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P46939

- UTRO_HUMAN

UniProt

P46939 - UTRO_HUMAN

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Protein

Utrophin

Gene
UTRN, DMDL, DRP1
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-typeAdd
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
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. neuromuscular junction Source: Ensembl
  10. nucleus Source: HPA
  11. plasma membrane Source: HPA
  12. postsynaptic membrane Source: UniProtKB-SubCell
  13. protein complex Source: MGI
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

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. 33 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.

Miscellaneous databases

EvolutionaryTraceiP46939.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 246246Actin-bindingAdd
BLAST
Domaini31 – 135105CH 1Add
BLAST
Domaini150 – 252103CH 2Add
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 – 284534WWAdd
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 20 spectrin repeats.
Contains 1 WW domain.

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.

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

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. VSP_054942Add
BLAST
Alternative sequencei1 – 2323MAKYG…SDIIK → MKFFDFLFIFKILPPYYINF FSS in isoform Up71. VSP_054943Add
BLAST
Alternative sequencei1 – 2222MAKYG…FSDII → MSGLAATTFHWKKCRLDLPG HVALQAC in isoform 2. VSP_047925Add
BLAST
Alternative sequencei24 – 28322809Missing in isoform Up71. VSP_054944Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361Q → R in CAA48829. 1 Publication
Isoform Up71 (identifier: P46939-3)
Sequence conflicti5 – 51D → N no nucleotide entry 1 Publication

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. 33 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

« 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: July 9, 2014
This is version 151 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

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