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P26039

- TLN1_MOUSE

UniProt

P26039 - TLN1_MOUSE

Protein

Talin-1

Gene

Tln1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: InterPro
    2. cell-substrate junction assembly Source: MGI
    3. cortical actin cytoskeleton organization Source: MGI
    4. cytoskeletal anchoring at plasma membrane Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Talin-1
    Gene namesi
    Name:Tln1
    Synonyms:Tln
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1099832. Tln1.

    Subcellular locationi

    Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Cell surface 1 Publication. Cell junctionfocal adhesion 1 Publication
    Note: Colocalizes with LAYN at the membrane ruffles By similarity. Localized preferentially in focal adhesions than fibrillar adhesions.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: InterPro
    2. cell surface Source: UniProtKB-SubCell
    3. centrosome Source: Ensembl
    4. cytoplasm Source: UniProtKB-KW
    5. extracellular vesicular exosome Source: Ensembl
    6. focal adhesion Source: HGNC
    7. intracellular membrane-bounded organelle Source: Ensembl
    8. ruffle Source: HGNC
    9. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25412541Talin-1PRO_0000219429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei425 – 4251PhosphoserineBy similarity
    Modified residuei1116 – 11161Phosphotyrosine2 Publications
    Modified residuei1544 – 15441N6-acetyllysine1 Publication
    Modified residuei2031 – 20311N6-acetyllysineBy similarity
    Modified residuei2040 – 20401PhosphoserineBy similarity
    Modified residuei2115 – 21151N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26039.
    PaxDbiP26039.
    PRIDEiP26039.

    PTM databases

    PhosphoSiteiP26039.

    Expressioni

    Gene expression databases

    ArrayExpressiP26039.
    BgeeiP26039.
    CleanExiMM_TLN1.
    GenevestigatoriP26039.

    Interactioni

    Subunit structurei

    Interacts with NRAP and LAYN. Interacts with SYNM. Interacts with ITGB1; the interaction is prevented by competitive binding of ITGB1BP1 By similarity. Binds with high affinity to VCL and with low affinity to integrins. Interacts with APBB1IP; this inhibits VCL binding. Interacts with PTK2/FAK1. Interacts with PIP5K1C.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ITGB3P051063EBI-1039593,EBI-702847From a different organism.
    VCLP120033EBI-1039593,EBI-1039563From a different organism.
    VclQ647272EBI-1039593,EBI-432047

    Protein-protein interaction databases

    BioGridi204222. 5 interactions.
    DIPiDIP-647N.
    IntActiP26039. 12 interactions.
    MINTiMINT-258500.

    Structurei

    Secondary structure

    1
    2541
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Beta strandi13 – 197
    Helixi25 – 339
    Helixi37 – 404
    Helixi44 – 463
    Beta strandi47 – 515
    Helixi56 – 583
    Beta strandi60 – 623
    Helixi68 – 714
    Beta strandi78 – 836
    Beta strandi85 – 917
    Beta strandi97 – 1037
    Helixi108 – 11811
    Helixi124 – 1263
    Beta strandi127 – 1304
    Beta strandi136 – 1383
    Beta strandi146 – 1505
    Beta strandi168 – 1747
    Beta strandi176 – 1783
    Helixi181 – 1833
    Beta strandi190 – 1956
    Helixi209 – 22416
    Beta strandi226 – 2283
    Helixi232 – 24716
    Turni252 – 2543
    Helixi262 – 2643
    Helixi268 – 2703
    Helixi275 – 28511
    Turni286 – 2883
    Helixi291 – 30414
    Turni306 – 3094
    Beta strandi311 – 3188
    Beta strandi325 – 3328
    Beta strandi334 – 3418
    Turni342 – 3443
    Beta strandi347 – 3526
    Helixi353 – 3553
    Beta strandi358 – 3625
    Beta strandi365 – 3695
    Helixi371 – 3733
    Beta strandi374 – 3763
    Beta strandi378 – 3814
    Helixi385 – 39713
    Helixi493 – 51220
    Helixi526 – 56035
    Beta strandi565 – 5673
    Helixi570 – 60031
    Helixi606 – 62621
    Helixi634 – 65219
    Helixi664 – 69027
    Beta strandi696 – 6994
    Helixi700 – 72324
    Turni724 – 7263
    Helixi730 – 75627
    Helixi762 – 78019
    Beta strandi787 – 7904
    Beta strandi792 – 7943
    Helixi799 – 81416
    Turni815 – 8173
    Helixi820 – 84324
    Helixi844 – 8463
    Helixi850 – 87627
    Beta strandi878 – 8803
    Helixi884 – 90724
    Helixi914 – 93825
    Beta strandi943 – 9464
    Helixi951 – 97525
    Helixi980 – 100728
    Helixi1008 – 10103
    Helixi1014 – 104229
    Helixi1049 – 107325
    Helixi1084 – 110522
    Helixi1115 – 114127
    Helixi1147 – 117226
    Beta strandi1174 – 11774
    Helixi1179 – 120123
    Helixi1207 – 122317
    Turni1224 – 12263
    Helixi1235 – 126026
    Helixi1264 – 128926
    Helixi1295 – 132430
    Helixi1329 – 135325
    Helixi1359 – 137315
    Helixi1374 – 13774
    Beta strandi1384 – 13863
    Helixi1389 – 141628
    Helixi1419 – 145032
    Helixi1465 – 148218
    Helixi1488 – 151326
    Helixi1521 – 154424
    Helixi1552 – 157625
    Beta strandi1578 – 15825
    Helixi1590 – 162031
    Helixi1627 – 165428
    Helixi1655 – 16584
    Turni1683 – 16853
    Helixi1695 – 172228
    Helixi1724 – 173613
    Helixi1738 – 175114
    Helixi1755 – 178228
    Helixi1787 – 17893
    Helixi1790 – 182031
    Beta strandi1822 – 18243
    Helixi1827 – 184014
    Helixi1847 – 187428
    Turni1875 – 18773
    Helixi1879 – 18813
    Helixi1882 – 190423
    Beta strandi1907 – 19093
    Helixi1910 – 193930
    Helixi1944 – 196825
    Helixi1969 – 19713
    Helixi1976 – 200025
    Helixi2012 – 20143
    Helixi2016 – 203621
    Beta strandi2037 – 20393
    Helixi2041 – 206828
    Helixi2074 – 210027
    Turni2101 – 21033
    Helixi2109 – 216153
    Beta strandi2162 – 21643
    Helixi2172 – 219524
    Helixi2198 – 222326
    Helixi2230 – 225930
    Helixi2263 – 228826
    Helixi2301 – 232424
    Beta strandi2332 – 23343
    Helixi2341 – 237333
    Helixi2380 – 23823
    Helixi2383 – 241634
    Helixi2421 – 244222
    Turni2443 – 24453
    Helixi2451 – 247626
    Helixi2497 – 252832

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SJ7X-ray2.50A/B/C482-655[»]
    1SJ8X-ray2.60A482-789[»]
    1T01X-ray2.06B605-628[»]
    1U89NMR-A755-889[»]
    1XWXmodel-A486-889[»]
    1Y19X-ray2.60B/D/F/H/J/L209-410[»]
    1ZW3X-ray3.30B1628-1652[»]
    2B0HNMR-A1843-1973[»]
    2G35NMR-A305-404[»]
    2JSWNMR-A2300-2482[»]
    2KBBNMR-A1655-1822[»]
    2KC1NMR-A1-85[»]
    2KC2NMR-A86-202[»]
    2KGXNMR-A1655-1822[»]
    B311-401[»]
    2KMANMR-A1-202[»]
    2KVPNMR-A1815-1973[»]
    2L10NMR-A1206-1357[»]
    2L7ANMR-A787-911[»]
    2L7NNMR-A1046-1207[»]
    2LQGNMR-A913-1044[»]
    2QDQX-ray2.20A/B2494-2541[»]
    2X0CX-ray2.00A1359-1659[»]
    3DYJX-ray1.85A/B1974-2293[»]
    3IVFX-ray1.94A1-400[»]
    3S90X-ray1.97C/D1512-1546[»]
    4F7GX-ray2.05A206-405[»]
    B1654-1847[»]
    DisProtiDP00653.
    ProteinModelPortaliP26039.
    SMRiP26039. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26039.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 403318FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini2293 – 2533241I/LWEQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni280 – 435156Interaction with LAYNBy similarityAdd
    BLAST
    Regioni1327 – 1948622Interaction with SYNMBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 1 I/LWEQ domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG324465.
    GeneTreeiENSGT00550000074542.
    HOVERGENiHBG023870.
    InParanoidiA2AIM8.
    KOiK06271.
    OMAiGAHIKHR.
    OrthoDBiEOG7TBC1J.
    TreeFamiTF314677.

    Family and domain databases

    Gene3Di1.20.1410.10. 3 hits.
    1.20.1420.10. 1 hit.
    1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR002558. ILWEQ_dom.
    IPR002404. Insln_rcpt_S1.
    IPR011993. PH_like_dom.
    IPR015710. Talin-1.
    IPR015224. Talin_cent.
    IPR029071. Ubiquitin-rel_dom.
    IPR015009. Vinculin-bd_dom.
    IPR006077. Vinculin/catenin.
    [Graphical view]
    PANTHERiPTHR19981:SF7. PTHR19981:SF7. 1 hit.
    PfamiPF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF01608. I_LWEQ. 1 hit.
    PF02174. IRS. 1 hit.
    PF09141. Talin_middle. 1 hit.
    PF08913. VBS. 2 hits.
    [Graphical view]
    ProDomiPD011820. ILWEQ. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00295. B41. 1 hit.
    SM00307. ILWEQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF109880. SSF109880. 1 hit.
    SSF109885. SSF109885. 4 hits.
    SSF47031. SSF47031. 1 hit.
    SSF47220. SSF47220. 5 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P26039-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF     50
    LSDDDPKKGI WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI 100
    MVDDSKTVTD MLMTICARIG ITNHDEYSLV RELMEEKKDE GTGTLRKDKT 150
    LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL REQGVEEHET LLLRRKFFYS 200
    DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG FQCQIQFGPH 250
    NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 300
    LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE 350
    WSLTNIKRWA ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL 400
    KKKKSKDHFG LEGDEESTML EDSVSPKKST VLQQQYNRVG KVEHGSVALP 450
    AIMRSGASGP ENFQVGSMPP AQQQITSGQM HRGHMPPLTS AQQALTGTIN 500
    SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK HEIHSQVDAI 550
    TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 600
    EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE 650
    LLQQIGESDT DPHFQDVLMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT 700
    QVIAAATQCA LSTSQLVACT KVVAPTISSP VCQEQLVEAG RLVAKAVEGC 750
    VSASQAATED GQLLRGVGAA ATAVTQALNE LLQHVKAHAT GAGPAGRYDQ 800
    ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI KADAEGESDL 850
    ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 900
    TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP 950
    LLVQSCKAVA EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM 1000
    VAAAKASVPT IQDQASAMQL SQCAKNLGTA LAELRTAAQK AQEACGPLEM 1050
    DSALSVVQNL EKDLQEIKAA ARDGKLKPLP GETMEKCTQD LGNSTKAVSS 1100
    AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA LTSDPAVQAI 1150
    VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV 1200
    SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN 1250
    QAATELVQAS RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ 1300
    VVSNLKGISM SSSKLLLAAK ALSTDPASPN LKSQLAAAAR AVTDSINQLI 1350
    TMCTQQAPGQ KECDNALRQL ETVRELLENP VQPINDMSYF GCLDSVMENS 1400
    KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA AQAAYLVGVS 1450
    DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 1500
    HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF 1550
    TEENRAQCRA ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV 1600
    ISAKTMLESA GGLIQTARAL AVNPRDPPRW SVLAGHSRTV SDSIKKLITS 1650
    MRDKAPGQLE CETAIAALNS CLRDLDQASL AAVSQQLAPR EGISQEALHT 1700
    QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP LTLAAVGAAS 1750
    KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 1800
    QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF 1850
    VDYQTTMVRT AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA 1900
    KPAAVAAENE EIGAHIKHRV QELGHGCSAL VTKAGALQCS PSDVYTKKEL 1950
    IECARRVSEK VSHVLAALQA GNRGTQACIT AASAVSGIIA DLDTTIMFAT 2000
    AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS QEKLAQAAQS 2050
    SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 2100
    AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT 2150
    EHIRQELAVF CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED 2200
    VIATANLSRR AIADMLRACK EAAFHPEVAP DVRLRALHYG RECANGYLEL 2250
    LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV TELIQAAEAM KGTEWVDPED 2300
    PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN FEEQILEAAK 2350
    SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 2400
    AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS 2450
    EAMKRLQAAG NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ 2500
    IIAAQEEMLR KERELEEARK KLAQIRQQQY KFLPSELRDE H 2541
    Length:2,541
    Mass (Da):269,821
    Last modified:July 27, 2011 - v2
    Checksum:i78832388E2392B8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti673 – 6731K → N in CAA39588. (PubMed:2120593)Curated
    Sequence conflicti1227 – 12271S → L in CAA39588. (PubMed:2120593)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1105 – 11051L → P.
    Natural varianti2180 – 21801K → M.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56123 mRNA. Translation: CAA39588.1.
    AL732506 Genomic DNA. Translation: CAM17190.1.
    BC018557 mRNA. Translation: AAH18557.1.
    BC150810 mRNA. Translation: AAI50811.1.
    CCDSiCCDS18101.1.
    PIRiS11661.
    RefSeqiNP_035732.2. NM_011602.5.
    UniGeneiMm.208601.

    Genome annotation databases

    EnsembliENSMUST00000030187; ENSMUSP00000030187; ENSMUSG00000028465.
    GeneIDi21894.
    KEGGimmu:21894.
    UCSCiuc008sqe.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56123 mRNA. Translation: CAA39588.1 .
    AL732506 Genomic DNA. Translation: CAM17190.1 .
    BC018557 mRNA. Translation: AAH18557.1 .
    BC150810 mRNA. Translation: AAI50811.1 .
    CCDSi CCDS18101.1.
    PIRi S11661.
    RefSeqi NP_035732.2. NM_011602.5.
    UniGenei Mm.208601.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SJ7 X-ray 2.50 A/B/C 482-655 [» ]
    1SJ8 X-ray 2.60 A 482-789 [» ]
    1T01 X-ray 2.06 B 605-628 [» ]
    1U89 NMR - A 755-889 [» ]
    1XWX model - A 486-889 [» ]
    1Y19 X-ray 2.60 B/D/F/H/J/L 209-410 [» ]
    1ZW3 X-ray 3.30 B 1628-1652 [» ]
    2B0H NMR - A 1843-1973 [» ]
    2G35 NMR - A 305-404 [» ]
    2JSW NMR - A 2300-2482 [» ]
    2KBB NMR - A 1655-1822 [» ]
    2KC1 NMR - A 1-85 [» ]
    2KC2 NMR - A 86-202 [» ]
    2KGX NMR - A 1655-1822 [» ]
    B 311-401 [» ]
    2KMA NMR - A 1-202 [» ]
    2KVP NMR - A 1815-1973 [» ]
    2L10 NMR - A 1206-1357 [» ]
    2L7A NMR - A 787-911 [» ]
    2L7N NMR - A 1046-1207 [» ]
    2LQG NMR - A 913-1044 [» ]
    2QDQ X-ray 2.20 A/B 2494-2541 [» ]
    2X0C X-ray 2.00 A 1359-1659 [» ]
    3DYJ X-ray 1.85 A/B 1974-2293 [» ]
    3IVF X-ray 1.94 A 1-400 [» ]
    3S90 X-ray 1.97 C/D 1512-1546 [» ]
    4F7G X-ray 2.05 A 206-405 [» ]
    B 1654-1847 [» ]
    DisProti DP00653.
    ProteinModelPortali P26039.
    SMRi P26039. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204222. 5 interactions.
    DIPi DIP-647N.
    IntActi P26039. 12 interactions.
    MINTi MINT-258500.

    PTM databases

    PhosphoSitei P26039.

    Proteomic databases

    MaxQBi P26039.
    PaxDbi P26039.
    PRIDEi P26039.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030187 ; ENSMUSP00000030187 ; ENSMUSG00000028465 .
    GeneIDi 21894.
    KEGGi mmu:21894.
    UCSCi uc008sqe.2. mouse.

    Organism-specific databases

    CTDi 7094.
    MGIi MGI:1099832. Tln1.

    Phylogenomic databases

    eggNOGi NOG324465.
    GeneTreei ENSGT00550000074542.
    HOVERGENi HBG023870.
    InParanoidi A2AIM8.
    KOi K06271.
    OMAi GAHIKHR.
    OrthoDBi EOG7TBC1J.
    TreeFami TF314677.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi TLN1. mouse.
    EvolutionaryTracei P26039.
    NextBioi 301428.
    PROi P26039.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26039.
    Bgeei P26039.
    CleanExi MM_TLN1.
    Genevestigatori P26039.

    Family and domain databases

    Gene3Di 1.20.1410.10. 3 hits.
    1.20.1420.10. 1 hit.
    1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR002558. ILWEQ_dom.
    IPR002404. Insln_rcpt_S1.
    IPR011993. PH_like_dom.
    IPR015710. Talin-1.
    IPR015224. Talin_cent.
    IPR029071. Ubiquitin-rel_dom.
    IPR015009. Vinculin-bd_dom.
    IPR006077. Vinculin/catenin.
    [Graphical view ]
    PANTHERi PTHR19981:SF7. PTHR19981:SF7. 1 hit.
    Pfami PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF01608. I_LWEQ. 1 hit.
    PF02174. IRS. 1 hit.
    PF09141. Talin_middle. 1 hit.
    PF08913. VBS. 2 hits.
    [Graphical view ]
    ProDomi PD011820. ILWEQ. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00295. B41. 1 hit.
    SM00307. ILWEQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109880. SSF109880. 1 hit.
    SSF109885. SSF109885. 4 hits.
    SSF47031. SSF47031. 1 hit.
    SSF47220. SSF47220. 5 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Fibroblast.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Tissue: Mammary gland.
    4. "Interaction of focal adhesion kinase with cytoskeletal protein talin."
      Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D., Guan J.L.
      J. Biol. Chem. 270:16995-16999(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1.
    5. "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-1116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
      Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
      J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
      Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
      J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBB1IP AND VCL.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle."
      Papagrigoriou E., Gingras A.R., Barsukov I.L., Bate N., Fillingham I.J., Patel B., Frank R., Ziegler W.H., Roberts G.C.K., Critchley D.R., Emsley J.
      EMBO J. 23:2942-2951(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 482-789 IN COMPLEX WITH VCL.
    12. "Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions."
      de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H., Critchley D.R., Campbell I.D., Liddington R.C.
      J. Biol. Chem. 280:8381-8386(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 209-410 IN COMPLEX WITH PIP5K1C.
    13. "A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head."
      Fillingham I., Gingras A.R., Papagrigoriou E., Patel B., Emsley J., Critchley D.R., Roberts G.C.K., Barsukov I.L.
      Structure 13:65-74(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 755-889, INTERACTION WITH VCL.

    Entry informationi

    Entry nameiTLN1_MOUSE
    AccessioniPrimary (citable) accession number: P26039
    Secondary accession number(s): A2AIM8, Q8VEF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3