Protein detail

UTRN

Utrophin (Dystrophin-related protein 1) (DRP-1)

Protein symbol UTRN	UniProt ID P46939	EVMP score 0.50
Frequency 2	Transmembrane count	Protein classification Plasma proteinsPredicted intracellular proteins

EVMP score: annotation confidence score.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information

Protein Names

Utrophin (Dystrophin-related protein 1) (DRP-1)

Protein Class

Plasma proteinsPredicted intracellular proteins

Protein Function

Predicted intracellular proteins

Ensembl

ENSG00000152818

Entrez Gene Symbol

UTRN

Gene Synonym

DMDLDRPDRP1

Gene Description

Utrophin

Chromosome

Position

144285335-144853034

Frequency

EVMP Score

0.50

Fluorescence & Localization

Tissue SpecificepididymisCell SpecificBreast myoepithelial cellsSingle-Nuclei Brain SpecificLAMP5-LHX6 and Chandelier

Function & Pathway

Protein Function

Predicted intracellular proteins

Cellular Component

Molecular Function

Biological Process

Reactome

Mediation Categories

Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediation

Relations & Evidence

Enzyme-Mediated Modification

2 records.

Substrate Gene Symbol	Enzyme Gene Symbol	Enzyme UniProt ID	Residue Type	Residue Offset	Modification	Database	References
UTRN	MARK2	Q7KZI7	S	1,258	phosphorylation	PhosphoSite_MIMPMIMPSIGNORProtMapperRLIMS-P_ProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper	ProtMapper:19945424 SIGNOR:19945424
UTRN	CSNK2A2	P19784	S	825	phosphorylation	KEA	KEA:17570479

Ligand-Receptor Signaling

4 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
intracellular	intracellular	ComPPI	No	No	No	No	No
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	UniProt_location	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No

Regulatory Interaction Network

1 record.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
MARK2	Q7KZI7	UTRN	P46939	Yes	Yes	No	PhosphoSite_MIMPMIMPiPTMnetSIGNORProtMapperRLIMS-P_ProtMapperHINTSIGNOR_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper	PhosphoSite:19945424 HINT:35271311 SIGNOR:19945424 HINT:19945424 ProtMapper:19945424 HINT:19615732

Protein Complex Composition

3 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs
IPO13 RRP9 THOC1 THOC2 THOC3 THOC5 THOC6 THOC7 UBE3C UBR7 USP13 UTRN VIM XPO4 ZC3H15 ZCRB1 ZKSCAN5	O43818 O94829 P08670 P46939 Q13769 Q15386 Q6I9Y2 Q86W42 Q8N806 Q8NI27 Q8TBF4 Q8WU90 Q92995 Q96FV9 Q96J01 Q9C0E2 Q9Y2L8	0:0:0:0:0:0:0:0:0:0:0:0:0:0:0:0:0	Havugimana2012	Havugimana2012:C_609
ALDH9A1 ANKRD26 CCSER1 CCSER2 DISC1 DIXDC1 L3HYPDH NDE1 NDEL1 PAFAH1B1 SLC25A43 TRIM7 UTRN	P43034 P46939 P49189 Q155Q3 Q8WUT9 Q96EM0 Q9C029 Q9C0I3 Q9GZM8 Q9H7U1 Q9NRI5 Q9NXR1 Q9UPS8	0:0:0:0:0:0:0:0:0:0:0:0:0	hu.MAP2
UTRN	P46939	2	PDB	PDB:1qagPDB:1bhd

Isolation & Detection Technology

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity Capture	Mass spectrometry	2	38113368 38207106

Sequence, Structure & Domains

Sequences

Length

3,433

Mass

394,466

Sequence

MAKYGEHEASPDNGQNEFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPINDMFTDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQVKDVMKDVMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPIERLEHAFSKAQTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEEEAINIQSTAPEEEHESPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEEVKDQFATHEAFMMELTAHQSSVGSVLQAGNQLITQGTLSDEEEFEIQEQMTLLNARWEALRVESMDRQSRLHDVLMELQKKQLQQLSAWLTLTEERIQKMETCPLDDDVKSLQKLLEEHKSLQSDLEAEQVKVNSLTHMVVIVDENSGESATAILEDQLQKLGERWTAVCRWTEERWNRLQEINILWQELLEEQCLLKAWLTEKEEALNKVQTSNFKDQKELSVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLDNSKASKKINSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVRVREQAITKKSKQELPPPPPPKKRQIHVDIEAKKKFDAISAELLNWILKWKTAIQTTEIKEYMKMQDTSEMKKKLKALEKEQRERIPRADELNQTGQILVEQMGKEGLPTEEIKNVLEKVSSEWKNVSQHLEDLERKIQLQEDINAYFKQLDELEKVIKTKEEWVKHTSISESSRQSLPSLKDSCQRELTNLLGLHPKIEMARASCSALMSQPSAPDFVQRGFDSFLGRYQAVQEAVEDRQQHLENELKGQPGHAYLETLKTLKDVLNDSENKAQVSLNVLNDLAKVEKALQEKKTLDEILENQKPALHKLAEETKALEKNVHPDVEKLYKQEFDDVQGKWNKLKVLVSKDLHLLEEIALTLRAFEADSTVIEKWMDGVKDFLMKQQAAQGDDAGLQRQLDQCSAFVNEIETIESSLKNMKEIETNLRSGPVAGIKTWVQTRLGDYQTQLEKLSKEIATQKSRLSESQEKAANLKKDLAEMQEWMTQAEEEYLERDFEYKSPEELESAVEEMKRAKEDVLQKEVRVKILKDNIKLLAAKVPSGGQELTSELNVVLENYQLLCNRIRGKCHTLEEVWSCWIELLHYLDLETTWLNTLEERMKSTEVLPEKTDAVNEALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEDLSHLAESKQISLEKQLQVLRETDQMLQVLQESLGELDKQLTTYLTDRIDAFQVPQEAQKIQAEISAHELTLEELRRNMRSQPLTSPESRTARGGSQMDVLQRKLREVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLDVKDVDPDVIQTHLDKCMKLYKTLSEVKLEVETVIKTGRHIVQKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLARKMKKEAASLSEWLSATETELVQKSTSEGLLGDLDTEISWAKNVLKDLEKRKADLNTITESSAALQNLIEGSEPILEERLCVLNAGWSRVRTWTEDWCNTLMNHQNQLEIFDGNVAHISTWLYQAEALLDEIEKKPTSKQEEIVKRLVSELDDANLQVENVRDQALILMNARGSSSRELVEPKLAELNRNFEKVSQHIKSAKLLIAQEPLYQCLVTTETFETGVPFSDLEKLENDIENMLKFVEKHLESSDEDEKMDEESAQIEEVLQRGEEMLHQPMEDNKKEKIRLQLLLLHTRYNKIKAIPIQQRKMGQLASGIRSSLLPTDYLVEINKILLCMDDVELSLNVPELNTAIYEDFSFQEDSLKNIKDQLDKLGEQIAVIHEKQPDVILEASGPEAIQIRDTLTQLNAKWDRINRMYSDRKGCFDRAMEEWRQFHCDLNDLTQWITEAEELLVDTCAPGGSLDLEKARIHQQELEVGISSHQPSFAALNRTGDGIVQKLSQADGSFLKEKLAGLNQRWDAIVAEVKDRQPRLKGESKQVMKYRHQLDEIICWLTKAEHAMQKRSTTELGENLQELRDLTQEMEVHAEKLKWLNRTELEMLSDKSLSLPERDKISESLRTVNMTWNKICREVPTTLKECIQEPSSVSQTRIAAHPNVQKVVLVSSASDIPVQSHRTSEISIPADLDKTITELADWLVLIDQMLKSNIVTVGDVEEINKTVSRMKITKADLEQRHPQLDYVFTLAQNLKNKASSSDMRTAITEKLERVKNQWDGTQHGVELRQQQLEDMIIDSLQWDDHREETEELMRKYEARLYILQQARRDPLTKQISDNQILLQELGPGDGIVMAFDNVLQKLLEEYGSDDTRNVKETTEYLKTSWINLKQSIADRQNALEAEWRTVQASRRDLENFLKWIQEAETTVNVLVDASHRENALQDSILARELKQQMQDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNLQSKTELTPEERAQKIAKAMRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAESVRNGWKPVGDLLIDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSISHNKVPYYINHQTQTTCWDHPKMTELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEYCIPTTSGEDVRDFTKVLKNKFRSKKYFAKHPRLGYLPVQTVLEGDNLETPITLISMWPEHYDPSQSPQLFHDDTHSRIEQYATRLAQMERTNGSFLTDSSSTTGSVEDEHALIQQYCQTLGGESPVSQPQSPAQILKSVEREERGELERIIADLEEEQRNLQVEYEQLKDQHLRRGLPVGSPPESIISPHHTSEDSELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPESDSRINGVSPWASPQHSALSYSLDPDASGPQFHQAAGEDLLAPPHDTSTDLTEVMEQIHSTFPSCCPNVPSRPQAM

Alternative Products

Event=Alternative promoter usage; Named isoforms=4; Name=1; IsoId=P46939-1; Sequence=Displayed; Name=2; IsoId=P46939-2; Sequence=VSP_047925; Name=Up71; IsoId=P46939-3; Sequence=VSP_054943, VSP_054944; Name=Up140; IsoId=P46939-4; Sequence=VSP_054942

Alternative Sequence

1..2086; Missing (in isoform Up140); 1..23; MAKYGEHEASPDNGQNEFSDIIK -> MKFFDFLFIFKILPPYYINFFSS (in isoform Up71); 1..22; MAKYGEHEASPDNGQNEFSDII -> MSGLAATTFHWKKCRLDLPGHVALQAC (in isoform 2); 24..2832; Missing (in isoform Up71)

3D Structural Models

Turn

47..49; 56..62

Helix

32..46; 64..74; 86..102; 112..117; 120..134; 136..149; 151..164; 177..179; 183..192; 194..196; 199..204; 207..222; 230..234; 240..253

Beta Strand

174..176

3D Structure

Electron microscopy (1); X-ray crystallography (2)

Domain & Motif Annotations

Repeat

312..416; Spectrin 1; 421..525; Spectrin 2; 532..636; Spectrin 3; 690..795; Spectrin 4; 801..901; Spectrin 5; 910..1012; Spectrin 6; 1019..1121; Spectrin 7; 1128..1229; Spectrin 8; 1236..1333; Spectrin 9; 1335..1436; Spectrin 10; 1438..1540; Spectrin 11; 1547..1648; Spectrin 12; 1653..1747; Spectrin 13; 1748..1848; Spectrin 14; 1849..1968; Spectrin 15; 1979..2080; Spectrin 16; 2087..2186; Spectrin 17; 2229..2332; Spectrin 18; 2349..2439; Spectrin 19; 2446..2555; Spectrin 20; 2562..2687; Spectrin 21; 2694..2796; Spectrin 22

Zinc Finger

3065..3121; ZZ-type; degenerate

Domain (CC)

Actin binding affinity is primarily determined by CH domain 1..

Domain (FT)

31..135; Calponin-homology (CH) 1; 150..255; Calponin-homology (CH) 2; 2812..2845; WW

Region

1..246; Actin-binding; 268..905; Interaction with SYNM; 284..303; Disordered; 1336..1768; Interaction with SYNM; 2798..3165; Interaction with SYNM; 3357..3390; Disordered

Clinical Relevance

Related Diseases

Muscular dystrophy

Biomarker

Phase 2

Drugs

EZUTROMID ENZYME INHIBITOR

Antibody

CAB016348 HPA018894

Interaction Protein

ENSG00000072518ENSG00000075413ENSG00000101400ENSG00000116141ENSG00000134769ENSG00000138101ENSG00000143324ENSG00000168807ENSG00000171873ENSG00000172164ENSG00000173402

Interaction Count

Interaction Dataset

biogrid_opencellintact_biogrid_opencellintact_biogrid