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Protein

Talin-1

Gene

Tln1

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

GO - Biological processi

  • cell-substrate junction assembly Source: MGI
  • cortical actin cytoskeleton organization Source: MGI
  • cytoskeletal anchoring at plasma membrane Source: InterPro
  • platelet aggregation Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-445355. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Talin-1
Gene namesi
Name:Tln1
Synonyms:Tln
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1099832. Tln1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194291 – 2541Talin-1Add BLAST2541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei167PhosphothreonineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Modified residuei425PhosphoserineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei620PhosphoserineCombined sources1
Modified residuei729PhosphoserineCombined sources1
Modified residuei1021PhosphoserineBy similarity1
Modified residuei1116PhosphotyrosineCombined sources1
Modified residuei1142PhosphothreonineBy similarity1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1225PhosphoserineBy similarity1
Modified residuei1263PhosphothreonineBy similarity1
Modified residuei1323PhosphoserineBy similarity1
Modified residuei1328PhosphoserineCombined sources1
Modified residuei1544N6-acetyllysineCombined sources1
Modified residuei1849PhosphoserineBy similarity1
Modified residuei1855PhosphothreonineBy similarity1
Modified residuei1878PhosphoserineCombined sources1
Modified residuei2031N6-acetyllysineBy similarity1
Modified residuei2040PhosphoserineCombined sources1
Modified residuei2115N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP26039.
MaxQBiP26039.
PaxDbiP26039.
PeptideAtlasiP26039.
PRIDEiP26039.

PTM databases

iPTMnetiP26039.
PhosphoSitePlusiP26039.
SwissPalmiP26039.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028465.
CleanExiMM_TLN1.
ExpressionAtlasiP26039. baseline and differential.
GenevisibleiP26039. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204222. 6 interactors.
DIPiDIP-647N.
IntActiP26039. 12 interactors.
MINTiMINT-258500.
STRINGi10090.ENSMUSP00000030187.

Structurei

Secondary structure

12541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi13 – 19Combined sources7
Helixi25 – 33Combined sources9
Helixi37 – 40Combined sources4
Helixi44 – 46Combined sources3
Beta strandi47 – 51Combined sources5
Helixi56 – 58Combined sources3
Beta strandi60 – 62Combined sources3
Helixi68 – 71Combined sources4
Beta strandi78 – 83Combined sources6
Beta strandi85 – 91Combined sources7
Beta strandi97 – 103Combined sources7
Helixi108 – 118Combined sources11
Helixi124 – 126Combined sources3
Beta strandi127 – 130Combined sources4
Beta strandi136 – 138Combined sources3
Beta strandi146 – 150Combined sources5
Beta strandi168 – 174Combined sources7
Beta strandi176 – 178Combined sources3
Helixi181 – 183Combined sources3
Beta strandi190 – 195Combined sources6
Helixi209 – 224Combined sources16
Beta strandi226 – 228Combined sources3
Helixi232 – 247Combined sources16
Turni252 – 254Combined sources3
Helixi262 – 264Combined sources3
Helixi268 – 270Combined sources3
Helixi275 – 285Combined sources11
Turni286 – 288Combined sources3
Helixi291 – 304Combined sources14
Turni306 – 309Combined sources4
Beta strandi311 – 318Combined sources8
Beta strandi325 – 332Combined sources8
Beta strandi334 – 341Combined sources8
Turni342 – 344Combined sources3
Beta strandi347 – 352Combined sources6
Helixi353 – 355Combined sources3
Beta strandi358 – 362Combined sources5
Beta strandi365 – 369Combined sources5
Helixi371 – 373Combined sources3
Beta strandi374 – 376Combined sources3
Beta strandi378 – 381Combined sources4
Helixi385 – 397Combined sources13
Helixi493 – 512Combined sources20
Helixi526 – 560Combined sources35
Beta strandi565 – 567Combined sources3
Helixi570 – 600Combined sources31
Helixi606 – 626Combined sources21
Helixi634 – 652Combined sources19
Helixi664 – 690Combined sources27
Beta strandi696 – 699Combined sources4
Helixi700 – 723Combined sources24
Turni724 – 726Combined sources3
Helixi730 – 756Combined sources27
Helixi762 – 780Combined sources19
Beta strandi787 – 790Combined sources4
Beta strandi792 – 794Combined sources3
Helixi799 – 814Combined sources16
Turni815 – 817Combined sources3
Helixi820 – 843Combined sources24
Helixi844 – 846Combined sources3
Helixi850 – 876Combined sources27
Beta strandi878 – 880Combined sources3
Helixi884 – 907Combined sources24
Helixi914 – 938Combined sources25
Beta strandi943 – 946Combined sources4
Helixi951 – 975Combined sources25
Helixi980 – 1007Combined sources28
Helixi1008 – 1010Combined sources3
Helixi1014 – 1042Combined sources29
Helixi1049 – 1073Combined sources25
Helixi1084 – 1105Combined sources22
Helixi1115 – 1141Combined sources27
Helixi1147 – 1172Combined sources26
Beta strandi1174 – 1177Combined sources4
Helixi1179 – 1201Combined sources23
Helixi1207 – 1223Combined sources17
Turni1224 – 1226Combined sources3
Helixi1235 – 1260Combined sources26
Helixi1264 – 1289Combined sources26
Helixi1295 – 1324Combined sources30
Helixi1329 – 1353Combined sources25
Helixi1360 – 1373Combined sources14
Helixi1374 – 1377Combined sources4
Beta strandi1384 – 1386Combined sources3
Helixi1389 – 1416Combined sources28
Helixi1419 – 1450Combined sources32
Helixi1464 – 1480Combined sources17
Helixi1488 – 1515Combined sources28
Helixi1519 – 1548Combined sources30
Helixi1552 – 1576Combined sources25
Helixi1579 – 1581Combined sources3
Helixi1590 – 1622Combined sources33
Helixi1627 – 1653Combined sources27
Helixi1658 – 1683Combined sources26
Helixi1695 – 1722Combined sources28
Helixi1724 – 1751Combined sources28
Helixi1755 – 1782Combined sources28
Helixi1786 – 1788Combined sources3
Helixi1790 – 1818Combined sources29
Beta strandi1822 – 1824Combined sources3
Helixi1827 – 1840Combined sources14
Helixi1847 – 1874Combined sources28
Turni1875 – 1877Combined sources3
Helixi1879 – 1881Combined sources3
Helixi1882 – 1904Combined sources23
Beta strandi1907 – 1909Combined sources3
Helixi1910 – 1939Combined sources30
Helixi1944 – 1968Combined sources25
Helixi1969 – 1971Combined sources3
Helixi1976 – 2000Combined sources25
Helixi2012 – 2014Combined sources3
Helixi2016 – 2036Combined sources21
Beta strandi2037 – 2039Combined sources3
Helixi2041 – 2068Combined sources28
Helixi2074 – 2100Combined sources27
Turni2101 – 2103Combined sources3
Helixi2109 – 2161Combined sources53
Beta strandi2162 – 2164Combined sources3
Helixi2172 – 2195Combined sources24
Helixi2198 – 2223Combined sources26
Helixi2230 – 2259Combined sources30
Helixi2263 – 2288Combined sources26
Helixi2301 – 2324Combined sources24
Beta strandi2332 – 2334Combined sources3
Helixi2341 – 2373Combined sources33
Helixi2380 – 2382Combined sources3
Helixi2383 – 2416Combined sources34
Helixi2421 – 2442Combined sources22
Turni2443 – 2445Combined sources3
Helixi2451 – 2476Combined sources26
Helixi2497 – 2528Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W8PX-ray1.50A1357-1657[»]
5FZTX-ray2.10A1359-1659[»]
5IC0X-ray1.97A1357-1822[»]
5IC1X-ray2.20A1357-1822[»]
DisProtiDP00653.
ProteinModelPortaliP26039.
SMRiP26039.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26039.

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 SYNMBy similarityAdd BLAST622

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4261. Eukaryota.
ENOG410XQ0V. LUCA.
GeneTreeiENSGT00550000074542.
HOVERGENiHBG023870.
InParanoidiP26039.
KOiK06271.
OMAiEHVLVII.
OrthoDBiEOG091G0644.
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.
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.
[Graphical view]
PANTHERiPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamiPF16511. 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.
[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.
SSF50729. SSF50729. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti673K → N in CAA39588 (PubMed:2120593).Curated1
Sequence conflicti1227S → L in CAA39588 (PubMed:2120593).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1105L → P.1
Natural varianti2180K → M.1

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.
XP_006537832.2. XM_006537769.3.
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.
CCDSiCCDS18101.1.
PIRiS11661.
RefSeqiNP_035732.2. NM_011602.5.
XP_006537832.2. XM_006537769.3.
UniGeneiMm.208601.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W8PX-ray1.50A1357-1657[»]
5FZTX-ray2.10A1359-1659[»]
5IC0X-ray1.97A1357-1822[»]
5IC1X-ray2.20A1357-1822[»]
DisProtiDP00653.
ProteinModelPortaliP26039.
SMRiP26039.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204222. 6 interactors.
DIPiDIP-647N.
IntActiP26039. 12 interactors.
MINTiMINT-258500.
STRINGi10090.ENSMUSP00000030187.

PTM databases

iPTMnetiP26039.
PhosphoSitePlusiP26039.
SwissPalmiP26039.

Proteomic databases

EPDiP26039.
MaxQBiP26039.
PaxDbiP26039.
PeptideAtlasiP26039.
PRIDEiP26039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7094.
MGIiMGI:1099832. Tln1.

Phylogenomic databases

eggNOGiKOG4261. Eukaryota.
ENOG410XQ0V. LUCA.
GeneTreeiENSGT00550000074542.
HOVERGENiHBG023870.
InParanoidiP26039.
KOiK06271.
OMAiEHVLVII.
OrthoDBiEOG091G0644.
TreeFamiTF314677.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-445355. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSiTln1. mouse.
EvolutionaryTraceiP26039.
PROiP26039.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028465.
CleanExiMM_TLN1.
ExpressionAtlasiP26039. baseline and differential.
GenevisibleiP26039. MM.

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.
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.
[Graphical view]
PANTHERiPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamiPF16511. 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.
[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.
SSF50729. SSF50729. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 170 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

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.