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P46939

- UTRO_HUMAN

UniProt

P46939 - UTRO_HUMAN

Protein

Utrophin

Gene

UTRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    May play a role in anchoring the cytoskeleton to the plasma membrane.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3064 – 311148ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. calcium ion binding Source: InterPro
    3. integrin binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: BHF-UCL
    6. vinculin binding Source: BHF-UCL
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. muscle contraction Source: ProtInc
    2. muscle organ development Source: ProtInc
    3. positive regulation of cell-matrix adhesion Source: UniProtKB
    4. regulation of sodium ion transmembrane transporter activity Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiP46939.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Utrophin
    Alternative name(s):
    Dystrophin-related protein 1
    Short name:
    DRP-1
    Gene namesi
    Name:UTRN
    Synonyms:DMDL, DRP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12635. UTRN.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: ProtInc
    4. dystrophin-associated glycoprotein complex Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. filopodium Source: BHF-UCL
    7. filopodium membrane Source: BHF-UCL
    8. membrane Source: ProtInc
    9. neuromuscular junction Source: Ensembl
    10. nucleus Source: HPA
    11. plasma membrane Source: HPA
    12. postsynaptic membrane Source: UniProtKB-SubCell
    13. protein complex Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37260.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 34333433UtrophinPRO_0000076082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphotyrosine1 Publication
    Modified residuei10 – 101Phosphoserine2 Publications
    Modified residuei295 – 2951Phosphoserine1 Publication
    Modified residuei3297 – 32971Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP46939.
    PaxDbiP46939.
    PRIDEiP46939.

    PTM databases

    PhosphoSiteiP46939.

    Expressioni

    Tissue specificityi

    Isoform 1 has high expression in muscle. Isoforms Up70 and Up140 were found in all the adult and fetal tissues tested and relatively abundant in lung and kidney.1 Publication

    Gene expression databases

    ArrayExpressiP46939.
    BgeeiP46939.
    CleanExiHS_UTRN.
    GenevestigatoriP46939.

    Organism-specific databases

    HPAiCAB016348.
    HPA018894.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the syntrophins SNTA1; SNTB1 and SNTB2. Interacts with SYNM. Interacts (via its WWW and ZZ domains) with DAG1 (via the PPXY motif of betaDAG1); the interaction is inhibited by the tyrosine phosphorylation of the PPXY motif of DAG1.6 Publications

    Protein-protein interaction databases

    BioGridi113245. 30 interactions.
    DIPiDIP-45639N.
    DIP-711N.
    IntActiP46939. 34 interactions.
    MINTiMINT-109722.
    STRINGi9606.ENSP00000356515.

    Structurei

    Secondary structure

    1
    3433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 4615
    Turni47 – 493
    Turni56 – 627
    Helixi64 – 7411
    Helixi86 – 10217
    Helixi112 – 1176
    Helixi120 – 13415
    Helixi136 – 14914
    Helixi151 – 16414
    Beta strandi174 – 1763
    Helixi177 – 1793
    Helixi183 – 19210
    Helixi194 – 1963
    Helixi199 – 2046
    Helixi207 – 22216
    Helixi230 – 2345
    Helixi240 – 25314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BHDX-ray2.00A/B144-261[»]
    1QAGX-ray3.00A/B31-256[»]
    ProteinModelPortaliP46939.
    SMRiP46939. Positions 31-255, 308-430, 2804-3063.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46939.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 246246Actin-bindingAdd
    BLAST
    Domaini31 – 135105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 252103CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati253 – 30856Spectrin 1Add
    BLAST
    Repeati309 – 417109Spectrin 2Add
    BLAST
    Repeati418 – 526109Spectrin 3Add
    BLAST
    Repeati541 – 63797Spectrin 4Add
    BLAST
    Repeati687 – 798112Spectrin 5Add
    BLAST
    Repeati803 – 902100Spectrin 6Add
    BLAST
    Repeati1016 – 108368Spectrin 7Add
    BLAST
    Repeati1125 – 1230106Spectrin 8Add
    BLAST
    Repeati1248 – 133487Spectrin 9Add
    BLAST
    Repeati1432 – 1541110Spectrin 10Add
    BLAST
    Repeati1544 – 1649106Spectrin 11Add
    BLAST
    Repeati1652 – 1753102Spectrin 12Add
    BLAST
    Repeati1910 – 196859Spectrin 13Add
    BLAST
    Repeati1976 – 2081106Spectrin 14Add
    BLAST
    Repeati2258 – 233376Spectrin 15Add
    BLAST
    Repeati2399 – 244042Spectrin 16Add
    BLAST
    Repeati2443 – 2556114Spectrin 17Add
    BLAST
    Repeati2559 – 263678Spectrin 18Add
    BLAST
    Repeati2658 – 268831Spectrin 19Add
    BLAST
    Repeati2691 – 2797107Spectrin 20Add
    BLAST
    Domaini2812 – 284534WWPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni268 – 905638Interaction with SYNMAdd
    BLAST
    Regioni1336 – 1768433Interaction with SYNMAdd
    BLAST
    Regioni2798 – 3165368Interaction with SYNMAdd
    BLAST

    Domaini

    Actin binding affinity is primarily determined by CH domain 1.1 Publication

    Sequence similaritiesi

    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 20 spectrin repeats.Curated
    Contains 1 WW domain.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3064 – 311148ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000231173.
    HOVERGENiHBG005495.
    InParanoidiP46939.
    OMAiIKWLNMK.
    OrthoDBiEOG7V765N.
    PhylomeDBiP46939.
    TreeFamiTF320178.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 10 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTiSM00033. CH. 2 hits.
    SM00150. SPEC. 18 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: P46939-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKYGEHEAS PDNGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK     50
    PPINDMFTDL KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL 100
    HQNNVELVNI GGTDIVDGNH KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT 150
    NSEKILLSWV RQTTRPYSQV NVLNFTTSWT DGLAFNAVLH RHKPDLFSWD 200
    KVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK KSIIMYLTSL 250
    FEVLPQQVTI DAIREVETLP RKYKKECEEE AINIQSTAPE EEHESPRAET 300
    PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKDQFA 350
    THEAFMMELT AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR 400
    WEALRVESMD RQSRLHDVLM ELQKKQLQQL SAWLTLTEER IQKMETCPLD 450
    DDVKSLQKLL EEHKSLQSDL EAEQVKVNSL THMVVIVDEN SGESATAILE 500
    DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL LKAWLTEKEE 550
    ALNKVQTSNF KDQKELSVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL 600
    LDNSKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK 650
    DLLETVRVRE QAITKKSKQE LPPPPPPKKR QIHVDIEAKK KFDAISAELL 700
    NWILKWKTAI QTTEIKEYMK MQDTSEMKKK LKALEKEQRE RIPRADELNQ 750
    TGQILVEQMG KEGLPTEEIK NVLEKVSSEW KNVSQHLEDL ERKIQLQEDI 800
    NAYFKQLDEL EKVIKTKEEW VKHTSISESS RQSLPSLKDS CQRELTNLLG 850
    LHPKIEMARA SCSALMSQPS APDFVQRGFD SFLGRYQAVQ EAVEDRQQHL 900
    ENELKGQPGH AYLETLKTLK DVLNDSENKA QVSLNVLNDL AKVEKALQEK 950
    KTLDEILENQ KPALHKLAEE TKALEKNVHP DVEKLYKQEF DDVQGKWNKL 1000
    KVLVSKDLHL LEEIALTLRA FEADSTVIEK WMDGVKDFLM KQQAAQGDDA 1050
    GLQRQLDQCS AFVNEIETIE SSLKNMKEIE TNLRSGPVAG IKTWVQTRLG 1100
    DYQTQLEKLS KEIATQKSRL SESQEKAANL KKDLAEMQEW MTQAEEEYLE 1150
    RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDNIK LLAAKVPSGG 1200
    QELTSELNVV LENYQLLCNR IRGKCHTLEE VWSCWIELLH YLDLETTWLN 1250
    TLEERMKSTE VLPEKTDAVN EALESLESVL RHPADNRTQI RELGQTLIDG 1300
    GILDDIISEK LEAFNSRYED LSHLAESKQI SLEKQLQVLR ETDQMLQVLQ 1350
    ESLGELDKQL TTYLTDRIDA FQVPQEAQKI QAEISAHELT LEELRRNMRS 1400
    QPLTSPESRT ARGGSQMDVL QRKLREVSTK FQLFQKPANF EQRMLDCKRV 1450
    LDGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR 1500
    HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK 1550
    KEAASLSEWL SATETELVQK STSEGLLGDL DTEISWAKNV LKDLEKRKAD 1600
    LNTITESSAA LQNLIEGSEP ILEERLCVLN AGWSRVRTWT EDWCNTLMNH 1650
    QNQLEIFDGN VAHISTWLYQ AEALLDEIEK KPTSKQEEIV KRLVSELDDA 1700
    NLQVENVRDQ ALILMNARGS SSRELVEPKL AELNRNFEKV SQHIKSAKLL 1750
    IAQEPLYQCL VTTETFETGV PFSDLEKLEN DIENMLKFVE KHLESSDEDE 1800
    KMDEESAQIE EVLQRGEEML HQPMEDNKKE KIRLQLLLLH TRYNKIKAIP 1850
    IQQRKMGQLA SGIRSSLLPT DYLVEINKIL LCMDDVELSL NVPELNTAIY 1900
    EDFSFQEDSL KNIKDQLDKL GEQIAVIHEK QPDVILEASG PEAIQIRDTL 1950
    TQLNAKWDRI NRMYSDRKGC FDRAMEEWRQ FHCDLNDLTQ WITEAEELLV 2000
    DTCAPGGSLD LEKARIHQQE LEVGISSHQP SFAALNRTGD GIVQKLSQAD 2050
    GSFLKEKLAG LNQRWDAIVA EVKDRQPRLK GESKQVMKYR HQLDEIICWL 2100
    TKAEHAMQKR STTELGENLQ ELRDLTQEME VHAEKLKWLN RTELEMLSDK 2150
    SLSLPERDKI SESLRTVNMT WNKICREVPT TLKECIQEPS SVSQTRIAAH 2200
    PNVQKVVLVS SASDIPVQSH RTSEISIPAD LDKTITELAD WLVLIDQMLK 2250
    SNIVTVGDVE EINKTVSRMK ITKADLEQRH PQLDYVFTLA QNLKNKASSS 2300
    DMRTAITEKL ERVKNQWDGT QHGVELRQQQ LEDMIIDSLQ WDDHREETEE 2350
    LMRKYEARLY ILQQARRDPL TKQISDNQIL LQELGPGDGI VMAFDNVLQK 2400
    LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQNALEA EWRTVQASRR 2450
    DLENFLKWIQ EAETTVNVLV DASHRENALQ DSILARELKQ QMQDIQAEID 2500
    AHNDIFKSID GNRQKMVKAL GNSEEATMLQ HRLDDMNQRW NDLKAKSASI 2550
    RAHLEASAEK WNRLLMSLEE LIKWLNMKDE ELKKQMPIGG DVPALQLQYD 2600
    HCKALRRELK EKEYSVLNAV DQARVFLADQ PIEAPEEPRR NLQSKTELTP 2650
    EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM 2700
    DDLDADMKEA ESVRNGWKPV GDLLIDSLQD HIEKIMAFRE EIAPINFKVK 2750
    TVNDLSSQLS PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR 2800
    DFGPSSQHFL STSVQLPWQR SISHNKVPYY INHQTQTTCW DHPKMTELFQ 2850
    SLADLNNVRF SAYRTAIKIR RLQKALCLDL LELSTTNEIF KQHKLNQNDQ 2900
    LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL NVYDTGRTGK 2950
    IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ 3000
    IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFID WMHLEPQSMV 3050
    WLPVLHRVAA AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS 3100
    GRTAKGHKLH YPMVEYCIPT TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG 3150
    YLPVQTVLEG DNLETPITLI SMWPEHYDPS QSPQLFHDDT HSRIEQYATR 3200
    LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES PVSQPQSPAQ 3250
    ILKSVEREER GELERIIADL EEEQRNLQVE YEQLKDQHLR RGLPVGSPPE 3300
    SIISPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR 3350
    QLLEQPESDS RINGVSPWAS PQHSALSYSL DPDASGPQFH QAAGEDLLAP 3400
    PHDTSTDLTE VMEQIHSTFP SCCPNVPSRP QAM 3433
    Length:3,433
    Mass (Da):394,466
    Last modified:November 25, 2008 - v2
    Checksum:iC72CADE8CD666993
    GO
    Isoform 2 (identifier: P46939-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MAKYGEHEASPDNGQNEFSDII → MSGLAATTFHWKKCRLDLPGHVALQAC

    Note: Produced by alternative promoter usage.

    Show »
    Length:3,438
    Mass (Da):394,969
    Checksum:i9242095AE3CD5F48
    GO
    Isoform Up71 (identifier: P46939-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MAKYGEHEASPDNGQNEFSDIIK → MKFFDFLFIFKILPPYYINFFSS
         24-2832: Missing.

    Note: =Produced by alternative promoter usage.Curated

    Show »
    Length:624
    Mass (Da):71,417
    Checksum:i0479238E557B0CEA
    GO
    Isoform Up140 (identifier: P46939-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2086: Missing.

    Note: =Produced by alternative promoter usage.

    Show »
    Length:1,347
    Mass (Da):155,026
    Checksum:iFDB1EF2EDB5092BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361Q → R in CAA48829. (PubMed:1461283)Curated
    Isoform Up71 (identifier: P46939-3)
    Sequence conflicti5 – 51D → N no nucleotide entry (PubMed:10369873)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1880 – 18801L → I.
    Corresponds to variant rs12204715 [ dbSNP | Ensembl ].
    VAR_047794
    Natural varianti1974 – 19741A → T.
    Corresponds to variant rs12204734 [ dbSNP | Ensembl ].
    VAR_047795
    Natural varianti2060 – 20601G → D.
    Corresponds to variant rs35676466 [ dbSNP | Ensembl ].
    VAR_047796
    Natural varianti2202 – 22021N → S.
    Corresponds to variant rs1534443 [ dbSNP | Ensembl ].
    VAR_047797

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 20862086Missing in isoform Up140. 1 PublicationVSP_054942Add
    BLAST
    Alternative sequencei1 – 2323MAKYG…SDIIK → MKFFDFLFIFKILPPYYINF FSS in isoform Up71. 1 PublicationVSP_054943Add
    BLAST
    Alternative sequencei1 – 2222MAKYG…FSDII → MSGLAATTFHWKKCRLDLPG HVALQAC in isoform 2. CuratedVSP_047925Add
    BLAST
    Alternative sequencei24 – 28322809Missing in isoform Up71. 1 PublicationVSP_054944Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69086 mRNA. Translation: CAA48829.1.
    AL590704
    , AL024474, AL357149, AL513184, AL513475, AL590488 Genomic DNA. Translation: CAI10894.1.
    AL590704, AL024474, AL590488 Genomic DNA. Translation: CAI10897.1.
    AL513475
    , AL024474, AL357149, AL513184, AL590488, AL590704 Genomic DNA. Translation: CAI13032.1.
    AL590488
    , AL024474, AL357149, AL513184, AL513475, AL590704 Genomic DNA. Translation: CAI16497.1.
    AL590488, AL024474, AL590704 Genomic DNA. Translation: CAI16498.1.
    AL024474
    , AL357149, AL513184, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI23353.1.
    AL024474, AL590488, AL590704 Genomic DNA. Translation: CAI23355.1.
    AL357149
    , AL024474, AL513184, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI40388.1.
    AL513184
    , AL024474, AL357149, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI40502.1.
    AJ250044 Genomic DNA. Translation: CAB61826.1.
    CCDSiCCDS34547.1. [P46939-1]
    PIRiS28381.
    RefSeqiNP_009055.2. NM_007124.2. [P46939-1]
    XP_005267187.1. XM_005267130.1. [P46939-1]
    UniGeneiHs.133135.

    Genome annotation databases

    EnsembliENST00000367545; ENSP00000356515; ENSG00000152818. [P46939-1]
    GeneIDi7402.
    KEGGihsa:7402.
    UCSCiuc003qkt.3. human. [P46939-1]

    Polymorphism databases

    DMDMi215274104.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Utrophin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69086 mRNA. Translation: CAA48829.1 .
    AL590704
    , AL024474 , AL357149 , AL513184 , AL513475 , AL590488 Genomic DNA. Translation: CAI10894.1 .
    AL590704 , AL024474 , AL590488 Genomic DNA. Translation: CAI10897.1 .
    AL513475
    , AL024474 , AL357149 , AL513184 , AL590488 , AL590704 Genomic DNA. Translation: CAI13032.1 .
    AL590488
    , AL024474 , AL357149 , AL513184 , AL513475 , AL590704 Genomic DNA. Translation: CAI16497.1 .
    AL590488 , AL024474 , AL590704 Genomic DNA. Translation: CAI16498.1 .
    AL024474
    , AL357149 , AL513184 , AL513475 , AL590488 , AL590704 Genomic DNA. Translation: CAI23353.1 .
    AL024474 , AL590488 , AL590704 Genomic DNA. Translation: CAI23355.1 .
    AL357149
    , AL024474 , AL513184 , AL513475 , AL590488 , AL590704 Genomic DNA. Translation: CAI40388.1 .
    AL513184
    , AL024474 , AL357149 , AL513475 , AL590488 , AL590704 Genomic DNA. Translation: CAI40502.1 .
    AJ250044 Genomic DNA. Translation: CAB61826.1 .
    CCDSi CCDS34547.1. [P46939-1 ]
    PIRi S28381.
    RefSeqi NP_009055.2. NM_007124.2. [P46939-1 ]
    XP_005267187.1. XM_005267130.1. [P46939-1 ]
    UniGenei Hs.133135.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BHD X-ray 2.00 A/B 144-261 [» ]
    1QAG X-ray 3.00 A/B 31-256 [» ]
    ProteinModelPortali P46939.
    SMRi P46939. Positions 31-255, 308-430, 2804-3063.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113245. 30 interactions.
    DIPi DIP-45639N.
    DIP-711N.
    IntActi P46939. 34 interactions.
    MINTi MINT-109722.
    STRINGi 9606.ENSP00000356515.

    PTM databases

    PhosphoSitei P46939.

    Polymorphism databases

    DMDMi 215274104.

    Proteomic databases

    MaxQBi P46939.
    PaxDbi P46939.
    PRIDEi P46939.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367545 ; ENSP00000356515 ; ENSG00000152818 . [P46939-1 ]
    GeneIDi 7402.
    KEGGi hsa:7402.
    UCSCi uc003qkt.3. human. [P46939-1 ]

    Organism-specific databases

    CTDi 7402.
    GeneCardsi GC06P144654.
    HGNCi HGNC:12635. UTRN.
    HPAi CAB016348.
    HPA018894.
    MIMi 128240. gene.
    neXtProti NX_P46939.
    PharmGKBi PA37260.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000231173.
    HOVERGENi HBG005495.
    InParanoidi P46939.
    OMAi IKWLNMK.
    OrthoDBi EOG7V765N.
    PhylomeDBi P46939.
    TreeFami TF320178.

    Enzyme and pathway databases

    SignaLinki P46939.

    Miscellaneous databases

    ChiTaRSi UTRN. human.
    EvolutionaryTracei P46939.
    GeneWikii Utrophin.
    GenomeRNAii 7402.
    NextBioi 28976.
    PROi P46939.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46939.
    Bgeei P46939.
    CleanExi HS_UTRN.
    Genevestigatori P46939.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 10 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTi SM00033. CH. 2 hits.
    SM00150. SPEC. 18 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Up71 and up140, two novel transcripts of utrophin that are homologues of short forms of dystrophin."
      Wilson J., Putt W., Jimenez C., Edwards Y.H.
      Hum. Mol. Genet. 8:1271-1278(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS UP71 AND UP140), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "A second promoter provides an alternative target for therapeutic up-regulation of utrophin in Duchenne muscular dystrophy."
      Burton E.A., Tinsley J.M., Holzfeind P.J., Rodrigues N.R., Davies K.E.
      Proc. Natl. Acad. Sci. U.S.A. 96:14025-14030(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 (ISOFORM 2), ALTERNATIVE PROMOTER USAGE.
    5. "Syntrophin binds to an alternatively spliced exon of dystrophin."
      Ahn A.H., Kunkel L.M.
      J. Cell Biol. 128:363-371(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTB1.
    6. "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
      Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
      J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTA1 AND SNTB2.
    7. "Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex."
      Tommasi di Vignano A., Di Zenzo G., Sudol M., Cesareni G., Dente L.
      FEBS Lett. 471:229-234(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAG1.
    8. "Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin."
      James M., Nuttall A., Ilsley J.L., Ottersbach K., Tinsley J.M., Sudol M., Winder S.J.
      J. Cell Sci. 113:1717-1726(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAG1.
    9. "Interactions of intermediate filament protein synemin with dystrophin and utrophin."
      Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.
      Biochem. Biophys. Res. Commun. 346:768-777(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNM.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4; SER-10 AND SER-3297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The actin binding affinity of the utrophin tandem calponin-homology domain is primarily determined by its N-terminal domain."
      Singh S.M., Bandi S., Winder S.J., Mallela K.M.
      Biochemistry 53:1801-1809(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN CH, ACTIN-BINDING.
    16. "The 2.0-A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin."
      Keep N.H., Norwood F.L.M., Moores C.A., Winder S.J., Kendrick-Jones J.
      J. Mol. Biol. 285:1257-1264(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-261.
    17. "Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer."
      Keep N.H., Winder S.J., Moores C.A., Walke S., Norwood F.L.M., Kendrick-Jones J.
      Structure 7:1539-1546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 31-256, SUBUNIT.
    18. "Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism."
      Moores C.A., Keep N.H., Kendrick-Jones J.
      J. Mol. Biol. 297:465-480(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYO-ELECTRON MICROSCOPY (20 ANGSTROMS), ACTIN-BINDING.

    Entry informationi

    Entry nameiUTRO_HUMAN
    AccessioniPrimary (citable) accession number: P46939
    Secondary accession number(s): Q5SYY1, Q5SZ57, Q9UJ40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3