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Q9Y490 (TLN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Talin-1
Gene names
Name:TLN1
Synonyms:KIAA1027, TLN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.13 Ref.20

Subcellular location

Cell projectionruffle membrane; Peripheral membrane protein; 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.

Sequence similarities

Contains 1 FERM domain.

Contains 1 I/LWEQ domain.

Sequence caution

The sequence BAA82979.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: InterPro

cell-cell junction assembly

Traceable author statement PubMed 15494027. Source: UniProtKB

cell-substrate junction assembly

Inferred from electronic annotation. Source: Ensembl

cellular component movement

Non-traceable author statement Ref.2. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

cytoskeletal anchoring at plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

muscle contraction

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell-cell junction

Inferred by curator PubMed 15494027. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

focal adhesion

Non-traceable author statement Ref.2. Source: UniProtKB

microtubule organizing center

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from sequence or structural similarity. Source: HGNC

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionLIM domain binding

Inferred from physical interaction Ref.9. Source: UniProtKB

integrin binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

structural constituent of cytoskeleton

Non-traceable author statement Ref.2. Source: UniProtKB

vinculin binding

Inferred from physical interaction Ref.23. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25412541Talin-1
PRO_0000219428

Regions

Domain86 – 403318FERM
Domain2293 – 2533241I/LWEQ
Region280 – 435156Interaction with LAYN By similarity
Region1327 – 1948622Interaction with SYNM

Amino acid modifications

Modified residue4251Phosphoserine Ref.15 Ref.16 Ref.18
Modified residue11161Phosphotyrosine By similarity
Modified residue15441N6-acetyllysine By similarity
Modified residue20311N6-acetyllysine Ref.17
Modified residue20401Phosphoserine Ref.21
Modified residue21151N6-acetyllysine Ref.17

Natural variations

Natural variant12271S → L. Ref.1
Corresponds to variant rs2295795 [ dbSNP | Ensembl ].
VAR_023751
Natural variant19191R → W. Ref.7
Corresponds to variant rs17854239 [ dbSNP | Ensembl ].
VAR_023752
Natural variant19841A → T.
Corresponds to variant rs35642290 [ dbSNP | Ensembl ].
VAR_055538

Experimental info

Sequence conflict8241R → G in AAD13152. Ref.1
Sequence conflict8241R → G in AAF23322. Ref.2
Sequence conflict15491A → P in AAD13152. Ref.1
Sequence conflict15491A → P in AAF23322. Ref.2
Sequence conflict16041K → Q in AAD13152. Ref.1
Sequence conflict16041K → Q in AAF23322. Ref.2
Sequence conflict17011Q → E in AAD13152. Ref.1
Sequence conflict17011Q → E in AAF23322. Ref.2
Sequence conflict17181N → H in AAD13152. Ref.1
Sequence conflict17181N → H in AAF23322. Ref.2
Sequence conflict19661A → R in AAD13152. Ref.1
Sequence conflict22561Missing in AAF27330. Ref.2

Secondary structure

..... 2541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y490 [UniParc].

Last modified November 8, 2005. Version 3.
Checksum: E21575E9199BBC5C

FASTA2,541269,767
        10         20         30         40         50         60 
MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF LSDDDPKKGI 

        70         80         90        100        110        120 
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG 

       130        140        150        160        170        180 
ITNHDEYSLV RELMEEKKEE ITGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 

       190        200        210        220        230        240 
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 

       250        260        270        280        290        300 
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 

       310        320        330        340        350        360 
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WNLTNIKRWA 

       370        380        390        400        410        420 
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML 

       430        440        450        460        470        480 
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM 

       490        500        510        520        530        540 
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK 

       550        560        570        580        590        600 
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 

       610        620        630        640        650        660 
EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT 

       670        680        690        700        710        720 
DPHFQDALMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT 

       730        740        750        760        770        780 
KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE 

       790        800        810        820        830        840 
LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI 

       850        860        870        880        890        900 
KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 

       910        920        930        940        950        960 
TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS TPKASAGPQP LLVQSCKAVA 

       970        980        990       1000       1010       1020 
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL 

      1030       1040       1050       1060       1070       1080 
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEVKAA ARDGKLKPLP 

      1090       1100       1110       1120       1130       1140 
GETMEKCTQD LGNSTKAVSS AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA 

      1150       1160       1170       1180       1190       1200 
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV 

      1210       1220       1230       1240       1250       1260 
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS 

      1270       1280       1290       1300       1310       1320 
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK 

      1330       1340       1350       1360       1370       1380 
ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALREL ETVRELLENP 

      1390       1400       1410       1420       1430       1440 
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA 

      1450       1460       1470       1480       1490       1500 
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 

      1510       1520       1530       1540       1550       1560 
HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA 

      1570       1580       1590       1600       1610       1620 
ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL 

      1630       1640       1650       1660       1670       1680 
AVNPRDPPSW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL 

      1690       1700       1710       1720       1730       1740 
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP 

      1750       1760       1770       1780       1790       1800 
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 

      1810       1820       1830       1840       1850       1860 
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT 

      1870       1880       1890       1900       1910       1920 
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA KPAAVAAENE EIGSHIKHRV 

      1930       1940       1950       1960       1970       1980 
QELGHGCAAL VTKAGALQCS PSDAYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT 

      1990       2000       2010       2020       2030       2040 
AASAVSGIIA DLDTTIMFAT AGTLNREGTE TFADHREGIL KTAKVLVEDT KVLVQNAAGS 

      2050       2060       2070       2080       2090       2100 
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 

      2110       2120       2130       2140       2150       2160 
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF 

      2170       2180       2190       2200       2210       2220 
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK 

      2230       2240       2250       2260       2270       2280 
EAAYHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PSPELKQQLT GHSKRVAGSV 

      2290       2300       2310       2320       2330       2340 
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN 

      2350       2360       2370       2380       2390       2400 
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 

      2410       2420       2430       2440       2450       2460 
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG 

      2470       2480       2490       2500       2510       2520 
NAVKRASDNL VKAAQKAAAF EEQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK 

      2530       2540 
KLAQIRQQQY KFLPSELRDE H 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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
Cited for: PROTEIN SEQUENCE OF 8-15; 34-82; 99-106; 119-131; 138-146; 148-156; 165-178; 182-194; 197-234; 257-268; 307-316; 344-358; 428-438; 442-454; 593-634; 674-685; 722-741; 766-824; 828-854; 862-869; 876-910; 923-943; 958-999; 1026-1035; 1076-1086; 1097-1122; 1130-1184; 1191-1198; 1208-1214; 1223-1269; 1274-1306; 1321-1340; 1362-1368; 1402-1431; 1531-1541; 1560-1646; 1674-1780; 1863-1917; 1961-1973; 2007-2016; 2025-2057; 2064-2085; 2090-2099; 2105-2115; 2120-2130; 2134-2141; 2145-2154; 2169-2177; 2198-2209; 2221-2233; 2267-2274; 2276-2321; 2322-2329; 2334-2361; 2369-2398; 2430-2443; 2456-2472; 2477-2491; 2494-2510 AND 2512-2519, IDENTIFICATION BY MASS SPECTROMETRY.
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS35009.1.
RefSeqNP_006280.3. NM_006289.3.
UniGeneHs.471014.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYQX-ray2.42B607-631[»]
4DJ9X-ray2.25B2075-2103[»]
ProteinModelPortalQ9Y490.
SMRQ9Y490. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112949. 40 interactions.
IntActQ9Y490. 10 interactions.
MINTMINT-5002070.
STRING9606.ENSP00000316029.

PTM databases

PhosphoSiteQ9Y490.

Polymorphism databases

DMDM81175200.

2D gel databases

OGPQ9Y490.

Proteomic databases

MaxQBQ9Y490.
PaxDbQ9Y490.
PRIDEQ9Y490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314888; ENSP00000316029; ENSG00000137076.
GeneID7094.
KEGGhsa:7094.
UCSCuc003zxt.2. human.

Organism-specific databases

CTD7094.
GeneCardsGC09M035687.
HGNCHGNC:11845. TLN1.
HPACAB002006.
HPA004748.
MIM186745. gene.
neXtProtNX_Q9Y490.
PharmGKBPA36547.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324465.
HOGENOMHOG000006734.
HOVERGENHBG023870.
InParanoidQ9Y490.
KOK06271.
OMAGAHIKHR.
OrthoDBEOG7TBC1J.
PhylomeDBQ9Y490.
TreeFamTF314677.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9Y490.
BgeeQ9Y490.
CleanExHS_TLN1.
GenevestigatorQ9Y490.

Family and domain databases

Gene3D1.20.1410.10. 3 hits.
1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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]
PANTHERPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamPF00373. 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]
ProDomPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMSSF109880. SSF109880. 1 hit.
SSF109885. SSF109885. 4 hits.
SSF47031. SSF47031. 1 hit.
SSF47220. SSF47220. 5 hits.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTLN1. human.
EvolutionaryTraceQ9Y490.
GeneWikiTLN1.
GenomeRNAi7094.
NextBio27751.
PROQ9Y490.
SOURCESearch...

Entry information

Entry nameTLN1_HUMAN
AccessionPrimary (citable) accession number: Q9Y490
Secondary accession number(s): A6NMY0 expand/collapse secondary AC list , Q86YD0, Q9NZQ2, Q9UHH8, Q9UPX3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM