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Q9Y490

- TLN1_HUMAN

UniProt

Q9Y490 - TLN1_HUMAN

Protein

Talin-1

Gene

TLN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (08 Nov 2005)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. integrin binding Source: UniProtKB
    2. LIM domain binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. structural constituent of cytoskeleton Source: UniProtKB
    5. vinculin binding Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. axon guidance Source: Reactome
    3. blood coagulation Source: Reactome
    4. cell adhesion Source: InterPro
    5. cell-cell junction assembly Source: UniProtKB
    6. cell-substrate junction assembly Source: Ensembl
    7. cellular component movement Source: UniProtKB
    8. cellular protein metabolic process Source: Reactome
    9. cortical actin cytoskeleton organization Source: Ensembl
    10. cytoskeletal anchoring at plasma membrane Source: UniProtKB
    11. endoplasmic reticulum unfolded protein response Source: Reactome
    12. muscle contraction Source: Reactome
    13. platelet activation Source: Reactome
    14. platelet degranulation Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    REACT_20558. Smooth Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Talin-1
    Gene namesi
    Name:TLN1
    Synonyms:KIAA1027, TLN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11845. TLN1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. actin cytoskeleton Source: InterPro
    2. cell-cell junction Source: UniProtKB
    3. cell surface Source: UniProtKB-SubCell
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. extracellular region Source: Reactome
    7. extracellular vesicular exosome Source: UniProtKB
    8. focal adhesion Source: UniProtKB
    9. microtubule organizing center Source: HPA
    10. plasma membrane Source: HPA
    11. ruffle Source: HGNC
    12. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36547.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25412541Talin-1PRO_0000219428Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei425 – 4251Phosphoserine3 Publications
    Modified residuei1116 – 11161PhosphotyrosineBy similarity
    Modified residuei1544 – 15441N6-acetyllysineBy similarity
    Modified residuei2031 – 20311N6-acetyllysine1 Publication
    Modified residuei2040 – 20401Phosphoserine1 Publication
    Modified residuei2115 – 21151N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y490.
    PaxDbiQ9Y490.
    PRIDEiQ9Y490.

    2D gel databases

    OGPiQ9Y490.

    PTM databases

    PhosphoSiteiQ9Y490.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y490.
    BgeeiQ9Y490.
    CleanExiHS_TLN1.
    GenevestigatoriQ9Y490.

    Organism-specific databases

    HPAiCAB002006.
    HPA004748.

    Interactioni

    Subunit structurei

    Binds with high affinity to VCL and with low affinity to integrins. Interacts with APBB1IP; this inhibits VCL binding. Interacts with PTK2/FAK1 By similarity. Interacts with PIP5K1C and NRAP. Interacts with LAYN. Interacts with SYNM. Interacts with ITGB1; the interaction is prevented by competitive binding of ITGB1BP1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP005332EBI-2462036,EBI-297353
    ERBB2P046263EBI-2462036,EBI-641062
    ITGB1P055562EBI-2462036,EBI-703066
    ITGB3P051064EBI-2462036,EBI-702847

    Protein-protein interaction databases

    BioGridi112949. 40 interactions.
    IntActiQ9Y490. 10 interactions.
    MINTiMINT-5002070.
    STRINGi9606.ENSP00000316029.

    Structurei

    Secondary structure

    1
    2541
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi608 – 62518
    Helixi2079 – 209820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SYQX-ray2.42B607-631[»]
    4DJ9X-ray2.25B2075-2103[»]
    ProteinModelPortaliQ9Y490.
    SMRiQ9Y490. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y490.

    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 SYNMAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG324465.
    HOGENOMiHOG000006734.
    HOVERGENiHBG023870.
    InParanoidiQ9Y490.
    KOiK06271.
    OMAiGAHIKHR.
    OrthoDBiEOG7TBC1J.
    PhylomeDBiQ9Y490.
    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.

    Q9Y490-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF     50
    LSDDDPKKGI WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI 100
    MVDDSKTVTD MLMTICARIG ITNHDEYSLV RELMEEKKEE ITGTLRKDKT 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
    WNLTNIKRWA ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL 400
    KKKKSKDHFG LEGDEESTML EDSVSPKKST VLQQQYNRVG KVEHGSVALP 450
    AIMRSGASGP ENFQVGSMPP AQQQITSGQM HRGHMPPLTS AQQALTGTIN 500
    SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK HEIHSQVDAI 550
    TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 600
    EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE 650
    LLQQIGESDT DPHFQDALMQ 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 TPKASAGPQP 950
    LLVQSCKAVA EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM 1000
    VAAAKASVPT IQDQASAMQL SQCAKNLGTA LAELRTAAQK AQEACGPLEM 1050
    DSALSVVQNL EKDLQEVKAA ARDGKLKPLP GETMEKCTQD LGNSTKAVSS 1100
    AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA LTSDPAVQAI 1150
    VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV 1200
    SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN 1250
    QAATELVQAS RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ 1300
    VVSNLKGISM SSSKLLLAAK ALSTDPAAPN LKSQLAAAAR AVTDSINQLI 1350
    TMCTQQAPGQ KECDNALREL ETVRELLENP VQPINDMSYF GCLDSVMENS 1400
    KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA AQAAYLVGVS 1450
    DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 1500
    HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF 1550
    TEENRAQCRA ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV 1600
    ISAKTMLESA GGLIQTARAL AVNPRDPPSW SVLAGHSRTV SDSIKKLITS 1650
    MRDKAPGQLE CETAIAALNS CLRDLDQASL AAVSQQLAPR EGISQEALHT 1700
    QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP LTLAAVGAAS 1750
    KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 1800
    QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF 1850
    VDYQTTMVRT AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA 1900
    KPAAVAAENE EIGSHIKHRV QELGHGCAAL VTKAGALQCS PSDAYTKKEL 1950
    IECARRVSEK VSHVLAALQA GNRGTQACIT AASAVSGIIA DLDTTIMFAT 2000
    AGTLNREGTE 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 EAAYHPEVAP DVRLRALHYG RECANGYLEL 2250
    LDHVLLTLQK PSPELKQQLT 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 EEQENETVVV KEKMVGGIAQ 2500
    IIAAQEEMLR KERELEEARK KLAQIRQQQY KFLPSELRDE H 2541
    Length:2,541
    Mass (Da):269,767
    Last modified:November 8, 2005 - v3
    Checksum:iE21575E9199BBC5C
    GO

    Sequence cautioni

    The sequence BAA82979.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti824 – 8241R → G in AAD13152. 1 PublicationCurated
    Sequence conflicti824 – 8241R → G in AAF23322. (PubMed:10610730)Curated
    Sequence conflicti1549 – 15491A → P in AAD13152. 1 PublicationCurated
    Sequence conflicti1549 – 15491A → P in AAF23322. (PubMed:10610730)Curated
    Sequence conflicti1604 – 16041K → Q in AAD13152. 1 PublicationCurated
    Sequence conflicti1604 – 16041K → Q in AAF23322. (PubMed:10610730)Curated
    Sequence conflicti1701 – 17011Q → E in AAD13152. 1 PublicationCurated
    Sequence conflicti1701 – 17011Q → E in AAF23322. (PubMed:10610730)Curated
    Sequence conflicti1718 – 17181N → H in AAD13152. 1 PublicationCurated
    Sequence conflicti1718 – 17181N → H in AAF23322. (PubMed:10610730)Curated
    Sequence conflicti1966 – 19661A → R in AAD13152. 1 PublicationCurated
    Sequence conflicti2256 – 22561Missing in AAF27330. (PubMed:10610730)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1227 – 12271S → L.1 Publication
    Corresponds to variant rs2295795 [ dbSNP | Ensembl ].
    VAR_023751
    Natural varianti1919 – 19191R → W.1 Publication
    Corresponds to variant rs17854239 [ dbSNP | Ensembl ].
    VAR_023752
    Natural varianti1984 – 19841A → T.
    Corresponds to variant rs35642290 [ dbSNP | Ensembl ].
    VAR_055538

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF078828 mRNA. Translation: AAD13152.1.
    AF177198 mRNA. Translation: AAF23322.1.
    AF178534, AF178081 Genomic DNA. Translation: AAF27330.1.
    AB028950 mRNA. Translation: BAA82979.2. Different initiation.
    AL133410 Genomic DNA. No translation available.
    CH471071 Genomic DNA. Translation: EAW58352.1.
    BC042923 mRNA. Translation: AAH42923.1.
    CCDSiCCDS35009.1.
    RefSeqiNP_006280.3. NM_006289.3.
    UniGeneiHs.471014.

    Genome annotation databases

    EnsembliENST00000314888; ENSP00000316029; ENSG00000137076.
    GeneIDi7094.
    KEGGihsa:7094.
    UCSCiuc003zxt.2. human.

    Polymorphism databases

    DMDMi81175200.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF078828 mRNA. Translation: AAD13152.1 .
    AF177198 mRNA. Translation: AAF23322.1 .
    AF178534 , AF178081 Genomic DNA. Translation: AAF27330.1 .
    AB028950 mRNA. Translation: BAA82979.2 . Different initiation.
    AL133410 Genomic DNA. No translation available.
    CH471071 Genomic DNA. Translation: EAW58352.1 .
    BC042923 mRNA. Translation: AAH42923.1 .
    CCDSi CCDS35009.1.
    RefSeqi NP_006280.3. NM_006289.3.
    UniGenei Hs.471014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SYQ X-ray 2.42 B 607-631 [» ]
    4DJ9 X-ray 2.25 B 2075-2103 [» ]
    ProteinModelPortali Q9Y490.
    SMRi Q9Y490. 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 112949. 40 interactions.
    IntActi Q9Y490. 10 interactions.
    MINTi MINT-5002070.
    STRINGi 9606.ENSP00000316029.

    PTM databases

    PhosphoSitei Q9Y490.

    Polymorphism databases

    DMDMi 81175200.

    2D gel databases

    OGPi Q9Y490.

    Proteomic databases

    MaxQBi Q9Y490.
    PaxDbi Q9Y490.
    PRIDEi Q9Y490.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314888 ; ENSP00000316029 ; ENSG00000137076 .
    GeneIDi 7094.
    KEGGi hsa:7094.
    UCSCi uc003zxt.2. human.

    Organism-specific databases

    CTDi 7094.
    GeneCardsi GC09M035687.
    HGNCi HGNC:11845. TLN1.
    HPAi CAB002006.
    HPA004748.
    MIMi 186745. gene.
    neXtProti NX_Q9Y490.
    PharmGKBi PA36547.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324465.
    HOGENOMi HOG000006734.
    HOVERGENi HBG023870.
    InParanoidi Q9Y490.
    KOi K06271.
    OMAi GAHIKHR.
    OrthoDBi EOG7TBC1J.
    PhylomeDBi Q9Y490.
    TreeFami TF314677.

    Enzyme and pathway databases

    Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    REACT_20558. Smooth Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi TLN1. human.
    EvolutionaryTracei Q9Y490.
    GeneWikii TLN1.
    GenomeRNAii 7094.
    NextBioi 27751.
    PROi Q9Y490.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y490.
    Bgeei Q9Y490.
    CleanExi HS_TLN1.
    Genevestigatori Q9Y490.

    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. "Complete cDNA sequence of human talin."
      Mao L., Fan Y.H.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-1227.
    2. "Characterization of the human talin (TLN) gene: genomic structure, chromosomal localization, and expression pattern."
      Ben-Yosef T., Francomano C.A.
      Genomics 62:316-319(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT TRP-1919.
      Tissue: Embryonic carcinoma.
    8. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Tissue: Platelet.
    9. "Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks."
      Luo G., Herrera A.H., Horowits R.
      Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRAP.
    10. "Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions."
      Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.
      Nature 420:89-93(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIP5K1C.
    11. "Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha."
      Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.
      J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1.
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin."
      Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
      Exp. Cell Res. 314:1839-1849(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNM.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2031 AND LYS-2115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: INTERACTION WITH ITGB1.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structural basis for amplifying vinculin activation by talin."
      Izard T., Vonrhein C.
      J. Biol. Chem. 279:27667-27678(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 607-631 IN COMPLEX WITH VCL.

    Entry informationi

    Entry nameiTLN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y490
    Secondary accession number(s): A6NMY0
    , Q86YD0, Q9NZQ2, Q9UHH8, Q9UPX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3