P97318 (DAB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disabled homolog 1

Gene names

Name:

Dab1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Neurogenesis
Coding sequence diversity	Alternative splicing
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi 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 cerebellum structural organization Inferred from mutant phenotype PubMed 9338785. Source: MGI dendrite development Inferred from mutant phenotype PubMed 14715136. Source: MGI intracellular protein kinase cascade Traceable author statement PubMed 10460257. Source: UniProtKB midgut development Inferred from electronic annotation. Source: Compara 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 neuron migration Inferred from mutant phenotype PubMed 20711475. Source: UniProtKB 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: Compara 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_component	apical part of cell Inferred from electronic annotation. Source: Compara brush border Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara intracellular Traceable author statement PubMed 10460257. Source: UniProtKB membrane Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	SH2 domain binding Traceable author statement PubMed 11716507. Source: UniProtKB phospholipid binding Traceable author statement PubMed 11716507. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Aplp1	Q03157	4	EBI-81680,EBI-399929
App	P12023	3	EBI-81680,EBI-78814
Dab2ip	Q3UHC7	3	EBI-81680,EBI-6306507
Lrp1	Q91ZX7	2	EBI-81680,EBI-300955
Lrp2	A2ARV4	2	EBI-81680,EBI-300875
Pcdh18	Q8VHR0	2	EBI-81680,EBI-399910
Siah1a	P61092	3	EBI-81680,EBI-446761

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 588

588

Disabled homolog 1

PRO_0000079769

Regions

Domain

36 – 189

154

PID

Amino acid modifications

Modified residue

198

1

Phosphotyrosine Ref.4 Ref.5

Modified residue

220

1

Phosphotyrosine Ref.5 Ref.8

Modified residue

232

1

Phosphotyrosine Ref.4 Ref.8

Modified residue

524

1

Phosphoserine; by CDK5 Ref.6

Natural variations

Alternative sequence

2 – 23

22

STETE…SRKKG → LC in isoform DAB197.

VSP_026205

Alternative sequence

187 – 221

35

Missing in isoform DAB553.

VSP_026206

Alternative sequence

200 – 217

18

YIVFE…PETEE → VISEPRQGFACSCEGSFD in isoform DAB197 and isoform DAB217.

VSP_003841

Alternative sequence

200 – 204

5

YIVFE → NLQKN in isoform DAB204.

VSP_026208

Alternative sequence

205 – 588

384

Missing in isoform DAB204.

VSP_026209

Alternative sequence

218 – 588

371

Missing in isoform DAB197 and isoform DAB217.

VSP_003842

Alternative sequence

240 – 272

33

Missing in isoform DAB555 and isoform DAB271.

VSP_003843

Alternative sequence

275 – 304

30

AVTQL…PGDAF → SLVQSPAAERAEAESRTGPA EPGSILRPLG in isoform DAB271.

VSP_003844

Alternative sequence

305 – 588

284

Missing in isoform DAB271.

VSP_003845

Experimental info

Mutagenesis

45

1

K → A: Impairs binding to PtdIns(4,5)P2. Ref.9

Mutagenesis

82

1

K → A: Abolishes binding to PtdIns(4,5)P2. Ref.9

Mutagenesis

114

1

S → T: Abolishes interaction with APLP1. Ref.9

Mutagenesis

136

1

H → R: Greatly impairs interaction with APLP1. Ref.9

Mutagenesis

158

1

F → V: Abolishes interaction with APLP1. Ref.9

Mutagenesis

185

1

Y → 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

Mutagenesis

198

1

Y → 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

Mutagenesis

200

1

Y → 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

Mutagenesis

220

1

Y → 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

Mutagenesis

232

1

Y → 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 conflict

29

1

A → R in BAB24163. Ref.2

Sequence conflict

239

1

P → PVS in CAM17685. Ref.3

Sequence conflict

239

1

P → PVS in CAM26758. Ref.3

Sequence conflict

248

1

E → D in CAM17685. Ref.3

Sequence conflict

248

1

E → D in CAM26758. Ref.3

Secondary structure

1

.

.

.

.

.

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.

.

.

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.

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.

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.

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588

Helix Strand Turn

Details...

Helix

28 – 35

8

Beta strand

40 – 51

12

Beta strand

53 – 55

3

Helix

58 – 76

19

Turn

77 – 79

3

Beta strand

83 – 90

8

Beta strand

93 – 98

6

Turn

99 – 101

3

Beta strand

104 – 108

5

Helix

110 – 112

3

Beta strand

113 – 118

6

Beta strand

125 – 132

8

Beta strand

137 – 145

9

Helix

148 – 166

19

Helix

170 – 173

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform DAB588 [UniParc]. Last modified June 1, 1998. Version 2. Checksum: 08404220792B1DB4	FASTA	588	63,578
	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
	Isoform DAB197 [UniParc]. Checksum: 6AF789B4EC7FF6E9	FASTA	197	22,236
	10 20 30 40 50 60 MLCQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL CQDSMMKLKG VVAGARSKGE 70 80 90 100 110 120 HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI TDHRAFGYVC GKEGNHRFVA 130 140 150 160 170 180 IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC EQAVYQTILE EDVEDPVYQV 190 ISEPRQGFAC SCEGSFD
	Isoform DAB204 [UniParc]. Checksum: 36271043EFC36BB4	FASTA	204	23,077
	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 EQAVYQTILE EDVEDPVYQN LQKN
	Isoform DAB217 [UniParc]. Checksum: 17E7E398F5D1DC01	FASTA	217	24,394
	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 EQAVYQTILE EDVEDPVYQV ISEPRQGFAC SCEGSFD
	Isoform DAB271 [UniParc]. Checksum: FA4A8CE9812EB55C	FASTA	271	30,296
	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 VYDVPKSQPV 250 260 270 SSLVQSPAAE RAEAESRTGP AEPGSILRPL G
	Isoform DAB553 [UniParc]. Checksum: 8B281EE7C3CFD2F2	FASTA	553	59,415
	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 EQAVYQVPTS QKKEGVYDVP KSQPNSQPLE DFESRFAAAT PNRNLSMDFD ELLEATKVSA 250 260 270 280 290 300 VTQLELFGDM STPPDITSPP TPATPGDAFL PSSSQTLPGS ADVFGSMSFG TAAVPSGYVA 310 320 330 340 350 360 MGAVLPSFWG QQPLVQQQIA MGAQPPVAQV IPGAQPIAWG QPGLFPATQQ AWPTVAGQFP 370 380 390 400 410 420 PAAFMPTQTV MPLAAAMFQG PLTPLATVPG TNDSARSSPQ SDKPRQKMGK ESFKDFQMVQ 430 440 450 460 470 480 PPPVPSRKPD QPSLTCTSEA FSSYFNKVGV AQDTDDCDDF DISQLNLTPV TSTTPSTNSP 490 500 510 520 530 540 PTPAPRQSSP SKSSASHVSD PTADDIFEEG FESPSKSEEQ EAPDGSQASS TSDPFGEPSG 550 EPSGDNISPQ DGS
	Isoform DAB555 [UniParc]. Checksum: 57A7130311954FE0	FASTA	555	59,838
	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 VYDVPKSQPV 250 260 270 280 290 300 SAVTQLELFG DMSTPPDITS PPTPATPGDA FLPSSSQTLP GSADVFGSMS FGTAAVPSGY 310 320 330 340 350 360 VAMGAVLPSF WGQQPLVQQQ IAMGAQPPVA QVIPGAQPIA WGQPGLFPAT QQAWPTVAGQ 370 380 390 400 410 420 FPPAAFMPTQ TVMPLAAAMF QGPLTPLATV PGTNDSARSS PQSDKPRQKM GKESFKDFQM 430 440 450 460 470 480 VQPPPVPSRK PDQPSLTCTS EAFSSYFNKV GVAQDTDDCD DFDISQLNLT PVTSTTPSTN 490 500 510 520 530 540 SPPTPAPRQS SPSKSSASHV SDPTADDIFE EGFESPSKSE EQEAPDGSQA SSTSDPFGEP 550 SGEPSGDNIS PQDGS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00123898.
IPI00230573.
IPI00230574.
IPI00230575.
IPI00750727.
IPI00849536.
IPI00850021.

RefSeq

NP_034144.1. NM_010014.2.
NP_796233.2. NM_177259.3.

UniGene

Mm.289682.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P97318.

SMR

P97318. Positions 23-174.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30902N.

IntAct

P97318. 15 interactions.

MINT

MINT-258594.

PTM databases

PhosphoSite

P97318.

Proteomic databases

PRIDE

P97318.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000106826; ENSMUSP00000102439; ENSMUSG00000028519.
ENSMUST00000106827; ENSMUSP00000102440; ENSMUSG00000028519.
ENSMUST00000106830; ENSMUSP00000102443; ENSMUSG00000028519.
ENSMUST00000143644; ENSMUSP00000118650; ENSMUSG00000028519.

GeneID

13131.

KEGG

mmu:13131.

UCSC

uc008txu.1. mouse.
uc008txv.1. mouse.

Organism-specific databases

CTD

1600.

MGI

MGI:108554. Dab1.

Phylogenomic databases

eggNOG

NOG313182.

GeneTree

ENSGT00520000055585.

HOVERGEN

HBG018945.

InParanoid

P97318.

OMA

AAFMPTQ.

OrthoDB

EOG4TB4BG.

Gene expression databases

ArrayExpress

P97318.

Bgee

P97318.

CleanEx

MM_DAB1.

Genevestigator

P97318.

GermOnline

ENSMUSG00000028519. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR006020. PTyr_interaction_dom.
[Graphical view]

Pfam

PF00640. PID. 1 hit.
[Graphical view]

SMART

SM00462. PTB. 1 hit.
[Graphical view]

PROSITE

PS01179. PID. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DAB1. mouse.

EvolutionaryTrace

P97318.

NextBio

283176.

SOURCE

Search...

Entry information

Entry name

DAB1_MOUSE

Accession

Primary (citable) accession number: P97318
Secondary accession number(s): A2A963 , 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 3, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program