CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026318
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Talin-1 
Protein Synonyms/Alias
  
Gene Name
 TLN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89RKKQRPLKIRMLDGTubiquitination[1]
98RMLDGTVKTIMVDDSacetylation[2]
278VKQKGERKIFQAHKNubiquitination[1]
295QMSEIEAKVRYVKLAubiquitination[3, 4]
334PRLLGITKECVMRVDubiquitination[1, 3, 4, 5, 6]
357EWNLTNIKRWAASPKubiquitination[5]
428EDSVSPKKSTVLQQQubiquitination[3]
841SDLVNAIKADAEGESubiquitination[1]
869ILADATAKMVEAAKGubiquitination[1, 3, 4, 5]
875AKMVEAAKGAAAHPDubiquitination[1]
1306AQVVSNLKGISMSSSubiquitination[1]
1530RQFVQSAKEVANSTAubiquitination[1]
1544ANLVKTIKALDGAFTacetylation[2, 4]
1854CARRVSEKVSHVLAAubiquitination[1, 3]
1915DHREGILKTAKVLVEubiquitination[7]
1918EGILKTAKVLVEDTKacetylation[2, 4]
1918EGILKTAKVLVEDTKubiquitination[1]
1925KVLVEDTKVLVQNAAacetylation[2, 4, 8]
1925KVLVEDTKVLVQNAAubiquitination[1]
1937NAAGSQEKLAQAAQSacetylation[2]
2009DPAVWQLKNSAKVMVacetylation[2]
2027TSLLKTVKAVEDEATacetylation[2, 4]
2419QIRQQQYKFLPSELRubiquitination[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] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2429 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
AAVSQQLAPL QEISHLIEPL ANAARAEASQ LGHKVSQMAQ YFEPLTLAAV GAASKTLSHP 1740
QQMALLDQTK TLAESALQLL YTAKEAGGNP KLDEGPMGEP EGSFVDYQTT MVRTAKAIAV 1800
TVQEMIGSHI KHRVQELGHG CAALVTKAGA LQCSPSDAYT KKELIECARR VSEKVSHVLA 1860
ALQAGNRGTQ ACITAASAVS GIIADLDTTI MFATAGTLNR EGTETFADHR EGILKTAKVL 1920
VEDTKVLVQN AAGSQEKLAQ AAQSSVATIT RLADVVKLGA ASLGAEDPET QVVLINAVKD 1980
VAKALGDLIS ATKAAAGKVG DDPAVWQLKN SAKVMVTNVT SLLKTVKAVE DEATKGTRAL 2040
EATTEHIRQE LAPPAKTSTP EDFIRMTKGI TMATAKAVAA GNSCRQEDVI ATANLSRRAI 2100
ADMLRACKEA AYHPEVAPDV RLRALHYGRE CANGYLELLD HVLLTLQKPS PELKQQLTGH 2160
SKRVAGSVTE LIQAAEAMKG TEWVDPEDPT VIAENELLGA AAAIEAAAKK LEQLKPRAKP 2220
KEADESLNFE EQILEAAKSI AAATSALVKA ASAAQRELVA QGKVGAIPAN ALDDGQWSQG 2280
LISAARMVAA ATNNLCEAAN AAVQGHASQE KLISSAKQVA ASTAQLLVAC KVKADQDSEA 2340
MKRLQAAGNA VKRASDNLVK AAQKAAAFEE QENETVVVKE KMVGGIAQII AAQEEMLRKE 2400
RELEEARKKL AQIRQQQYKF LPSELRDEH 2429 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0005925; C:focal adhesion; IEA:InterPro.
 GO:0001726; C:ruffle; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
 GO:0007155; P:cell adhesion; IEA:InterPro.
 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