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P97318

- DAB1_MOUSE

UniProt

P97318 - DAB1_MOUSE

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Protein

Disabled homolog 1

Gene

Dab1

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

Functioni

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

GO - Molecular functioni

  1. phospholipid binding Source: UniProtKB
  2. SH2 domain binding Source: UniProtKB

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration Source: MGI
  3. central nervous system development Source: UniProtKB
  4. cerebellum structural organization Source: MGI
  5. cerebral cortex cell migration Source: MGI
  6. cerebral cortex radially oriented cell migration Source: MGI
  7. dendrite development Source: MGI
  8. Golgi localization Source: MGI
  9. intracellular signal transduction Source: UniProtKB
  10. lateral motor column neuron migration Source: UniProtKB
  11. midgut development Source: Ensembl
  12. negative regulation of astrocyte differentiation Source: MGI
  13. negative regulation of axonogenesis Source: MGI
  14. negative regulation of cell adhesion Source: MGI
  15. negative regulation of JAK-STAT cascade Source: MGI
  16. nervous system development Source: UniProtKB
  17. neuron migration Source: MGI
  18. positive regulation of neuron differentiation Source: MGI
  19. positive regulation of protein kinase activity Source: MGI
  20. radial glia guided migration of Purkinje cell Source: MGI
  21. response to drug Source: Ensembl
  22. small GTPase mediated signal transduction Source: MGI
  23. ventral spinal cord development Source: UniProtKB
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:108554. Dab1.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. brush border Source: Ensembl
  3. cytosol Source: Ensembl
  4. intracellular Source: UniProtKB
  5. membrane Source: Ensembl
  6. neuronal cell body Source: Ensembl
  7. neuron projection Source: Ensembl
  8. postsynaptic density Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451K → A: Impairs binding to PtdIns(4,5)P2. 1 Publication
Mutagenesisi82 – 821K → A: Abolishes binding to PtdIns(4,5)P2. 1 Publication
Mutagenesisi114 – 1141S → T: Abolishes interaction with APLP1. 1 Publication
Mutagenesisi136 – 1361H → R: Greatly impairs interaction with APLP1. 1 Publication
Mutagenesisi158 – 1581F → V: Abolishes interaction with APLP1. 1 Publication
Mutagenesisi185 – 1851Y → 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. 1 Publication
Mutagenesisi198 – 1981Y → 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. 1 Publication
Mutagenesisi200 – 2001Y → 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. 1 Publication
Mutagenesisi220 – 2201Y → 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. 2 Publications
Mutagenesisi232 – 2321Y → 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. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Disabled homolog 1PRO_0000079769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphotyrosine2 Publications
Modified residuei220 – 2201Phosphotyrosine2 Publications
Modified residuei232 – 2321Phosphotyrosine2 Publications
Modified residuei524 – 5241Phosphoserine; by CDK51 Publication

Post-translational modificationi

Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons (PubMed:11279201). Also found phosphorylated on Tyr-232 upon reelin induction (PubMed:15062102). Also phosphorylated on Ser-524 independently of reelin signaling.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP97318.
PRIDEiP97318.

PTM databases

PhosphoSiteiP97318.

Expressioni

Tissue specificityi

Expressed mainly in brain.1 Publication

Gene expression databases

BgeeiP97318.
CleanExiMM_DAB1.
ExpressionAtlasiP97318. baseline and differential.
GenevestigatoriP97318.

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, LRP1, LRP8 and VLDLR. Interacts with APLP1 (via NPXY motif).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Aplp1Q031574EBI-81680,EBI-399929
AppP120233EBI-81680,EBI-78814
Dab2ipQ3UHC73EBI-81680,EBI-6306507
Lrp1Q91ZX72EBI-81680,EBI-300955
Lrp2A2ARV42EBI-81680,EBI-300875
Pcdh18Q8VHR02EBI-81680,EBI-399910
Siah1aP610923EBI-81680,EBI-446761

Protein-protein interaction databases

BioGridi199042. 14 interactions.
DIPiDIP-30902N.
IntActiP97318. 16 interactions.
MINTiMINT-258594.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 358Combined sources
Beta strandi40 – 5112Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 7619Combined sources
Turni77 – 793Combined sources
Beta strandi83 – 908Combined sources
Beta strandi93 – 986Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1085Combined sources
Helixi110 – 1123Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi137 – 1459Combined sources
Helixi148 – 16619Combined sources
Helixi170 – 1734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NTVX-ray1.50A23-174[»]
1NU2X-ray1.90A23-174[»]
1OQNX-ray2.30A/B25-183[»]
ProteinModelPortaliP97318.
SMRiP97318. Positions 23-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97318.

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

eggNOGiNOG313182.
GeneTreeiENSGT00520000055585.
HOVERGENiHBG018945.
InParanoidiP97318.
OMAiFQMAQPP.
OrthoDBiEOG7HQN7R.
PhylomeDBiP97318.
TreeFamiTF316724.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform DAB588 (identifier: P97318-1) [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
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 VYDVPKSQPN SQPLEDFESR
260 270 280 290 300
FAAATPNRNL SMDFDELLEA TKVSAVTQLE LFGDMSTPPD ITSPPTPATP
310 320 330 340 350
GDAFLPSSSQ TLPGSADVFG SMSFGTAAVP SGYVAMGAVL PSFWGQQPLV
360 370 380 390 400
QQQIAMGAQP PVAQVIPGAQ PIAWGQPGLF PATQQAWPTV AGQFPPAAFM
410 420 430 440 450
PTQTVMPLAA AMFQGPLTPL ATVPGTNDSA RSSPQSDKPR QKMGKESFKD
460 470 480 490 500
FQMVQPPPVP SRKPDQPSLT CTSEAFSSYF NKVGVAQDTD DCDDFDISQL
510 520 530 540 550
NLTPVTSTTP STNSPPTPAP RQSSPSKSSA SHVSDPTADD IFEEGFESPS
560 570 580
KSEEQEAPDG SQASSTSDPF GEPSGEPSGD NISPQDGS

Note: No experimental confirmation available.

Length:588
Mass (Da):63,578
Last modified:June 1, 1998 - v2
Checksum:i08404220792B1DB4
GO
Isoform DAB197 (identifier: P97318-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:197
Mass (Da):22,236
Checksum:i6AF789B4EC7FF6E9
GO
Isoform DAB204 (identifier: P97318-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-204: YIVFE → NLQKN
     205-588: Missing.

Note: No experimental confirmation available.

Show »
Length:204
Mass (Da):23,077
Checksum:i36271043EFC36BB4
GO
Isoform DAB217 (identifier: P97318-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-217: YIVFEAGHEPIRDPETEE → VISEPRQGFACSCEGSFD
     218-588: Missing.

Show »
Length:217
Mass (Da):24,394
Checksum:i17E7E398F5D1DC01
GO
Isoform DAB271 (identifier: P97318-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     240-272: Missing.
     275-304: AVTQLELFGDMSTPPDITSPPTPATPGDAF → SLVQSPAAERAEAESRTGPAEPGSILRPLG
     305-588: Missing.

Show »
Length:271
Mass (Da):30,296
Checksum:iFA4A8CE9812EB55C
GO
Isoform DAB553 (identifier: P97318-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-221: Missing.

Note: No experimental confirmation available.

Show »
Length:553
Mass (Da):59,415
Checksum:i8B281EE7C3CFD2F2
GO
Isoform DAB555 (identifier: P97318-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:555
Mass (Da):59,838
Checksum:i57A7130311954FE0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291A → R in BAB24163. (PubMed:16141072)Curated
Sequence conflicti239 – 2391P → PVS in CAM17685. (PubMed:19468303)Curated
Sequence conflicti239 – 2391P → PVS in CAM26758. (PubMed:19468303)Curated
Sequence conflicti248 – 2481E → D in CAM17685. (PubMed:19468303)Curated
Sequence conflicti248 – 2481E → D in CAM26758. (PubMed:19468303)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 2322STETE…SRKKG → LC in isoform DAB197. 1 PublicationVSP_026205Add
BLAST
Alternative sequencei187 – 22135Missing in isoform DAB553. CuratedVSP_026206Add
BLAST
Alternative sequencei200 – 21718YIVFE…PETEE → VISEPRQGFACSCEGSFD in isoform DAB197 and isoform DAB217. 2 PublicationsVSP_003841Add
BLAST
Alternative sequencei200 – 2045YIVFE → NLQKN in isoform DAB204. CuratedVSP_026208
Alternative sequencei205 – 588384Missing in isoform DAB204. CuratedVSP_026209Add
BLAST
Alternative sequencei218 – 588371Missing in isoform DAB197 and isoform DAB217. 2 PublicationsVSP_003842Add
BLAST
Alternative sequencei240 – 27233Missing in isoform DAB555 and isoform DAB271. 1 PublicationVSP_003843Add
BLAST
Alternative sequencei275 – 30430AVTQL…PGDAF → SLVQSPAAERAEAESRTGPA EPGSILRPLG in isoform DAB271. 1 PublicationVSP_003844Add
BLAST
Alternative sequencei305 – 588284Missing in isoform DAB271. 1 PublicationVSP_003845Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18413.1. [P97318-2]
RefSeqiNP_034144.1. NM_010014.3. [P97318-6]
NP_796233.2. NM_177259.4. [P97318-2]
XP_006502794.1. XM_006502731.1. [P97318-2]
UniGeneiMm.289682.

Genome annotation databases

EnsembliENSMUST00000106826; ENSMUSP00000102439; ENSMUSG00000028519. [P97318-4]
ENSMUST00000106827; ENSMUSP00000102440; ENSMUSG00000028519. [P97318-5]
ENSMUST00000106830; ENSMUSP00000102443; ENSMUSG00000028519. [P97318-2]
GeneIDi13131.
KEGGimmu:13131.
UCSCiuc008txu.1. mouse. [P97318-5]
uc008txv.1. mouse. [P97318-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS18413.1. [P97318-2 ]
RefSeqi NP_034144.1. NM_010014.3. [P97318-6 ]
NP_796233.2. NM_177259.4. [P97318-2 ]
XP_006502794.1. XM_006502731.1. [P97318-2 ]
UniGenei Mm.289682.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NTV X-ray 1.50 A 23-174 [» ]
1NU2 X-ray 1.90 A 23-174 [» ]
1OQN X-ray 2.30 A/B 25-183 [» ]
ProteinModelPortali P97318.
SMRi P97318. Positions 23-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199042. 14 interactions.
DIPi DIP-30902N.
IntActi P97318. 16 interactions.
MINTi MINT-258594.

PTM databases

PhosphoSitei P97318.

Proteomic databases

MaxQBi P97318.
PRIDEi P97318.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000106826 ; ENSMUSP00000102439 ; ENSMUSG00000028519 . [P97318-4 ]
ENSMUST00000106827 ; ENSMUSP00000102440 ; ENSMUSG00000028519 . [P97318-5 ]
ENSMUST00000106830 ; ENSMUSP00000102443 ; ENSMUSG00000028519 . [P97318-2 ]
GeneIDi 13131.
KEGGi mmu:13131.
UCSCi uc008txu.1. mouse. [P97318-5 ]
uc008txv.1. mouse. [P97318-6 ]

Organism-specific databases

CTDi 1600.
MGIi MGI:108554. Dab1.

Phylogenomic databases

eggNOGi NOG313182.
GeneTreei ENSGT00520000055585.
HOVERGENi HBG018945.
InParanoidi P97318.
OMAi FQMAQPP.
OrthoDBi EOG7HQN7R.
PhylomeDBi P97318.
TreeFami TF316724.

Miscellaneous databases

ChiTaRSi Dab1. mouse.
EvolutionaryTracei P97318.
NextBioi 283176.
PROi P97318.
SOURCEi Search...

Gene expression databases

Bgeei P97318.
CleanExi MM_DAB1.
ExpressionAtlasi P97318. baseline and differential.
Genevestigatori P97318.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view ]
Pfami PF00640. PID. 1 hit.
[Graphical view ]
SMARTi SM00462. PTB. 1 hit.
[Graphical view ]
PROSITEi PS01179. PID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiDAB1_MOUSE
AccessioniPrimary (citable) accession number: P97318
Secondary accession number(s): A2A963
, A2A964, A2A965, A2A966, A2A967, A2A970, P97316, P97317, Q9DAP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3