Q62418 (DBNL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Drebrin-like protein

Alternative name(s):
Actin-binding protein 1
SH3 domain-containing protein 7

Gene names

Name:	Dbnl
Synonyms:	Abp1, Sh3p7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15 Ref.16
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.14 Ref.15 Ref.16
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cell projection › ruffle. Cytoplasm › cell cortex. Cytoplasm › cytosol By similarity. Cell junction › synapse By similarity. Cell projection By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle › clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › podosome. 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.15 Ref.16
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.16
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 process	Adaptive immunity Endocytosis Immunity Transport
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Golgi apparatus Membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rac protein signal transduction Inferred from direct assay Ref.7. Source: MGI endocytosis 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.15. Source: UniProtKB synapse assembly Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	cell cortex Inferred from direct assay Ref.3. Source: MGI lamellipodium Inferred from direct assay Ref.3. Source: UniProtKB podosome Inferred from direct assay Ref.15. Source: UniProtKB postsynaptic density Inferred from electronic annotation. Source: Compara ruffle Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	actin filament binding Inferred from direct assay Ref.7. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Drebrin-like protein		PRO_0000079794
Regions
	Domain	2 – 133	132	ADF-H
	Domain	377 – 436	60	SH3
	Coiled coil	179 – 233	55	Potential
Sites
	Site	367 – 368	2	Cleavage; by caspase-3 By similarity
Amino acid modifications
	Modified residue	176	1	N6-acetyllysine By similarity
	Modified residue	277	1	Phosphoserine Ref.11
	Modified residue	278	1	Phosphothreonine Ref.11
	Modified residue	280	1	Phosphoserine By similarity
	Modified residue	291	1	Phosphoserine By similarity
	Modified residue	296	1	N6-acetyllysine By similarity
	Modified residue	299	1	Phosphothreonine Ref.13
	Modified residue	340	1	Phosphotyrosine Ref.2 Ref.15
	Modified residue	350	1	Phosphotyrosine Ref.2 Ref.15
Natural variations
	Alternative sequence	235 – 238	4	Missing in isoform 3.		VSP_050789
	Alternative sequence	236 – 238	3	Missing in isoform 2. Ref.2		VSP_050790
Experimental info
	Mutagenesis	340	1	Y → F: Reduces phosphorylation. Abolishes phosphorylation; when associated with F-350. Ref.2 Ref.15
	Mutagenesis	350	1	Y → F: Reduces phosphorylation. Impairs podosome rosette formation. Abolishes phosphorylation; when associated with F-340. Ref.2 Ref.15
	Sequence conflict	30	1	L → F in BAE40714. Ref.4
	Sequence conflict	101	1	V → D in BAE31953. Ref.4
	Sequence conflict	135	1	A → V in BAE30108. Ref.4
	Sequence conflict	135	1	A → V in BAE31033. Ref.4
	Sequence conflict	327	1	S → C in BAE22028. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 85AEF9781C698A3F	FASTA	436	48,700
	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
	Isoform 2 [UniParc]. Checksum: 602D3862C446FA4D	FASTA	433	48,428
	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 AGAPSRTGEP 250 260 270 280 290 300 EQEAVSRTRQ EWESAGQQAP HPREIFKQKE RAMSTTSVTS SQPGKLRSPF LQKQLTQPET 310 320 330 340 350 360 SYGREPTAPV SRPAAGVCEE PAPSTLSSAQ TEEEPTYEVP PEQDTLYEEP PLVQQQGAGS 370 380 390 400 410 420 EHIDNYMQSQ GFSGQGLCAR ALYDYQAADD TEISFDPENL ITGIEVIDEG WWRGYGPDGH 430 FGMFPANYVE LIE
	Isoform 3 [UniParc]. Checksum: 4A36D3B6E59C707F	FASTA	432	48,341
	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 AGAPRTGEPE 250 260 270 280 290 300 QEAVSRTRQE WESAGQQAPH PREIFKQKER AMSTTSVTSS QPGKLRSPFL QKQLTQPETS 310 320 330 340 350 360 YGREPTAPVS RPAAGVCEEP APSTLSSAQT EEEPTYEVPP EQDTLYEEPP LVQQQGAGSE 370 380 390 400 410 420 HIDNYMQSQG FSGQGLCARA LYDYQAADDT EISFDPENLI TGIEVIDEGW WRGYGPDGHF 430 GMFPANYVEL IE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 AND THR-278, MASS SPECTROMETRY. 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-299, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"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.
[15]	"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.
[16]	"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.
IPI	IPI00308222. IPI00378015. IPI00458127.
RefSeq	NP_001139780.1. NM_001146308.1. NP_001139781.1. NM_001146309.1. NP_038838.1. NM_013810.3.
UniGene	Mm.256925.
3D structure databases
ProteinModelPortal	Q62418.
SMR	Q62418. Positions 1-133, 379-434.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62418. 3 interactions.
MINT	MINT-100768.
PTM databases
PhosphoSite	Q62418.
Proteomic databases
PaxDb	Q62418.
PRIDE	Q62418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020769; ENSMUSP00000020769; ENSMUSG00000020476. ENSMUST00000102928; ENSMUSP00000099992; ENSMUSG00000020476. ENSMUST00000109845; ENSMUSP00000105471; ENSMUSG00000020476.
GeneID	13169.
KEGG	mmu:13169.
UCSC	uc007hxb.2. mouse. uc007hxc.2. mouse. uc007hxd.2. mouse.
Organism-specific databases
CTD	28988.
MGI	MGI:700006. Dbnl.
Phylogenomic databases
eggNOG	NOG265859.
GeneTree	ENSGT00530000062953.
HOVERGEN	HBG051316.
InParanoid	Q62418.
OMA	EQETFYE.
Gene expression databases
Bgee	Q62418.
CleanEx	MM_DBNL.
Genevestigator	Q62418.
GermOnline	ENSMUSG00000020476. Mus musculus.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00241. Cofilin_ADF. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00102. ADF. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS51263. ADF_H. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DBNL. mouse.
NextBio	283260.
SOURCE	Search...

Entry information

Entry name

DBNL_MOUSE

Accession

Primary (citable) accession number: Q62418
Secondary accession number(s): Q3TG34 , 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:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program