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P46939

- UTRO_HUMAN

UniProt

P46939 - UTRO_HUMAN

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Protein

Utrophin

Gene

UTRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase binding Source: BHF-UCL
  5. vinculin binding Source: BHF-UCL
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. aging Source: Ensembl
  2. muscle cell differentiation Source: Ensembl
  3. muscle contraction Source: ProtInc
  4. muscle organ development Source: ProtInc
  5. neuron projection morphogenesis Source: Ensembl
  6. positive regulation of cell-matrix adhesion Source: UniProtKB
  7. positive regulation of neuron differentiation Source: Ensembl
  8. positive regulation of neuron projection development Source: Ensembl
  9. regulation of cellular response to growth factor stimulus Source: Ensembl
  10. regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
Complete GO annotation...

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. membrane raft Source: Ensembl
  10. myofibril Source: Ensembl
  11. neuromuscular junction Source: Ensembl
  12. nucleus Source: HPA
  13. plasma membrane Source: HPA
  14. postsynaptic membrane Source: UniProtKB-KW
  15. protein complex Source: MGI
  16. sarcolemma Source: Ensembl
Complete GO annotation...

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

BgeeiP46939.
CleanExiHS_UTRN.
ExpressionAtlasiP46939. baseline and differential.
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. 32 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 – 4615Combined sources
Turni47 – 493Combined sources
Turni56 – 627Combined sources
Helixi64 – 7411Combined sources
Helixi86 – 10217Combined sources
Helixi112 – 1176Combined sources
Helixi120 – 13415Combined sources
Helixi136 – 14914Combined sources
Helixi151 – 16414Combined sources
Beta strandi174 – 1763Combined sources
Helixi177 – 1793Combined sources
Helixi183 – 19210Combined sources
Helixi194 – 1963Combined sources
Helixi199 – 2046Combined sources
Helixi207 – 22216Combined sources
Helixi230 – 2345Combined sources
Helixi240 – 25314Combined sources

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.
GeneTreeiENSGT00760000119237.
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

        10         20         30         40         50
MAKYGEHEAS PDNGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK
60 70 80 90 100
PPINDMFTDL KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL
110 120 130 140 150
HQNNVELVNI GGTDIVDGNH KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT
160 170 180 190 200
NSEKILLSWV RQTTRPYSQV NVLNFTTSWT DGLAFNAVLH RHKPDLFSWD
210 220 230 240 250
KVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK KSIIMYLTSL
260 270 280 290 300
FEVLPQQVTI DAIREVETLP RKYKKECEEE AINIQSTAPE EEHESPRAET
310 320 330 340 350
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKDQFA
360 370 380 390 400
THEAFMMELT AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR
410 420 430 440 450
WEALRVESMD RQSRLHDVLM ELQKKQLQQL SAWLTLTEER IQKMETCPLD
460 470 480 490 500
DDVKSLQKLL EEHKSLQSDL EAEQVKVNSL THMVVIVDEN SGESATAILE
510 520 530 540 550
DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL LKAWLTEKEE
560 570 580 590 600
ALNKVQTSNF KDQKELSVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL
610 620 630 640 650
LDNSKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK
660 670 680 690 700
DLLETVRVRE QAITKKSKQE LPPPPPPKKR QIHVDIEAKK KFDAISAELL
710 720 730 740 750
NWILKWKTAI QTTEIKEYMK MQDTSEMKKK LKALEKEQRE RIPRADELNQ
760 770 780 790 800
TGQILVEQMG KEGLPTEEIK NVLEKVSSEW KNVSQHLEDL ERKIQLQEDI
810 820 830 840 850
NAYFKQLDEL EKVIKTKEEW VKHTSISESS RQSLPSLKDS CQRELTNLLG
860 870 880 890 900
LHPKIEMARA SCSALMSQPS APDFVQRGFD SFLGRYQAVQ EAVEDRQQHL
910 920 930 940 950
ENELKGQPGH AYLETLKTLK DVLNDSENKA QVSLNVLNDL AKVEKALQEK
960 970 980 990 1000
KTLDEILENQ KPALHKLAEE TKALEKNVHP DVEKLYKQEF DDVQGKWNKL
1010 1020 1030 1040 1050
KVLVSKDLHL LEEIALTLRA FEADSTVIEK WMDGVKDFLM KQQAAQGDDA
1060 1070 1080 1090 1100
GLQRQLDQCS AFVNEIETIE SSLKNMKEIE TNLRSGPVAG IKTWVQTRLG
1110 1120 1130 1140 1150
DYQTQLEKLS KEIATQKSRL SESQEKAANL KKDLAEMQEW MTQAEEEYLE
1160 1170 1180 1190 1200
RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDNIK LLAAKVPSGG
1210 1220 1230 1240 1250
QELTSELNVV LENYQLLCNR IRGKCHTLEE VWSCWIELLH YLDLETTWLN
1260 1270 1280 1290 1300
TLEERMKSTE VLPEKTDAVN EALESLESVL RHPADNRTQI RELGQTLIDG
1310 1320 1330 1340 1350
GILDDIISEK LEAFNSRYED LSHLAESKQI SLEKQLQVLR ETDQMLQVLQ
1360 1370 1380 1390 1400
ESLGELDKQL TTYLTDRIDA FQVPQEAQKI QAEISAHELT LEELRRNMRS
1410 1420 1430 1440 1450
QPLTSPESRT ARGGSQMDVL QRKLREVSTK FQLFQKPANF EQRMLDCKRV
1460 1470 1480 1490 1500
LDGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR
1510 1520 1530 1540 1550
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK
1560 1570 1580 1590 1600
KEAASLSEWL SATETELVQK STSEGLLGDL DTEISWAKNV LKDLEKRKAD
1610 1620 1630 1640 1650
LNTITESSAA LQNLIEGSEP ILEERLCVLN AGWSRVRTWT EDWCNTLMNH
1660 1670 1680 1690 1700
QNQLEIFDGN VAHISTWLYQ AEALLDEIEK KPTSKQEEIV KRLVSELDDA
1710 1720 1730 1740 1750
NLQVENVRDQ ALILMNARGS SSRELVEPKL AELNRNFEKV SQHIKSAKLL
1760 1770 1780 1790 1800
IAQEPLYQCL VTTETFETGV PFSDLEKLEN DIENMLKFVE KHLESSDEDE
1810 1820 1830 1840 1850
KMDEESAQIE EVLQRGEEML HQPMEDNKKE KIRLQLLLLH TRYNKIKAIP
1860 1870 1880 1890 1900
IQQRKMGQLA SGIRSSLLPT DYLVEINKIL LCMDDVELSL NVPELNTAIY
1910 1920 1930 1940 1950
EDFSFQEDSL KNIKDQLDKL GEQIAVIHEK QPDVILEASG PEAIQIRDTL
1960 1970 1980 1990 2000
TQLNAKWDRI NRMYSDRKGC FDRAMEEWRQ FHCDLNDLTQ WITEAEELLV
2010 2020 2030 2040 2050
DTCAPGGSLD LEKARIHQQE LEVGISSHQP SFAALNRTGD GIVQKLSQAD
2060 2070 2080 2090 2100
GSFLKEKLAG LNQRWDAIVA EVKDRQPRLK GESKQVMKYR HQLDEIICWL
2110 2120 2130 2140 2150
TKAEHAMQKR STTELGENLQ ELRDLTQEME VHAEKLKWLN RTELEMLSDK
2160 2170 2180 2190 2200
SLSLPERDKI SESLRTVNMT WNKICREVPT TLKECIQEPS SVSQTRIAAH
2210 2220 2230 2240 2250
PNVQKVVLVS SASDIPVQSH RTSEISIPAD LDKTITELAD WLVLIDQMLK
2260 2270 2280 2290 2300
SNIVTVGDVE EINKTVSRMK ITKADLEQRH PQLDYVFTLA QNLKNKASSS
2310 2320 2330 2340 2350
DMRTAITEKL ERVKNQWDGT QHGVELRQQQ LEDMIIDSLQ WDDHREETEE
2360 2370 2380 2390 2400
LMRKYEARLY ILQQARRDPL TKQISDNQIL LQELGPGDGI VMAFDNVLQK
2410 2420 2430 2440 2450
LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQNALEA EWRTVQASRR
2460 2470 2480 2490 2500
DLENFLKWIQ EAETTVNVLV DASHRENALQ DSILARELKQ QMQDIQAEID
2510 2520 2530 2540 2550
AHNDIFKSID GNRQKMVKAL GNSEEATMLQ HRLDDMNQRW NDLKAKSASI
2560 2570 2580 2590 2600
RAHLEASAEK WNRLLMSLEE LIKWLNMKDE ELKKQMPIGG DVPALQLQYD
2610 2620 2630 2640 2650
HCKALRRELK EKEYSVLNAV DQARVFLADQ PIEAPEEPRR NLQSKTELTP
2660 2670 2680 2690 2700
EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM
2710 2720 2730 2740 2750
DDLDADMKEA ESVRNGWKPV GDLLIDSLQD HIEKIMAFRE EIAPINFKVK
2760 2770 2780 2790 2800
TVNDLSSQLS PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR
2810 2820 2830 2840 2850
DFGPSSQHFL STSVQLPWQR SISHNKVPYY INHQTQTTCW DHPKMTELFQ
2860 2870 2880 2890 2900
SLADLNNVRF SAYRTAIKIR RLQKALCLDL LELSTTNEIF KQHKLNQNDQ
2910 2920 2930 2940 2950
LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL NVYDTGRTGK
2960 2970 2980 2990 3000
IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ
3010 3020 3030 3040 3050
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFID WMHLEPQSMV
3060 3070 3080 3090 3100
WLPVLHRVAA AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS
3110 3120 3130 3140 3150
GRTAKGHKLH YPMVEYCIPT TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG
3160 3170 3180 3190 3200
YLPVQTVLEG DNLETPITLI SMWPEHYDPS QSPQLFHDDT HSRIEQYATR
3210 3220 3230 3240 3250
LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES PVSQPQSPAQ
3260 3270 3280 3290 3300
ILKSVEREER GELERIIADL EEEQRNLQVE YEQLKDQHLR RGLPVGSPPE
3310 3320 3330 3340 3350
SIISPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR
3360 3370 3380 3390 3400
QLLEQPESDS RINGVSPWAS PQHSALSYSL DPDASGPQFH QAAGEDLLAP
3410 3420 3430
PHDTSTDLTE VMEQIHSTFP SCCPNVPSRP QAM
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. 32 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.
GeneTreei ENSGT00760000119237.
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

Bgeei P46939.
CleanExi HS_UTRN.
ExpressionAtlasi P46939. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 153 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