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O75553 (DAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity.

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. Ref.7

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 By similarity. Also phosphorylated on Ser-524 independently of reelin signaling By similarity.

Sequence similarities

Contains 1 PID domain.

Sequence caution

The sequence BAE06094.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from electronic annotation. Source: Ensembl

adult walking behavior

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

cerebellum structural organization

Inferred from electronic annotation. Source: Ensembl

dendrite development

Inferred from electronic annotation. Source: Ensembl

lateral motor column neuron migration

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

negative regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

radial glia guided migration of Purkinje cell

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

ventral spinal cord development

Inferred from electronic annotation. Source: Ensembl

   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

membrane

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform DAB588 (identifier: O75553-1)

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 DAB213 (identifier: O75553-2)

The sequence of this isoform differs from the canonical sequence as follows:
     200-213: YIVFEAGHEPIRDP → VISETSRGFRFKSD
     214-588: Missing.
Note: No experimental confirmation available.
Isoform DAB469 (identifier: O75553-3)

The sequence of this isoform differs from the canonical sequence as follows:
     103-221: Missing.
Note: No experimental confirmation available.
Isoform DAB537 (identifier: O75553-4)

The sequence of this isoform differs from the canonical sequence as follows:
     185-219: Missing.
     259-274: Missing.
Note: No experimental confirmation available.
Isoform DAB553 (identifier: O75553-5)

The sequence of this isoform differs from the canonical sequence as follows:
     185-219: Missing.
Note: No experimental confirmation available.
Isoform DAB555 (identifier: O75553-6)

The sequence of this isoform differs from the canonical sequence as follows:
     242-274: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Disabled homolog 1
PRO_0000079767

Regions

Domain36 – 189154PID

Amino acid modifications

Modified residue1981Phosphotyrosine By similarity
Modified residue2201Phosphotyrosine By similarity
Modified residue2321Phosphotyrosine By similarity
Modified residue5241Phosphoserine; by CDK5 By similarity

Natural variations

Alternative sequence103 – 221119Missing in isoform DAB469.
VSP_026166
Alternative sequence185 – 21935Missing in isoform DAB553 and isoform DAB537.
VSP_026167
Alternative sequence200 – 21314YIVFE…PIRDP → VISETSRGFRFKSD in isoform DAB213.
VSP_026168
Alternative sequence214 – 588375Missing in isoform DAB213.
VSP_026169
Alternative sequence242 – 27433Missing in isoform DAB555.
VSP_026170
Alternative sequence259 – 27416Missing in isoform DAB537.
VSP_026171
Natural variant711V → I.
Corresponds to variant rs1855377 [ dbSNP | Ensembl ].
VAR_056857

Experimental info

Sequence conflict151A → T in AAI12939. Ref.6
Sequence conflict591K → M in AAH67447. Ref.6
Sequence conflict861F → L in AAF73058. Ref.2
Sequence conflict2951P → S in AAH67447. Ref.6
Sequence conflict3241F → L in AAC70068. Ref.1
Sequence conflict3311S → P in AAC70068. Ref.1
Sequence conflict3591Q → H in AAC70068. Ref.1
Sequence conflict3681G → R in AAF73058. Ref.2
Sequence conflict4121M → V in AAF73058. Ref.2
Sequence conflict5861A → D in AAC70068. Ref.1

Sequences

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

Last modified June 26, 2007. Version 3.
Checksum: DAD4024364113AC5

FASTA58863,775
        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 
SNGYSFEDFE ERFAAATPNR NLPTDFDEIF EATKAVTQLE LFGDMSTPPD ITSPPTPATP 

       310        320        330        340        350        360 
GDAFIPSSSQ TLPASADVFS SVPFGTAAVP SGYVAMGAVL PSFWGQQPLV QQQMVMGAQP 

       370        380        390        400        410        420 
PVAQVMPGAQ PIAWGQPGLF PATQQPWPTV AGQFPPAAFM PTQTVMPLPA AMFQGPLTPL 

       430        440        450        460        470        480 
ATVPGTSDST RSSPQTDKPR QKMGKETFKD FQMAQPPPVP SRKPDQPSLT CTSEAFSSYF 

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

       550        560        570        580 
IFEEGFESPS KSEEQEAPDG SQASSNSDPF GEPSGEPSGD NISPQAGS 

« Hide

Isoform DAB213 [UniParc].

Checksum: 9A3ADE86341D96E1
Show »

FASTA21324,091
Isoform DAB469 [UniParc].

Checksum: 5A03F93BDB4BAF42
Show »

FASTA46949,856
Isoform DAB537 [UniParc].

Checksum: 6626BD99FE7C098C
Show »

FASTA53757,720
Isoform DAB553 [UniParc].

Checksum: 59BC5E84DEF5F583
Show »

FASTA55359,612
Isoform DAB555 [UniParc].

Checksum: 9EB4FC3D31BBF8CB
Show »

FASTA55559,950

References

« Hide 'large scale' references
[1]"Cloning of human DAB1 and mapping to chromosome 1p31-p32."
Lambert de Rouvroit C., Goffinet A.M.
Genomics 53:246-247(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DAB555).
[2]"Aberrant disabled-1 expression in tumors."
Fazili Z., Sun W., Xu X.-X.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DAB555).
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DAB555).
Tissue: Brain.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DAB469; DAB537 AND DAB553).
[7]"Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules."
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.
J. Biol. Chem. 279:40536-40544(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071062 mRNA. Translation: AAC70068.1.
AF263547 mRNA. Translation: AAF73058.1.
AL139219, AL354883 Genomic DNA. Translation: CAI19217.1.
AL139219, AL161740, AL354883 Genomic DNA. Translation: CAI19218.1.
AL139219, AL161740, AL354883 Genomic DNA. Translation: CAI19219.1.
AL139219, AL354883 Genomic DNA. Translation: CAI19220.1.
AL139219, AL161740, AL354883 Genomic DNA. Translation: CAI19221.1.
AL161740, AL139219, AL354883 Genomic DNA. Translation: CAI18815.1.
AL161740, AL139219, AL354883 Genomic DNA. Translation: CAI18816.1.
AL161740, AL139219, AL354883 Genomic DNA. Translation: CAI18817.1.
AL354883, AL139219 Genomic DNA. Translation: CAI22360.1.
AL354883, AL139219, AL161740 Genomic DNA. Translation: CAI22361.1.
AL354883, AL139219, AL161740 Genomic DNA. Translation: CAI22362.1.
AL354883, AL139219 Genomic DNA. Translation: CAI22363.1.
AL354883, AL139219, AL161740 Genomic DNA. Translation: CAI22364.1.
AK095513 mRNA. Translation: BAG53075.1.
AB210012 mRNA. Translation: BAE06094.1. Different initiation.
CH471059 Genomic DNA. Translation: EAX06637.1.
BC067445 mRNA. Translation: AAH67445.1.
BC067446 mRNA. Translation: AAH67446.1.
BC067447 mRNA. Translation: AAH67447.1.
BC112938 mRNA. Translation: AAI12939.1.
CCDSCCDS607.1. [O75553-6]
RefSeqNP_066566.3. NM_021080.3. [O75553-6]
UniGeneHs.477370.

3D structure databases

ProteinModelPortalO75553.
SMRO75553. Positions 23-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107970. 17 interactions.
IntActO75553. 2 interactions.
MINTMINT-156038.

PTM databases

PhosphoSiteO75553.

Proteomic databases

PaxDbO75553.
PRIDEO75553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371230; ENSP00000360274; ENSG00000173406. [O75553-2]
ENST00000371231; ENSP00000360275; ENSG00000173406. [O75553-1]
ENST00000371234; ENSP00000360278; ENSG00000173406. [O75553-6]
ENST00000371236; ENSP00000360280; ENSG00000173406. [O75553-6]
ENST00000414851; ENSP00000387581; ENSG00000173406. [O75553-4]
ENST00000420954; ENSP00000395296; ENSG00000173406. [O75553-5]
ENST00000439789; ENSP00000409328; ENSG00000173406. [O75553-3]
GeneID1600.
KEGGhsa:1600.
UCSCuc001cyq.1. human. [O75553-5]
uc001cyr.1. human. [O75553-3]
uc001cys.1. human. [O75553-6]
uc001cyt.1. human. [O75553-1]
uc009vzw.1. human. [O75553-4]

Organism-specific databases

CTD1600.
GeneCardsGC01M057460.
HGNCHGNC:2661. DAB1.
HPACAB032329.
MIM603448. gene.
neXtProtNX_O75553.
PharmGKBPA27131.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313182.
HOVERGENHBG018945.
InParanoidO75553.
OMAFQMAQPP.
OrthoDBEOG7HQN7R.
PhylomeDBO75553.
TreeFamTF316724.

Enzyme and pathway databases

SignaLinkO75553.

Gene expression databases

ArrayExpressO75553.
BgeeO75553.
GenevestigatorO75553.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamPF00640. PID. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
[Graphical view]
PROSITEPS01179. PID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAB1. human.
GeneWikiDAB1.
GenomeRNAi1600.
NextBio6562.
PROO75553.
SOURCESearch...

Entry information

Entry nameDAB1_HUMAN
AccessionPrimary (citable) accession number: O75553
Secondary accession number(s): A4FU90 expand/collapse secondary AC list , B3KTG3, Q4LE59, Q5T6M6, Q5T6M9, Q5T835, Q5T836, Q5T837, Q6NWS9, Q6NWT0, Q6NWT1, Q9NYA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM