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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

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • integrin binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: UniProtKB
  • vinculin binding Source: UniProtKB

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
  • 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...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137076-MONOMER.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11845. TLN1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell junction Source: UniProtKB
  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • focal adhesion Source: UniProtKB
  • microtubule organizing center Source: HPA
  • plasma membrane Source: HPA
  • 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

WithEntry#Exp.IntActNotes
EGFRP005332EBI-2462036,EBI-297353
ERBB2P046263EBI-2462036,EBI-641062
ITGB1P055562EBI-2462036,EBI-703066
ITGB3P051064EBI-2462036,EBI-702847

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • integrin binding Source: UniProtKB
  • LIM domain binding Source: UniProtKB
  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112949. 68 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

Sequence similaritiesi

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

Phylogenomic databases

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

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 → L.1 PublicationCorresponds to variant rs2295795dbSNPEnsembl.1
Natural variantiVAR_0237521919R → W.1 PublicationCorresponds to variant rs17854239dbSNPEnsembl.1
Natural variantiVAR_0555381984A → T.Corresponds to variant rs35642290dbSNPEnsembl.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

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi112949. 68 interactors.
IntActiQ9Y490. 23 interactors.
MINTiMINT-5002070.
STRINGi9606.ENSP00000316029.

PTM databases

iPTMnetiQ9Y490.
PhosphoSitePlusiQ9Y490.
SwissPalmiQ9Y490.

Polymorphism and mutation databases

BioMutaiTLN1.
DMDMi81175200.

2D gel databases

OGPiQ9Y490.

Proteomic databases

EPDiQ9Y490.
MaxQBiQ9Y490.
PaxDbiQ9Y490.
PeptideAtlasiQ9Y490.
PRIDEiQ9Y490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314888; ENSP00000316029; ENSG00000137076.
GeneIDi7094.
KEGGihsa:7094.
UCSCiuc003zxt.3. human.

Organism-specific databases

CTDi7094.
DisGeNETi7094.
GeneCardsiTLN1.
HGNCiHGNC:11845. TLN1.
HPAiCAB002006.
HPA004748.
MIMi186745. gene.
neXtProtiNX_Q9Y490.
OpenTargetsiENSG00000137076.
PharmGKBiPA36547.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137076-MONOMER.
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.

Miscellaneous databases

ChiTaRSiTLN1. human.
EvolutionaryTraceiQ9Y490.
GeneWikiiTLN1.
GenomeRNAii7094.
PROiQ9Y490.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137076.
CleanExiHS_TLN1.
GenevisibleiQ9Y490. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9Y490
Secondary accession number(s): A6NMY0
, Q86YD0, Q9NZQ2, Q9UHH8, Q9UPX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2005
Last modified: November 30, 2016
This is version 174 of the entry and version 3 of the sequence. [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
  6. 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.