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O70585 (DTNB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystrobrevin beta

Short name=DTN-B
Short name=mDTN-B
Alternative name(s):
Beta-dystrobrevin
Gene names
Name:Dtnb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Interacts with dystrophin short form DP71 and syntrophins SNTG1 and SNTG2 By similarity. Binds dystrobrevin binding protein 1. Ref.6

Subcellular location

Cytoplasm.

Tissue specificity

Expressed mainly in brain, kidney, liver and lung. In brain expressed in neurons of the cortex and hippocampus.

Domain

The coiled coil domain may mediate the interaction with dystrophin.

Sequence similarities

Belongs to the dystrophin family. Dystrobrevin subfamily.

Contains 1 ZZ-type zinc finger.

Sequence caution

The sequence CAA75752.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA75752.1 differs from that shown. Reason: Frameshift at position 621.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

synapse

Inferred from direct assay PubMed 10995443. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.6PubMed 12923531. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kif5aP331754EBI-349714,EBI-349710

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O70585-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O70585-2)

The sequence of this isoform differs from the canonical sequence as follows:
     518-518: K → KEEEQKQA
     603-608: AEAEEQ → EVTPVS
     609-659: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 659659Dystrobrevin beta
PRO_0000086879

Regions

Zinc finger237 – 28448ZZ-type
Region369 – 41850Syntrophin-binding region
Coiled coil429 – 51991 Potential

Natural variations

Alternative sequence5181K → KEEEQKQA in isoform 2.
VSP_004227
Alternative sequence603 – 6086AEAEEQ → EVTPVS in isoform 2.
VSP_004228
Alternative sequence609 – 65951Missing in isoform 2.
VSP_004229

Experimental info

Sequence conflict4121L → P in CAA75752. Ref.1
Sequence conflict4651S → F in CAA05796. Ref.2
Sequence conflict4651S → F in CAA09038. Ref.3

Sequences

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

Last modified June 28, 2011. Version 3.
Checksum: 27AB3141A65797A8

FASTA65974,399
        10         20         30         40         50         60 
MIEEGGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE 

        70         80         90        100        110        120 
AFRDNGLNTL DHSTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMVAAYD 

       130        140        150        160        170        180 
SEGRGKLTVF SVKAMLATMC GGKMLDKLRY IFSQMSDSNG LMMFGKLDQF LKEALKLPTA 

       190        200        210        220        230        240 
VFEGPSFGYT EHAVRTCFPQ QKKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP 

       250        260        270        280        290        300 
VECSYCHCES MMGFRYRCQQ CHNYQLCQNC FWRGHASGAH SNQHQMKEHS SWKSPAKKLS 

       310        320        330        340        350        360 
HAISKSLGCV PSREPPHPVF PEQPEKPLDL AHLVPPRPLT NMNDTVVSHM SSGVPTPTKR 

       370        380        390        400        410        420 
LQYSQDMPNL LADEHALIAS YVARLQHCTR VLDSPSRLDE EHRLIARYAA RLAAEAGNMT 

       430        440        450        460        470        480 
RPPTDASFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPMLLA 

       490        500        510        520        530        540 
ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EGLMKLLKAQ ATGSPHTSPT HGGGRPMPMP 

       550        560        570        580        590        600 
VRSTSAGSTP THGPQDSLSG VGGDVQEAFA QGTRRNLRND LLVAADSITN TMSSLVKELH 

       610        620        630        640        650 
SGAEAEEQAG TEKTREGLPP RGTFLSVFLL HTWTKLAGCQ THSTSRERSQ AYGKWGGTA 

« Hide

Isoform 2 [UniParc].

Checksum: 58AA5C4DA74227EA
Show »

FASTA61569,637

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel member of the dystrobrevin gene family."
Puca A.A., Piluso V.N.G., Belsito A., Sampaolo S., Quaderi N., Rossi E., Di Iorio G., Ballabio A., Franco B.
FEBS Lett. 425:7-13(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Beta-dystrobrevin, a member of the dystrophin-related protein family."
Blake D.J., Nawrotzki R., Loh N.Y., Gorecki D.C., Davies K.E.
Proc. Natl. Acad. Sci. U.S.A. 95:241-246(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Genomic organization and refined mapping of the mouse beta-dystrobrevin gene."
Loh N.Y., Ambrose H.J., Guay-Woodford L.M., Dasgupta S., Nawrotzki R.A., Blake D.J., Davies K.E.
Mamm. Genome 9:857-862(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-608 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Stomach.
[6]"Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain."
Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.
J. Biol. Chem. 276:24232-24241(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYSTROBREVIN BINDING PROTEIN 1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15742 mRNA. Translation: CAA75752.1. Sequence problems.
AJ003007 mRNA. Translation: CAA05796.1.
AJ010204 expand/collapse EMBL AC list , AJ010205, AJ010206, AJ010207, AJ010208, AJ010209, AJ010210, AJ010211, AJ010212, AJ010213, AJ010214, AJ010215, AJ010216, AJ010217, AJ010218, AJ010219, AJ010220, AJ010221 Genomic DNA. Translation: CAA09038.1.
AC155273 Genomic DNA. No translation available.
CR974568 Genomic DNA. No translation available.
AK019068 mRNA. No translation available.
CCDSCCDS49015.1. [O70585-1]
RefSeqNP_001155937.1. NM_001162465.1. [O70585-1]
UniGeneMm.286202.

3D structure databases

ProteinModelPortalO70585.
SMRO70585. Positions 26-235, 237-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO70585. 7 interactions.
MINTMINT-197260.

PTM databases

PhosphoSiteO70585.

Proteomic databases

PaxDbO70585.
PRIDEO70585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101637; ENSMUSP00000099161; ENSMUSG00000071454. [O70585-2]
ENSMUST00000164578; ENSMUSP00000126194; ENSMUSG00000071454. [O70585-1]
GeneID13528.
KEGGmmu:13528.
UCSCuc007mww.2. mouse. [O70585-2]
uc007mwy.2. mouse. [O70585-1]

Organism-specific databases

CTD1838.
MGIMGI:1203728. Dtnb.

Phylogenomic databases

eggNOGNOG251970.
GeneTreeENSGT00740000115370.
HOGENOMHOG000230684.
HOVERGENHBG005539.
InParanoidO70585.
OMALEEENSM.
TreeFamTF343849.

Gene expression databases

ArrayExpressO70585.
BgeeO70585.
CleanExMM_DTNB.
GenevestigatorO70585.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR017432. Distrobrevin.
IPR011992. EF-hand-dom_pair.
IPR015153. EF-hand_dom_typ1.
IPR015154. EF-hand_dom_typ2.
IPR000433. Znf_ZZ.
[Graphical view]
PfamPF09068. EF-hand_2. 1 hit.
PF09069. EF-hand_3. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
PIRSFPIRSF038204. Distrobrevin. 1 hit.
SMARTSM00291. ZnF_ZZ. 1 hit.
[Graphical view]
PROSITEPS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284118.
PROO70585.
SOURCESearch...

Entry information

Entry nameDTNB_MOUSE
AccessionPrimary (citable) accession number: O70585
Secondary accession number(s): E9Q0F2, O70563, Q9CTZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot