CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038056
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Talin-2 
Protein Synonyms/Alias
  
Gene Name
 Tln2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
337PRLLGITKDSVMRVDubiquitination[1]
690AMLVLKAKNVAQVAEubiquitination[1]
1543NSTANLVKTIKALDGacetylation[2, 3]
1543NSTANLVKTIKALDGubiquitination[1]
2131TNVTSLLKTVKAVEDacetylation[2, 3]
2131TNVTSLLKTVKAVEDubiquitination[1]
2189GITMATAKAVAAGNSubiquitination[1]
2323SIEAAAKKLEQLKPRacetylation[2]
2328AKKLEQLKPRAKPKQacetylation[2]
2465QAAGNAVKRASDNLVacetylation[4]
2465QAAGNAVKRASDNLVsuccinylation[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2542 AA 
Protein Sequence
MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK 60
GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR 120
IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR 180
TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF 240
GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK 300
YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK 360
RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES 420
TMLEESVSPK KSTILQQQFN RTGKAEHGSV ALPAVMRSGS SGPETFNVGS MPSPQQQVMV 480
GQMHRGHMPP LTSAQQALMG TINTSMHAVQ QAQDDLSELD SLPPLGQDMA SRVWVQNKVD 540
ESKHEIHSQV DAITAGTASV VNLTAGDPAD TDYTAVGCAI TTISSNLTEM SKGVKLLAAL 600
MDDDVGSGED LLRAARTLAG AVSDLLKAVQ PTSGEPRQTV LTAAGSIGQA SGDLLRQIGE 660
NETDERFQDV LMSLAKAVAN AAAMLVLKAK NVAQVAEDTV LQNRVIAAAT QCALSTSQLV 720
ACAKVVSPTI SSPVCQEQLI EAGKLVDRSV ENCVRACQAA TSDSELLKQV SAAASVVSQA 780
LHDLLQHVRQ FASRGEPIGR YDQATDTIMC VTESIFSSMG DAGEMVRQAR VLAQATSDLV 840
NAMRSDAEAE IDMENSKKLL AAAKLLADST ARMVEAAKGA AANPENEDQQ QRLREAAEGL 900
RVATNAAAQN AIKKKIVNRL EVAAKQAAAA ATQTIAASQN AAISNKNPSA QQQLVQSCKA 960
VADHIPQLVQ GVRGSQAQAE DLSAQLALII SSQNFLQPGS KMVSSAKAAV PTVSDQAAAM 1020
QLSQCAKNLA TSLAELRTAS QKAHEACGPM EIDSALNTVQ TLKNELQDAK MAAAESQLKP 1080
LPGETLEKCA QDLGSTSKGV GSSMAQLLTC AAQGNEHYTG VAARETAQAL KTLAQAARGV 1140
AASTNDPEAA HAMLDSARDV MEGSAMLIQE AKQALIAPGD TESQQRLAQV AKAVSHSLNN 1200
CVNCLPGQKD VDVALKSIGE ASKKLLVDSL PPSTKPFQEA QSELNQAAAD LNQSAGEVVH 1260
ATRGQSGELA AASGKFSDDF DEFLDAGIEM AGQAQTKEDQ MQVIGNLKNI SMASSKLLLA 1320
AKSLSVDPGA PNAKNLLAAA ARAVTESINQ LIMLCTQQAP GQKECDNALR ELETVKGMLE 1380
NPNEPVSDLS YFDCIESVME NSKVLGESMA GISQNAKTGD LPAFGECVGI ASKALCGLTE 1440
AAAQAAYLVG ISDPNSQAGH QGLVDPIQFA RANQAIQMAC QNLVDPGSSP SQVLSAATIV 1500
AKHTSALCNA CRIASSKTAN PVAKRHFVQS AKEVANSTAN LVKTIKALDG DFSEDNRNKC 1560
RIATTPLIEA VENLTAFASN PEFASIPAQI SSEGSQAQEP ILVSAKTMLE SSSYLIRTAR 1620
SLAINPKDPP TWSVLAGHSH TVSDSIKSLI TSIRDKAPGQ RECDYSIDGI NRCIRDIEQA 1680
SLAAVSQSLA TRDDISVEAL QEQLTSVVQE IGHLIDPIAT AARGEAAQLG HKVTQLASYF 1740
EPLILAAVGV ASKMLDHQQQ MTVLDQTKTL AESALQMLYA AKEGGGNPKA QHTHDAITEA 1800
AQLMKEAVDD IMVTLNEAAS EVGLVGGMVD AIAEAMSKLD EGTPPEPKGT FVDYQTTVVK 1860
YSKAIAVTAQ EMMTKSVTNP EELGGLASQM TTDYGHLALQ GQMAAATAEP EEIGFQIRTR 1920
VQDLGHGCIF LVQKAGALQV CPTDSYTKRE LIECARSVTE KVSLVLSALQ AGNKGTQACI 1980
TAATAVSGII ADLDTTIMFA TAGTLNAENG ETFADHRENI LKTAKALVED TKLLVSGAAS 2040
TPDKLAQAAQ SSAATITQLA EVVKLGAASL GSNDPETQVV LINAIKDVAK ALSDLIGATK 2100
GAASKPADDP SMYQLKGAAK VMVTNVTSLL KTVKAVEDEA TRGTRALEAT IEYIKQELTV 2160
FQSKDIPEKT SSPEESIRMT KGITMATAKA VAAGNSCRQE DVIATANLSR KAVSDMLIAC 2220
KQASFYPDVS EEVRTRALRY GTECTLGYLD LLEHVLVILQ KPTPELKHQL AAFSKRVAGA 2280
VTELIQAAEA MKGTEWVDPE DPTVIAETEL LGAAASIEAA AKKLEQLKPR AKPKQADETL 2340
DFEEQILEAA KSIAAATSAL VKSASAAQRE LVAQGKVGSI PANAADDGQW SQGLISAARM 2400
VAAATSSLCE AANASVQGHA SEEKLISSAK QVAASTAQLL VACKVKADQD SEAMKRLQAA 2460
GNAVKRASDN LVRAAQKAAF GKADDDDVVV KTKFVGGIAQ IIAAQEEMLK KERELEEARK 2520
KLAQIRQQQY KFLPTELRED EG 2542 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0005916; C:fascia adherens; IDA:MGI.
 GO:0005925; C:focal adhesion; IEA:InterPro.
 GO:0001726; C:ruffle; IEA:InterPro.
 GO:0045202; C:synapse; IDA:MGI.
 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.
 IPR015711; Talin-2.
 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 
PROSITE
 PS00661; FERM_2
 PS50057; FERM_3
 PS50945; I_LWEQ 
PRINTS