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Q62418

- DBNL_MOUSE

UniProt

Q62418 - DBNL_MOUSE

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Protein

Drebrin-like protein

Gene

Dbnl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 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
Complete GO annotation...

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. cytoplasm Source: MGI
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. dendrite Source: Ensembl
  6. extracellular vesicular exosome Source: Ensembl
  7. Golgi apparatus Source: UniProtKB-KW
  8. lamellipodium Source: UniProtKB
  9. plasma membrane Source: UniProtKB-KW
  10. podosome Source: UniProtKB
  11. postsynaptic density Source: Ensembl
  12. ruffle Source: UniProtKB
Complete GO annotation...

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

        10         20         30         40         50
MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL
60 70 80 90 100
EELVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH
110 120 130 140 150
VSTMANFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESTSFQ
160 170 180 190 200
DVGPQAPVGS VYQKTNAISE IKRVGKDNFW AKAEKEEENR RLEEKRRAEE
210 220 230 240 250
ERQRLEEERR ERELQEAARR EQRYQEQHRS AGAPSPSSRT GEPEQEAVSR
260 270 280 290 300
TRQEWESAGQ QAPHPREIFK QKERAMSTTS VTSSQPGKLR SPFLQKQLTQ
310 320 330 340 350
PETSYGREPT APVSRPAAGV CEEPAPSTLS SAQTEEEPTY EVPPEQDTLY
360 370 380 390 400
EEPPLVQQQG AGSEHIDNYM QSQGFSGQGL CARALYDYQA ADDTEISFDP
410 420 430
ENLITGIEVI DEGWWRGYGP DGHFGMFPAN YVELIE
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

« Hide 'large scale' publications
  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 29, 2014
This is version 124 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