Full text data of TWF2
TWF2
(PTK9L)
[Confidence: low (only semi-automatic identification from reviews)]
Twinfilin-2 (A6-related protein; hA6RP; Protein tyrosine kinase 9-like; Twinfilin-1-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Twinfilin-2 (A6-related protein; hA6RP; Protein tyrosine kinase 9-like; Twinfilin-1-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6IBS0
ID TWF2_HUMAN Reviewed; 349 AA.
AC Q6IBS0; Q9Y3F5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Twinfilin-2;
DE AltName: Full=A6-related protein;
DE Short=hA6RP;
DE AltName: Full=Protein tyrosine kinase 9-like;
DE AltName: Full=Twinfilin-1-like protein;
GN Name=TWF2; Synonyms=PTK9L; ORFNames=MSTP011;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RC TISSUE=Keratinocyte;
RX PubMed=10406962; DOI=10.1046/j.1432-1327.1999.00537.x;
RA Rohwer A., Kittstein W., Marks F., Gschwendt M.;
RT "Cloning, expression and characterization of an A6 related protein.";
RL Eur. J. Biochem. 263:518-525(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-19 AND 279-293, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND SER-349, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-14, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-72; ARG-76 AND THR-103.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Actin-binding protein involved in motile and
CC morphological processes. Inhibits actin polymerization, likely by
CC sequestering G-actin. By capping the barbed ends of filaments, it
CC also regulates motility. Seems to play an important role in
CC clathrin-mediated endocytosis and distribution of endocytic
CC organelles. May play a role in regulating the mature length of the
CC middle and short rows of stereocilia (By similarity).
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping
CC protein (CP). May also be able to interact with TWF1 and
CC phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-
CC regulated. Interacts with MYO7A (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC perinuclear region. Cell projection, stereocilium (By similarity).
CC Note=Perinuclear and G-actin-rich cortical actin structure
CC sublocalization.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC -!- PTM: In vitro, phosphorylated by PRKCZ, CK2 and SRC.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC Twinfilin subfamily.
CC -!- SIMILARITY: Contains 2 ADF-H domains.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace -
CC Issue 73 of August 2006;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt073.shtml";
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DR EMBL; Y17169; CAB38055.1; -; mRNA.
DR EMBL; AL136773; CAB66707.1; -; mRNA.
DR EMBL; AF109365; AAQ13513.1; -; mRNA.
DR EMBL; CR456732; CAG33013.1; -; mRNA.
DR EMBL; CR533520; CAG38551.1; -; mRNA.
DR EMBL; BC000327; AAH00327.1; -; mRNA.
DR EMBL; BC003161; AAH03161.1; -; mRNA.
DR EMBL; BC016452; AAH16452.1; -; mRNA.
DR PIR; T46362; T46362.
DR RefSeq; NP_009215.1; NM_007284.3.
DR UniGene; Hs.436439; -.
DR PDB; 2VAC; X-ray; 1.70 A; A=6-137.
DR PDB; 2W0I; X-ray; 1.80 A; A=181-313.
DR PDBsum; 2VAC; -.
DR PDBsum; 2W0I; -.
DR ProteinModelPortal; Q6IBS0; -.
DR SMR; Q6IBS0; 6-137, 181-313.
DR IntAct; Q6IBS0; 6.
DR MINT; MINT-1414584; -.
DR STRING; 9606.ENSP00000303908; -.
DR PhosphoSite; Q6IBS0; -.
DR DMDM; 94730596; -.
DR OGP; Q9Y3F5; -.
DR PaxDb; Q6IBS0; -.
DR PeptideAtlas; Q6IBS0; -.
DR PRIDE; Q6IBS0; -.
DR DNASU; 11344; -.
DR Ensembl; ENST00000305533; ENSP00000303908; ENSG00000247596.
DR GeneID; 11344; -.
DR KEGG; hsa:11344; -.
DR UCSC; uc003ddd.3; human.
DR CTD; 11344; -.
DR GeneCards; GC03M052262; -.
DR HGNC; HGNC:9621; TWF2.
DR HPA; HPA053874; -.
DR MIM; 607433; gene.
DR neXtProt; NX_Q6IBS0; -.
DR PharmGKB; PA162407429; -.
DR eggNOG; NOG263290; -.
DR HOGENOM; HOG000168296; -.
DR HOVERGEN; HBG000848; -.
DR InParanoid; Q6IBS0; -.
DR KO; K08870; -.
DR OMA; HATPELK; -.
DR OrthoDB; EOG79GT6W; -.
DR EvolutionaryTrace; Q6IBS0; -.
DR GeneWiki; TWF2; -.
DR GenomeRNAi; 11344; -.
DR NextBio; 43112; -.
DR PRO; PR:Q6IBS0; -.
DR ArrayExpress; Q6IBS0; -.
DR Bgee; Q6IBS0; -.
DR CleanEx; HS_TWF2; -.
DR Genevestigator; Q6IBS0; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:BHF-UCL.
DR GO; GO:0030426; C:growth cone; IDA:BHF-UCL.
DR GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0032420; C:stereocilium; ISS:BHF-UCL.
DR GO; GO:0003785; F:actin monomer binding; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISS:BHF-UCL.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:BHF-UCL.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0032532; P:regulation of microvillus length; IC:BHF-UCL.
DR GO; GO:0042989; P:sequestering of actin monomers; ISS:BHF-UCL.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR028458; Twinfilin.
DR PANTHER; PTHR13759; PTHR13759; 1.
DR Pfam; PF00241; Cofilin_ADF; 2.
DR SMART; SM00102; ADF; 2.
DR PROSITE; PS51263; ADF_H; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection;
KW Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 349 Twinfilin-2.
FT /FTId=PRO_0000233136.
FT DOMAIN 4 139 ADF-H 1.
FT DOMAIN 177 313 ADF-H 2.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 N6-acetyllysine.
FT MOD_RES 309 309 Phosphotyrosine.
FT MOD_RES 349 349 Phosphoserine.
FT VARIANT 72 72 R -> C (in dbSNP:rs35114109).
FT /FTId=VAR_042407.
FT VARIANT 76 76 Q -> R (in dbSNP:rs35711542).
FT /FTId=VAR_042408.
FT VARIANT 103 103 A -> T (in a lung neuroendocrine
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_042409.
FT CONFLICT 110 110 K -> R (in Ref. 4; CAG33013).
FT HELIX 11 22
FT STRAND 26 33
FT STRAND 36 43
FT HELIX 49 57
FT HELIX 58 60
FT STRAND 67 77
FT STRAND 80 88
FT HELIX 95 112
FT HELIX 114 116
FT STRAND 117 125
FT HELIX 126 129
FT HELIX 131 136
FT HELIX 184 194
FT STRAND 199 206
FT TURN 207 210
FT STRAND 211 216
FT HELIX 222 228
FT STRAND 231 233
FT STRAND 235 245
FT STRAND 248 258
FT HELIX 261 263
FT HELIX 266 285
FT STRAND 291 298
FT HELIX 300 302
FT HELIX 305 312
SQ SEQUENCE 349 AA; 39548 MW; 635EF8C04EFCE92B CRC64;
MAHQTGIHAT EELKEFFAKA RAGSVRLIKV VIEDEQLVLG ASQEPVGRWD QDYDRAVLPL
LDAQQPCYLL YRLDSQNAQG FEWLFLAWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE
LFGTVKDDLS FAGYQKHLSS CAAPAPLTSA ERELQQIRIN EVKTEISVES KHQTLQGLAF
PLQPEAQRAL QQLKQKMVNY IQMKLDLERE TIELVHTEPT DVAQLPSRVP RDAARYHFFL
YKHTHEGDPL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFHLE IAKKIEIGDG
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGDDS
//
ID TWF2_HUMAN Reviewed; 349 AA.
AC Q6IBS0; Q9Y3F5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Twinfilin-2;
DE AltName: Full=A6-related protein;
DE Short=hA6RP;
DE AltName: Full=Protein tyrosine kinase 9-like;
DE AltName: Full=Twinfilin-1-like protein;
GN Name=TWF2; Synonyms=PTK9L; ORFNames=MSTP011;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RC TISSUE=Keratinocyte;
RX PubMed=10406962; DOI=10.1046/j.1432-1327.1999.00537.x;
RA Rohwer A., Kittstein W., Marks F., Gschwendt M.;
RT "Cloning, expression and characterization of an A6 related protein.";
RL Eur. J. Biochem. 263:518-525(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-19 AND 279-293, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND SER-349, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-14, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-72; ARG-76 AND THR-103.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Actin-binding protein involved in motile and
CC morphological processes. Inhibits actin polymerization, likely by
CC sequestering G-actin. By capping the barbed ends of filaments, it
CC also regulates motility. Seems to play an important role in
CC clathrin-mediated endocytosis and distribution of endocytic
CC organelles. May play a role in regulating the mature length of the
CC middle and short rows of stereocilia (By similarity).
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping
CC protein (CP). May also be able to interact with TWF1 and
CC phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-
CC regulated. Interacts with MYO7A (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC perinuclear region. Cell projection, stereocilium (By similarity).
CC Note=Perinuclear and G-actin-rich cortical actin structure
CC sublocalization.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC -!- PTM: In vitro, phosphorylated by PRKCZ, CK2 and SRC.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC Twinfilin subfamily.
CC -!- SIMILARITY: Contains 2 ADF-H domains.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace -
CC Issue 73 of August 2006;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt073.shtml";
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DR EMBL; Y17169; CAB38055.1; -; mRNA.
DR EMBL; AL136773; CAB66707.1; -; mRNA.
DR EMBL; AF109365; AAQ13513.1; -; mRNA.
DR EMBL; CR456732; CAG33013.1; -; mRNA.
DR EMBL; CR533520; CAG38551.1; -; mRNA.
DR EMBL; BC000327; AAH00327.1; -; mRNA.
DR EMBL; BC003161; AAH03161.1; -; mRNA.
DR EMBL; BC016452; AAH16452.1; -; mRNA.
DR PIR; T46362; T46362.
DR RefSeq; NP_009215.1; NM_007284.3.
DR UniGene; Hs.436439; -.
DR PDB; 2VAC; X-ray; 1.70 A; A=6-137.
DR PDB; 2W0I; X-ray; 1.80 A; A=181-313.
DR PDBsum; 2VAC; -.
DR PDBsum; 2W0I; -.
DR ProteinModelPortal; Q6IBS0; -.
DR SMR; Q6IBS0; 6-137, 181-313.
DR IntAct; Q6IBS0; 6.
DR MINT; MINT-1414584; -.
DR STRING; 9606.ENSP00000303908; -.
DR PhosphoSite; Q6IBS0; -.
DR DMDM; 94730596; -.
DR OGP; Q9Y3F5; -.
DR PaxDb; Q6IBS0; -.
DR PeptideAtlas; Q6IBS0; -.
DR PRIDE; Q6IBS0; -.
DR DNASU; 11344; -.
DR Ensembl; ENST00000305533; ENSP00000303908; ENSG00000247596.
DR GeneID; 11344; -.
DR KEGG; hsa:11344; -.
DR UCSC; uc003ddd.3; human.
DR CTD; 11344; -.
DR GeneCards; GC03M052262; -.
DR HGNC; HGNC:9621; TWF2.
DR HPA; HPA053874; -.
DR MIM; 607433; gene.
DR neXtProt; NX_Q6IBS0; -.
DR PharmGKB; PA162407429; -.
DR eggNOG; NOG263290; -.
DR HOGENOM; HOG000168296; -.
DR HOVERGEN; HBG000848; -.
DR InParanoid; Q6IBS0; -.
DR KO; K08870; -.
DR OMA; HATPELK; -.
DR OrthoDB; EOG79GT6W; -.
DR EvolutionaryTrace; Q6IBS0; -.
DR GeneWiki; TWF2; -.
DR GenomeRNAi; 11344; -.
DR NextBio; 43112; -.
DR PRO; PR:Q6IBS0; -.
DR ArrayExpress; Q6IBS0; -.
DR Bgee; Q6IBS0; -.
DR CleanEx; HS_TWF2; -.
DR Genevestigator; Q6IBS0; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:BHF-UCL.
DR GO; GO:0030426; C:growth cone; IDA:BHF-UCL.
DR GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0032420; C:stereocilium; ISS:BHF-UCL.
DR GO; GO:0003785; F:actin monomer binding; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISS:BHF-UCL.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:BHF-UCL.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0032532; P:regulation of microvillus length; IC:BHF-UCL.
DR GO; GO:0042989; P:sequestering of actin monomers; ISS:BHF-UCL.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR028458; Twinfilin.
DR PANTHER; PTHR13759; PTHR13759; 1.
DR Pfam; PF00241; Cofilin_ADF; 2.
DR SMART; SM00102; ADF; 2.
DR PROSITE; PS51263; ADF_H; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection;
KW Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 349 Twinfilin-2.
FT /FTId=PRO_0000233136.
FT DOMAIN 4 139 ADF-H 1.
FT DOMAIN 177 313 ADF-H 2.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 N6-acetyllysine.
FT MOD_RES 309 309 Phosphotyrosine.
FT MOD_RES 349 349 Phosphoserine.
FT VARIANT 72 72 R -> C (in dbSNP:rs35114109).
FT /FTId=VAR_042407.
FT VARIANT 76 76 Q -> R (in dbSNP:rs35711542).
FT /FTId=VAR_042408.
FT VARIANT 103 103 A -> T (in a lung neuroendocrine
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_042409.
FT CONFLICT 110 110 K -> R (in Ref. 4; CAG33013).
FT HELIX 11 22
FT STRAND 26 33
FT STRAND 36 43
FT HELIX 49 57
FT HELIX 58 60
FT STRAND 67 77
FT STRAND 80 88
FT HELIX 95 112
FT HELIX 114 116
FT STRAND 117 125
FT HELIX 126 129
FT HELIX 131 136
FT HELIX 184 194
FT STRAND 199 206
FT TURN 207 210
FT STRAND 211 216
FT HELIX 222 228
FT STRAND 231 233
FT STRAND 235 245
FT STRAND 248 258
FT HELIX 261 263
FT HELIX 266 285
FT STRAND 291 298
FT HELIX 300 302
FT HELIX 305 312
SQ SEQUENCE 349 AA; 39548 MW; 635EF8C04EFCE92B CRC64;
MAHQTGIHAT EELKEFFAKA RAGSVRLIKV VIEDEQLVLG ASQEPVGRWD QDYDRAVLPL
LDAQQPCYLL YRLDSQNAQG FEWLFLAWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE
LFGTVKDDLS FAGYQKHLSS CAAPAPLTSA ERELQQIRIN EVKTEISVES KHQTLQGLAF
PLQPEAQRAL QQLKQKMVNY IQMKLDLERE TIELVHTEPT DVAQLPSRVP RDAARYHFFL
YKHTHEGDPL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFHLE IAKKIEIGDG
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGDDS
//
MIM
607433
*RECORD*
*FIELD* NO
607433
*FIELD* TI
*607433 TWINFILIN, DROSOPHILA, HOMOLOG OF, 2; TWF2
;;PROTEIN TYROSINE KINASE 9-LIKE; PTK9L;;
read moreA6-RELATED PROTEIN; A6RP
*FIELD* TX
CLONING
Using the catalytic domain of rat Pkc-zeta (176982) as bait in a yeast
2-hybrid screen, Rohwer et al. (1999) cloned PTK9L, which they called
A6RP, from a human keratinocyte cell line cDNA library. The deduced
349-amino acid protein has a calculated molecular mass of 39.5 kD. PTK9L
contains a consensus sequence for actin-depolymerizing proteins and 2
ATP-binding motifs. It shares 64% amino acid identity with the human A6
protein (PTK9), 97% identity with mouse Ptk9l, 34% identity with C.
elegans A6, and 26% identity with yeast twinfilin (see 610932). RT-PCR
and Western blot analysis detected PTK9L in all human and mouse tissues
and cells tested. Immunofluorescence localization revealed spotty
accumulation of PTK9L in the cytoplasm close to nuclei.
GENE FUNCTION
Rohwer et al. (1999) found that PTK9L was phosphorylated by PKC-zeta,
but not significantly by other PKC isoenzymes. It was also
phosphorylated by casein kinase II (see 115442) and most effectively by
the tyrosine kinase SRC (190090). In accordance with its potential
ATP-binding site, PTK9L was able to bind ATP.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PTK9L
gene to chromosome 3 (TMAP stSG1676).
*FIELD* RF
1. Rohwer, A.; Kittstein, W.; Marks, F.; Gschwendt, M.: Cloning,
expression and characterization of an A6-related protein. Europ.
J. Biochem. 263: 518-525, 1999.
*FIELD* CD
Patricia A. Hartz: 12/20/2002
*FIELD* ED
mgross: 09/01/2009
mgross: 4/16/2007
mgross: 12/20/2002
*RECORD*
*FIELD* NO
607433
*FIELD* TI
*607433 TWINFILIN, DROSOPHILA, HOMOLOG OF, 2; TWF2
;;PROTEIN TYROSINE KINASE 9-LIKE; PTK9L;;
read moreA6-RELATED PROTEIN; A6RP
*FIELD* TX
CLONING
Using the catalytic domain of rat Pkc-zeta (176982) as bait in a yeast
2-hybrid screen, Rohwer et al. (1999) cloned PTK9L, which they called
A6RP, from a human keratinocyte cell line cDNA library. The deduced
349-amino acid protein has a calculated molecular mass of 39.5 kD. PTK9L
contains a consensus sequence for actin-depolymerizing proteins and 2
ATP-binding motifs. It shares 64% amino acid identity with the human A6
protein (PTK9), 97% identity with mouse Ptk9l, 34% identity with C.
elegans A6, and 26% identity with yeast twinfilin (see 610932). RT-PCR
and Western blot analysis detected PTK9L in all human and mouse tissues
and cells tested. Immunofluorescence localization revealed spotty
accumulation of PTK9L in the cytoplasm close to nuclei.
GENE FUNCTION
Rohwer et al. (1999) found that PTK9L was phosphorylated by PKC-zeta,
but not significantly by other PKC isoenzymes. It was also
phosphorylated by casein kinase II (see 115442) and most effectively by
the tyrosine kinase SRC (190090). In accordance with its potential
ATP-binding site, PTK9L was able to bind ATP.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PTK9L
gene to chromosome 3 (TMAP stSG1676).
*FIELD* RF
1. Rohwer, A.; Kittstein, W.; Marks, F.; Gschwendt, M.: Cloning,
expression and characterization of an A6-related protein. Europ.
J. Biochem. 263: 518-525, 1999.
*FIELD* CD
Patricia A. Hartz: 12/20/2002
*FIELD* ED
mgross: 09/01/2009
mgross: 4/16/2007
mgross: 12/20/2002