Full text data of TLN2
TLN2
(KIAA0320)
[Confidence: low (only semi-automatic identification from reviews)]
Talin-2
Talin-2
UniProt
Q9Y4G6
ID TLN2_HUMAN Reviewed; 2542 AA.
AC Q9Y4G6; A6NLB8;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Talin-2;
GN Name=TLN2; Synonyms=KIAA0320;
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].
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=12422219; DOI=10.1038/nature01147;
RA Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R.,
RA Voronov S., Chang S., Guo J., Wenk M.R., De Camilli P.;
RT "Recruitment and regulation of phosphatidylinositol phosphate kinase
RT type 1 gamma by the FERM domain of talin.";
RL Nature 420:85-89(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11527381; DOI=10.1006/bbrc.2001.5497;
RA Monkley S.J., Pritchard C.A., Critchley D.R.;
RT "Analysis of the mammalian talin2 gene TLN2.";
RL Biochem. Biophys. Res. Commun. 286:880-885(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-2542.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, 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).
CC -!- FUNCTION: As a major component of focal adhesion plaques that
CC links integrin to the actin cytoskeleton, may play an important
CC role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques
CC and strongly activates its kinase activity (By similarity).
CC -!- SUBUNIT: Interacts directly with PIP5K1C.
CC -!- INTERACTION:
CC P00519:ABL1; NbExp=3; IntAct=EBI-1220811, EBI-375543;
CC P05107:ITGB2; NbExp=5; IntAct=EBI-1220811, EBI-300173;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
CC junction, synapse. Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Focal adhesion
CC plaques and synapses.
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SIMILARITY: Contains 1 I/LWEQ domain.
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DR EMBL; AF402000; AAM73764.1; -; mRNA.
DR EMBL; AC068233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002318; BAA20778.2; -; mRNA.
DR RefSeq; NP_055874.2; NM_015059.2.
DR RefSeq; XP_005254773.1; XM_005254716.1.
DR UniGene; Hs.569438; -.
DR UniGene; Hs.610975; -.
DR ProteinModelPortal; Q9Y4G6; -.
DR SMR; Q9Y4G6; 1-408, 488-914, 916-1046, 1048-1359, 1361-1974, 1976-2292, 2297-2479, 2496-2529.
DR DIP; DIP-17039N; -.
DR IntAct; Q9Y4G6; 6.
DR MINT; MINT-5005773; -.
DR STRING; 9606.ENSP00000303476; -.
DR PhosphoSite; Q9Y4G6; -.
DR DMDM; 229463036; -.
DR PaxDb; Q9Y4G6; -.
DR PRIDE; Q9Y4G6; -.
DR Ensembl; ENST00000306829; ENSP00000303476; ENSG00000171914.
DR Ensembl; ENST00000561311; ENSP00000453508; ENSG00000171914.
DR GeneID; 83660; -.
DR KEGG; hsa:83660; -.
DR UCSC; uc002alb.4; human.
DR CTD; 83660; -.
DR GeneCards; GC15P062682; -.
DR H-InvDB; HIX0012315; -.
DR HGNC; HGNC:15447; TLN2.
DR HPA; CAB017194; -.
DR MIM; 607349; gene.
DR neXtProt; NX_Q9Y4G6; -.
DR PharmGKB; PA37958; -.
DR eggNOG; NOG324465; -.
DR HOGENOM; HOG000006734; -.
DR HOVERGEN; HBG023870; -.
DR InParanoid; Q9Y4G6; -.
DR KO; K06271; -.
DR OMA; QVCPTDS; -.
DR OrthoDB; EOG7TBC1J; -.
DR GeneWiki; TLN2; -.
DR GenomeRNAi; 83660; -.
DR NextBio; 72631; -.
DR PRO; PR:Q9Y4G6; -.
DR ArrayExpress; Q9Y4G6; -.
DR Bgee; Q9Y4G6; -.
DR CleanEx; HS_TLN2; -.
DR Genevestigator; Q9Y4G6; -.
DR GO; GO:0015629; C:actin cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IC:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:InterPro.
DR GO; GO:0045202; C:synapse; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
DR Gene3D; 1.20.1420.10; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR002404; Insln_rcpt_S1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR015711; Talin-2.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR19981:SF3; PTHR19981:SF3; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF08913; VBS; 1.
DR ProDom; PD011820; ILWEQ; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109880; SSF109880; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF47220; SSF47220; 5.
DR PROSITE; PS00660; FERM_1; FALSE_NEG.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Complete proteome; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Synapse.
FT CHAIN 1 2542 Talin-2.
FT /FTId=PRO_0000219431.
FT DOMAIN 88 406 FERM.
FT DOMAIN 2294 2533 I/LWEQ.
FT REGION 312 406 Interaction with PIP5K1C (By similarity).
FT COMPBIAS 861 1193 Ala-rich.
FT MOD_RES 1665 1665 Phosphotyrosine (By similarity).
FT MOD_RES 1843 1843 Phosphothreonine.
FT VARIANT 340 340 V -> A (in dbSNP:rs11634784).
FT /FTId=VAR_055313.
FT VARIANT 1148 1148 A -> S (in dbSNP:rs2280279).
FT /FTId=VAR_014432.
FT VARIANT 1148 1148 A -> T (in dbSNP:rs2280279).
FT /FTId=VAR_059136.
FT VARIANT 1877 1877 V -> I (in dbSNP:rs7182971).
FT /FTId=VAR_055314.
FT VARIANT 2144 2144 T -> I (in dbSNP:rs11633796).
FT /FTId=VAR_055315.
FT VARIANT 2266 2266 F -> L (in dbSNP:rs3816988).
FT /FTId=VAR_014433.
FT CONFLICT 285 285 E -> A (in Ref. 1; AAM73764).
FT CONFLICT 1269 1269 L -> F (in Ref. 1; AAM73764).
SQ SEQUENCE 2542 AA; 271613 MW; 802D50915F4FD4B0 CRC64;
MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK
GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR
IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR
TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF
GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK
YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK
RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES
TMLEESVSPK KSTILQQQFN RTGKAEHGSV ALPAVMRSGS SGPETFNVGS MPSPQQQVMV
GQMHRGHMPP LTSAQQALMG TINTSMHAVQ QAQDDLSELD SLPPLGQDMA SRVWVQNKVD
ESKHEIHSQV DAITAGTASV VNLTAGDPAD TDYTAVGCAI TTISSNLTEM SKGVKLLAAL
MDDEVGSGED LLRAARTLAG AVSDLLKAVQ PTSGEPRQTV LTAAGSIGQA SGDLLRQIGE
NETDERFQDV LMSLAKAVAN AAAMLVLKAK NVAQVAEDTV LQNRVIAAAT QCALSTSQLV
ACAKVVSPTI SSPVCQEQLI EAGKLVDRSV ENCVRACQAA TTDSELLKQV SAAASVVSQA
LHDLLQHVRQ FASRGEPIGR YDQATDTIMC VTESIFSSMG DAGEMVRQAR VLAQATSDLV
NAMRSDAEAE IDMENSKKLL AAAKLLADST ARMVEAAKGA AANPENEDQQ QRLREAAEGL
RVATNAAAQN AIKKKIVNRL EVAAKQAAAA ATQTIAASQN AAVSNKNPAA QQQLVQSCKA
VADHIPQLVQ GVRGSQAQAE DLSAQLALII SSQNFLQPGS KMVSSAKAAV PTVSDQAAAM
QLSQCAKNLA TSLAELRTAS QKAHEACGPM EIDSALNTVQ TLKNELQDAK MAAVESQLKP
LPGETLEKCA QDLGSTSKAV GSSMAQLLTC AAQGNEHYTG VAARETAQAL KTLAQAARGV
AASTTDPAAA HAMLDSARDV MEGSAMLIQE AKQALIAPGD AERQQRLAQV AKAVSHSLNN
CVNCLPGQKD VDVALKSIGE SSKKLLVDSL PPSTKPFQEA QSELNQAAAD LNQSAGEVVH
ATRGQSGELA AASGKFSDDF DEFLDAGIEM AGQAQTKEDQ IQVIGNLKNI SMASSKLLLA
AKSLSVDPGA PNAKNLLAAA ARAVTESINQ LITLCTQQAP GQKECDNALR ELETVKGMLD
NPNEPVSDLS YFDCIESVME NSKVLGESMA GISQNAKTGD LPAFGECVGI ASKALCGLTE
AAAQAAYLVG ISDPNSQAGH QGLVDPIQFA RANQAIQMAC QNLVDPGSSP SQVLSAATIV
AKHTSALCNA CRIASSKTAN PVAKRHFVQS AKEVANSTAN LVKTIKALDG DFSEDNRNKC
RIATAPLIEA VENLTAFASN PEFVSIPAQI SSEGSQAQEP ILVSAKTMLE SSSYLIRTAR
SLAINPKDPP TWSVLAGHSH TVSDSIKSLI TSIRDKAPGQ RECDYSIDGI NRCIRDIEQA
SLAAVSQSLA TRDDISVEAL QEQLTSVVQE IGHLIDPIAT AARGEAAQLG HKVTQLASYF
EPLILAAVGV ASKILDHQQQ MTVLDQTKTL AESALQMLYA AKEGGGNPKA QHTHDAITEA
AQLMKEAVDD IMVTLNEAAS EVGLVGGMVD AIAEAMSKLD EGTPPEPKGT FVDYQTTVVK
YSKAIAVTAQ EMMTKSVTNP EELGGLASQM TSDYGHLAFQ GQMAAATAEP EEIGFQIRTR
VQDLGHGCIF LVQKAGALQV CPTDSYTKRE LIECARAVTE KVSLVLSALQ AGNKGTQACI
TAATAVSGII ADLDTTIMFA TAGTLNAENS ETFADHRENI LKTAKALVED TKLLVSGAAS
TPDKLAQAAQ SSAATITQLA EVVKLGAASL GSDDPETQVV LINAIKDVAK ALSDLISATK
GAASKPVDDP SMYQLKGAAK VMVTNVTSLL KTVKAVEDEA TRGTRALEAT IECIKQELTV
FQSKDVPEKT SSPEESIRMT KGITMATAKA VAAGNSCRQE DVIATANLSR KAVSDMLTAC
KQASFHPDVS DEVRTRALRF GTECTLGYLD LLEHVLVILQ KPTPEFKQQL AAFSKRVAGA
VTELIQAAEA MKGTEWVDPE DPTVIAETEL LGAAASIEAA AKKLEQLKPR AKPKQADETL
DFEEQILEAA KSIAAATSAL VKSASAAQRE LVAQGKVGSI PANAADDGQW SQGLISAARM
VAAATSSLCE AANASVQGHA SEEKLISSAK QVAASTAQLL VACKVKADQD SEAMRRLQAA
GNAVKRASDN LVRAAQKAAF GKADDDDVVV KTKFVGGIAQ IIAAQEEMLK KERELEEARK
KLAQIRQQQY KFLPTELRED EG
//
ID TLN2_HUMAN Reviewed; 2542 AA.
AC Q9Y4G6; A6NLB8;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Talin-2;
GN Name=TLN2; Synonyms=KIAA0320;
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].
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=12422219; DOI=10.1038/nature01147;
RA Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R.,
RA Voronov S., Chang S., Guo J., Wenk M.R., De Camilli P.;
RT "Recruitment and regulation of phosphatidylinositol phosphate kinase
RT type 1 gamma by the FERM domain of talin.";
RL Nature 420:85-89(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11527381; DOI=10.1006/bbrc.2001.5497;
RA Monkley S.J., Pritchard C.A., Critchley D.R.;
RT "Analysis of the mammalian talin2 gene TLN2.";
RL Biochem. Biophys. Res. Commun. 286:880-885(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-2542.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, 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).
CC -!- FUNCTION: As a major component of focal adhesion plaques that
CC links integrin to the actin cytoskeleton, may play an important
CC role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques
CC and strongly activates its kinase activity (By similarity).
CC -!- SUBUNIT: Interacts directly with PIP5K1C.
CC -!- INTERACTION:
CC P00519:ABL1; NbExp=3; IntAct=EBI-1220811, EBI-375543;
CC P05107:ITGB2; NbExp=5; IntAct=EBI-1220811, EBI-300173;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
CC junction, synapse. Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Focal adhesion
CC plaques and synapses.
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SIMILARITY: Contains 1 I/LWEQ domain.
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DR EMBL; AF402000; AAM73764.1; -; mRNA.
DR EMBL; AC068233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002318; BAA20778.2; -; mRNA.
DR RefSeq; NP_055874.2; NM_015059.2.
DR RefSeq; XP_005254773.1; XM_005254716.1.
DR UniGene; Hs.569438; -.
DR UniGene; Hs.610975; -.
DR ProteinModelPortal; Q9Y4G6; -.
DR SMR; Q9Y4G6; 1-408, 488-914, 916-1046, 1048-1359, 1361-1974, 1976-2292, 2297-2479, 2496-2529.
DR DIP; DIP-17039N; -.
DR IntAct; Q9Y4G6; 6.
DR MINT; MINT-5005773; -.
DR STRING; 9606.ENSP00000303476; -.
DR PhosphoSite; Q9Y4G6; -.
DR DMDM; 229463036; -.
DR PaxDb; Q9Y4G6; -.
DR PRIDE; Q9Y4G6; -.
DR Ensembl; ENST00000306829; ENSP00000303476; ENSG00000171914.
DR Ensembl; ENST00000561311; ENSP00000453508; ENSG00000171914.
DR GeneID; 83660; -.
DR KEGG; hsa:83660; -.
DR UCSC; uc002alb.4; human.
DR CTD; 83660; -.
DR GeneCards; GC15P062682; -.
DR H-InvDB; HIX0012315; -.
DR HGNC; HGNC:15447; TLN2.
DR HPA; CAB017194; -.
DR MIM; 607349; gene.
DR neXtProt; NX_Q9Y4G6; -.
DR PharmGKB; PA37958; -.
DR eggNOG; NOG324465; -.
DR HOGENOM; HOG000006734; -.
DR HOVERGEN; HBG023870; -.
DR InParanoid; Q9Y4G6; -.
DR KO; K06271; -.
DR OMA; QVCPTDS; -.
DR OrthoDB; EOG7TBC1J; -.
DR GeneWiki; TLN2; -.
DR GenomeRNAi; 83660; -.
DR NextBio; 72631; -.
DR PRO; PR:Q9Y4G6; -.
DR ArrayExpress; Q9Y4G6; -.
DR Bgee; Q9Y4G6; -.
DR CleanEx; HS_TLN2; -.
DR Genevestigator; Q9Y4G6; -.
DR GO; GO:0015629; C:actin cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IC:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:InterPro.
DR GO; GO:0045202; C:synapse; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
DR Gene3D; 1.20.1420.10; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR002404; Insln_rcpt_S1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR015711; Talin-2.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR19981:SF3; PTHR19981:SF3; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF08913; VBS; 1.
DR ProDom; PD011820; ILWEQ; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109880; SSF109880; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF47220; SSF47220; 5.
DR PROSITE; PS00660; FERM_1; FALSE_NEG.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Complete proteome; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Synapse.
FT CHAIN 1 2542 Talin-2.
FT /FTId=PRO_0000219431.
FT DOMAIN 88 406 FERM.
FT DOMAIN 2294 2533 I/LWEQ.
FT REGION 312 406 Interaction with PIP5K1C (By similarity).
FT COMPBIAS 861 1193 Ala-rich.
FT MOD_RES 1665 1665 Phosphotyrosine (By similarity).
FT MOD_RES 1843 1843 Phosphothreonine.
FT VARIANT 340 340 V -> A (in dbSNP:rs11634784).
FT /FTId=VAR_055313.
FT VARIANT 1148 1148 A -> S (in dbSNP:rs2280279).
FT /FTId=VAR_014432.
FT VARIANT 1148 1148 A -> T (in dbSNP:rs2280279).
FT /FTId=VAR_059136.
FT VARIANT 1877 1877 V -> I (in dbSNP:rs7182971).
FT /FTId=VAR_055314.
FT VARIANT 2144 2144 T -> I (in dbSNP:rs11633796).
FT /FTId=VAR_055315.
FT VARIANT 2266 2266 F -> L (in dbSNP:rs3816988).
FT /FTId=VAR_014433.
FT CONFLICT 285 285 E -> A (in Ref. 1; AAM73764).
FT CONFLICT 1269 1269 L -> F (in Ref. 1; AAM73764).
SQ SEQUENCE 2542 AA; 271613 MW; 802D50915F4FD4B0 CRC64;
MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK
GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR
IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR
TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF
GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK
YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK
RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES
TMLEESVSPK KSTILQQQFN RTGKAEHGSV ALPAVMRSGS SGPETFNVGS MPSPQQQVMV
GQMHRGHMPP LTSAQQALMG TINTSMHAVQ QAQDDLSELD SLPPLGQDMA SRVWVQNKVD
ESKHEIHSQV DAITAGTASV VNLTAGDPAD TDYTAVGCAI TTISSNLTEM SKGVKLLAAL
MDDEVGSGED LLRAARTLAG AVSDLLKAVQ PTSGEPRQTV LTAAGSIGQA SGDLLRQIGE
NETDERFQDV LMSLAKAVAN AAAMLVLKAK NVAQVAEDTV LQNRVIAAAT QCALSTSQLV
ACAKVVSPTI SSPVCQEQLI EAGKLVDRSV ENCVRACQAA TTDSELLKQV SAAASVVSQA
LHDLLQHVRQ FASRGEPIGR YDQATDTIMC VTESIFSSMG DAGEMVRQAR VLAQATSDLV
NAMRSDAEAE IDMENSKKLL AAAKLLADST ARMVEAAKGA AANPENEDQQ QRLREAAEGL
RVATNAAAQN AIKKKIVNRL EVAAKQAAAA ATQTIAASQN AAVSNKNPAA QQQLVQSCKA
VADHIPQLVQ GVRGSQAQAE DLSAQLALII SSQNFLQPGS KMVSSAKAAV PTVSDQAAAM
QLSQCAKNLA TSLAELRTAS QKAHEACGPM EIDSALNTVQ TLKNELQDAK MAAVESQLKP
LPGETLEKCA QDLGSTSKAV GSSMAQLLTC AAQGNEHYTG VAARETAQAL KTLAQAARGV
AASTTDPAAA HAMLDSARDV MEGSAMLIQE AKQALIAPGD AERQQRLAQV AKAVSHSLNN
CVNCLPGQKD VDVALKSIGE SSKKLLVDSL PPSTKPFQEA QSELNQAAAD LNQSAGEVVH
ATRGQSGELA AASGKFSDDF DEFLDAGIEM AGQAQTKEDQ IQVIGNLKNI SMASSKLLLA
AKSLSVDPGA PNAKNLLAAA ARAVTESINQ LITLCTQQAP GQKECDNALR ELETVKGMLD
NPNEPVSDLS YFDCIESVME NSKVLGESMA GISQNAKTGD LPAFGECVGI ASKALCGLTE
AAAQAAYLVG ISDPNSQAGH QGLVDPIQFA RANQAIQMAC QNLVDPGSSP SQVLSAATIV
AKHTSALCNA CRIASSKTAN PVAKRHFVQS AKEVANSTAN LVKTIKALDG DFSEDNRNKC
RIATAPLIEA VENLTAFASN PEFVSIPAQI SSEGSQAQEP ILVSAKTMLE SSSYLIRTAR
SLAINPKDPP TWSVLAGHSH TVSDSIKSLI TSIRDKAPGQ RECDYSIDGI NRCIRDIEQA
SLAAVSQSLA TRDDISVEAL QEQLTSVVQE IGHLIDPIAT AARGEAAQLG HKVTQLASYF
EPLILAAVGV ASKILDHQQQ MTVLDQTKTL AESALQMLYA AKEGGGNPKA QHTHDAITEA
AQLMKEAVDD IMVTLNEAAS EVGLVGGMVD AIAEAMSKLD EGTPPEPKGT FVDYQTTVVK
YSKAIAVTAQ EMMTKSVTNP EELGGLASQM TSDYGHLAFQ GQMAAATAEP EEIGFQIRTR
VQDLGHGCIF LVQKAGALQV CPTDSYTKRE LIECARAVTE KVSLVLSALQ AGNKGTQACI
TAATAVSGII ADLDTTIMFA TAGTLNAENS ETFADHRENI LKTAKALVED TKLLVSGAAS
TPDKLAQAAQ SSAATITQLA EVVKLGAASL GSDDPETQVV LINAIKDVAK ALSDLISATK
GAASKPVDDP SMYQLKGAAK VMVTNVTSLL KTVKAVEDEA TRGTRALEAT IECIKQELTV
FQSKDVPEKT SSPEESIRMT KGITMATAKA VAAGNSCRQE DVIATANLSR KAVSDMLTAC
KQASFHPDVS DEVRTRALRF GTECTLGYLD LLEHVLVILQ KPTPEFKQQL AAFSKRVAGA
VTELIQAAEA MKGTEWVDPE DPTVIAETEL LGAAASIEAA AKKLEQLKPR AKPKQADETL
DFEEQILEAA KSIAAATSAL VKSASAAQRE LVAQGKVGSI PANAADDGQW SQGLISAARM
VAAATSSLCE AANASVQGHA SEEKLISSAK QVAASTAQLL VACKVKADQD SEAMRRLQAA
GNAVKRASDN LVRAAQKAAF GKADDDDVVV KTKFVGGIAQ IIAAQEEMLK KERELEEARK
KLAQIRQQQY KFLPTELRED EG
//
MIM
607349
*RECORD*
*FIELD* NO
607349
*FIELD* TI
*607349 TALIN 2; TLN2
;;KIAA0320
*FIELD* TX
CLONING
By randomly sequencing clones from a brain cDNA library, Nagase et al.
read more(1997) obtained a partial cDNA encoding TLN2, which they called
KIAA0320. RT-PCR detected expression in heart, brain, kidney, thymus,
testis, and small intestine.
Using genomic and cDNA/EST sequences, Monkley et al. (2001) assembled
the complete coding sequence for TLN2. The deduced 2,532-amino acid
protein contains a FERM domain. In TLN1 (186745), the FERM domain binds
the cytodomains of beta-1 (135630) and beta-3 (173470) integrins, as
well as to F-actin (see 102610) and other proteins. TLN2 shares 74%
identity with TLN1, and the N- and C-terminal regions of TLN2 are highly
conserved across species. Analysis of EST databases indicated that both
TLN1 and TLN2 are expressed in brain, lung, heart, eye, mammary gland,
colon, stomach, lymphocytes, germ cells, liver, spleen, bone, and many
tumors. Northern blot analysis of adult mouse tissues revealed multiple
Tln2 transcripts, with highest expression in heart and undetectable
expression in spleen.
GENE FUNCTION
DiPaolo et al. (2002) and Ling et al. (2002) presented evidence that
talin, through its FERM domain, interacts with the C-terminal tail of
the 90-kD PIP5K1C (606102) isoform. DiPaolo et al. (2002) determined
that, in rat brain, the predominant talin that interacts with PIP5K1C is
Tln2. The authors showed that this interaction induces clustering of
PIP5D1C and talin at focal adhesions and increases the local production
of phosphatidylinositol-4,5-bisphosphate.
GENE STRUCTURE
Monkley et al. (2001) determined that the TLN2 gene contains 55 exons
and spans about 190 kb.
MAPPING
By radiation hybrid analysis, Nagase et al. (1997) mapped the TLN2 gene
to chromosome 15. By genomic sequence analysis, Monkley et al. (2001)
mapped the TLN2 gene to chromosome 15q15-q21.
*FIELD* RF
1. Di Paolo, G.; Pellegrini, L.; Letinic, K.; Cestra, G.; Zoncu, R.;
Voronov, S.; Chang, S.; Guo, J.; Wenk, M. R.; De Camill, P.: Recruitment
and regulation of phosphatidylinositol phosphate kinase type I-gamma
by the FERM domain of talin. Nature 420: 85-89, 2002.
2. Ling, K.; Doughman, R. L.; Firestone, A. J.; Bunce, M. W.; Anderson,
R. A.: Type I-gamma phosphatidylinositol phosphate kinase targets
and regulates focal adhesions. Nature 420: 89-93, 2002.
3. Monkley, S. J.; Pritchard, C. A.; Critchley, D. R.: Analysis of
the mammalian talin2 gene TLN2. Biochem. Biophys. Res. Commun. 286:
880-885, 2001.
4. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
*FIELD* CD
Patricia A. Hartz: 11/14/2002
*FIELD* ED
mgross: 11/14/2002
*RECORD*
*FIELD* NO
607349
*FIELD* TI
*607349 TALIN 2; TLN2
;;KIAA0320
*FIELD* TX
CLONING
By randomly sequencing clones from a brain cDNA library, Nagase et al.
read more(1997) obtained a partial cDNA encoding TLN2, which they called
KIAA0320. RT-PCR detected expression in heart, brain, kidney, thymus,
testis, and small intestine.
Using genomic and cDNA/EST sequences, Monkley et al. (2001) assembled
the complete coding sequence for TLN2. The deduced 2,532-amino acid
protein contains a FERM domain. In TLN1 (186745), the FERM domain binds
the cytodomains of beta-1 (135630) and beta-3 (173470) integrins, as
well as to F-actin (see 102610) and other proteins. TLN2 shares 74%
identity with TLN1, and the N- and C-terminal regions of TLN2 are highly
conserved across species. Analysis of EST databases indicated that both
TLN1 and TLN2 are expressed in brain, lung, heart, eye, mammary gland,
colon, stomach, lymphocytes, germ cells, liver, spleen, bone, and many
tumors. Northern blot analysis of adult mouse tissues revealed multiple
Tln2 transcripts, with highest expression in heart and undetectable
expression in spleen.
GENE FUNCTION
DiPaolo et al. (2002) and Ling et al. (2002) presented evidence that
talin, through its FERM domain, interacts with the C-terminal tail of
the 90-kD PIP5K1C (606102) isoform. DiPaolo et al. (2002) determined
that, in rat brain, the predominant talin that interacts with PIP5K1C is
Tln2. The authors showed that this interaction induces clustering of
PIP5D1C and talin at focal adhesions and increases the local production
of phosphatidylinositol-4,5-bisphosphate.
GENE STRUCTURE
Monkley et al. (2001) determined that the TLN2 gene contains 55 exons
and spans about 190 kb.
MAPPING
By radiation hybrid analysis, Nagase et al. (1997) mapped the TLN2 gene
to chromosome 15. By genomic sequence analysis, Monkley et al. (2001)
mapped the TLN2 gene to chromosome 15q15-q21.
*FIELD* RF
1. Di Paolo, G.; Pellegrini, L.; Letinic, K.; Cestra, G.; Zoncu, R.;
Voronov, S.; Chang, S.; Guo, J.; Wenk, M. R.; De Camill, P.: Recruitment
and regulation of phosphatidylinositol phosphate kinase type I-gamma
by the FERM domain of talin. Nature 420: 85-89, 2002.
2. Ling, K.; Doughman, R. L.; Firestone, A. J.; Bunce, M. W.; Anderson,
R. A.: Type I-gamma phosphatidylinositol phosphate kinase targets
and regulates focal adhesions. Nature 420: 89-93, 2002.
3. Monkley, S. J.; Pritchard, C. A.; Critchley, D. R.: Analysis of
the mammalian talin2 gene TLN2. Biochem. Biophys. Res. Commun. 286:
880-885, 2001.
4. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
*FIELD* CD
Patricia A. Hartz: 11/14/2002
*FIELD* ED
mgross: 11/14/2002