CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011722
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nexilin 
Protein Synonyms/Alias
 F-actin-binding protein; Nelin 
Gene Name
 NEXN 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
136IEQDMLEKRKIQRELubiquitination[1]
203REEKERIKYEEDKRIacetylation[2]
311GYRPGKLKLSFEEMEubiquitination[1]
405KHKLEMEKQEFEQLRacetylation[2]
436REYEELIKLKRSGSIubiquitination[1]
446RSGSIQAKNLKSKFEacetylation[2]
Reference
 [1] 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]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. 
Sequence Annotation
 DOMAIN 582 670 Ig-like.
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 241 241 Phosphoserine.
 MOD_RES 357 357 Phosphoserine.
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 370 370 Phosphothreonine.  
Keyword
 Actin-binding; Alternative splicing; Cardiomyopathy; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Immunoglobulin domain; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 675 AA 
Protein Sequence
MNDISQKAEI LLSSSKPVPK TYVPKLGKGD VKDKFEAMQR AREERNQRRS RDEKQRRKEQ 60
YIREREWNRR KQEIKEMLAS DDEEDVSSKV EKAYVPKLTG TVKGRFAEME KQRQEEQRKR 120
TEEERKRRIE QDMLEKRKIQ RELAKRAEQI EDINNTGTES ASEEGDDSLL ITVVPVKSYK 180
TSGKMKKNFE DLEKEREEKE RIKYEEDKRI RYEEQRPSLK EAKCLSLVMD DEIESEAKKE 240
SLSPGKLKLT FEELERQRQE NRKKQAEEEA RKRLEEEKRA FEEARRQMVN EDEENQDTAK 300
IFKGYRPGKL KLSFEEMERQ RREDEKRKAE EEARRRIEEE KKAFAEARRN MVVDDDSPEM 360
YKTISQEFLT PGKLEINFEE LLKQKMEEEK RRTEEERKHK LEMEKQEFEQ LRQEMGEEEE 420
ENETFGLSRE YEELIKLKRS GSIQAKNLKS KFEKIGQLSE KEIQKKIEEE RARRRAIDLE 480
IKEREAENFH EEDDVDVRPA RKSEAPFTHK VNMKARFEQM AKAREEEEQR RIEEQKLLRM 540
QFEQREIDAA LQKKREEEEE EEGSIMNGST AEDEEQTRSG APWFKKPLKN TSVVDSEPVR 600
FTVKVTGEPK PEITWWFEGE ILQDGEDYQY IERGETYCLY LPETFPEDGG EYMCKAVNNK 660
GSAASTCILT IESKN 675 
Gene Ontology
 GO:0005924; C:cell-substrate adherens junction; IEA:Compara.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; ISS:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
 GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
 GO:0051493; P:regulation of cytoskeleton organization; IEP:UniProtKB. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR013098; Ig_I-set.
 IPR003599; Ig_sub.
 IPR020675; Myosin_light_ch_kinase-rel.
 IPR020678; Nexilin. 
Pfam
 PF07679; I-set 
SMART
 SM00409; IG 
PROSITE
 PS50835; IG_LIKE 
PRINTS