Q12792 (TWF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Twinfilin-1

Alternative name(s):
Protein A6
Protein tyrosine kinase 9

Gene names

Name:	TWF1
Synonyms:	PTK9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton 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 Ref.8 Ref.9 Ref.10 Ref.11
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 component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of actin phosphorylation Inferred from direct assay. Source: BHF-UCL sequestering of actin monomers Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	actin cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB cell-cell junction Inferred from sequence or structural similarity. Source: BHF-UCL filopodium Inferred from sequence or structural similarity. Source: BHF-UCL myofibril Inferred from sequence or structural similarity. Source: BHF-UCL perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	ATP binding Inferred from direct assay. Source: BHF-UCL actin monomer binding Inferred from sequence or structural similarity. Source: BHF-UCL phosphatidylinositol-4,5-bisphosphate binding Inferred from sequence or structural similarity. Source: BHF-UCL protein tyrosine kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 350	349	Twinfilin-1		PRO_0000214950
Regions
	Domain	2 – 139	138	ADF-H 1
	Domain	175 – 313	139	ADF-H 2
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.7
	Modified residue	143	1	Phosphoserine Ref.9
	Modified residue	309	1	Phosphotyrosine Ref.8 Ref.11
	Modified residue	349	1	Phosphothreonine Ref.10
Natural variations
	Alternative sequence	1 – 98	98	Missing in isoform 4.		VSP_038075
	Alternative sequence	161	1	E → ESPEDHIG in isoform 3.		VSP_017899
Experimental info
	Sequence conflict	12	1	D → Y in CAG46561. Ref.3
	Sequence conflict	246	1	E → V in BAG54588. Ref.2
	Sequence conflict	269	1	R → W in CAG46536. Ref.3
	Sequence conflict	302	1	E → G in BAF83912. Ref.2
	Sequence conflict	329	1	P → H in BAG59691. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 5F68A6946E969A80	FASTA	350	40,283
	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
	Isoform 3 [UniParc]. Checksum: 826E95A7D995033B	FASTA	357	41,018
	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 ESPEDHIGVQ TDVGVDTKHQ 190 200 210 220 230 240 TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS 250 260 270 280 290 300 ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR 310 320 330 340 350 KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD
	Isoform 4 [UniParc]. Checksum: CCE0A5A82BBE109D	FASTA	252	28,823
	10 20 30 40 50 60 MLYAATRATL KKEFGGGHIK DEVFGTVKED VSLHGYKKYL LSQSSPAPLT AAEEELRQIK 70 80 90 100 110 120 INEVQTDVGV DTKHQTLQGV AFPISREAFQ ALEKLNNRQL NYVQLEIDIK NEIIILANTT 130 140 150 160 170 180 NTELKDLPKR IPKDSARYHF FLYKHSHEGD YLESIVFIYS MPGYTCSIRE RMLYSSCKSR 190 200 210 220 230 240 LLEIVERQLQ MDVIRKIEID NGDELTADFL YEEVHPKQHA HKQSFAKPKG PAGKRGIRRL 250 IRGPAETEAT TD

References

	« Hide 'large scale' referencesShow '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: 7507208] [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: 14702039] [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: 15489334] [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, 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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, MASS SPECTROMETRY.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [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.
IPI	IPI00815767. IPI00816829. IPI01022451.
PIR	A55922.
RefSeq	NP_001229326.1. NM_001242397.1. NP_002813.3. NM_002822.4.
UniGene	Hs.189075.
3D structure databases
ProteinModelPortal	Q12792.
SMR	Q12792. Positions 7-139, 176-316.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12792. 1 interaction.
STRING	Q12792.
PTM databases
PhosphoSite	Q12792.
Polymorphism databases
DMDM	259016376.
2D gel databases
OGP	Q12792.
Proteomic databases
PRIDE	Q12792.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000325127; ENSP00000321058; ENSG00000151239. ENST00000334878; ENSP00000335569; ENSG00000151239.
GeneID	5756.
KEGG	hsa:5756.
UCSC	uc001rnz.1. human. uc001rob.1. human.
Organism-specific databases
CTD	5756.
GeneCards	GC12M044187.
HGNC	HGNC:9620. TWF1.
HPA	HPA018116.
MIM	610932. gene.
neXtProt	NX_Q12792.
PharmGKB	PA162407406.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18388.
GeneTree	ENSGT00530000063868.
HOVERGEN	HBG000848.
OrthoDB	EOG4TTGJJ.
Gene expression databases
ArrayExpress	Q12792.
Bgee	Q12792.
Genevestigator	Q12792.
GermOnline	ENSG00000151239. Homo sapiens.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. [Graphical view]
KO	K08870.
Pfam	PF00241. Cofilin_ADF. 2 hits. [Graphical view]
SMART	SM00102. ADF. 2 hits. [Graphical view]
PROSITE	PS51263. ADF_H. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	22400.
SOURCE	Search...

Entry information

Entry name

TWF1_HUMAN

Accession

Primary (citable) accession number: Q12792
Secondary accession number(s): A8K5A8 , 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:	January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.