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P97318 (DAB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disabled homolog 1
Gene names
Name:Dab1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter molecule functioning in neural development. May regulate SIAH1 activity. Ref.1

Subunit structure

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, LRP1, LRP8 and VLDLR. Interacts with APLP1 (via NPXY motif). Ref.1 Ref.7 Ref.8 Ref.9 Ref.10

Tissue specificity

Expressed mainly in brain. Ref.1

Domain

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

Post-translational modification

Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons (Ref.5). Also found phosphorylated on Tyr-232 upon reelin induction (Ref.8). Also phosphorylated on Ser-524 independently of reelin signaling. Ref.4 Ref.5 Ref.6 Ref.8

Sequence similarities

Contains 1 PID domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Coding sequence diversityAlternative splicing
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from mutant phenotype PubMed 21111240. Source: MGI

adult walking behavior

Inferred from mutant phenotype PubMed 8875886. Source: MGI

cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration

Inferred from mutant phenotype PubMed 15091337. Source: MGI

central nervous system development

Traceable author statement Ref.1. Source: UniProtKB

cerebellum structural organization

Inferred from mutant phenotype PubMed 9338785. Source: MGI

cerebral cortex cell migration

Inferred from mutant phenotype PubMed 15249135. Source: MGI

cerebral cortex radially oriented cell migration

Inferred from mutant phenotype PubMed 9338785. Source: MGI

dendrite development

Inferred from mutant phenotype PubMed 14715136. Source: MGI

intracellular signal transduction

Traceable author statement PubMed 10460257. Source: UniProtKB

lateral motor column neuron migration

Inferred from mutant phenotype PubMed 20711475. Source: UniProtKB

midgut development

Inferred from electronic annotation. Source: Ensembl

negative regulation of JAK-STAT cascade

Inferred from mutant phenotype PubMed 18848628. Source: MGI

negative regulation of astrocyte differentiation

Inferred from mutant phenotype PubMed 18848628. Source: MGI

negative regulation of axonogenesis

Inferred from mutant phenotype PubMed 21111240. Source: MGI

negative regulation of cell adhesion

Inferred from mutant phenotype PubMed 15091337. Source: MGI

nervous system development

Non-traceable author statement Ref.1. Source: UniProtKB

neuron migration

Inferred from mutant phenotype PubMed 15091337PubMed 15703280PubMed 8875886. Source: MGI

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 18848628. Source: MGI

positive regulation of protein kinase activity

Inferred from genetic interaction PubMed 12526740. Source: MGI

radial glia guided migration of Purkinje cell

Inferred from mutant phenotype PubMed 9338785. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from mutant phenotype Ref.8. Source: MGI

ventral spinal cord development

Inferred from expression pattern PubMed 20711475. Source: UniProtKB

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

brush border

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

intracellular

Traceable author statement PubMed 10460257. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH2 domain binding

Traceable author statement PubMed 11716507. Source: UniProtKB

phospholipid binding

Traceable author statement PubMed 11716507. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform DAB588 (identifier: P97318-1)

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.
Note: No experimental confirmation available.
Isoform DAB197 (identifier: P97318-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-23: STETELQVAVKTSAKKDSRKKG → LC
     200-217: YIVFEAGHEPIRDPETEE → VISEPRQGFACSCEGSFD
     218-588: Missing.
Note: No experimental confirmation available.
Isoform DAB204 (identifier: P97318-5)

The sequence of this isoform differs from the canonical sequence as follows:
     200-204: YIVFE → NLQKN
     205-588: Missing.
Note: No experimental confirmation available.
Isoform DAB217 (identifier: P97318-6)

The sequence of this isoform differs from the canonical sequence as follows:
     200-217: YIVFEAGHEPIRDPETEE → VISEPRQGFACSCEGSFD
     218-588: Missing.
Isoform DAB271 (identifier: P97318-3)

The sequence of this isoform differs from the canonical sequence as follows:
     240-272: Missing.
     275-304: AVTQLELFGDMSTPPDITSPPTPATPGDAF → SLVQSPAAERAEAESRTGPAEPGSILRPLG
     305-588: Missing.
Isoform DAB553 (identifier: P97318-8)

The sequence of this isoform differs from the canonical sequence as follows:
     187-221: Missing.
Note: No experimental confirmation available.
Isoform DAB555 (identifier: P97318-2)

The sequence of this isoform differs from the canonical sequence as follows:
     240-272: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Disabled homolog 1
PRO_0000079769

Regions

Domain36 – 189154PID

Amino acid modifications

Modified residue1981Phosphotyrosine Ref.4 Ref.5
Modified residue2201Phosphotyrosine Ref.5 Ref.8
Modified residue2321Phosphotyrosine Ref.4 Ref.8
Modified residue5241Phosphoserine; by CDK5 Ref.6

Natural variations

Alternative sequence2 – 2322STETE…SRKKG → LC in isoform DAB197.
VSP_026205
Alternative sequence187 – 22135Missing in isoform DAB553.
VSP_026206
Alternative sequence200 – 21718YIVFE…PETEE → VISEPRQGFACSCEGSFD in isoform DAB197 and isoform DAB217.
VSP_003841
Alternative sequence200 – 2045YIVFE → NLQKN in isoform DAB204.
VSP_026208
Alternative sequence205 – 588384Missing in isoform DAB204.
VSP_026209
Alternative sequence218 – 588371Missing in isoform DAB197 and isoform DAB217.
VSP_003842
Alternative sequence240 – 27233Missing in isoform DAB555 and isoform DAB271.
VSP_003843
Alternative sequence275 – 30430AVTQL…PGDAF → SLVQSPAAERAEAESRTGPA EPGSILRPLG in isoform DAB271.
VSP_003844
Alternative sequence305 – 588284Missing in isoform DAB271.
VSP_003845

Experimental info

Mutagenesis451K → A: Impairs binding to PtdIns(4,5)P2. Ref.9
Mutagenesis821K → A: Abolishes binding to PtdIns(4,5)P2. Ref.9
Mutagenesis1141S → T: Abolishes interaction with APLP1. Ref.9
Mutagenesis1361H → R: Greatly impairs interaction with APLP1. Ref.9
Mutagenesis1581F → V: Abolishes interaction with APLP1. Ref.9
Mutagenesis1851Y → F: Reduces phosphorylation by SRC or downstream kinase; when associated with F-198 and F-200. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-198; F-200; F-220 and F-232. Ref.4
Mutagenesis1981Y → F: Reduces phosphorylation by SRC or downstream kinase; when associated with F-185 and F-200. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-200; F-220 and F-232. Ref.4
Mutagenesis2001Y → F: Reduces phosphorylation by SRC or downstream kinase; when associated with F-185 and F-198. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-220 and F-232. Ref.4
Mutagenesis2201Y → F: Reduces phosphorylation by SRC or downstream kinase; when associated with F-232. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-200 and F-232. Abolishes interaction with CRKL SH2 domain; when associated with F-232. Ref.4 Ref.8
Mutagenesis2321Y → F: Reduces phosphorylation by SRC or downstream kinase; when associated with F-220. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-200 and F-220. Abolishes interaction with CRKL SH2 domain; when associated with F-220. Ref.4 Ref.8
Sequence conflict291A → R in BAB24163. Ref.2
Sequence conflict2391P → PVS in CAM17685. Ref.3
Sequence conflict2391P → PVS in CAM26758. Ref.3
Sequence conflict2481E → D in CAM17685. Ref.3
Sequence conflict2481E → D in CAM26758. Ref.3

Secondary structure

............................ 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform DAB588 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 08404220792B1DB4

FASTA58863,578
        10         20         30         40         50         60 
MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL 

        70         80         90        100        110        120 
CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI 

       130        140        150        160        170        180 
TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC 

       190        200        210        220        230        240 
EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPN 

       250        260        270        280        290        300 
SQPLEDFESR FAAATPNRNL SMDFDELLEA TKVSAVTQLE LFGDMSTPPD ITSPPTPATP 

       310        320        330        340        350        360 
GDAFLPSSSQ TLPGSADVFG SMSFGTAAVP SGYVAMGAVL PSFWGQQPLV QQQIAMGAQP 

       370        380        390        400        410        420 
PVAQVIPGAQ PIAWGQPGLF PATQQAWPTV AGQFPPAAFM PTQTVMPLAA AMFQGPLTPL 

       430        440        450        460        470        480 
ATVPGTNDSA RSSPQSDKPR QKMGKESFKD FQMVQPPPVP SRKPDQPSLT CTSEAFSSYF 

       490        500        510        520        530        540 
NKVGVAQDTD DCDDFDISQL NLTPVTSTTP STNSPPTPAP RQSSPSKSSA SHVSDPTADD 

       550        560        570        580 
IFEEGFESPS KSEEQEAPDG SQASSTSDPF GEPSGEPSGD NISPQDGS 

« Hide

Isoform DAB197 [UniParc].

Checksum: 6AF789B4EC7FF6E9
Show »

FASTA19722,236
Isoform DAB204 [UniParc].

Checksum: 36271043EFC36BB4
Show »

FASTA20423,077
Isoform DAB217 [UniParc].

Checksum: 17E7E398F5D1DC01
Show »

FASTA21724,394
Isoform DAB271 [UniParc].

Checksum: FA4A8CE9812EB55C
Show »

FASTA27130,296
Isoform DAB553 [UniParc].

Checksum: 8B281EE7C3CFD2F2
Show »

FASTA55359,415
Isoform DAB555 [UniParc].

Checksum: 57A7130311954FE0
Show »

FASTA55559,838

References

« Hide 'large scale' references
[1]"Mouse disabled (mDab1): a Src binding protein implicated in neuronal development."
Howell B.W., Gertler F.B., Cooper J.A.
EMBO J. 16:121-132(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS DAB217; DAB271 AND DAB555), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Embryonic brain.
[2]"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. expand/collapse author list , 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] (ISOFORM DAB197).
Strain: C57BL/6J.
Tissue: Testis.
[3]"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. expand/collapse author list , 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.
[4]"Dab1 tyrosine phosphorylation sites relay positional signals during mouse brain development."
Howell B.W., Herrick T.M., Hildebrand J.D., Zhang Y., Cooper J.A.
Curr. Biol. 10:877-885(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-198 AND TYR-232, MUTAGENESIS OF TYR-185; TYR-198; TYR-200; TYR-220 AND TYR-232.
[5]"Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1."
Keshvara L., Benhayon D., Magdaleno S., Curran T.
J. Biol. Chem. 276:16008-16014(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-198 AND TYR-220.
[6]"Cyclin-dependent kinase 5 phosphorylates disabled 1 independently of reelin signaling."
Keshvara L., Magdaleno S., Benhayon D., Curran T.
J. Neurosci. 22:4869-4877(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-524.
[7]"Inhibition of ubiquitin ligase Siah-1A by disabled-1."
Park T.-J., Hamanaka H., Ohshima T., Watanabe N., Mikoshiba K., Nukina N.
Biochem. Biophys. Res. Commun. 302:671-678(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1.
[8]"Activation of a Dab1/CrkL/C3G/Rap1 pathway in Reelin-stimulated neurons."
Ballif B.A., Arnaud L., Arthur W.T., Guris D., Imamoto A., Cooper J.A.
Curr. Biol. 14:606-610(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-220 AND TYR-232, INTERACTION WITH CRK AND CRKL, MUTAGENESIS OF TYR-220 AND TYR-232.
[9]"Crystal structures of the Dab homology domains of mouse disabled 1 and 2."
Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J., Rock C.O., Curran T., Park H.W.
J. Biol. Chem. 278:36572-36581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-183, INTERACTION WITH PHOSPHATIDYLINOSITIDES AND APLP1, MUTAGENESIS OF LYS-45; LYS-82; SER-114; HIS-136 AND PHE-158.
[10]"Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes."
Stolt P.C., Jeon H., Song H.K., Herz J., Eck M.J., Blacklow S.C.
Structure 11:569-579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-174, INTERACTION WITH LRP8 AND VLDLR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08380 mRNA. Translation: CAA69663.1.
Y08379 mRNA. Translation: CAA69662.1.
Y08381 mRNA. Translation: CAA69664.1.
Y08383 Genomic DNA. No translation available.
AK005640 mRNA. Translation: BAB24163.1.
AL627134, AL645483 Genomic DNA. Translation: CAM26758.1.
AL627134, AL645483, AL669938 Genomic DNA. Translation: CAM26759.1.
AL627134, AL645483, AL669938 Genomic DNA. Translation: CAM26760.1.
AL627134, AL645483, AL669938 Genomic DNA. Translation: CAM26762.1.
AL627134, AL645483, AL669938 Genomic DNA. Translation: CAM26765.1.
AL645483, AL627134 Genomic DNA. Translation: CAM17685.1.
AL645483, AL627134, AL669938 Genomic DNA. Translation: CAM17686.1.
AL645483, AL627134, AL669938 Genomic DNA. Translation: CAM17687.1.
AL645483, AL627134, AL669938 Genomic DNA. Translation: CAM17689.1.
AL645483, AL627134, AL669938 Genomic DNA. Translation: CAM17690.1.
AL669938, AL627134, AL645483 Genomic DNA. Translation: CAM19059.1.
AL669938, AL627134, AL645483 Genomic DNA. Translation: CAM19060.1.
AL669938, AL627134, AL645483 Genomic DNA. Translation: CAM19062.1.
AL669938, AL627134, AL645483 Genomic DNA. Translation: CAM19063.1.
RefSeqNP_034144.1. NM_010014.3.
NP_796233.2. NM_177259.4.
XP_006502794.1. XM_006502731.1.
UniGeneMm.289682.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NTVX-ray1.50A23-174[»]
1NU2X-ray1.90A23-174[»]
1OQNX-ray2.30A/B25-183[»]
ProteinModelPortalP97318.
SMRP97318. Positions 23-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199042. 14 interactions.
DIPDIP-30902N.
IntActP97318. 16 interactions.
MINTMINT-258594.

PTM databases

PhosphoSiteP97318.

Proteomic databases

PRIDEP97318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106826; ENSMUSP00000102439; ENSMUSG00000028519. [P97318-4]
ENSMUST00000106827; ENSMUSP00000102440; ENSMUSG00000028519. [P97318-5]
ENSMUST00000106830; ENSMUSP00000102443; ENSMUSG00000028519. [P97318-2]
GeneID13131.
KEGGmmu:13131.
UCSCuc008txu.1. mouse. [P97318-5]
uc008txv.1. mouse. [P97318-6]

Organism-specific databases

CTD1600.
MGIMGI:108554. Dab1.

Phylogenomic databases

eggNOGNOG313182.
GeneTreeENSGT00520000055585.
HOVERGENHBG018945.
InParanoidP97318.
OMATCTSEAF.
OrthoDBEOG7HQN7R.
PhylomeDBP97318.
TreeFamTF316724.

Gene expression databases

ArrayExpressP97318.
BgeeP97318.
CleanExMM_DAB1.
GenevestigatorP97318.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR028761. Dab.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PANTHERPTHR11232:SF1. PTHR11232:SF1. 1 hit.
PfamPF00640. PID. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
[Graphical view]
PROSITEPS01179. PID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAB1. mouse.
EvolutionaryTraceP97318.
NextBio283176.
PROP97318.
SOURCESearch...

Entry information

Entry nameDAB1_MOUSE
AccessionPrimary (citable) accession number: P97318
Secondary accession number(s): A2A963 expand/collapse secondary AC list , A2A964, A2A965, A2A966, A2A967, A2A970, P97316, P97317, Q9DAP9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot