CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041617
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Utrn 
Protein Synonyms/Alias
  
Gene Name
 Utrn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
3*****MAKYGHLEASacetylation[1]
240VAVQLPDKKSIIMYLacetylation[1]
961DETLENQKPTLHKLSacetylation[1]
1536GAQVTEGKQDLERASacetylation[1]
2047DASFLKDKLASLNQRacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
  
Keyword
 Actin-binding; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2416 AA 
Protein Sequence
MAKYGHLEAS PDDGQNQFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFSDL 60
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNP 120
KLTLGLLWSI ILHWQVKDVM KDIMSDLQQT NSEKILLSWV RQTTRPYSQV NVLNFTTSWT 180
DGLAFNAVLH RHKPDLFSWD RVVKMSPTER LEHAFSKAHT YLGIEKLLDP EDVAVQLPDK 240
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEGE EINIQSAVLT EEGQSPRAET 300
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEDVKEQFA THETFMMELT 360
AHQSSVGSVL QAGNQLMTQG TLSDEEEFEI QEQMTLLNAR WEALRVESME RQSRLHDALM 420
ELQKKQLQQL SGWLTLTEER IQKMESLPVG DDLPSLQNLL EEHKSLQSDL EAEQVKVNSL 480
THMVVIVDEN SGESATAVLE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL 540
LEAWLTEKEE ALNKVQTGNF KDQKELGVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL 600
LSNPKASEKM NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVHVRE 660
QGMIKKPKQE LPPPPPPKKR QIHVDVEAKK KFDATSAELQ SWILRSKAAL QNTEMNEYKK 720
SQETSGVRKK WKGLEKEQKE KIPQLDELNQ TGQILQEQMG KEGLLAEEIN DVLERVLLEW 780
KMISQQLEDL GRKIQLQEDI NAYFRQLDAL EKTIRAKEEW LRDASFSESP QRSLPSLKDS 840
CQRELTDLLG LHPRIEILCA SCSALRSQPS VPGFVQQGFD DLRRHYQAVQ KALEEYQQQL 900
ENELKSQPEP AYLDTLNTLK KMLSESEKAA QASLSALNDP SAVEQALQEK KALDETLENQ 960
KPTLHKLSEE TKALEKNMLP DVGKTYRQEF DDAQGKWNKV KTKVSRDLRS LEEIIPRLRD 1020
FKADSEVIEK WTNGVKDFLM KEQAAQGDTT ALQRQLDQCT TFANEIETIE SSLKNLRDIE 1080
TSLQRCPVTG VKTWVQTRLA DYQSQLEKFS QEIDIQKSRL SDSQEKAMNL KKDLAEMQEW 1140
MAQAEEDYLE RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDSIK LVAARVPSGG 1200
QELTSEFNEV LESYQLLCNR IRGKCHTLEE VWSCWVELLH YLDLETSWLN TLEERMQSTE 1260
ALPERAEAVH DALESLESVL RHPADNRTQI RELGQTLIDG GILDDIISEK LEAFNSRYEE 1320
LSHLAESKQI SLEKQLQVLR ETDHMLQVLK ESLGELDKQL TTYLTDRIDA FQLPQEAQKI 1380
QAEISAHELT LEELKKNVRP QPPTSPEGRT TRGGSQMDLL QRKLREVSTK FQLFQKPANF 1440
EQRMLDCKRV LDGVKAELHV LSVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR 1500
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLSRKLK KEAAILSEWL 1560
STTEAELVQK STSEGVIGDL DTEISWAKNI LKDLERRKVD LNAITESSAA LQHLVVGSES 1620
VLEDTLCVLN AGWSRVRTWT EDWRNTLLNH QNQLEVFDGH VAHISTWLYQ AEALLDEIEK 1680
KPASKQEEIV KRLLSELSDA SIQVENVREQ AIVLVNARGS SSRELVEPKL AELSKNFEKV 1740
SQHINSAQML IGQDPAGTVE AVGPFSDLES LESDIENMLK VVEKHLDPSN DEKMDEERAQ 1800
IEEVLQRGEH LLHEPMEDSK KEKIRLQLLL LHTRYNKIKA IPQRKTIPLS SGIMSSALPA 1860
DYLVEINKIL LTLDDIELSL NIPELNTTVY EDFSFQEDSL KRIKDQLDRL GEQLAAVHEK 1920
QPDVILEASG PEAIQIRDML SQLNAKWDRV NRLYSDRRGS FARAVEEWKQ FHCDLDDLTQ 1980
WLSEAEDLLV GTCAPDGSLD LEKARTHQLE LEDGLSSHQP CLIDVNQKGE DIVQRLRPSD 2040
ASFLKDKLAS LNQRWSALVA EVKDLQPRLK GESKQVSGYR KRLDEVVCWL TKVENAVQKR 2100
STPDPEENPW ELTDLAQEMD AQAENIKWLN RAELEMLSDK NLSLCERDNL SESLRNVNTM 2160
WTKICREVPS LLKTRTQDPC SAPQTRIAAH PNVQKVALVS SASDAPLRGP EISVPADLDK 2220
TITELADWLV LIDQMLKSNI VTVGDVKEIN KTVSRMKITK ADLEQRHPQL DFVFTLAQNL 2280
KNKASSSDLR TAITEKLEKL KTQWESTQHG VELRRQQLED MVVDSLQWDD HREETEELMR 2340
KHEARFYMLQ QARRDPLSKQ VSDNQLLLQE LGSGDGVIMA FDNVLQKLLE EYSSDDTRNV 2400
EETTEYLKTS WINLKQ 2416 
Gene Ontology
 GO:0070938; C:contractile ring; IEA:Compara.
 GO:0030864; C:cortical actin cytoskeleton; IDA:RGD.
 GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Compara.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0030426; C:growth cone; IDA:RGD.
 GO:0031594; C:neuromuscular junction; IDA:RGD.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0051015; F:actin filament binding; IDA:RGD.
 GO:0007528; P:neuromuscular junction development; IDA:RGD.
 GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH 
PRINTS