CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023814
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Talin-1 
Protein Synonyms/Alias
  
Gene Name
 TLN1 
Gene Synonyms/Alias
 KIAA1027; TLN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89RKKQRPLKIRMLDGTubiquitination[1]
278VKQKGERKIFQAHKNubiquitination[1]
295QMSEIEAKVRYVKLAubiquitination[2]
334PRLLGITKECVMRVDubiquitination[1, 2, 3, 4, 5]
357EWNLTNIKRWAASPKubiquitination[3, 5]
428EDSVSPKKSTVLQQQubiquitination[2]
441QQYNRVGKVEHGSVAubiquitination[6]
841SDLVNAIKADAEGESubiquitination[1]
861RKLLSAAKILADATAubiquitination[6]
869ILADATAKMVEAAKGubiquitination[1, 2, 3, 5, 6]
875AKMVEAAKGAAAHPDubiquitination[1]
1306AQVVSNLKGISMSSSubiquitination[1]
1530RQFVQSAKEVANSTAubiquitination[1]
1541NSTANLVKTIKALDGacetylation[7]
1541NSTANLVKTIKALDGubiquitination[1, 2, 5, 6]
1917EEIGSHIKHRVQELGacetylation[8]
1960CARRVSEKVSHVLAAubiquitination[1, 2]
2021DHREGILKTAKVLVEubiquitination[9]
2024EGILKTAKVLVEDTKubiquitination[1]
2031KVLVEDTKVLVQNAAacetylation[7]
2031KVLVEDTKVLVQNAAubiquitination[1]
2115DPAVWQLKNSAKVMVacetylation[7]
2130TNVTSLLKTVKAVEDubiquitination[6]
2133TSLLKTVKAVEDEATubiquitination[1]
2361AATSALVKAASAAQRubiquitination[6]
2531QIRQQQYKFLPSELRubiquitination[3, 5]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
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 (By similarity). 
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.
 MOD_RES 425 425 Phosphoserine.
 MOD_RES 1116 1116 Phosphotyrosine (By similarity).
 MOD_RES 2031 2031 N6-acetyllysine.
 MOD_RES 2040 2040 Phosphoserine.
 MOD_RES 2115 2115 N6-acetyllysine.
 MOD_RES 2273 2273 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2541 AA 
Protein Sequence
MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF LSDDDPKKGI 60
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG 120
ITNHDEYSLV RELMEEKKEE ITGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 180
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 240
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 300
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WNLTNIKRWA 360
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML 420
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM 480
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK 540
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 600
EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT 660
DPHFQDALMQ 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 TPKASAGPQP LLVQSCKAVA 960
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL 1020
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEVKAA ARDGKLKPLP 1080
GETMEKCTQD LGNSTKAVSS AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA 1140
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV 1200
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS 1260
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK 1320
ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALREL ETVRELLENP 1380
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA 1440
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 1500
HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA 1560
ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL 1620
AVNPRDPPSW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL 1680
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP 1740
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 1800
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT 1860
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA KPAAVAAENE EIGSHIKHRV 1920
QELGHGCAAL VTKAGALQCS PSDAYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT 1980
AASAVSGIIA DLDTTIMFAT AGTLNREGTE 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
EAAYHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PSPELKQQLT 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 EEQENETVVV 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:0005911; C:cell-cell junction; IC:UniProtKB.
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005925; C:focal adhesion; NAS:UniProtKB.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0001726; C:ruffle; ISS:HGNC.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007155; P:cell adhesion; IEA:InterPro.
 GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
 GO:0007044; P:cell-substrate junction assembly; IEA:Compara.
 GO:0006928; P:cellular component movement; NAS:UniProtKB.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0030866; P:cortical actin cytoskeleton organization; IEA:Compara.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
 GO:0006936; P:muscle contraction; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome. 
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