Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q62418

- DBNL_MOUSE

UniProt

Q62418 - DBNL_MOUSE

Protein

Drebrin-like protein

Gene

Dbnl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei367 – 3682Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    1. actin binding Source: MGI
    2. actin filament binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein domain specific binding Source: MGI

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. immune system process Source: UniProtKB-KW
    3. neuron projection morphogenesis Source: UniProtKB
    4. podosome assembly Source: UniProtKB
    5. Rac protein signal transduction Source: MGI
    6. synapse assembly Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Endocytosis, Immunity, Transport

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Drebrin-like protein
    Alternative name(s):
    Actin-binding protein 1
    SH3 domain-containing protein 7
    Gene namesi
    Name:DbnlImported
    Synonyms:Abp1Imported, Sh3p71 Publication
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:700006. Dbnl.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell cortex Source: MGI
    2. cell junction Source: UniProtKB-KW
    3. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
    4. cytoplasm Source: MGI
    5. cytosol Source: UniProtKB-SubCell
    6. dendrite Source: Ensembl
    7. Golgi membrane Source: UniProtKB-SubCell
    8. lamellipodium Source: UniProtKB
    9. plasma membrane Source: UniProtKB-SubCell
    10. podosome Source: UniProtKB
    11. postsynaptic density Source: Ensembl
    12. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi340 – 3401Y → F: Reduces phosphorylation. Abolishes phosphorylation; when associated with F-350. 2 Publications
    Mutagenesisi350 – 3501Y → F: Reduces phosphorylation. Impairs podosome rosette formation. Abolishes phosphorylation; when associated with F-340. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Drebrin-like proteinPRO_0000079794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761N6-acetyllysineBy similarity
    Modified residuei277 – 2771Phosphoserine1 Publication
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei296 – 2961N6-acetyllysineBy similarity
    Modified residuei340 – 3401Phosphotyrosine2 Publications
    Modified residuei350 – 3501Phosphotyrosine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ62418.
    PaxDbiQ62418.
    PRIDEiQ62418.

    PTM databases

    PhosphoSiteiQ62418.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Developmental stagei

    In the embryo, expression is high during early development but drops during later development.1 Publication

    Gene expression databases

    BgeeiQ62418.
    CleanExiMM_DBNL.
    GenevestigatoriQ62418.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Protein-protein interaction databases

    BioGridi199059. 3 interactions.
    IntActiQ62418. 6 interactions.
    MINTiMINT-100768.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62418.
    SMRiQ62418. Positions 1-133, 379-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 133132ADF-HPROSITE-ProRule annotationAdd
    BLAST
    Domaini377 – 43660SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili179 – 23355Sequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the ABP1 family.Curated
    Contains 1 ADF-H domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG265859.
    GeneTreeiENSGT00530000062953.
    HOVERGENiHBG051316.
    InParanoidiQ62418.
    OMAiFQDTGPQ.
    OrthoDBiEOG7X3QR9.
    PhylomeDBiQ62418.
    TreeFamiTF318935.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    InterProiIPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00241. Cofilin_ADF. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q62418-1) [UniParc]FASTAAdd to Basket

    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

    MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL    50
    EELVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH 100
    VSTMANFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESTSFQ 150
    DVGPQAPVGS VYQKTNAISE IKRVGKDNFW AKAEKEEENR RLEEKRRAEE 200
    ERQRLEEERR ERELQEAARR EQRYQEQHRS AGAPSPSSRT GEPEQEAVSR 250
    TRQEWESAGQ QAPHPREIFK QKERAMSTTS VTSSQPGKLR SPFLQKQLTQ 300
    PETSYGREPT APVSRPAAGV CEEPAPSTLS SAQTEEEPTY EVPPEQDTLY 350
    EEPPLVQQQG AGSEHIDNYM QSQGFSGQGL CARALYDYQA ADDTEISFDP 400
    ENLITGIEVI DEGWWRGYGP DGHFGMFPAN YVELIE 436
    Length:436
    Mass (Da):48,700
    Last modified:July 19, 2004 - v2
    Checksum:i85AEF9781C698A3F
    GO
    Isoform 21 Publication (identifier: Q62418-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         236-238: Missing.

    Show »
    Length:433
    Mass (Da):48,428
    Checksum:i602D3862C446FA4D
    GO
    Isoform 3Curated (identifier: Q62418-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:432
    Mass (Da):48,341
    Checksum:i4A36D3B6E59C707F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301L → F in BAE40714. (PubMed:16141072)Curated
    Sequence conflicti101 – 1011V → D in BAE31953. (PubMed:16141072)Curated
    Sequence conflicti135 – 1351A → V in BAE30108. (PubMed:16141072)Curated
    Sequence conflicti135 – 1351A → V in BAE31033. (PubMed:16141072)Curated
    Sequence conflicti327 – 3271S → C in BAE22028. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei235 – 2384Missing in isoform 3. 2 PublicationsVSP_050789
    Alternative sequencei236 – 2383Missing in isoform 2. 3 PublicationsVSP_050790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS24403.1. [Q62418-2]
    CCDS48746.1. [Q62418-1]
    CCDS48747.1. [Q62418-3]
    RefSeqiNP_001139780.1. NM_001146308.1. [Q62418-1]
    NP_001139781.1. NM_001146309.1. [Q62418-3]
    NP_038838.1. NM_013810.3. [Q62418-2]
    UniGeneiMm.256925.

    Genome annotation databases

    EnsembliENSMUST00000020769; ENSMUSP00000020769; ENSMUSG00000020476. [Q62418-1]
    ENSMUST00000102928; ENSMUSP00000099992; ENSMUSG00000020476. [Q62418-2]
    ENSMUST00000109845; ENSMUSP00000105471; ENSMUSG00000020476. [Q62418-3]
    GeneIDi13169.
    KEGGimmu:13169.
    UCSCiuc007hxb.2. mouse. [Q62418-2]
    uc007hxc.2. mouse. [Q62418-3]
    uc007hxd.2. mouse. [Q62418-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS24403.1. [Q62418-2 ]
    CCDS48746.1. [Q62418-1 ]
    CCDS48747.1. [Q62418-3 ]
    RefSeqi NP_001139780.1. NM_001146308.1. [Q62418-1 ]
    NP_001139781.1. NM_001146309.1. [Q62418-3 ]
    NP_038838.1. NM_013810.3. [Q62418-2 ]
    UniGenei Mm.256925.

    3D structure databases

    ProteinModelPortali Q62418.
    SMRi Q62418. Positions 1-133, 379-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199059. 3 interactions.
    IntActi Q62418. 6 interactions.
    MINTi MINT-100768.

    PTM databases

    PhosphoSitei Q62418.

    Proteomic databases

    MaxQBi Q62418.
    PaxDbi Q62418.
    PRIDEi Q62418.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020769 ; ENSMUSP00000020769 ; ENSMUSG00000020476 . [Q62418-1 ]
    ENSMUST00000102928 ; ENSMUSP00000099992 ; ENSMUSG00000020476 . [Q62418-2 ]
    ENSMUST00000109845 ; ENSMUSP00000105471 ; ENSMUSG00000020476 . [Q62418-3 ]
    GeneIDi 13169.
    KEGGi mmu:13169.
    UCSCi uc007hxb.2. mouse. [Q62418-2 ]
    uc007hxc.2. mouse. [Q62418-3 ]
    uc007hxd.2. mouse. [Q62418-1 ]

    Organism-specific databases

    CTDi 28988.
    MGIi MGI:700006. Dbnl.

    Phylogenomic databases

    eggNOGi NOG265859.
    GeneTreei ENSGT00530000062953.
    HOVERGENi HBG051316.
    InParanoidi Q62418.
    OMAi FQDTGPQ.
    OrthoDBi EOG7X3QR9.
    PhylomeDBi Q62418.
    TreeFami TF318935.

    Enzyme and pathway databases

    Reactomei REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Miscellaneous databases

    ChiTaRSi DBNL. mouse.
    NextBioi 283260.
    PROi Q62418.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q62418.
    CleanExi MM_DBNL.
    Genevestigatori Q62418.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00241. Cofilin_ADF. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: Myeloma1 Publication.
    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/6JImported.
      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. 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/NImported.
      Tissue: ColonImported.
    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. 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.

    Entry informationi

    Entry nameiDBNL_MOUSE
    AccessioniPrimary (citable) accession number: Q62418
    Secondary accession number(s): Q3TG34
    , Q3U5X3, Q3U8I5, Q3UZ33, Q5NCI5, Q5NCI6, Q5NCI7, Q80WP1, Q8BH56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3