12792.

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

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTWF1_HUMAN
AccessioniPrimary (citable) accession number: Q12792
Secondary accession number(s): A8K5A8
, B3KXS6, B4DLX9, Q59G07, Q5U0B1, Q6FHJ1, Q6FHL6, Q6NUK9, Q86XL6, Q8TCD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: September 22, 2009
Last modified: October 29, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was originally thought to have protein tyrosine kinase activity.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3