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Q9Y490

- TLN1_HUMAN

UniProt

Q9Y490 - TLN1_HUMAN

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Protein

Talin-1

Gene

TLN1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

  1. integrin binding Source: UniProtKB
  2. LIM domain binding Source: UniProtKB
  3. structural constituent of cytoskeleton Source: UniProtKB
  4. vinculin binding Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. axon guidance Source: Reactome
  3. blood coagulation Source: Reactome
  4. cell-cell junction assembly Source: UniProtKB
  5. cell-substrate junction assembly Source: Ensembl
  6. cellular component movement Source: UniProtKB
  7. cellular protein metabolic process Source: Reactome
  8. cortical actin cytoskeleton organization Source: Ensembl
  9. cytoskeletal anchoring at plasma membrane Source: UniProtKB
  10. endoplasmic reticulum unfolded protein response Source: Reactome
  11. muscle contraction Source: Reactome
  12. platelet activation Source: Reactome
  13. platelet aggregation Source: UniProtKB
  14. platelet degranulation Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_18273. XBP1(S) activates chaperone genes.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Talin-1
Gene namesi
Name:TLN1
Synonyms:KIAA1027, TLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11845. TLN1.

Subcellular locationi

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

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. cell-cell junction Source: UniProtKB
  3. cytoplasm Source: HPA
  4. cytosol Source: Reactome
  5. extracellular region Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. microtubule organizing center Source: HPA
  9. plasma membrane Source: HPA
  10. ruffle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36547.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25412541Talin-1PRO_0000219428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei425 – 4251Phosphoserine3 Publications
Modified residuei1116 – 11161PhosphotyrosineBy similarity
Modified residuei1544 – 15441N6-acetyllysineBy similarity
Modified residuei2031 – 20311N6-acetyllysine1 Publication
Modified residuei2040 – 20401Phosphoserine1 Publication
Modified residuei2115 – 21151N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y490.
PaxDbiQ9Y490.
PRIDEiQ9Y490.

2D gel databases

OGPiQ9Y490.

PTM databases

PhosphoSiteiQ9Y490.

Expressioni

Gene expression databases

BgeeiQ9Y490.
CleanExiHS_TLN1.
GenevestigatoriQ9Y490.

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.By similarity6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112949. 43 interactions.
IntActiQ9Y490. 10 interactions.
MINTiMINT-5002070.
STRINGi9606.ENSP00000316029.

Structurei

Secondary structure

1
2541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi608 – 62518Combined sources
Helixi2079 – 209820Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYQX-ray2.42B607-631[»]
4DJ9X-ray2.25B2075-2103[»]
ProteinModelPortaliQ9Y490.
SMRiQ9Y490. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y490.

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 SYNMAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG324465.
GeneTreeiENSGT00550000074542.
HOGENOMiHOG000006734.
HOVERGENiHBG023870.
InParanoidiQ9Y490.
KOiK06271.
OMAiGAHIKHR.
OrthoDBiEOG7TBC1J.
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.
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.

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 BAA82979.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti824 – 8241R → G in AAD13152. 1 PublicationCurated
Sequence conflicti824 – 8241R → G in AAF23322. (PubMed:10610730)Curated
Sequence conflicti1549 – 15491A → P in AAD13152. 1 PublicationCurated
Sequence conflicti1549 – 15491A → P in AAF23322. (PubMed:10610730)Curated
Sequence conflicti1604 – 16041K → Q in AAD13152. 1 PublicationCurated
Sequence conflicti1604 – 16041K → Q in AAF23322. (PubMed:10610730)Curated
Sequence conflicti1701 – 17011Q → E in AAD13152. 1 PublicationCurated
Sequence conflicti1701 – 17011Q → E in AAF23322. (PubMed:10610730)Curated
Sequence conflicti1718 – 17181N → H in AAD13152. 1 PublicationCurated
Sequence conflicti1718 – 17181N → H in AAF23322. (PubMed:10610730)Curated
Sequence conflicti1966 – 19661A → R in AAD13152. 1 PublicationCurated
Sequence conflicti2256 – 22561Missing in AAF27330. (PubMed:10610730)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1227 – 12271S → L.1 Publication
Corresponds to variant rs2295795 [ dbSNP | Ensembl ].
VAR_023751
Natural varianti1919 – 19191R → W.1 Publication
Corresponds to variant rs17854239 [ dbSNP | Ensembl ].
VAR_023752
Natural varianti1984 – 19841A → T.
Corresponds to variant rs35642290 [ dbSNP | Ensembl ].
VAR_055538

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.2. human.

Polymorphism databases

DMDMi81175200.

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 .
CCDSi CCDS35009.1.
RefSeqi NP_006280.3. NM_006289.3.
UniGenei Hs.471014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SYQ X-ray 2.42 B 607-631 [» ]
4DJ9 X-ray 2.25 B 2075-2103 [» ]
ProteinModelPortali Q9Y490.
SMRi Q9Y490. 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 112949. 43 interactions.
IntActi Q9Y490. 10 interactions.
MINTi MINT-5002070.
STRINGi 9606.ENSP00000316029.

PTM databases

PhosphoSitei Q9Y490.

Polymorphism databases

DMDMi 81175200.

2D gel databases

OGPi Q9Y490.

Proteomic databases

MaxQBi Q9Y490.
PaxDbi Q9Y490.
PRIDEi Q9Y490.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314888 ; ENSP00000316029 ; ENSG00000137076 .
GeneIDi 7094.
KEGGi hsa:7094.
UCSCi uc003zxt.2. human.

Organism-specific databases

CTDi 7094.
GeneCardsi GC09M035687.
HGNCi HGNC:11845. TLN1.
HPAi CAB002006.
HPA004748.
MIMi 186745. gene.
neXtProti NX_Q9Y490.
PharmGKBi PA36547.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324465.
GeneTreei ENSGT00550000074542.
HOGENOMi HOG000006734.
HOVERGENi HBG023870.
InParanoidi Q9Y490.
KOi K06271.
OMAi GAHIKHR.
OrthoDBi EOG7TBC1J.
PhylomeDBi Q9Y490.
TreeFami TF314677.

Enzyme and pathway databases

Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_18273. XBP1(S) activates chaperone genes.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSi TLN1. human.
EvolutionaryTracei Q9Y490.
GeneWikii TLN1.
GenomeRNAii 7094.
NextBioi 27751.
PROi Q9Y490.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y490.
CleanExi HS_TLN1.
Genevestigatori Q9Y490.

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. "Complete cDNA sequence of human talin."
    Mao L., Fan Y.H.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-1227.
  2. "Characterization of the human talin (TLN) gene: genomic structure, chromosomal localization, and expression pattern."
    Ben-Yosef T., Francomano C.A.
    Genomics 62:316-319(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT TRP-1919.
    Tissue: Embryonic carcinoma.
  8. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Tissue: Platelet.
  9. "Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks."
    Luo G., Herrera A.H., Horowits R.
    Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRAP.
  10. "Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions."
    Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.
    Nature 420:89-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIP5K1C.
  11. "Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha."
    Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.
    J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin."
    Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
    Exp. Cell Res. 314:1839-1849(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNM.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2031 AND LYS-2115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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: INTERACTION WITH ITGB1.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Structural basis for amplifying vinculin activation by talin."
    Izard T., Vonrhein C.
    J. Biol. Chem. 279:27667-27678(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 607-631 IN COMPLEX WITH VCL.

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 26, 2014
This is version 152 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

External Data

Dasty 3