Q9Y490 (TLN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Talin-1

Gene names

Name:	TLN1
Synonyms:	KIAA1027, TLN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2541 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.9 Ref.10 Ref.12
Subcellular location	Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Note: Colocalizes with LAYN at the membrane ruffles 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 component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome axon guidance 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: Compara cellular component movement Non-traceable author statement Ref.2. Source: UniProtKB cortical actin cytoskeleton organization Inferred from electronic annotation. Source: Compara cytoskeletal anchoring at plasma membrane Non-traceable author statement Ref.2. Source: UniProtKB muscle contraction Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro cell-cell junction Inferred by curator PubMed 15494027. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA cytosol 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 intracellular membrane-bounded organelle 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_function	structural constituent of cytoskeleton Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2541

2541

Talin-1

PRO_0000219428

Regions

Domain

86 – 403

318

FERM

Domain

2293 – 2533

241

I/LWEQ

Region

280 – 435

156

Interaction with LAYN By similarity

Region

1327 – 1948

622

Interaction with SYNM

Amino acid modifications

Modified residue

425

1

Phosphoserine Ref.14 Ref.15 Ref.17

Modified residue

1116

1

Phosphotyrosine By similarity

Modified residue

2031

1

N6-acetyllysine Ref.16

Modified residue

2040

1

Phosphoserine Ref.19

Modified residue

2115

1

N6-acetyllysine Ref.16

Modified residue

2273

1

Phosphoserine By similarity

Natural variations

Natural variant

1227

1

S → L. Ref.1
Corresponds to variant rs2295795 [ dbSNP | Ensembl ].

VAR_023751

Natural variant

1919

1

R → W. Ref.7
Corresponds to variant rs17854239 [ dbSNP | Ensembl ].

VAR_023752

Natural variant

1984

1

A → T.
Corresponds to variant rs35642290 [ dbSNP | Ensembl ].

VAR_055538

Experimental info

Sequence conflict

824

1

R → G in AAD13152. Ref.1

Sequence conflict

824

1

R → G in AAF23322. Ref.2

Sequence conflict

1549

1

A → P in AAD13152. Ref.1

Sequence conflict

1549

1

A → P in AAF23322. Ref.2

Sequence conflict

1604

1

K → Q in AAD13152. Ref.1

Sequence conflict

1604

1

K → Q in AAF23322. Ref.2

Sequence conflict

1701

1

Q → E in AAD13152. Ref.1

Sequence conflict

1701

1

Q → E in AAF23322. Ref.2

Sequence conflict

1718

1

N → H in AAD13152. Ref.1

Sequence conflict

1718

1

N → H in AAF23322. Ref.2

Sequence conflict

1966

1

A → R in AAD13152. Ref.1

Sequence conflict

2256

1

Missing in AAF27330. Ref.2

Secondary structure

1

.

.

.

.

.

2541

Helix Strand Turn

Details...

Helix

608 – 625

18

Helix

2079 – 2098

20

Sequences

	Sequence		Length	Mass (Da)
	Q9Y490 [UniParc]. Last modified November 8, 2005. Version 3. Checksum: E21575E9199BBC5C	FASTA	2,541	269,767
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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]	"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.
[12]	"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.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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, MASS SPECTROMETRY.
[20]	"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.

IPI

IPI00298994.

RefSeq

NP_006280.3. NM_006289.3.

UniGene

Hs.471014.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SYQ	X-ray	2.42	B	607-631	[»]
4DJ9	X-ray	2.25	B	2075-2103	[»]

ProteinModelPortal

Q9Y490.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y490. 3 interactions.

MINT

MINT-5002070.

STRING

9606.ENSP00000316029.

PTM databases

PhosphoSite

Q9Y490.

Polymorphism databases

DMDM

81175200.

2D gel databases

OGP

Q9Y490.

Proteomic databases

PaxDb

Q9Y490.

PRIDE

Q9Y490.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314888; ENSP00000316029; ENSG00000137076.

GeneID

7094.

KEGG

hsa:7094.

UCSC

uc003zxt.2. human.

Organism-specific databases

CTD

7094.

GeneCards

GC09M035687.

HGNC

HGNC:11845. TLN1.

HPA

CAB002006.
HPA004748.

MIM

186745. gene.

neXtProt

NX_Q9Y490.

PharmGKB

PA36547.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG324465.

HOGENOM

HOG000006734.

HOVERGEN

HBG023870.

InParanoid

Q9Y490.

KO

K06271.

OMA

ELGHGCA.

OrthoDB

EOG48PMJ8.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
avb3_integrin_pathway. Integrins in angiogenesis.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9Y490.

Bgee

Q9Y490.

CleanEx

HS_TLN1.

Genevestigator

Q9Y490.

GermOnline

ENSG00000137076. Homo sapiens.

Family and domain databases

Gene3D

1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

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.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view]

PANTHER

PTHR19981:SF7. PTHR19981:SF7. 1 hit.

Pfam

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]

ProDom

PD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF109880. Talin_cent. 1 hit.
SSF47220. Vinculin/catenin. 6 hits.

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TLN1. human.

EvolutionaryTrace

Q9Y490.

GenomeRNAi

7094.

NextBio

27751.

SOURCE

Search...

Entry information

Entry name

TLN1_HUMAN

Accession

Primary (citable) accession number: Q9Y490
Secondary accession number(s): A6NMY0 , Q86YD0, Q9NZQ2, Q9UHH8, Q9UPX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.