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P26039

- TLN1_MOUSE

UniProt

P26039 - TLN1_MOUSE

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Protein

Talin-1

Gene

Tln1

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. 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
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
REACT_235059. Smooth Muscle Contraction.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_246176. Integrin alphaIIb beta3 signaling.

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. cytoplasm Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: Ensembl
  4. focal adhesion Source: HGNC
  5. microtubule organizing center Source: Ensembl
  6. plasma membrane Source: UniProtKB-KW
  7. ruffle Source: HGNC
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-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

BgeeiP26039.
CleanExiMM_TLN1.
ExpressionAtlasiP26039. baseline and differential.
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 – 107Combined sources
Beta strandi13 – 197Combined sources
Helixi25 – 339Combined sources
Helixi37 – 404Combined sources
Helixi44 – 463Combined sources
Beta strandi47 – 515Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 623Combined sources
Helixi68 – 714Combined sources
Beta strandi78 – 836Combined sources
Beta strandi85 – 917Combined sources
Beta strandi97 – 1037Combined sources
Helixi108 – 11811Combined sources
Helixi124 – 1263Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi168 – 1747Combined sources
Beta strandi176 – 1783Combined sources
Helixi181 – 1833Combined sources
Beta strandi190 – 1956Combined sources
Helixi209 – 22416Combined sources
Beta strandi226 – 2283Combined sources
Helixi232 – 24716Combined sources
Turni252 – 2543Combined sources
Helixi262 – 2643Combined sources
Helixi268 – 2703Combined sources
Helixi275 – 28511Combined sources
Turni286 – 2883Combined sources
Helixi291 – 30414Combined sources
Turni306 – 3094Combined sources
Beta strandi311 – 3188Combined sources
Beta strandi325 – 3328Combined sources
Beta strandi334 – 3418Combined sources
Turni342 – 3443Combined sources
Beta strandi347 – 3526Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi365 – 3695Combined sources
Helixi371 – 3733Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi378 – 3814Combined sources
Helixi385 – 39713Combined sources
Helixi493 – 51220Combined sources
Helixi526 – 56035Combined sources
Beta strandi565 – 5673Combined sources
Helixi570 – 60031Combined sources
Helixi606 – 62621Combined sources
Helixi634 – 65219Combined sources
Helixi664 – 69027Combined sources
Beta strandi696 – 6994Combined sources
Helixi700 – 72324Combined sources
Turni724 – 7263Combined sources
Helixi730 – 75627Combined sources
Helixi762 – 78019Combined sources
Beta strandi787 – 7904Combined sources
Beta strandi792 – 7943Combined sources
Helixi799 – 81416Combined sources
Turni815 – 8173Combined sources
Helixi820 – 84324Combined sources
Helixi844 – 8463Combined sources
Helixi850 – 87627Combined sources
Beta strandi878 – 8803Combined sources
Helixi884 – 90724Combined sources
Helixi914 – 93825Combined sources
Beta strandi943 – 9464Combined sources
Helixi951 – 97525Combined sources
Helixi980 – 100728Combined sources
Helixi1008 – 10103Combined sources
Helixi1014 – 104229Combined sources
Helixi1049 – 107325Combined sources
Helixi1084 – 110522Combined sources
Helixi1115 – 114127Combined sources
Helixi1147 – 117226Combined sources
Beta strandi1174 – 11774Combined sources
Helixi1179 – 120123Combined sources
Helixi1359 – 137315Combined sources
Helixi1374 – 13774Combined sources
Beta strandi1384 – 13863Combined sources
Helixi1389 – 141628Combined sources
Helixi1419 – 145032Combined sources
Helixi1465 – 148218Combined sources
Helixi1488 – 151326Combined sources
Helixi1521 – 154424Combined sources
Helixi1552 – 157625Combined sources
Beta strandi1578 – 15825Combined sources
Helixi1590 – 162031Combined sources
Helixi1627 – 165428Combined sources
Helixi1655 – 16584Combined sources
Turni1683 – 16853Combined sources
Helixi1695 – 172228Combined sources
Helixi1724 – 173613Combined sources
Helixi1738 – 175114Combined sources
Helixi1755 – 178228Combined sources
Helixi1787 – 17893Combined sources
Helixi1790 – 182031Combined sources
Beta strandi1822 – 18243Combined sources
Helixi1827 – 184014Combined sources
Helixi1847 – 187428Combined sources
Turni1875 – 18773Combined sources
Helixi1879 – 18813Combined sources
Helixi1882 – 190423Combined sources
Beta strandi1907 – 19093Combined sources
Helixi1910 – 193930Combined sources
Helixi1944 – 196825Combined sources
Helixi1969 – 19713Combined sources
Helixi1976 – 200025Combined sources
Helixi2012 – 20143Combined sources
Helixi2016 – 203621Combined sources
Beta strandi2037 – 20393Combined sources
Helixi2041 – 206828Combined sources
Helixi2074 – 210027Combined sources
Turni2101 – 21033Combined sources
Helixi2109 – 216153Combined sources
Beta strandi2162 – 21643Combined sources
Helixi2172 – 219524Combined sources
Helixi2198 – 222326Combined sources
Helixi2230 – 225930Combined sources
Helixi2263 – 228826Combined sources
Helixi2301 – 232424Combined sources
Beta strandi2332 – 23343Combined sources
Helixi2341 – 237333Combined sources
Helixi2380 – 23823Combined sources
Helixi2383 – 241634Combined sources
Helixi2421 – 244222Combined sources
Turni2443 – 24453Combined sources
Helixi2451 – 247626Combined sources
Helixi2497 – 252832Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP26039.
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

        10         20         30         40         50
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF
60 70 80 90 100
LSDDDPKKGI WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI
110 120 130 140 150
MVDDSKTVTD MLMTICARIG ITNHDEYSLV RELMEEKKDE GTGTLRKDKT
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
WSLTNIKRWA 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 ATLDDFETLP PLGQDAASKA WRKNKMDESK HEIHSQVDAI
560 570 580 590 600
TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
610 620 630 640 650
EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE
660 670 680 690 700
LLQQIGESDT DPHFQDVLMQ 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 APKASAGPQP
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 EKDLQEIKAA ARDGKLKPLP GETMEKCTQD LGNSTKAVSS
1110 1120 1130 1140 1150
AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA LTSDPAVQAI
1160 1170 1180 1190 1200
VLDTASDVLD KASSLIEEAK KASGHPGDPE 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 ALSTDPASPN LKSQLAAAAR AVTDSINQLI
1360 1370 1380 1390 1400
TMCTQQAPGQ KECDNALRQL ETVRELLENP VQPINDMSYF GCLDSVMENS
1410 1420 1430 1440 1450
KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA AQAAYLVGVS
1460 1470 1480 1490 1500
DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
1510 1520 1530 1540 1550
HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF
1560 1570 1580 1590 1600
TEENRAQCRA ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV
1610 1620 1630 1640 1650
ISAKTMLESA GGLIQTARAL AVNPRDPPRW SVLAGHSRTV SDSIKKLITS
1660 1670 1680 1690 1700
MRDKAPGQLE CETAIAALNS CLRDLDQASL AAVSQQLAPR EGISQEALHT
1710 1720 1730 1740 1750
QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP LTLAAVGAAS
1760 1770 1780 1790 1800
KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
1810 1820 1830 1840 1850
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF
1860 1870 1880 1890 1900
VDYQTTMVRT AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA
1910 1920 1930 1940 1950
KPAAVAAENE EIGAHIKHRV QELGHGCSAL VTKAGALQCS PSDVYTKKEL
1960 1970 1980 1990 2000
IECARRVSEK VSHVLAALQA GNRGTQACIT AASAVSGIIA DLDTTIMFAT
2010 2020 2030 2040 2050
AGTLNREGAE 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 EAAFHPEVAP DVRLRALHYG RECANGYLEL
2260 2270 2280 2290 2300
LDHVLLTLQK PNPDLKQQLT 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 EDQENETVVV KEKMVGGIAQ
2510 2520 2530 2540
IIAAQEEMLR KERELEEARK KLAQIRQQQY KFLPSELRDE H
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 P26039.
KOi K06271.
OMAi GAHIKHR.
OrthoDBi EOG7TBC1J.
TreeFami TF314677.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.
REACT_235059. Smooth Muscle Contraction.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_246176. Integrin alphaIIb beta3 signaling.

Miscellaneous databases

ChiTaRSi Tln1. mouse.
EvolutionaryTracei P26039.
NextBioi 301428.
PROi P26039.
SOURCEi Search...

Gene expression databases

Bgeei P26039.
CleanExi MM_TLN1.
ExpressionAtlasi P26039. baseline and differential.
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: November 26, 2014
This is version 151 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