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Protein

Drebrin-like protein

Gene

Abp1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Actin-binding adapter protein. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin (By similarity). Does not seem to be involved in actin-based lamella protrusion during cell migration.By similarity1 Publication

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. actin filament binding Source: FlyBase
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: FlyBase
  4. phosphatidylinositol-4,5-bisphosphate binding Source: FlyBase
  5. phosphatidylserine binding Source: FlyBase

GO - Biological processi

  1. chaeta development Source: FlyBase
  2. positive regulation of synaptic growth at neuromuscular junction Source: FlyBase
  3. terminal button organization Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_236010. Caspase-mediated cleavage of cytoskeletal proteins.
SignaLinkiQ9VU84.

Names & Taxonomyi

Protein namesi
Recommended name:
Drebrin-like protein
Alternative name(s):
Actin binding protein 1
Gene namesi
Name:Abp1
ORF Names:CG10083
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036372. Abp1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. axon Source: FlyBase
  2. cell cortex Source: FlyBase
  3. cytoskeleton Source: UniProtKB
  4. growth cone Source: FlyBase
  5. neuromuscular junction Source: FlyBase
  6. type Ib terminal bouton Source: FlyBase
  7. type Is terminal bouton Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Drebrin-like proteinPRO_0000270188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VU84.
PRIDEiQ9VU84.

Expressioni

Gene expression databases

BgeeiQ9VU84.

Interactioni

Protein-protein interaction databases

BioGridi64863. 1 interaction.
IntActiQ9VU84. 3 interactions.
MINTiMINT-1645145.

Structurei

3D structure databases

ProteinModelPortaliQ9VU84.
SMRiQ9VU84. Positions 1-138, 472-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 133132ADF-HPROSITE-ProRule annotationAdd
BLAST
Domaini472 – 53160SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili177 – 22044Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi321 – 35838Pro-richAdd
BLAST

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, Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG265859.
GeneTreeiENSGT00530000062953.
InParanoidiQ9VU84.
OMAiFQDTGPQ.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ9VU84.

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.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VU84-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVSFEKNRA QIVAAWKDVL DDKSDTNWSL FGYEGQTNEL KVVATGDGGV
60 70 80 90 100
DELNEDLNSG KIMYAFVRIE DPKTGLNKYL LINWQGEGAP VLRKGTCANH
110 120 130 140 150
IRDVSNLLSG AHLTINARNE DDIDLDRLLK KLSTVSSAYS FKEPRGAMEE
160 170 180 190 200
QKAPVGTNYT RVIPTKELNA SVMQDFWKKE EAEEKLRQEA EKESKRLELQ
210 220 230 240 250
KLEQEQRSRE EKEHKEREKL VISTTKLQPA HVPIKTSPQP LSPEKTAPGF
260 270 280 290 300
ANNLTDAERM RQARNQEARE LIGSRVGAAK AMFTKHTSEG QLQSKLNTQP
310 320 330 340 350
PAKPARNSIA QRINVFNQNQ PQDAPVPSPP RAASPAKPLP VEAPEPVVPA
360 370 380 390 400
PAIAPAAPVA AEVVSTIAEV EESQPVDDLP LAHESEQFST IKRSPHSKSN
410 420 430 440 450
SLQSQSPDET TSSNETDTAV SQEQEEEVRT KVSVTVQQSQ SVKSSGMSTL
460 470 480 490 500
ERNALTDLVN EDDFICQETL GDLGQRARAL YDYQAADETE ITFDPGDVIT
510 520 530
HIDQIDEGWW QGLGPDGTYG LFPANYVEII N
Length:531
Mass (Da):58,729
Last modified:May 1, 2000 - v1
Checksum:iA1CAAFA251F151C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49805.1.
AY119287 mRNA. Translation: AAM51147.1.
BT021389 mRNA. Translation: AAX33537.1.
RefSeqiNP_648657.1. NM_140400.2.
UniGeneiDm.13622.

Genome annotation databases

EnsemblMetazoaiFBtr0075819; FBpp0075561; FBgn0036372.
GeneIDi39520.
KEGGidme:Dmel_CG10083.
UCSCiCG10083-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49805.1.
AY119287 mRNA. Translation: AAM51147.1.
BT021389 mRNA. Translation: AAX33537.1.
RefSeqiNP_648657.1. NM_140400.2.
UniGeneiDm.13622.

3D structure databases

ProteinModelPortaliQ9VU84.
SMRiQ9VU84. Positions 1-138, 472-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64863. 1 interaction.
IntActiQ9VU84. 3 interactions.
MINTiMINT-1645145.

Proteomic databases

PaxDbiQ9VU84.
PRIDEiQ9VU84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075819; FBpp0075561; FBgn0036372.
GeneIDi39520.
KEGGidme:Dmel_CG10083.
UCSCiCG10083-RA. d. melanogaster.

Organism-specific databases

CTDi39520.
FlyBaseiFBgn0036372. Abp1.

Phylogenomic databases

eggNOGiNOG265859.
GeneTreeiENSGT00530000062953.
InParanoidiQ9VU84.
OMAiFQDTGPQ.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ9VU84.

Enzyme and pathway databases

ReactomeiREACT_236010. Caspase-mediated cleavage of cytoskeletal proteins.
SignaLinkiQ9VU84.

Miscellaneous databases

GenomeRNAii39520.
NextBioi814077.
PROiQ9VU84.

Gene expression databases

BgeeiQ9VU84.

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.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Flying through the Drosophila cytoskeletal genome."
    Goldstein L.S., Gunawardena S.
    J. Cell Biol. 150:F63-F68(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "Molecular requirements for actin-based lamella formation in Drosophila S2 cells."
    Rogers S.L., Wiedemann U., Stuurman N., Vale R.D.
    J. Cell Biol. 162:1079-1088(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDBNL_DROME
AccessioniPrimary (citable) accession number: Q9VU84
Secondary accession number(s): Q8MRS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.