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UniProtKB/Swiss-Prot entry P97318


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DAB1_MOUSE
Primary accession number P97318
Secondary accession numbers A2A963 A2A964 A2A965 A2A966 A2A967 A2A970 P97316 P97317 Q9DAP9
Integrated into Swiss-Prot on February 11, 2002
Sequence was last modified on June 1, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name Disabled homolog 1
Synonyms None
Gene name
Name: Dab1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS DAB217; DAB271 AND DAB555), FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Embryonic brain;
DOI=10.1093/emboj/16.1.121; PubMed=9009273 [NCBI, ExPASy, EBI, Israel, Japan]
Howell B.W., Gertler F.B., Cooper J.A.;
"Mouse disabled (mDab1): a Src binding protein implicated in neuronal development.";
EMBO J. 16:121-132(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DAB197).
STRAIN=C57BL/6J;
TISSUE=Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION AT TYR-198 AND TYR-220.
DOI=10.1074/jbc.M101422200; PubMed=11279201 [NCBI, ExPASy, EBI, Israel, Japan]
Keshvara L., Benhayon D., Magdaleno S., Curran T.;
"Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1.";
J. Biol. Chem. 276:16008-16014(2001).
[5]
PHOSPHORYLATION AT SER-524.
PubMed=12077184 [NCBI, ExPASy, EBI, Israel, Japan]
Keshvara L., Magdaleno S., Benhayon D., Curran T.;
"Cyclin-dependent kinase 5 phosphorylates disabled 1 independently of reelin signaling.";
J. Neurosci. 22:4869-4877(2002).
[6]
INTERACTION WITH SIAH1.
DOI=10.1016/S0006-291X(03)00247-X; PubMed=12646221 [NCBI, ExPASy, EBI, Israel, Japan]
Park T.-J., Hamanaka H., Ohshima T., Watanabe N., Mikoshiba K., Nukina N.;
"Inhibition of ubiquitin ligase Siah-1A by disabled-1.";
Biochem. Biophys. Res. Commun. 302:671-678(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y08380; CAA69663.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y08379; CAA69662.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y08381; CAA69664.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y08383; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AK005640; BAB24163.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM26758.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM26758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM26759.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM26759.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM26759.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM26760.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM26760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM26760.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM26762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM26762.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM26762.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM26765.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM26765.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM26765.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM17685.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM17685.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM17686.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM17686.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM17686.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM17687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM17687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM17687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM17689.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM17689.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM17689.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM17690.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM17690.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM17690.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM19059.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM19059.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM19059.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM19060.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM19060.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM19060.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM19062.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM19062.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM19062.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669938; CAM19063.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627134; CAM19063.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645483; CAM19063.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_034144.1; -.
NP_796233.2; -.
UniGene Mm.289682
3D structure databases
PDB
1NTV; X-ray; 1.50 A; A=23-174.[ExPASy / RCSB / EBI]
1NU2; X-ray; 1.90 A; A=23-174.[ExPASy / RCSB / EBI]
1OQN; X-ray; 2.30 A; A/B=25-183.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NTV; -.
1NU2; -.
1OQN; -.
ModBase P97318.
Protein-protein interaction databases
IntAct P97318; -.
PTM databases
PhosphoSite P97318; -.
Organism-specific databases
MGI MGI:108554; Dab1.
Gene expression databases
ArrayExpress P97318; -.
CleanEx MM_DAB1; -.
GermOnline ENSMUSG00000028519; Mus musculus.
Ontologies
GO
GO:0005622; Cellular component: intracellular (traceable author statement from UniProtKB).
GO:0005543; Molecular function: phospholipid binding (traceable author statement from UniProtKB).
GO:0042169; Molecular function: SH2 domain binding (traceable author statement from UniProtKB).
GO:0021813; Biological process: cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration (inferred from mutant phenotype from MGI).
GO:0021589; Biological process: cerebellum structural organization (inferred from mutant phenotype from MGI).
GO:0007162; Biological process: negative regulation of cell adhesion (inferred from mutant phenotype from MGI).
GO:0001764; Biological process: neuron migration (inferred from mutant phenotype from MGI).
GO:0045860; Biological process: positive regulation of protein kinase activity (inferred from genetic interaction from MGI).
GO:0007243; Biological process: protein kinase cascade (traceable author statement from UniProtKB).
GO:0021942; Biological process: radial glia guided migration of Purkinje cell (inferred from mutant phenotype from MGI).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR011993; PH_type.
IPR006020; PTB_PID.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
Pfam PF00640; PID; 1.
Pfam graphical view of domain structure.
SMART SM00462; PTB; 1.
SMART graphical view of domain structure.
PROSITE PS01179; PID; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P97318.
Genome annotation databases
Ensembl ENSMUSG00000028519; Mus musculus. [Contig view]
GeneID 13131; -.
KEGG mmu:13131; -.
Phylogenomic databases
HOGENOM P97318; -.
HOVERGEN P97318; -.
Other
SOURCE Dab1; Mus musculus.
ProtoNet P97318.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Developmental protein; Differentiation; Neurogenesis; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   588  588     Disabled homolog 1. PRO_0000079769
DOMAIN   36   189  154     PID. 
MOD_RES   198   198        Phosphotyrosine. 
MOD_RES   220   220        Phosphotyrosine. 
MOD_RES   524   524        Phosphoserine; by CDK5. 
VAR_SEQ   2    23        STETELQVAVKTSAKKDSRKKG -> LC (in isoform DAB197). VSP_026205
VAR_SEQ   187   221        Missing (in isoform DAB553). VSP_026206
VAR_SEQ   200   217        YIVFEAGHEPIRDPETEE -> VISEPRQGFACSCEGSFD (in isoform DAB197 and isoform DAB217). VSP_003841
VAR_SEQ   200   204        YIVFE -> NLQKN (in isoform DAB204). VSP_026208
VAR_SEQ   205   588        Missing (in isoform DAB204). VSP_026209
VAR_SEQ   218   588        Missing (in isoform DAB197 and isoform DAB217). VSP_003842
VAR_SEQ   240   272        Missing (in isoform DAB555 and isoform DAB271). VSP_003843
VAR_SEQ   275   304        AVTQLELFGDMSTPPDITSPPTPATPGDAF -> SLVQSPAAERAEAESRTGPAEPGSILRPLG (in isoform DAB271). VSP_003844
VAR_SEQ   305   588        Missing (in isoform DAB271). VSP_003845
CONFLICT   29    29        A -> R (in Ref. 2; BAB24163). 
CONFLICT   239   239        P -> PVS (in Ref. 3; CAM17685/CAM26758). 
CONFLICT   248   248        E -> D (in Ref. 3; CAM17685/CAM26758). 
HELIX   28    35  8      
STRAND   40    51  12      
STRAND   53    55  3      
HELIX   58    76  19      
TURN   77    79  3      
STRAND   83    90  8      
STRAND   93    98  6      
TURN   99   101  3      
STRAND   104   108  5      
HELIX   110   112  3      
STRAND   113   118  6      
STRAND   125   132  8      
STRAND   137   145  9      
HELIX   148   166  19      
HELIX   170   173  4      
Sequence information
Length: 588 AA [This is the length of the unprocessed precursor] Molecular weight: 63578 Da [This is the MW of the unprocessed precursor] CRC64: 08404220792B1DB4 [This is a checksum on the sequence]
        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 

P97318 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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