CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007856
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Utrophin 
Protein Synonyms/Alias
 Dystrophin-related protein 1; DRP-1 
Gene Name
 UTRN 
Gene Synonyms/Alias
 DMDL; DRP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1334SKQISLEKQLQVLREubiquitination[1, 2, 3]
2573MSLEELIKWLNMKDEubiquitination[4]
3065VAAAETAKHQAKCNIubiquitination[2, 3, 4]
3074QAKCNICKECPIVGFubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 May play a role in anchoring the cytoskeleton to the plasma membrane (By similarity). 
Sequence Annotation
 DOMAIN 1 246 Actin-binding.
 DOMAIN 31 135 CH 1.
 DOMAIN 150 252 CH 2.
 REPEAT 253 308 Spectrin 1.
 REPEAT 309 417 Spectrin 2.
 REPEAT 418 526 Spectrin 3.
 REPEAT 541 637 Spectrin 4.
 REPEAT 687 798 Spectrin 5.
 REPEAT 803 902 Spectrin 6.
 REPEAT 1016 1083 Spectrin 7.
 REPEAT 1125 1230 Spectrin 8.
 REPEAT 1248 1334 Spectrin 9.
 REPEAT 1432 1541 Spectrin 10.
 REPEAT 1544 1649 Spectrin 11.
 REPEAT 1652 1753 Spectrin 12.
 REPEAT 1910 1968 Spectrin 13.
 REPEAT 1976 2081 Spectrin 14.
 REPEAT 2258 2333 Spectrin 15.
 REPEAT 2399 2440 Spectrin 16.
 REPEAT 2443 2556 Spectrin 17.
 REPEAT 2559 2636 Spectrin 18.
 REPEAT 2658 2688 Spectrin 19.
 REPEAT 2691 2797 Spectrin 20.
 DOMAIN 2812 2845 WW.
 ZN_FING 3064 3111 ZZ-type.
 REGION 268 905 Interaction with SYNM.
 REGION 1336 1768 Interaction with SYNM.
 REGION 2798 3165 Interaction with SYNM.
 MOD_RES 4 4 Phosphotyrosine.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 3297 3297 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Calcium; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3433 AA 
Protein Sequence
MAKYGEHEAS PDNGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFTDL 60
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNH 120
KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT NSEKILLSWV RQTTRPYSQV NVLNFTTSWT 180
DGLAFNAVLH RHKPDLFSWD KVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK 240
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEEE AINIQSTAPE EEHESPRAET 300
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKDQFA THEAFMMELT 360
AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR WEALRVESMD RQSRLHDVLM 420
ELQKKQLQQL SAWLTLTEER IQKMETCPLD DDVKSLQKLL EEHKSLQSDL EAEQVKVNSL 480
THMVVIVDEN SGESATAILE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL 540
LKAWLTEKEE ALNKVQTSNF KDQKELSVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL 600
LDNSKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVRVRE 660
QAITKKSKQE LPPPPPPKKR QIHVDIEAKK KFDAISAELL NWILKWKTAI QTTEIKEYMK 720
MQDTSEMKKK LKALEKEQRE RIPRADELNQ TGQILVEQMG KEGLPTEEIK NVLEKVSSEW 780
KNVSQHLEDL ERKIQLQEDI NAYFKQLDEL EKVIKTKEEW VKHTSISESS RQSLPSLKDS 840
CQRELTNLLG LHPKIEMARA SCSALMSQPS APDFVQRGFD SFLGRYQAVQ EAVEDRQQHL 900
ENELKGQPGH AYLETLKTLK DVLNDSENKA QVSLNVLNDL AKVEKALQEK KTLDEILENQ 960
KPALHKLAEE TKALEKNVHP DVEKLYKQEF DDVQGKWNKL KVLVSKDLHL LEEIALTLRA 1020
FEADSTVIEK WMDGVKDFLM KQQAAQGDDA GLQRQLDQCS AFVNEIETIE SSLKNMKEIE 1080
TNLRSGPVAG IKTWVQTRLG DYQTQLEKLS KEIATQKSRL SESQEKAANL KKDLAEMQEW 1140
MTQAEEEYLE RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDNIK LLAAKVPSGG 1200
QELTSELNVV LENYQLLCNR IRGKCHTLEE VWSCWIELLH YLDLETTWLN TLEERMKSTE 1260
VLPEKTDAVN EALESLESVL RHPADNRTQI RELGQTLIDG GILDDIISEK LEAFNSRYED 1320
LSHLAESKQI SLEKQLQVLR ETDQMLQVLQ ESLGELDKQL TTYLTDRIDA FQVPQEAQKI 1380
QAEISAHELT LEELRRNMRS QPLTSPESRT ARGGSQMDVL QRKLREVSTK FQLFQKPANF 1440
EQRMLDCKRV LDGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR 1500
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK KEAASLSEWL 1560
SATETELVQK STSEGLLGDL DTEISWAKNV LKDLEKRKAD LNTITESSAA LQNLIEGSEP 1620
ILEERLCVLN AGWSRVRTWT EDWCNTLMNH QNQLEIFDGN VAHISTWLYQ AEALLDEIEK 1680
KPTSKQEEIV KRLVSELDDA NLQVENVRDQ ALILMNARGS SSRELVEPKL AELNRNFEKV 1740
SQHIKSAKLL IAQEPLYQCL VTTETFETGV PFSDLEKLEN DIENMLKFVE KHLESSDEDE 1800
KMDEESAQIE EVLQRGEEML HQPMEDNKKE KIRLQLLLLH TRYNKIKAIP IQQRKMGQLA 1860
SGIRSSLLPT DYLVEINKIL LCMDDVELSL NVPELNTAIY EDFSFQEDSL KNIKDQLDKL 1920
GEQIAVIHEK QPDVILEASG PEAIQIRDTL TQLNAKWDRI NRMYSDRKGC FDRAMEEWRQ 1980
FHCDLNDLTQ WITEAEELLV DTCAPGGSLD LEKARIHQQE LEVGISSHQP SFAALNRTGD 2040
GIVQKLSQAD GSFLKEKLAG LNQRWDAIVA EVKDRQPRLK GESKQVMKYR HQLDEIICWL 2100
TKAEHAMQKR STTELGENLQ ELRDLTQEME VHAEKLKWLN RTELEMLSDK SLSLPERDKI 2160
SESLRTVNMT WNKICREVPT TLKECIQEPS SVSQTRIAAH PNVQKVVLVS SASDIPVQSH 2220
RTSEISIPAD LDKTITELAD WLVLIDQMLK SNIVTVGDVE EINKTVSRMK ITKADLEQRH 2280
PQLDYVFTLA QNLKNKASSS DMRTAITEKL ERVKNQWDGT QHGVELRQQQ LEDMIIDSLQ 2340
WDDHREETEE LMRKYEARLY ILQQARRDPL TKQISDNQIL LQELGPGDGI VMAFDNVLQK 2400
LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQNALEA EWRTVQASRR DLENFLKWIQ 2460
EAETTVNVLV DASHRENALQ DSILARELKQ QMQDIQAEID AHNDIFKSID GNRQKMVKAL 2520
GNSEEATMLQ HRLDDMNQRW NDLKAKSASI RAHLEASAEK WNRLLMSLEE LIKWLNMKDE 2580
ELKKQMPIGG DVPALQLQYD HCKALRRELK EKEYSVLNAV DQARVFLADQ PIEAPEEPRR 2640
NLQSKTELTP EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM 2700
DDLDADMKEA ESVRNGWKPV GDLLIDSLQD HIEKIMAFRE EIAPINFKVK TVNDLSSQLS 2760
PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR DFGPSSQHFL STSVQLPWQR 2820
SISHNKVPYY INHQTQTTCW DHPKMTELFQ SLADLNNVRF SAYRTAIKIR RLQKALCLDL 2880
LELSTTNEIF KQHKLNQNDQ LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL 2940
NVYDTGRTGK IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ 3000
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFID WMHLEPQSMV WLPVLHRVAA 3060
AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS GRTAKGHKLH YPMVEYCIPT 3120
TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG YLPVQTVLEG DNLETPITLI SMWPEHYDPS 3180
QSPQLFHDDT HSRIEQYATR LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES 3240
PVSQPQSPAQ ILKSVEREER GELERIIADL EEEQRNLQVE YEQLKDQHLR RGLPVGSPPE 3300
SIISPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR QLLEQPESDS 3360
RINGVSPWAS PQHSALSYSL DPDASGPQFH QAAGEDLLAP PHDTSTDLTE VMEQIHSTFP 3420
SCCPNVPSRP QAM 3433 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Compara.
 GO:0030175; C:filopodium; IDA:BHF-UCL.
 GO:0031594; C:neuromuscular junction; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0003779; F:actin binding; IDA:BHF-UCL.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006936; P:muscle contraction; TAS:ProtInc.
 GO:0007517; P:muscle organ development; TAS:ProtInc.
 GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:UniProtKB.
 GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR016344; Dystrophin/utrophin.
 IPR011992; EF-hand-like_dom.
 IPR015153; EF-hand_dom_typ1.
 IPR015154; EF-hand_dom_typ2.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat.
 IPR001202; WW_dom.
 IPR000433; Znf_ZZ. 
Pfam
 PF00307; CH
 PF09068; efhand_1
 PF09069; efhand_2
 PF00435; Spectrin
 PF00397; WW
 PF00569; ZZ 
SMART
 SM00033; CH
 SM00150; SPEC
 SM00456; WW
 SM00291; ZnF_ZZ 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS