Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9Y490 (TLN1_HUMAN)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Talin-1

Gene

TLN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • actin filament binding Source: InterPro
  • cadherin binding Source: BHF-UCL
  • integrin binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • phosphatidylinositol binding Source: Ensembl
  • phosphatidylserine binding Source: Ensembl
  • structural constituent of cytoskeleton Source: UniProtKB
  • vinculin binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • cell-cell junction assembly Source: UniProtKB
  • cell-substrate junction assembly Source: Ensembl
  • cortical actin cytoskeleton organization Source: Ensembl
  • cytoskeletal anchoring at plasma membrane Source: UniProtKB
  • integrin activation Source: Ensembl
  • integrin-mediated signaling pathway Source: Ensembl
  • IRE1-mediated unfolded protein response Source: Reactome
  • movement of cell or subcellular component Source: UniProtKB
  • muscle contraction Source: Reactome
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Biological processHost-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-381038. XBP1(S) activates chaperone genes.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNORiQ9Y490.

Names & Taxonomyi

Protein namesi
Recommended name:
Talin-1
Gene namesi
Name:TLN1
Synonyms:KIAA1027, TLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11845. TLN1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell surface Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • focal adhesion Source: UniProtKB
  • ruffle Source: HGNC
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi7094.
OpenTargetsiENSG00000137076.
PharmGKBiPA36547.

Polymorphism and mutation databases

BioMutaiTLN1.
DMDMi81175200.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194281 – 2541Talin-1Add BLAST2541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei167PhosphothreonineCombined sources1
Modified residuei405PhosphoserineCombined sources1
Modified residuei425PhosphoserineCombined sources1
Modified residuei446PhosphoserineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1
Modified residuei1021PhosphoserineCombined sources1
Modified residuei1116PhosphotyrosineBy similarity1
Modified residuei1142PhosphothreonineCombined sources1
Modified residuei1201PhosphoserineCombined sources1
Modified residuei1225PhosphoserineCombined sources1
Modified residuei1263PhosphothreonineCombined sources1
Modified residuei1323PhosphoserineCombined sources1
Modified residuei1544N6-acetyllysineBy similarity1
Modified residuei1849PhosphoserineCombined sources1
Modified residuei1855PhosphothreonineCombined sources1
Modified residuei1878PhosphoserineBy similarity1
Modified residuei2031N6-acetyllysineCombined sources1
Modified residuei2040PhosphoserineCombined sources1
Modified residuei2115N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y490.
MaxQBiQ9Y490.
PaxDbiQ9Y490.
PeptideAtlasiQ9Y490.
PRIDEiQ9Y490.

2D gel databases

OGPiQ9Y490.

PTM databases

iPTMnetiQ9Y490.
PhosphoSitePlusiQ9Y490.
SwissPalmiQ9Y490.

Expressioni

Gene expression databases

BgeeiENSG00000137076.
CleanExiHS_TLN1.
GenevisibleiQ9Y490. HS.

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. Interacts with human cytomegalovirus protein UL135.By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: InterPro
  • cadherin binding Source: BHF-UCL
  • integrin binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • vinculin binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi112949. 71 interactors.
IntActiQ9Y490. 23 interactors.
MINTiMINT-5002070.
STRINGi9606.ENSP00000316029.

Structurei

Secondary structure

12541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi311 – 313Combined sources3
Beta strandi316 – 318Combined sources3
Beta strandi320 – 327Combined sources8
Beta strandi329 – 333Combined sources5
Beta strandi336 – 340Combined sources5
Turni342 – 344Combined sources3
Beta strandi363 – 369Combined sources7
Beta strandi377 – 381Combined sources5
Helixi385 – 399Combined sources15
Helixi608 – 625Combined sources18
Helixi2079 – 2098Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SYQX-ray2.42B607-631[»]
2MWNNMR-B308-400[»]
4DJ9X-ray2.25B2075-2103[»]
ProteinModelPortaliQ9Y490.
SMRiQ9Y490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y490.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini86 – 403FERMPROSITE-ProRule annotationAdd BLAST318
Domaini2293 – 2533I/LWEQPROSITE-ProRule annotationAdd BLAST241

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni280 – 435Interaction with LAYNBy similarityAdd BLAST156
Regioni1327 – 1948Interaction with SYNM1 PublicationAdd BLAST622

Phylogenomic databases

eggNOGiKOG4261. Eukaryota.
ENOG410XQ0V. LUCA.
GeneTreeiENSGT00550000074542.
HOGENOMiHOG000006734.
HOVERGENiHBG023870.
InParanoidiQ9Y490.
KOiK06271.
OMAiPTAKRQF.
OrthoDBiEOG091G0644.
PhylomeDBiQ9Y490.
TreeFamiTF314677.

Family and domain databases

CDDicd14473. FERM_B-lobe. 1 hit.
Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiView protein in InterPro
IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR032425. FERM_f0.
IPR018979. FERM_N.
IPR002558. ILWEQ_dom.
IPR011993. PH_dom-like.
IPR015710. Talin-1.
IPR015224. Talin_cent.
IPR029071. Ubiquitin-rel_dom.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
PANTHERiPTHR19981:SF24. PTHR19981:SF24. 1 hit.
PfamiView protein in Pfam
PF16511. FERM_f0. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF01608. I_LWEQ. 1 hit.
PF09141. Talin_middle. 1 hit.
PF08913. VBS. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD011820. ILWEQ. 1 hit.
SMARTiView protein in SMART
SM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
SUPFAMiSSF109880. SSF109880. 1 hit.
SSF109885. SSF109885. 4 hits.
SSF47031. SSF47031. 1 hit.
SSF47220. SSF47220. 5 hits.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiView protein in PROSITE
PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF 
        60         70         80         90        100
LSDDDPKKGI WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI 
       110        120        130        140        150
MVDDSKTVTD MLMTICARIG ITNHDEYSLV RELMEEKKEE ITGTLRKDKT 
       160        170        180        190        200
LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL REQGVEEHET LLLRRKFFYS 
       210        220        230        240        250
DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG FQCQIQFGPH 
       260        270        280        290        300
NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 
       310        320        330        340        350
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE 
       360        370        380        390        400
WNLTNIKRWA ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL 
       410        420        430        440        450
KKKKSKDHFG LEGDEESTML EDSVSPKKST VLQQQYNRVG KVEHGSVALP 
       460        470        480        490        500
AIMRSGASGP ENFQVGSMPP AQQQITSGQM HRGHMPPLTS AQQALTGTIN 
       510        520        530        540        550
SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK HEIHSQVDAI 
       560        570        580        590        600
TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 
       610        620        630        640        650
EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE 
       660        670        680        690        700
LLQQIGESDT DPHFQDALMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT 
       710        720        730        740        750
QVIAAATQCA LSTSQLVACT KVVAPTISSP VCQEQLVEAG RLVAKAVEGC 
       760        770        780        790        800
VSASQAATED GQLLRGVGAA ATAVTQALNE LLQHVKAHAT GAGPAGRYDQ 
       810        820        830        840        850
ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI KADAEGESDL 
       860        870        880        890        900
ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 
       910        920        930        940        950
TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS TPKASAGPQP 
       960        970        980        990       1000
LLVQSCKAVA EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM 
      1010       1020       1030       1040       1050
VAAAKASVPT IQDQASAMQL SQCAKNLGTA LAELRTAAQK AQEACGPLEM 
      1060       1070       1080       1090       1100
DSALSVVQNL EKDLQEVKAA ARDGKLKPLP GETMEKCTQD LGNSTKAVSS 
      1110       1120       1130       1140       1150
AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA LTSDPAVQAI 
      1160       1170       1180       1190       1200
VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV 
      1210       1220       1230       1240       1250
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN 
      1260       1270       1280       1290       1300
QAATELVQAS RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ 
      1310       1320       1330       1340       1350
VVSNLKGISM SSSKLLLAAK ALSTDPAAPN LKSQLAAAAR AVTDSINQLI 
      1360       1370       1380       1390       1400
TMCTQQAPGQ KECDNALREL ETVRELLENP VQPINDMSYF GCLDSVMENS 
      1410       1420       1430       1440       1450
KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA AQAAYLVGVS 
      1460       1470       1480       1490       1500
DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 
      1510       1520       1530       1540       1550
HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF 
      1560       1570       1580       1590       1600
TEENRAQCRA ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV 
      1610       1620       1630       1640       1650
ISAKTMLESA GGLIQTARAL AVNPRDPPSW SVLAGHSRTV SDSIKKLITS 
      1660       1670       1680       1690       1700
MRDKAPGQLE CETAIAALNS CLRDLDQASL AAVSQQLAPR EGISQEALHT 
      1710       1720       1730       1740       1750
QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP LTLAAVGAAS 
      1760       1770       1780       1790       1800
KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 
      1810       1820       1830       1840       1850
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF 
      1860       1870       1880       1890       1900
VDYQTTMVRT AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA 
      1910       1920       1930       1940       1950
KPAAVAAENE EIGSHIKHRV QELGHGCAAL VTKAGALQCS PSDAYTKKEL 
      1960       1970       1980       1990       2000
IECARRVSEK VSHVLAALQA GNRGTQACIT AASAVSGIIA DLDTTIMFAT 
      2010       2020       2030       2040       2050
AGTLNREGTE TFADHREGIL KTAKVLVEDT KVLVQNAAGS QEKLAQAAQS 
      2060       2070       2080       2090       2100
SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 
      2110       2120       2130       2140       2150
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT 
      2160       2170       2180       2190       2200
EHIRQELAVF CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED 
      2210       2220       2230       2240       2250
VIATANLSRR AIADMLRACK EAAYHPEVAP DVRLRALHYG RECANGYLEL 
      2260       2270       2280       2290       2300
LDHVLLTLQK PSPELKQQLT GHSKRVAGSV TELIQAAEAM KGTEWVDPED 
      2310       2320       2330       2340       2350
PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN FEEQILEAAK 
      2360       2370       2380       2390       2400
SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 
      2410       2420       2430       2440       2450
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS 
      2460       2470       2480       2490       2500
EAMKRLQAAG NAVKRASDNL VKAAQKAAAF EEQENETVVV KEKMVGGIAQ 
      2510       2520       2530       2540 
IIAAQEEMLR KERELEEARK KLAQIRQQQY KFLPSELRDE H
Length:2,541
Mass (Da):269,767
Last modified:November 8, 2005 - v3
Checksum:iE21575E9199BBC5C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti824R → G in AAD13152 (Ref. 1) Curated1
Sequence conflicti824R → G in AAF23322 (PubMed:10610730).Curated1
Sequence conflicti1549A → P in AAD13152 (Ref. 1) Curated1
Sequence conflicti1549A → P in AAF23322 (PubMed:10610730).Curated1
Sequence conflicti1604K → Q in AAD13152 (Ref. 1) Curated1
Sequence conflicti1604K → Q in AAF23322 (PubMed:10610730).Curated1
Sequence conflicti1701Q → E in AAD13152 (Ref. 1) Curated1
Sequence conflicti1701Q → E in AAF23322 (PubMed:10610730).Curated1
Sequence conflicti1718N → H in AAD13152 (Ref. 1) Curated1
Sequence conflicti1718N → H in AAF23322 (PubMed:10610730).Curated1
Sequence conflicti1966A → R in AAD13152 (Ref. 1) Curated1
Sequence conflicti2256Missing in AAF27330 (PubMed:10610730).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0237511227S → L1 PublicationCorresponds to variant dbSNP:rs2295795Ensembl.1
Natural variantiVAR_0237521919R → W1 PublicationCorresponds to variant dbSNP:rs17854239Ensembl.1
Natural variantiVAR_0555381984A → T. Corresponds to variant dbSNP:rs35642290Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiTLN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y490
Secondary accession number(s): A6NMY0
, Q86YD0, Q9NZQ2, Q9UHH8, Q9UPX3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2005
Last modified: July 5, 2017
This is version 181 of the entry and version 3 of the sequence. See 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