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P46939 (UTRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Utrophin
Alternative name(s):
Dystrophin-related protein 1
Short name=DRP-1
Gene names
Name:UTRN
Synonyms:DMDL, DRP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3433 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Note: Neuromuscular junction.

Tissue specificity

Muscle.

Sequence similarities

Contains 2 CH (calponin-homology) domains.

Contains 20 spectrin repeats.

Contains 1 WW domain.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative promoter usage
Polymorphism
   DomainRepeat
Zinc-finger
   LigandActin-binding
Calcium
Metal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmuscle contraction

Traceable author statement PubMed 9288751. Source: ProtInc

muscle organ development

Traceable author statement PubMed 9288751. Source: ProtInc

positive regulation of cell-matrix adhesion

Inferred from mutant phenotype PubMed 19786618. Source: UniProtKB

regulation of sodium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 21677768. Source: BHF-UCL

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 19786618. Source: UniProtKB

cytoskeleton

Traceable author statement PubMed 8977119. Source: ProtInc

dystrophin-associated glycoprotein complex

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

filopodium

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

membrane

Traceable author statement PubMed 1426262. Source: ProtInc

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 18468998. Source: MGI

   Molecular_functionactin binding

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

integrin binding

Inferred from physical interaction PubMed 16803572. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction PubMed 16803572. Source: BHF-UCL

vinculin binding

Inferred from physical interaction PubMed 16803572. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: P46939-1)

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.
Isoform 2 (identifier: P46939-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAKYGEHEASPDNGQNEFSDII → MSGLAATTFHWKKCRLDLPGHVALQAC
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 34333433Utrophin
PRO_0000076082

Regions

Domain1 – 246246Actin-binding
Domain31 – 135105CH 1
Domain150 – 252103CH 2
Repeat253 – 30856Spectrin 1
Repeat309 – 417109Spectrin 2
Repeat418 – 526109Spectrin 3
Repeat541 – 63797Spectrin 4
Repeat687 – 798112Spectrin 5
Repeat803 – 902100Spectrin 6
Repeat1016 – 108368Spectrin 7
Repeat1125 – 1230106Spectrin 8
Repeat1248 – 133487Spectrin 9
Repeat1432 – 1541110Spectrin 10
Repeat1544 – 1649106Spectrin 11
Repeat1652 – 1753102Spectrin 12
Repeat1910 – 196859Spectrin 13
Repeat1976 – 2081106Spectrin 14
Repeat2258 – 233376Spectrin 15
Repeat2399 – 244042Spectrin 16
Repeat2443 – 2556114Spectrin 17
Repeat2559 – 263678Spectrin 18
Repeat2658 – 268831Spectrin 19
Repeat2691 – 2797107Spectrin 20
Domain2812 – 284534WW
Zinc finger3064 – 311148ZZ-type
Region268 – 905638Interaction with SYNM
Region1336 – 1768433Interaction with SYNM
Region2798 – 3165368Interaction with SYNM

Amino acid modifications

Modified residue41Phosphotyrosine Ref.10
Modified residue101Phosphoserine Ref.10 Ref.12
Modified residue2951Phosphoserine Ref.9
Modified residue32971Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 2222MAKYG…FSDII → MSGLAATTFHWKKCRLDLPG HVALQAC in isoform 2.
VSP_047925
Natural variant18801L → I.
Corresponds to variant rs12204715 [ dbSNP | Ensembl ].
VAR_047794
Natural variant19741A → T.
Corresponds to variant rs12204734 [ dbSNP | Ensembl ].
VAR_047795
Natural variant20601G → D.
Corresponds to variant rs35676466 [ dbSNP | Ensembl ].
VAR_047796
Natural variant22021N → S.
Corresponds to variant rs1534443 [ dbSNP | Ensembl ].
VAR_047797

Experimental info

Sequence conflict2361Q → R in CAA48829. Ref.1

Secondary structure

................................. 3433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: C72CADE8CD666993

FASTA3,433394,466
        10         20         30         40         50         60 
MAKYGEHEAS PDNGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFTDL 

        70         80         90        100        110        120 
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNH 

       130        140        150        160        170        180 
KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT NSEKILLSWV RQTTRPYSQV NVLNFTTSWT 

       190        200        210        220        230        240 
DGLAFNAVLH RHKPDLFSWD KVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK 

       250        260        270        280        290        300 
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEEE AINIQSTAPE EEHESPRAET 

       310        320        330        340        350        360 
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKDQFA THEAFMMELT 

       370        380        390        400        410        420 
AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR WEALRVESMD RQSRLHDVLM 

       430        440        450        460        470        480 
ELQKKQLQQL SAWLTLTEER IQKMETCPLD DDVKSLQKLL EEHKSLQSDL EAEQVKVNSL 

       490        500        510        520        530        540 
THMVVIVDEN SGESATAILE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL 

       550        560        570        580        590        600 
LKAWLTEKEE ALNKVQTSNF KDQKELSVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL 

       610        620        630        640        650        660 
LDNSKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVRVRE 

       670        680        690        700        710        720 
QAITKKSKQE LPPPPPPKKR QIHVDIEAKK KFDAISAELL NWILKWKTAI QTTEIKEYMK 

       730        740        750        760        770        780 
MQDTSEMKKK LKALEKEQRE RIPRADELNQ TGQILVEQMG KEGLPTEEIK NVLEKVSSEW 

       790        800        810        820        830        840 
KNVSQHLEDL ERKIQLQEDI NAYFKQLDEL EKVIKTKEEW VKHTSISESS RQSLPSLKDS 

       850        860        870        880        890        900 
CQRELTNLLG LHPKIEMARA SCSALMSQPS APDFVQRGFD SFLGRYQAVQ EAVEDRQQHL 

       910        920        930        940        950        960 
ENELKGQPGH AYLETLKTLK DVLNDSENKA QVSLNVLNDL AKVEKALQEK KTLDEILENQ 

       970        980        990       1000       1010       1020 
KPALHKLAEE TKALEKNVHP DVEKLYKQEF DDVQGKWNKL KVLVSKDLHL LEEIALTLRA 

      1030       1040       1050       1060       1070       1080 
FEADSTVIEK WMDGVKDFLM KQQAAQGDDA GLQRQLDQCS AFVNEIETIE SSLKNMKEIE 

      1090       1100       1110       1120       1130       1140 
TNLRSGPVAG IKTWVQTRLG DYQTQLEKLS KEIATQKSRL SESQEKAANL KKDLAEMQEW 

      1150       1160       1170       1180       1190       1200 
MTQAEEEYLE RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDNIK LLAAKVPSGG 

      1210       1220       1230       1240       1250       1260 
QELTSELNVV LENYQLLCNR IRGKCHTLEE VWSCWIELLH YLDLETTWLN TLEERMKSTE 

      1270       1280       1290       1300       1310       1320 
VLPEKTDAVN EALESLESVL RHPADNRTQI RELGQTLIDG GILDDIISEK LEAFNSRYED 

      1330       1340       1350       1360       1370       1380 
LSHLAESKQI SLEKQLQVLR ETDQMLQVLQ ESLGELDKQL TTYLTDRIDA FQVPQEAQKI 

      1390       1400       1410       1420       1430       1440 
QAEISAHELT LEELRRNMRS QPLTSPESRT ARGGSQMDVL QRKLREVSTK FQLFQKPANF 

      1450       1460       1470       1480       1490       1500 
EQRMLDCKRV LDGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR 

      1510       1520       1530       1540       1550       1560 
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK KEAASLSEWL 

      1570       1580       1590       1600       1610       1620 
SATETELVQK STSEGLLGDL DTEISWAKNV LKDLEKRKAD LNTITESSAA LQNLIEGSEP 

      1630       1640       1650       1660       1670       1680 
ILEERLCVLN AGWSRVRTWT EDWCNTLMNH QNQLEIFDGN VAHISTWLYQ AEALLDEIEK 

      1690       1700       1710       1720       1730       1740 
KPTSKQEEIV KRLVSELDDA NLQVENVRDQ ALILMNARGS SSRELVEPKL AELNRNFEKV 

      1750       1760       1770       1780       1790       1800 
SQHIKSAKLL IAQEPLYQCL VTTETFETGV PFSDLEKLEN DIENMLKFVE KHLESSDEDE 

      1810       1820       1830       1840       1850       1860 
KMDEESAQIE EVLQRGEEML HQPMEDNKKE KIRLQLLLLH TRYNKIKAIP IQQRKMGQLA 

      1870       1880       1890       1900       1910       1920 
SGIRSSLLPT DYLVEINKIL LCMDDVELSL NVPELNTAIY EDFSFQEDSL KNIKDQLDKL 

      1930       1940       1950       1960       1970       1980 
GEQIAVIHEK QPDVILEASG PEAIQIRDTL TQLNAKWDRI NRMYSDRKGC FDRAMEEWRQ 

      1990       2000       2010       2020       2030       2040 
FHCDLNDLTQ WITEAEELLV DTCAPGGSLD LEKARIHQQE LEVGISSHQP SFAALNRTGD 

      2050       2060       2070       2080       2090       2100 
GIVQKLSQAD GSFLKEKLAG LNQRWDAIVA EVKDRQPRLK GESKQVMKYR HQLDEIICWL 

      2110       2120       2130       2140       2150       2160 
TKAEHAMQKR STTELGENLQ ELRDLTQEME VHAEKLKWLN RTELEMLSDK SLSLPERDKI 

      2170       2180       2190       2200       2210       2220 
SESLRTVNMT WNKICREVPT TLKECIQEPS SVSQTRIAAH PNVQKVVLVS SASDIPVQSH 

      2230       2240       2250       2260       2270       2280 
RTSEISIPAD LDKTITELAD WLVLIDQMLK SNIVTVGDVE EINKTVSRMK ITKADLEQRH 

      2290       2300       2310       2320       2330       2340 
PQLDYVFTLA QNLKNKASSS DMRTAITEKL ERVKNQWDGT QHGVELRQQQ LEDMIIDSLQ 

      2350       2360       2370       2380       2390       2400 
WDDHREETEE LMRKYEARLY ILQQARRDPL TKQISDNQIL LQELGPGDGI VMAFDNVLQK 

      2410       2420       2430       2440       2450       2460 
LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQNALEA EWRTVQASRR DLENFLKWIQ 

      2470       2480       2490       2500       2510       2520 
EAETTVNVLV DASHRENALQ DSILARELKQ QMQDIQAEID AHNDIFKSID GNRQKMVKAL 

      2530       2540       2550       2560       2570       2580 
GNSEEATMLQ HRLDDMNQRW NDLKAKSASI RAHLEASAEK WNRLLMSLEE LIKWLNMKDE 

      2590       2600       2610       2620       2630       2640 
ELKKQMPIGG DVPALQLQYD HCKALRRELK EKEYSVLNAV DQARVFLADQ PIEAPEEPRR 

      2650       2660       2670       2680       2690       2700 
NLQSKTELTP EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM 

      2710       2720       2730       2740       2750       2760 
DDLDADMKEA ESVRNGWKPV GDLLIDSLQD HIEKIMAFRE EIAPINFKVK TVNDLSSQLS 

      2770       2780       2790       2800       2810       2820 
PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR DFGPSSQHFL STSVQLPWQR 

      2830       2840       2850       2860       2870       2880 
SISHNKVPYY INHQTQTTCW DHPKMTELFQ SLADLNNVRF SAYRTAIKIR RLQKALCLDL 

      2890       2900       2910       2920       2930       2940 
LELSTTNEIF KQHKLNQNDQ LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL 

      2950       2960       2970       2980       2990       3000 
NVYDTGRTGK IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ 

      3010       3020       3030       3040       3050       3060 
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFID WMHLEPQSMV WLPVLHRVAA 

      3070       3080       3090       3100       3110       3120 
AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS GRTAKGHKLH YPMVEYCIPT 

      3130       3140       3150       3160       3170       3180 
TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG YLPVQTVLEG DNLETPITLI SMWPEHYDPS 

      3190       3200       3210       3220       3230       3240 
QSPQLFHDDT HSRIEQYATR LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES 

      3250       3260       3270       3280       3290       3300 
PVSQPQSPAQ ILKSVEREER GELERIIADL EEEQRNLQVE YEQLKDQHLR RGLPVGSPPE 

      3310       3320       3330       3340       3350       3360 
SIISPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR QLLEQPESDS 

      3370       3380       3390       3400       3410       3420 
RINGVSPWAS PQHSALSYSL DPDASGPQFH QAAGEDLLAP PHDTSTDLTE VMEQIHSTFP 

      3430 
SCCPNVPSRP QAM 

« Hide

Isoform 2 [UniParc].

Checksum: 9242095AE3CD5F48
Show »

FASTA3,438394,969

References

« Hide 'large scale' references
[1]"Primary structure of dystrophin-related protein."
Tinsley J.M., Blake D.J., Roche A., Fairbrother U., Riss J., Byth B.C., Knight A.E., Kendrick-Jones J., Suthers G.K., Love D.R., Edwards Y.H., Davies K.E.
Nature 360:591-593(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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. expand/collapse author list , 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].
[3]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4; SER-10 AND SER-3297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
[12]"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.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
+Additional computationally mapped references.

Web resources

Wikipedia

Utrophin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69086 mRNA. Translation: CAA48829.1.
AL590704 expand/collapse EMBL AC list , AL024474, AL357149, AL513184, AL513475, AL590488 Genomic DNA. Translation: CAI10894.1.
AL590704, AL024474, AL590488 Genomic DNA. Translation: CAI10897.1.
AL513475 expand/collapse EMBL AC list , AL024474, AL357149, AL513184, AL590488, AL590704 Genomic DNA. Translation: CAI13032.1.
AL590488 expand/collapse EMBL AC list , AL024474, AL357149, AL513184, AL513475, AL590704 Genomic DNA. Translation: CAI16497.1.
AL590488, AL024474, AL590704 Genomic DNA. Translation: CAI16498.1.
AL024474 expand/collapse EMBL AC list , AL357149, AL513184, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI23353.1.
AL024474, AL590488, AL590704 Genomic DNA. Translation: CAI23355.1.
AL357149 expand/collapse EMBL AC list , AL024474, AL513184, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI40388.1.
AL513184 expand/collapse EMBL AC list , AL024474, AL357149, AL513475, AL590488, AL590704 Genomic DNA. Translation: CAI40502.1.
AJ250044 Genomic DNA. Translation: CAB61826.1.
PIRS28381.
RefSeqNP_009055.2. NM_007124.2.
XP_005267187.1. XM_005267130.1.
UniGeneHs.133135.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHDX-ray2.00A/B144-261[»]
1QAGX-ray3.00A/B31-256[»]
ProteinModelPortalP46939.
SMRP46939. Positions 31-255, 308-535, 943-1039, 1095-1120, 2695-2799, 2804-3118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113245. 30 interactions.
DIPDIP-45639N.
DIP-711N.
IntActP46939. 33 interactions.
MINTMINT-109722.
STRING9606.ENSP00000356515.

PTM databases

PhosphoSiteP46939.

Polymorphism databases

DMDM215274104.

Proteomic databases

PaxDbP46939.
PRIDEP46939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367545; ENSP00000356515; ENSG00000152818. [P46939-1]
GeneID7402.
KEGGhsa:7402.
UCSCuc003qkt.3. human. [P46939-1]

Organism-specific databases

CTD7402.
GeneCardsGC06P144654.
HGNCHGNC:12635. UTRN.
HPACAB016348.
HPA018894.
MIM128240. gene.
neXtProtNX_P46939.
PharmGKBPA37260.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000231173.
HOVERGENHBG005495.
InParanoidP46939.
OMALIKWLNM.
OrthoDBEOG7V765N.
PhylomeDBP46939.
TreeFamTF320178.

Enzyme and pathway databases

SignaLinkP46939.

Gene expression databases

ArrayExpressP46939.
BgeeP46939.
CleanExHS_UTRN.
GenevestigatorP46939.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. 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]
PfamPF00307. 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]
PIRSFPIRSF002341. Dystrophin/utrophin. 1 hit.
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 18 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

ChiTaRSUTRN. human.
EvolutionaryTraceP46939.
GeneWikiUtrophin.
GenomeRNAi7402.
NextBio28976.
PROP46939.
SOURCESearch...

Entry information

Entry nameUTRO_HUMAN
AccessionPrimary (citable) accession number: P46939
Secondary accession number(s): Q5SYY1, Q5SZ57, Q9UJ40
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM