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 - 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

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

  • actin filament binding Source: InterPro
  • cadherin binding Source: MGI
  • integrin binding Source: CAFA
  • LIM domain binding Source: MGI
  • phosphatidylinositol binding Source: CAFA
  • phosphatidylserine binding Source: CAFA
  • structural constituent of cytoskeleton Source: InterPro
  • vinculin binding Source: MGI
Complete GO annotation...

GO - Biological processi

  • cell-substrate junction assembly Source: MGI
  • cortical actin cytoskeleton organization Source: MGI
  • cytoskeletal anchoring at plasma membrane Source: InterPro
  • integrin activation Source: CAFA
  • integrin-mediated signaling pathway Source: CAFA
  • 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1099832. Tln1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • ruffle Source: HGNC
  • 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)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

Show more details

GO - Molecular functioni

  • actin filament binding Source: InterPro
  • cadherin binding Source: MGI
  • integrin binding Source: CAFA
  • LIM domain binding Source: MGI
  • vinculin binding Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi204222. 6 interactors.
DIPiDIP-647N.
IntActiP26039. 14 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

Phylogenomic databases

eggNOGiKOG4261. Eukaryota.
ENOG410XQ0V. LUCA.
GeneTreeiENSGT00550000074542.
HOVERGENiHBG023870.
InParanoidiP26039.
KOiK06271.
OMAiPTAKRQF.
OrthoDBiEOG091G0644.
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.

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.

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_MOUSE
AccessioniPrimary (citable) accession number: P26039
Secondary accession number(s): A2AIM8, Q8VEF0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: June 7, 2017
This is version 175 of the entry and version 2 of the sequence. See 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