SubmitCancel

Skip Header

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

P26039

- TLN1_MOUSE

UniProt

P26039 - TLN1_MOUSE

(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, Tln
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

GO - Molecular functioni

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

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
Complete GO annotation...

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

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
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei425 – 4251Phosphoserine By similarity
Modified residuei1116 – 11161Phosphotyrosine2 Publications
Modified residuei1544 – 15441N6-acetyllysine1 Publication
Modified residuei2031 – 20311N6-acetyllysine By similarity
Modified residuei2040 – 20401Phosphoserine By similarity
Modified residuei2115 – 21151N6-acetyllysine By 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.3 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

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.

Miscellaneous databases

EvolutionaryTraceiP26039.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 403318FERM
Add
BLAST
Domaini2293 – 2533241I/LWEQ
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 435156Interaction with LAYN By similarity
Add
BLAST
Regioni1327 – 1948622Interaction with SYNM By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 FERM domain.
Contains 1 I/LWEQ domain.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti673 – 6731K → N in CAA39588. 1 Publication
Sequence conflicti1227 – 12271S → L in CAA39588. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 148 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

Similar proteinsi