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Protein

Disabled homolog 1

Gene

Dab1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter molecule functioning in neural development. May regulate SIAH1 activity (By similarity).By similarity

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Disabled homolog 1
Gene namesi
Name:Dab1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi628770. Dab1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: RGD
  • brush border Source: RGD
  • cytosol Source: RGD
  • membrane Source: RGD
  • microtubule organizing center Source: Ensembl
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleolus Source: Ensembl
  • perinuclear region of cytoplasm Source: Ensembl
  • postsynaptic density Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Disabled homolog 1PRO_0000253324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981PhosphotyrosineBy similarity
Modified residuei220 – 2201PhosphotyrosineBy similarity
Modified residuei232 – 2321PhosphotyrosineBy similarity
Modified residuei491 – 4911Phosphoserine; by CDK5By similarity

Post-translational modificationi

Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons. Also phosphorylated on Ser-491 independently of reelin signaling.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8CJH2.

PTM databases

PhosphoSiteiQ8CJH2.

Expressioni

Gene expression databases

ExpressionAtlasiQ8CJH2. baseline and differential.

Interactioni

Subunit structurei

Associates with the SH2 domains of SRC, FYN and ABL. Interacts (phosphorylated on tyrosine residues) with CRK and CRKL (via respective SH2 domain). Interacts with DAB2IP, SIAH1 and LRP1.1 Publication

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: RGD

Protein-protein interaction databases

BioGridi251792. 2 interactions.
STRINGi10116.ENSRNOP00000009977.

Structurei

3D structure databases

ProteinModelPortaliQ8CJH2.
SMRiQ8CJH2. Positions 23-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 189154PIDPROSITE-ProRule annotationAdd
BLAST

Domaini

The PID domain specifically binds to the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins.

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
GeneTreeiENSGT00520000055585.
HOGENOMiHOG000060157.
HOVERGENiHBG018945.
InParanoidiQ8CJH2.
OMAiFQMAQPP.
OrthoDBiEOG7HQN7R.
PhylomeDBiQ8CJH2.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CJH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID
60 70 80 90 100
EVSAARGDKL CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK
110 120 130 140 150
TGALQHHHAV HEISYIAKDI TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV
160 170 180 190 200
ILDLRDLFQL IYELKQREEL EKKAQKDKQC EQAVYQTILE EDVEDPVYQY
210 220 230 240 250
IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPV SAVTQLELFG
260 270 280 290 300
DMSTPPDITS PPTPATPGDA FLPAPSQTLP GSADVFGSMS FGTAAVPSGY
310 320 330 340 350
VAMGAVLPSF WGQQPLVQQQ IAMGAQPPVA QVIPGAQPIA WGQPGLFPAT
360 370 380 390 400
QQPWPTVAGQ FPPAAFMPTQ TVMPLPAAMF QGPLTPLATV PGTNDSARSS
410 420 430 440 450
PQSDKPRQKM GKEMFKDFQM AQPPPVPSRK PDQPSLTCTS EAFSSYFNKV
460 470 480 490 500
GVAQDTDDCD DFDISQLNLT PVTSTTPSTN SPPTPAPRQS SPSKSSASHV
510 520 530 540 550
SDPTADDIFE EGFESPSKSE EQEAPDGSQA SSTSDPFGEP SGEPSGDNIS

PQDGS
Length:555
Mass (Da):59,900
Last modified:March 1, 2003 - v1
Checksum:i24270CD20873CDAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072426 mRNA. Translation: BAC20288.1.
RefSeqiNP_705885.1. NM_153621.1.
UniGeneiRn.206534.

Genome annotation databases

EnsembliENSRNOT00000009977; ENSRNOP00000009977; ENSRNOG00000007410.
GeneIDi266729.
KEGGirno:266729.
UCSCiRGD:628770. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072426 mRNA. Translation: BAC20288.1.
RefSeqiNP_705885.1. NM_153621.1.
UniGeneiRn.206534.

3D structure databases

ProteinModelPortaliQ8CJH2.
SMRiQ8CJH2. Positions 23-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251792. 2 interactions.
STRINGi10116.ENSRNOP00000009977.

PTM databases

PhosphoSiteiQ8CJH2.

Proteomic databases

PaxDbiQ8CJH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009977; ENSRNOP00000009977; ENSRNOG00000007410.
GeneIDi266729.
KEGGirno:266729.
UCSCiRGD:628770. rat.

Organism-specific databases

CTDi1600.
RGDi628770. Dab1.

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
GeneTreeiENSGT00520000055585.
HOGENOMiHOG000060157.
HOVERGENiHBG018945.
InParanoidiQ8CJH2.
OMAiFQMAQPP.
OrthoDBiEOG7HQN7R.
PhylomeDBiQ8CJH2.

Miscellaneous databases

NextBioi624564.
PROiQ8CJH2.

Gene expression databases

ExpressionAtlasiQ8CJH2. baseline and differential.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dab1 gene in the rat brain."
    Kikkawa S., Misaki K., Terashima T.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cerebellum.
  2. "The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate cancer. Characterization of a novel GTPase-activating protein associated with N-terminal domain of DOC-2/DAB2."
    Wang Z., Tseng C.-P., Pong R.-C., Chen H., McConnell J.D., Navone N., Hsieh J.-T.
    J. Biol. Chem. 277:12622-12631(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
    Tissue: Brain.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDAB1_RAT
AccessioniPrimary (citable) accession number: Q8CJH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.