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Q9NR56 (MBNL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Muscleblind-like protein 1
Alternative name(s):
Triplet-expansion RNA-binding protein
Gene names
Name:MBNL1
Synonyms:EXP, KIAA0428, MBNL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the interaction in RNA-independent. Ref.12 Ref.13

Subcellular location

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. Ref.3 Ref.4 Ref.10 Ref.13

Tissue specificity

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. Ref.3 Ref.10

Involvement in disease

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.

Sequence similarities

Belongs to the muscleblind family.

Contains 4 C3H1-type zinc fingers.

Sequence caution

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

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from direct assay Ref.13. Source: UniProtKB

alternative mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA splice site selection

Inferred from electronic annotation. Source: Ensembl

myoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of RNA splicing

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay Ref.3Ref.11. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay Ref.3. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NR56-1)

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.
Isoform 2 (identifier: Q9NR56-2)

Also known as: EXP40;

The sequence of this isoform differs from the canonical sequence as follows:
     270-287: Missing.
Isoform 3 (identifier: Q9NR56-3)

Also known as: EXP35;

The sequence of this isoform differs from the canonical sequence as follows:
     116-183: Missing.
     270-287: Missing.
Isoform 4 (identifier: Q9NR56-4)

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
Isoform 5 (identifier: Q9NR56-5)

Also known as: EXP41;

The sequence of this isoform differs from the canonical sequence as follows:
     270-287: Missing.
     338-338: P → PGSILCMTPATSV
Isoform 6 (identifier: Q9NR56-6)

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
Isoform 7 (identifier: Q9NR56-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Muscleblind-like protein 1
PRO_0000089178

Regions

Zinc finger13 – 4129C3H1-type 1
Zinc finger47 – 7327C3H1-type 2
Zinc finger179 – 20729C3H1-type 3
Zinc finger215 – 24127C3H1-type 4

Natural variations

Alternative sequence116 – 18368Missing in isoform 3 and isoform 4.
VSP_006429
Alternative sequence270 – 370101TQSAV…ATANQ → FPWCTVLRQPLCPQQQHLPQ VFPSLQQPQPTSPILDASTL LGATSCPAAAGKM in isoform 7.
VSP_044903
Alternative sequence270 – 28718Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_006430
Alternative sequence3381P → PGSILCMTPATSV in isoform 4, isoform 5 and isoform 6.
VSP_043799
Alternative sequence339 – 38850VPMVH…YVTQM → DTHNICRTSD in isoform 6.
VSP_043800

Experimental info

Isoform 7:
Sequence conflict3171A → AA in AAP30726. Ref.6

Secondary structure

................................. 388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EXP42) [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: 118D256A81A86695

FASTA38841,817
        10         20         30         40         50         60 
MAVSVTPIRD TKWLTLEVCR EFQRGTCSRP DTECKFAHPS KSCQVENGRV IACFDSLKGR 

        70         80         90        100        110        120 
CSRENCKYLH PPPHLKTQLE INGRNNLIQQ KNMAMLAQQM QLANAMMPGA PLQPVPMFSV 

       130        140        150        160        170        180 
APSLATNASA AAFNPYLGPV SPSLVPAEIL PTAPMLVTGN PGVPVPAAAA AAAQKLMRTD 

       190        200        210        220        230        240 
RLEVCREYQR GNCNRGENDC RFAHPADSTM IDTNDNTVTV CMDYIKGRCS REKCKYFHPP 

       250        260        270        280        290        300 
AHLQAKIKAA QYQVNQAAAA QAAATAAAMT QSAVKSLKRP LEATFDLGIP QAVLPPLPKR 

       310        320        330        340        350        360 
PALEKTNGAT AVFNTGIFQY QQALANMQLQ QHTAFLPPVP MVHGATPATV SAATTSATSV 

       370        380 
PFAATATANQ IPIISAEHLT SHKYVTQM 

« Hide

Isoform 2 (EXP40) [UniParc].

Checksum: ABF12CBCCDE1FF5C
Show »

FASTA37039,831
Isoform 3 (EXP35) [UniParc].

Checksum: 5D1D1AE2D6219425
Show »

FASTA30233,050
Isoform 4 (EXP36) [UniParc].

Checksum: 9535C699B3BBE210
Show »

FASTA31434,211
Isoform 5 (EXP41) [UniParc].

Checksum: BE7176F8F2928ACF
Show »

FASTA38240,992
Isoform 6 (EXP41S) [UniParc].

Checksum: 179E9FA2F1A02FC4
Show »

FASTA34237,074
Isoform 7 [UniParc].

Checksum: 9A605A3824FDA8FA
Show »

FASTA34036,992

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Muscleblind proteins regulate alternative splicing."
Ho T.H., Charlet-B N., Poulos M.G., Singh G., Swanson M.S., Cooper T.A.
EMBO J. 23:3103-3112(2004) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_066368.2. NM_021038.3.
NP_997175.1. NM_207292.1.
NP_997176.1. NM_207293.1.
NP_997177.1. NM_207294.1.
NP_997178.1. NM_207295.1.
NP_997179.1. NM_207296.1.
NP_997180.1. NM_207297.1.
XP_005247523.1. XM_005247466.2.
XP_005247528.1. XM_005247471.2.
UniGeneHs.201858.
Hs.725347.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D2NX-ray2.70A9-90[»]
3D2QX-ray1.50A/B/C/D178-246[»]
3D2SX-ray1.70A/B/C/D178-246[»]
ProteinModelPortalQ9NR56.
SMRQ9NR56. Positions 11-86, 178-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110324. 21 interactions.
IntActQ9NR56. 16 interactions.
MINTMINT-3072751.
STRING9606.ENSP00000282486.

Chemistry

ChEMBLCHEMBL1293317.

PTM databases

PhosphoSiteQ9NR56.

Polymorphism databases

DMDM17369313.

Proteomic databases

PaxDbQ9NR56.
PeptideAtlasQ9NR56.
PRIDEQ9NR56.

Protocols and materials databases

DNASU4154.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282486; ENSP00000282486; ENSG00000152601. [Q9NR56-1]
ENST00000282488; ENSP00000282488; ENSG00000152601. [Q9NR56-3]
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]
GeneID4154.
KEGGhsa:4154.
UCSCuc003ezh.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

CTD4154.
GeneCardsGC03P151961.
HGNCHGNC:6923. MBNL1.
HPACAB016398.
HPA035098.
MIM160900. phenotype.
606516. gene.
neXtProtNX_Q9NR56.
PharmGKBPA30666.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241142.
HOGENOMHOG000230928.
HOVERGENHBG006999.
InParanoidQ9NR56.
KOK14943.
OMAYQRGNCT.
OrthoDBEOG7BKCXK.
PhylomeDBQ9NR56.
TreeFamTF321931.

Gene expression databases

ArrayExpressQ9NR56.
BgeeQ9NR56.
CleanExHS_MBNL1.
GenevestigatorQ9NR56.

Family and domain databases

Gene3D4.10.1000.10. 1 hit.
InterProIPR000571. Znf_CCCH.
[Graphical view]
PfamPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTSM00356. ZnF_C3H1. 4 hits.
[Graphical view]
PROSITEPS50103. ZF_C3H1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMBNL1. human.
EvolutionaryTraceQ9NR56.
GeneWikiMBNL1.
GenomeRNAi4154.
NextBio16346.
PROQ9NR56.
SOURCESearch...

Entry information

Entry nameMBNL1_HUMAN
AccessionPrimary (citable) accession number: Q9NR56
Secondary accession number(s): E9PBW7 expand/collapse secondary AC list , O43311, O43797, Q86UV8, Q86UV9, Q96P92, Q96RE3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 114 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM