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Q62418 (DBNL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Drebrin-like protein
Alternative name(s):
Actin-binding protein 1
SH3 domain-containing protein 7
Gene names
Name:Dbnl
Synonyms:Abp1, Sh3p7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. Ref.8 Ref.10 Ref.12 Ref.14 Ref.15

Subunit structure

Interacts with SHANK3, SYN1 and PRAM1 By similarity. Interacts with SHANK2. Interacts with FGD1, DNM1 and MAP4K1. Interacts with ANKRD54. Interacts with COBL. Interacts with WASL and WIPF1. Ref.3 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle. Cytoplasmcell cortex. Cytoplasmcytosol By similarity. Cell junctionsynapse By similarity. Cell projection By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleclathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionpodosome. Note: Detected in neuron cell body and cell projections, such as neurites. Colocalizes with cytosolic dynamin in hippocampus neurons By similarity. Cortical actin cytoskeleton. Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.14 Ref.15

Tissue specificity

Detected in hippocampus neurons and in the Purkinje cell layer in cerebellum (at protein level). Predominantly expressed in brain, thymus and spleen. Also found in testis, heart and lung. Little or no expression detected in ovary or muscle. Ref.2 Ref.7 Ref.15

Developmental stage

In the embryo, expression is high during early development but drops during later development. Ref.7

Domain

The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1 By similarity.

Sequence similarities

Belongs to the ABP1 family.

Contains 1 ADF-H domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Endocytosis
Immunity
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Golgi apparatus
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from direct assay Ref.7. Source: MGI

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection morphogenesis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

podosome assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

synapse assembly

Inferred from mutant phenotype Ref.12. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from direct assay Ref.3. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.7Ref.3. Source: MGI

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

podosome

Inferred from direct assay Ref.14. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay Ref.7. Source: MGI

actin filament binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein domain specific binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q62418-1)

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 Ref.2 (identifier: Q62418-2)

The sequence of this isoform differs from the canonical sequence as follows:
     236-238: Missing.
Isoform 3 (identifier: Q62418-3)

The sequence of this isoform differs from the canonical sequence as follows:
     235-238: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Drebrin-like protein
PRO_0000079794

Regions

Domain2 – 133132ADF-H
Domain377 – 43660SH3
Coiled coil179 – 23355 Potential

Sites

Site367 – 3682Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue1761N6-acetyllysine By similarity
Modified residue2771Phosphoserine Ref.11
Modified residue2911Phosphoserine By similarity
Modified residue2961N6-acetyllysine By similarity
Modified residue3401Phosphotyrosine Ref.2 Ref.14
Modified residue3501Phosphotyrosine Ref.2 Ref.14

Natural variations

Alternative sequence235 – 2384Missing in isoform 3.
VSP_050789
Alternative sequence236 – 2383Missing in isoform 2. Ref.2
VSP_050790

Experimental info

Mutagenesis3401Y → F: Reduces phosphorylation. Abolishes phosphorylation; when associated with F-350. Ref.2 Ref.14
Mutagenesis3501Y → F: Reduces phosphorylation. Impairs podosome rosette formation. Abolishes phosphorylation; when associated with F-340. Ref.2 Ref.14
Sequence conflict301L → F in BAE40714. Ref.4
Sequence conflict1011V → D in BAE31953. Ref.4
Sequence conflict1351A → V in BAE30108. Ref.4
Sequence conflict1351A → V in BAE31033. Ref.4
Sequence conflict3271S → C in BAE22028. Ref.4

Sequences

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

Last modified July 19, 2004. Version 2.
Checksum: 85AEF9781C698A3F

FASTA43648,700
        10         20         30         40         50         60 
MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EELVEELNSG 

        70         80         90        100        110        120 
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH VSTMANFLKG AHVTINARAE 

       130        140        150        160        170        180 
EDVEPECIME KVAKASGANY SFHKESTSFQ DVGPQAPVGS VYQKTNAISE IKRVGKDNFW 

       190        200        210        220        230        240 
AKAEKEEENR RLEEKRRAEE ERQRLEEERR ERELQEAARR EQRYQEQHRS AGAPSPSSRT 

       250        260        270        280        290        300 
GEPEQEAVSR TRQEWESAGQ QAPHPREIFK QKERAMSTTS VTSSQPGKLR SPFLQKQLTQ 

       310        320        330        340        350        360 
PETSYGREPT APVSRPAAGV CEEPAPSTLS SAQTEEEPTY EVPPEQDTLY EEPPLVQQQG 

       370        380        390        400        410        420 
AGSEHIDNYM QSQGFSGQGL CARALYDYQA ADDTEISFDP ENLITGIEVI DEGWWRGYGP 

       430 
DGHFGMFPAN YVELIE 

« Hide

Isoform 2 [UniParc].

Checksum: 602D3862C446FA4D
Show »

FASTA43348,428
Isoform 3 [UniParc].

Checksum: 4A36D3B6E59C707F
Show »

FASTA43248,341

References

« Hide 'large scale' references
[1]"Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
Nat. Biotechnol. 14:741-744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Embryo.
[2]"SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors."
Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., Wienands J.
Mol. Cell. Biol. 19:1539-1546(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 79-94 AND 135-144, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-340 AND TYR-350, PHOSPHORYLATION AT TYR-340 AND TYR-350.
Tissue: Myeloma.
[3]"Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly interacts with cortactin and mAbp1 to modulate cell shape."
Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B., Gorski J.L.
Hum. Mol. Genet. 12:1981-1993(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH FGD1.
Strain: C57BL/6J.
Tissue: Osteoblast.
[4]"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] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Amnion, Bone marrow, Corpora quadrigemina, Eye, Head, Kidney, Medulla oblongata, Spleen and Thymus.
[5]"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.
[6]"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 3).
Strain: FVB/N.
Tissue: Colon.
[7]"Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation."
Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G.
Mol. Biol. Cell 11:393-412(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin."
Kessels M.M., Engqvist-Goldstein A.E., Drubin D.G., Qualmann B.
J. Cell Biol. 153:351-366(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM1, ACTIN-BINDING, SUBCELLULAR LOCATION.
[9]"The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin."
Xu W., Stamnes M.
J. Biol. Chem. 281:11826-11833(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIN-BINDING, SUBCELLULAR LOCATION.
[10]"Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal morphology."
Pinyol R., Haeckel A., Ritter A., Qualmann B., Kessels M.M.
PLoS ONE 2:E400-E400(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"The actin-binding protein Abp1 controls dendritic spine morphology and is important for spine head and synapse formation."
Haeckel A., Ahuja R., Gundelfinger E.D., Qualmann B., Kessels M.M.
J. Neurosci. 28:10031-10044(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHANK2.
[13]"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
Samuels A.L., Klinken S.P., Ingley E.
Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD54.
[14]"Src-mediated phosphorylation of mammalian Abp1 (DBNL) regulates podosome rosette formation in transformed fibroblasts."
Boateng L.R., Cortesio C.L., Huttenlocher A.
J. Cell Sci. 125:1329-1341(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WIPF1, PHOSPHORYLATION AT TYR-340 AND TYR-350, MUTAGENESIS OF TYR-340 AND TYR-350, SUBCELLULAR LOCATION.
[15]"The actin nucleator Cobl is crucial for Purkinje cell development and works in close conjunction with the F-actin binding protein Abp1."
Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B., Kessels M.M.
J. Neurosci. 32:17842-17856(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH COBL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58884 mRNA. Translation: AAC52640.1.
AY098595 mRNA. Translation: AAM28340.1.
AK046073 mRNA. Translation: BAC32592.1.
AK053796 mRNA. Translation: BAC35528.1.
AK078082 mRNA. Translation: BAC37118.1.
AK134136 mRNA. Translation: BAE22028.1.
AK134487 mRNA. Translation: BAE22160.1.
AK140752 mRNA. Translation: BAE24466.1.
AK142818 mRNA. Translation: BAE25201.1.
AK146920 mRNA. Translation: BAE27532.1.
AK151096 mRNA. Translation: BAE30108.1.
AK152204 mRNA. Translation: BAE31033.1.
AK153389 mRNA. Translation: BAE31953.1.
AK159984 mRNA. Translation: BAE35535.1.
AK168898 mRNA. Translation: BAE40714.1.
AK172471 mRNA. Translation: BAE43024.1.
AL627069 Genomic DNA. Translation: CAI25434.1.
AL627069 Genomic DNA. Translation: CAI25435.1.
AL627069 Genomic DNA. Translation: CAI25436.1.
BC046430 mRNA. Translation: AAH46430.1.
CCDSCCDS24403.1. [Q62418-2]
CCDS48746.1. [Q62418-1]
CCDS48747.1. [Q62418-3]
RefSeqNP_001139780.1. NM_001146308.1. [Q62418-1]
NP_001139781.1. NM_001146309.1. [Q62418-3]
NP_038838.1. NM_013810.3. [Q62418-2]
UniGeneMm.256925.

3D structure databases

ProteinModelPortalQ62418.
SMRQ62418. Positions 1-133, 379-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199059. 3 interactions.
IntActQ62418. 6 interactions.
MINTMINT-100768.

PTM databases

PhosphoSiteQ62418.

Proteomic databases

MaxQBQ62418.
PaxDbQ62418.
PRIDEQ62418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020769; ENSMUSP00000020769; ENSMUSG00000020476. [Q62418-1]
ENSMUST00000102928; ENSMUSP00000099992; ENSMUSG00000020476. [Q62418-2]
ENSMUST00000109845; ENSMUSP00000105471; ENSMUSG00000020476. [Q62418-3]
GeneID13169.
KEGGmmu:13169.
UCSCuc007hxb.2. mouse. [Q62418-2]
uc007hxc.2. mouse. [Q62418-3]
uc007hxd.2. mouse. [Q62418-1]

Organism-specific databases

CTD28988.
MGIMGI:700006. Dbnl.

Phylogenomic databases

eggNOGNOG265859.
GeneTreeENSGT00530000062953.
HOVERGENHBG051316.
InParanoidQ62418.
OMAFQDTGPQ.
OrthoDBEOG7X3QR9.
PhylomeDBQ62418.
TreeFamTF318935.

Gene expression databases

BgeeQ62418.
CleanExMM_DBNL.
GenevestigatorQ62418.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
InterProIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDBNL. mouse.
NextBio283260.
PROQ62418.
SOURCESearch...

Entry information

Entry nameDBNL_MOUSE
AccessionPrimary (citable) accession number: Q62418
Secondary accession number(s): Q3TG34 expand/collapse secondary AC list , Q3U5X3, Q3U8I5, Q3UZ33, Q5NCI5, Q5NCI6, Q5NCI7, Q80WP1, Q8BH56
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 2 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