CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005479
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Talin-1 
Protein Synonyms/Alias
  
Gene Name
 Tln1 
Gene Synonyms/Alias
 Tln 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
334PRLLGITKECVMRVDacetylation[1]
406ILKKKKSKDHFGLEGubiquitination[2]
428EDSVSPKKSTVLQQQacetylation[3]
428EDSVSPKKSTVLQQQsuccinylation[3]
428EDSVSPKKSTVLQQQubiquitination[2]
745EAGRLVAKAVEGCVSacetylation[1]
841SDLVNAIKADAEGESubiquitination[2]
861RKLLSAAKILADATAubiquitination[2]
869ILADATAKMVEAAKGacetylation[3]
869ILADATAKMVEAAKGsuccinylation[3]
869ILADATAKMVEAAKGubiquitination[2]
910AAAQNAIKKKLVQRLubiquitination[2]
999SFLQPGGKMVAAAKAubiquitination[2]
1068EKDLQEIKAAARDGKubiquitination[2]
1096QDLGNSTKAVSSAIAubiquitination[2]
1190QRLAQVAKAVTQALNacetylation[1]
1190QRLAQVAKAVTQALNubiquitination[2]
1306AQVVSNLKGISMSSSacetylation[3]
1306AQVVSNLKGISMSSSsuccinylation[3]
1306AQVVSNLKGISMSSSubiquitination[2]
1314GISMSSSKLLLAAKAacetylation[1]
1332DPASPNLKSQLAAAAubiquitination[2]
1541NSTANLVKTIKALDGubiquitination[2]
1544ANLVKTIKALDGDFTacetylation[1, 3, 4]
1544ANLVKTIKALDGDFTubiquitination[2]
1780LQLLYTAKEAGGNPKacetylation[1]
1917EEIGAHIKHRVQELGacetylation[1]
1960CARRVSEKVSHVLAAubiquitination[2]
2021DHREGILKTAKVLVEubiquitination[2]
2031KVLVEDTKVLVQNAAacetylation[4]
2043NAAGSQEKLAQAAQSacetylation[4]
2043NAAGSQEKLAQAAQSubiquitination[2]
2089NAVKDVAKALGDLISubiquitination[2]
2099GDLISATKAAAGKVGacetylation[3]
2099GDLISATKAAAGKVGsuccinylation[3]
2099GDLISATKAAAGKVGubiquitination[2]
2115DPAVWQLKNSAKVMVacetylation[4]
2130TNVTSLLKTVKAVEDubiquitination[2]
2188GITMATAKAVAAGNSubiquitination[2]
2333LKPRAKPKEADESLNubiquitination[2]
2476NLVKAAQKAAAFEDQubiquitination[2]
2491ENETVVVKEKMVGGIubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 86 403 FERM.
 DOMAIN 2293 2533 I/LWEQ.
 REGION 280 435 Interaction with LAYN (By similarity).
 REGION 1327 1948 Interaction with SYNM (By similarity).
 MOD_RES 425 425 Phosphoserine (By similarity).
 MOD_RES 1116 1116 Phosphotyrosine.
 MOD_RES 2031 2031 N6-acetyllysine (By similarity).
 MOD_RES 2040 2040 Phosphoserine.
 MOD_RES 2115 2115 N6-acetyllysine (By similarity).
 MOD_RES 2273 2273 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2541 AA 
Protein Sequence
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF LSDDDPKKGI 60
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG 120
ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 180
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 240
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 300
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA 360
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML 420
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM 480
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK 540
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 600
EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT 660
DPHFQDVLMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT 720
KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE 780
LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI 840
KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 900
TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP LLVQSCKAVA 960
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL 1020
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA ARDGKLKPLP 1080
GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA 1140
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV 1200
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS 1260
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK 1320
ALSTDPASPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP 1380
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA 1440
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 1500
HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF TEENRAQCRA 1560
ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL 1620
AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL 1680
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP 1740
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 1800
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF VDYQTTMVRT 1860
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV 1920
QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT 1980
AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS 2040
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 2100
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF 2160
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK 2220
EAAFHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV 2280
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN 2340
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 2400
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG 2460
NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK 2520
KLAQIRQQQY KFLPSELRDE H 2541 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005925; C:focal adhesion; ISS:HGNC.
 GO:0043231; C:intracellular membrane-bounded organelle; IEA:Compara.
 GO:0001726; C:ruffle; ISS:HGNC.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
 GO:0007155; P:cell adhesion; IEA:InterPro.
 GO:0007044; P:cell-substrate junction assembly; IMP:MGI.
 GO:0030866; P:cortical actin cytoskeleton organization; IMP:MGI.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro. 
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. 
Pfam
 PF00373; FERM_M
 PF09379; FERM_N
 PF01608; I_LWEQ
 PF02174; IRS
 PF09141; Talin_middle
 PF08913; VBS 
SMART
 SM00295; B41
 SM00307; ILWEQ 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3
 PS50945; I_LWEQ 
PRINTS