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Q9NR56

- MBNL1_HUMAN

UniProt

Q9NR56 - MBNL1_HUMAN

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Protein

Muscleblind-like protein 1

Gene

MBNL1

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

Functioni

Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 4129C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri47 – 7327C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri179 – 20729C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri215 – 24127C3H1-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. double-stranded RNA binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: UniProtKB

GO - Biological processi

  1. alternative mRNA splicing, via spliceosome Source: Ensembl
  2. embryonic limb morphogenesis Source: UniProtKB
  3. in utero embryonic development Source: UniProtKB
  4. mRNA splice site selection Source: Ensembl
  5. myoblast differentiation Source: UniProtKB
  6. nervous system development Source: UniProtKB
  7. regulation of alternative mRNA splicing, via spliceosome Source: Ensembl
  8. regulation of RNA splicing Source: UniProtKB
  9. RNA splicing Source: UniProtKB
  10. skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Muscleblind-like protein 1
Alternative name(s):
Triplet-expansion RNA-binding protein
Gene namesi
Name:MBNL1
Synonyms:EXP, KIAA0428, MBNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6923. MBNL1.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmic granule
Note: Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress. Localized in the cytoplasm of multinucleated myotubes. Colocalizes with nuclear foci of retained expanded-repeat transcripts in myotubes from patients affected by myotonic dystrophy.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic stress granule Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias.
Note: The protein represented in this entry may be involved in disease pathogenesis. In muscle cells from patients, MBNL1 is sequestered by DMPK RNAs containing pathogenic CUG triplet repeat expansions. MBNL1 binding is proportional to repeat length consistent with the direct correlation between the length of repeat expansion and disease severity.

Organism-specific databases

MIMi160900. phenotype.
PharmGKBiPA30666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Muscleblind-like protein 1PRO_0000089178Add
BLAST

Proteomic databases

MaxQBiQ9NR56.
PaxDbiQ9NR56.
PeptideAtlasiQ9NR56.
PRIDEiQ9NR56.

PTM databases

PhosphoSiteiQ9NR56.

Expressioni

Tissue specificityi

Highly expressed in cardiac, skeletal muscle and during myoblast differentiation. Weakly expressed in other tissues (at protein level). Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.2 Publications

Gene expression databases

BgeeiQ9NR56.
CleanExiHS_MBNL1.
ExpressionAtlasiQ9NR56. baseline and differential.
GenevestigatoriQ9NR56.

Organism-specific databases

HPAiCAB016398.
HPA035098.

Interactioni

Subunit structurei

Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the interaction in RNA-independent.3 Publications

Protein-protein interaction databases

BioGridi110324. 25 interactions.
IntActiQ9NR56. 16 interactions.
MINTiMINT-3072751.
STRINGi9606.ENSP00000282486.

Structurei

Secondary structure

1
388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143Combined sources
Beta strandi15 – 184Combined sources
Helixi22 – 243Combined sources
Turni31 – 333Combined sources
Beta strandi35 – 373Combined sources
Beta strandi49 – 513Combined sources
Helixi54 – 574Combined sources
Helixi73 – 8210Combined sources
Beta strandi181 – 1844Combined sources
Helixi186 – 1894Combined sources
Turni197 – 1993Combined sources
Beta strandi201 – 2033Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 2204Combined sources
Helixi222 – 2254Combined sources
Beta strandi235 – 2373Combined sources
Helixi241 – 2444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D2NX-ray2.70A9-90[»]
3D2QX-ray1.50A/B/C/D178-246[»]
3D2SX-ray1.70A/B/C/D178-246[»]
ProteinModelPortaliQ9NR56.
SMRiQ9NR56. Positions 11-86, 178-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NR56.

Family & Domainsi

Sequence similaritiesi

Belongs to the muscleblind family.Curated
Contains 4 C3H1-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 4129C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri47 – 7327C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri179 – 20729C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri215 – 24127C3H1-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG241142.
GeneTreeiENSGT00390000001586.
HOGENOMiHOG000230928.
HOVERGENiHBG006999.
InParanoidiQ9NR56.
KOiK14943.
OMAiKVPMVHG.
OrthoDBiEOG7BKCXK.
PhylomeDBiQ9NR56.
TreeFamiTF321931.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 4 hits.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 4 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NR56-1) [UniParc]FASTAAdd to Basket

Also known as: EXP42

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
MAVSVTPIRD TKWLTLEVCR EFQRGTCSRP DTECKFAHPS KSCQVENGRV
60 70 80 90 100
IACFDSLKGR CSRENCKYLH PPPHLKTQLE INGRNNLIQQ KNMAMLAQQM
110 120 130 140 150
QLANAMMPGA PLQPVPMFSV APSLATNASA AAFNPYLGPV SPSLVPAEIL
160 170 180 190 200
PTAPMLVTGN PGVPVPAAAA AAAQKLMRTD RLEVCREYQR GNCNRGENDC
210 220 230 240 250
RFAHPADSTM IDTNDNTVTV CMDYIKGRCS REKCKYFHPP AHLQAKIKAA
260 270 280 290 300
QYQVNQAAAA QAAATAAAMT QSAVKSLKRP LEATFDLGIP QAVLPPLPKR
310 320 330 340 350
PALEKTNGAT AVFNTGIFQY QQALANMQLQ QHTAFLPPVP MVHGATPATV
360 370 380
SAATTSATSV PFAATATANQ IPIISAEHLT SHKYVTQM
Length:388
Mass (Da):41,817
Last modified:November 16, 2001 - v2
Checksum:i118D256A81A86695
GO
Isoform 2 (identifier: Q9NR56-2) [UniParc]FASTAAdd to Basket

Also known as: EXP40

The sequence of this isoform differs from the canonical sequence as follows:
     270-287: Missing.

Show »
Length:370
Mass (Da):39,831
Checksum:iABF12CBCCDE1FF5C
GO
Isoform 3 (identifier: Q9NR56-3) [UniParc]FASTAAdd to Basket

Also known as: EXP35

The sequence of this isoform differs from the canonical sequence as follows:
     116-183: Missing.
     270-287: Missing.

Show »
Length:302
Mass (Da):33,050
Checksum:i5D1D1AE2D6219425
GO
Isoform 4 (identifier: Q9NR56-4) [UniParc]FASTAAdd to Basket

Also known as: EXP36

The sequence of this isoform differs from the canonical sequence as follows:
     116-183: Missing.
     270-287: Missing.
     338-338: P → PGSILCMTPATSV

Show »
Length:314
Mass (Da):34,211
Checksum:i9535C699B3BBE210
GO
Isoform 5 (identifier: Q9NR56-5) [UniParc]FASTAAdd to Basket

Also known as: EXP41

The sequence of this isoform differs from the canonical sequence as follows:
     270-287: Missing.
     338-338: P → PGSILCMTPATSV

Show »
Length:382
Mass (Da):40,992
Checksum:iBE7176F8F2928ACF
GO
Isoform 6 (identifier: Q9NR56-6) [UniParc]FASTAAdd to Basket

Also known as: EXP41S

The sequence of this isoform differs from the canonical sequence as follows:
     270-287: Missing.
     338-338: P → PGSILCMTPATSV
     339-388: VPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM → DTHNICRTSD

Show »
Length:342
Mass (Da):37,074
Checksum:i179E9FA2F1A02FC4
GO
Isoform 7 (identifier: Q9NR56-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-370: TQSAVKSLKR...PFAATATANQ → FPWCTVLRQP...TSCPAAAGKM

Show »
Length:340
Mass (Da):36,992
Checksum:i9A605A3824FDA8FA
GO

Sequence cautioni

The sequence BAA24858.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 7 (identifier: Q9NR56-7)
Sequence conflicti317 – 3171A → AA in AAP30726. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 18368Missing in isoform 3 and isoform 4. 1 PublicationVSP_006429Add
BLAST
Alternative sequencei270 – 370101TQSAV…ATANQ → FPWCTVLRQPLCPQQQHLPQ VFPSLQQPQPTSPILDASTL LGATSCPAAAGKM in isoform 7. 1 PublicationVSP_044903Add
BLAST
Alternative sequencei270 – 28718Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6. 6 PublicationsVSP_006430Add
BLAST
Alternative sequencei338 – 3381P → PGSILCMTPATSV in isoform 4, isoform 5 and isoform 6. 5 PublicationsVSP_043799
Alternative sequencei339 – 38850VPMVH…YVTQM → DTHNICRTSD in isoform 6. 1 PublicationVSP_043800Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13829 mRNA. Translation: CAA74155.1.
AB007888 mRNA. Translation: BAA24858.2. Different initiation.
AF255334 mRNA. Translation: AAF76138.1.
AF395876 mRNA. Translation: AAK82889.1.
AF401998 mRNA. Translation: AAK94915.1.
AJ308400 mRNA. Translation: CAC83727.1.
AF497718 mRNA. Translation: AAP30726.1.
AF497719 mRNA. Translation: AAP30727.1.
AC026347 Genomic DNA. No translation available.
AC106722 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78775.1.
BC043493 mRNA. Translation: AAH43493.1.
CCDSiCCDS3163.1. [Q9NR56-5]
CCDS3164.1. [Q9NR56-2]
CCDS3165.1. [Q9NR56-1]
CCDS3166.1. [Q9NR56-4]
CCDS3167.1. [Q9NR56-7]
CCDS3168.1. [Q9NR56-6]
CCDS54656.1. [Q9NR56-3]
RefSeqiNP_066368.2. NM_021038.3. [Q9NR56-5]
NP_997175.1. NM_207292.1. [Q9NR56-2]
NP_997176.1. NM_207293.1. [Q9NR56-1]
NP_997177.1. NM_207294.1. [Q9NR56-3]
NP_997178.1. NM_207295.1. [Q9NR56-4]
NP_997179.1. NM_207296.1. [Q9NR56-7]
NP_997180.1. NM_207297.1. [Q9NR56-6]
XP_005247523.1. XM_005247466.2. [Q9NR56-1]
XP_005247528.1. XM_005247471.2. [Q9NR56-6]
UniGeneiHs.201858.
Hs.725347.

Genome annotation databases

EnsembliENST00000282486; ENSP00000282486; ENSG00000152601. [Q9NR56-1]
ENST00000324196; ENSP00000319374; ENSG00000152601. [Q9NR56-7]
ENST00000324210; ENSP00000319429; ENSG00000152601. [Q9NR56-5]
ENST00000355460; ENSP00000347637; ENSG00000152601. [Q9NR56-2]
ENST00000357472; ENSP00000350064; ENSG00000152601. [Q9NR56-6]
ENST00000463374; ENSP00000418108; ENSG00000152601. [Q9NR56-1]
ENST00000465907; ENSP00000417630; ENSG00000152601. [Q9NR56-4]
ENST00000485509; ENSP00000418876; ENSG00000152601. [Q9NR56-7]
ENST00000485910; ENSP00000418427; ENSG00000152601. [Q9NR56-3]
ENST00000492948; ENSP00000420103; ENSG00000152601. [Q9NR56-6]
ENST00000545754; ENSP00000437491; ENSG00000152601. [Q9NR56-4]
GeneIDi4154.
KEGGihsa:4154.
UCSCiuc003ezh.3. human. [Q9NR56-5]
uc003ezi.3. human. [Q9NR56-2]
uc003ezl.3. human. [Q9NR56-6]
uc003ezm.3. human. [Q9NR56-1]
uc003ezn.3. human. [Q9NR56-4]
uc003ezo.3. human. [Q9NR56-3]
uc003ezp.3. human.

Polymorphism databases

DMDMi17369313.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13829 mRNA. Translation: CAA74155.1 .
AB007888 mRNA. Translation: BAA24858.2 . Different initiation.
AF255334 mRNA. Translation: AAF76138.1 .
AF395876 mRNA. Translation: AAK82889.1 .
AF401998 mRNA. Translation: AAK94915.1 .
AJ308400 mRNA. Translation: CAC83727.1 .
AF497718 mRNA. Translation: AAP30726.1 .
AF497719 mRNA. Translation: AAP30727.1 .
AC026347 Genomic DNA. No translation available.
AC106722 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78775.1 .
BC043493 mRNA. Translation: AAH43493.1 .
CCDSi CCDS3163.1. [Q9NR56-5 ]
CCDS3164.1. [Q9NR56-2 ]
CCDS3165.1. [Q9NR56-1 ]
CCDS3166.1. [Q9NR56-4 ]
CCDS3167.1. [Q9NR56-7 ]
CCDS3168.1. [Q9NR56-6 ]
CCDS54656.1. [Q9NR56-3 ]
RefSeqi NP_066368.2. NM_021038.3. [Q9NR56-5 ]
NP_997175.1. NM_207292.1. [Q9NR56-2 ]
NP_997176.1. NM_207293.1. [Q9NR56-1 ]
NP_997177.1. NM_207294.1. [Q9NR56-3 ]
NP_997178.1. NM_207295.1. [Q9NR56-4 ]
NP_997179.1. NM_207296.1. [Q9NR56-7 ]
NP_997180.1. NM_207297.1. [Q9NR56-6 ]
XP_005247523.1. XM_005247466.2. [Q9NR56-1 ]
XP_005247528.1. XM_005247471.2. [Q9NR56-6 ]
UniGenei Hs.201858.
Hs.725347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D2N X-ray 2.70 A 9-90 [» ]
3D2Q X-ray 1.50 A/B/C/D 178-246 [» ]
3D2S X-ray 1.70 A/B/C/D 178-246 [» ]
ProteinModelPortali Q9NR56.
SMRi Q9NR56. Positions 11-86, 178-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110324. 25 interactions.
IntActi Q9NR56. 16 interactions.
MINTi MINT-3072751.
STRINGi 9606.ENSP00000282486.

Chemistry

ChEMBLi CHEMBL1293317.

PTM databases

PhosphoSitei Q9NR56.

Polymorphism databases

DMDMi 17369313.

Proteomic databases

MaxQBi Q9NR56.
PaxDbi Q9NR56.
PeptideAtlasi Q9NR56.
PRIDEi Q9NR56.

Protocols and materials databases

DNASUi 4154.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282486 ; ENSP00000282486 ; ENSG00000152601 . [Q9NR56-1 ]
ENST00000324196 ; ENSP00000319374 ; ENSG00000152601 . [Q9NR56-7 ]
ENST00000324210 ; ENSP00000319429 ; ENSG00000152601 . [Q9NR56-5 ]
ENST00000355460 ; ENSP00000347637 ; ENSG00000152601 . [Q9NR56-2 ]
ENST00000357472 ; ENSP00000350064 ; ENSG00000152601 . [Q9NR56-6 ]
ENST00000463374 ; ENSP00000418108 ; ENSG00000152601 . [Q9NR56-1 ]
ENST00000465907 ; ENSP00000417630 ; ENSG00000152601 . [Q9NR56-4 ]
ENST00000485509 ; ENSP00000418876 ; ENSG00000152601 . [Q9NR56-7 ]
ENST00000485910 ; ENSP00000418427 ; ENSG00000152601 . [Q9NR56-3 ]
ENST00000492948 ; ENSP00000420103 ; ENSG00000152601 . [Q9NR56-6 ]
ENST00000545754 ; ENSP00000437491 ; ENSG00000152601 . [Q9NR56-4 ]
GeneIDi 4154.
KEGGi hsa:4154.
UCSCi uc003ezh.3. human. [Q9NR56-5 ]
uc003ezi.3. human. [Q9NR56-2 ]
uc003ezl.3. human. [Q9NR56-6 ]
uc003ezm.3. human. [Q9NR56-1 ]
uc003ezn.3. human. [Q9NR56-4 ]
uc003ezo.3. human. [Q9NR56-3 ]
uc003ezp.3. human.

Organism-specific databases

CTDi 4154.
GeneCardsi GC03P151961.
HGNCi HGNC:6923. MBNL1.
HPAi CAB016398.
HPA035098.
MIMi 160900. phenotype.
606516. gene.
neXtProti NX_Q9NR56.
PharmGKBi PA30666.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241142.
GeneTreei ENSGT00390000001586.
HOGENOMi HOG000230928.
HOVERGENi HBG006999.
InParanoidi Q9NR56.
KOi K14943.
OMAi KVPMVHG.
OrthoDBi EOG7BKCXK.
PhylomeDBi Q9NR56.
TreeFami TF321931.

Miscellaneous databases

ChiTaRSi MBNL1. human.
EvolutionaryTracei Q9NR56.
GeneWikii MBNL1.
GenomeRNAii 4154.
NextBioi 16346.
PROi Q9NR56.
SOURCEi Search...

Gene expression databases

Bgeei Q9NR56.
CleanExi HS_MBNL1.
ExpressionAtlasi Q9NR56. baseline and differential.
Genevestigatori Q9NR56.

Family and domain databases

Gene3Di 4.10.1000.10. 1 hit.
InterProi IPR000571. Znf_CCCH.
[Graphical view ]
Pfami PF00642. zf-CCCH. 1 hit.
[Graphical view ]
SMARTi SM00356. ZnF_C3H1. 4 hits.
[Graphical view ]
PROSITEi PS50103. ZF_C3H1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Borsani G., Barbieri A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy."
    Miller J.W., Urbinati C.R., Teng-Umnuay P., Stenberg M.G., Byrne B.J., Thornton C.A., Swanson M.S.
    EMBO J. 19:4439-4448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, ROLE IN MYOTONIC DYSTROPHY, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "Muscleblind localizes to nuclear foci of aberrant RNA in myotonic dystrophy types 1 and 2."
    Mankodi A., Urbinati C.R., Yuan Q.P., Moxley R.T., Sansone V., Krym M., Henderson D., Schalling M., Swanson M.S., Thornton C.A.
    Hum. Mol. Genet. 10:2165-2170(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
  5. "Study of the role of the MBNL gene in the origin myotonic dystrophies in humans."
    Pascual M., Terol J., Perez-Alonso M.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Blood.
  6. "Direct evidence that EXP/muscleblind interacts with CCUG tetranucleotide repeats."
    Kino Y., Ishiura S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7).
    Tissue: Muscle.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Testis.
  10. "Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells."
    Fardaei M., Rogers M.T., Thorpe H.M., Larkin K., Hamshere M.G., Harper P.S., Brook J.D.
    Hum. Mol. Genet. 11:805-814(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. Cited for: FUNCTION, RNA-BINDING.
  12. "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing."
    Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.
    EMBO J. 25:4271-4283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HNRNPH1, RNA-BINDING.
  13. "MBNL1 associates with YB-1 in cytoplasmic stress granules."
    Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.
    J. Neurosci. Res. 86:1994-2002(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDX1 AND YBX1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing."
    Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1."
    Teplova M., Patel D.J.
    Nat. Struct. Mol. Biol. 15:1343-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 9-90 IN COMPLEX WITH ZINC IONS AND 178-246 IN COMPLEX WITH ZINC IONS AND RNA, RNA-BINDING.

Entry informationi

Entry nameiMBNL1_HUMAN
AccessioniPrimary (citable) accession number: Q9NR56
Secondary accession number(s): E9PBW7
, O43311, O43797, Q86UV8, Q86UV9, Q96P92, Q96RE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: November 26, 2014
This is version 120 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3