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Q5VWQ8 (DAB2P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disabled homolog 2-interacting protein

Short name=DAB2 interaction protein
Short name=DAB2-interacting protein
Alternative name(s):
ASK-interacting protein 1
Gene names
Name:DAB2IP
Synonyms:AF9Q34, AIP1, KIAA1743
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1189 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a Ras GTPase-activating protein By similarity. Through its interaction with MAP3K5 disrupts the association of MAP3K5 with the inhibitory 14-3-3 complex. Mediates TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. May act as a tumor suppressor gene. Ref.8

Subunit structure

Interacts with MAP3K5, preferentially with its 'Ser-966' dephosphorylated form. On plasma membrane, exists in an inactive form complexed with TNFR1. In response to TNF, dissociates from TNFR1 complex, tranlocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Binding to MAP3K5 is induced by TNF. Interacts with DAB1 and DAB2 By similarity. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF. This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Ref.8 Ref.9 Ref.10

Subcellular location

Membrane. Cytoplasm. Note: Translocates to the cytoplasm in response to TNF. Ref.9 Ref.10

Tissue specificity

Low expression in prostate. Down-regulated in prostate cancer. Ref.1

Domain

The C2 and Ras-GAP domains are required for the interaction with MAP3K5.

Involvement in disease

A chromosomal aberration involving DAB2IP is found in a patient with acute myeloid leukemia (AML). Translocation t(9;11)(q34;q23) with MLL. May give rise to a MLL-DAB2IP fusion protein lacking the PH domain.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PH domain.

Contains 1 Ras-GAP domain.

Sequence caution

The sequence CAH72155.3 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseTumor suppressor
   DomainCoiled coil
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Inferred from direct assay Ref.8. Source: BHF-UCL

cellular protein catabolic process

Inferred from direct assay PubMed 17389591. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity PubMed 11812785. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from direct assay PubMed 17389591. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity PubMed 18281285. Source: BHF-UCL

negative regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from direct assay PubMed 17389591. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from direct assay Ref.8. Source: BHF-UCL

negative regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 20154697. Source: BHF-UCL

negative regulation of Ras GTPase activity

Inferred from mutant phenotype PubMed 20154697. Source: BHF-UCL

negative regulation of Ras protein signal transduction

Inferred by curator PubMed 20154697. Source: BHF-UCL

negative regulation of canonical Wnt receptor signaling pathway

Inferred from mutant phenotype PubMed 20080667. Source: BHF-UCL

negative regulation of catenin import into nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity PubMed 11812785. Source: BHF-UCL

negative regulation of epithelial cell migration

Traceable author statement PubMed 20080667. Source: BHF-UCL

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 20154697. Source: BHF-UCL

negative regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 20080667. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: BHF-UCL

positive regulation of JNK cascade

Inferred from direct assay PubMed 17389591. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 17389591. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17389591. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: BHF-UCL

intrinsic to internal side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function14-3-3 protein binding

Inferred from direct assay PubMed 17389591. Source: BHF-UCL

Ras GTPase activator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

phospholipid binding

Inferred from electronic annotation. Source: InterPro

protein phosphatase 2A binding

Inferred from direct assay PubMed 20080667. Source: BHF-UCL

signaling adaptor activity

Inferred from direct assay PubMed 20080667. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5VWQ8-1)

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: Gene prediction based on EST data.
Isoform 2 (identifier: Q5VWQ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.
Isoform 3 (identifier: Q5VWQ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-193: Missing.
     1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH
Isoform 4 (identifier: Q5VWQ8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.
     1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11891189Disabled homolog 2-interacting protein
PRO_0000252407

Regions

Domain101 – 202102PH
Domain200 – 29596C2
Domain371 – 563193Ras-GAP
Coiled coil1026 – 1159134 Potential
Compositional bias8 – 5245Arg-rich
Compositional bias112 – 1176Poly-Ala
Compositional bias867 – 8704Poly-Ala
Compositional bias903 – 94846Pro-rich

Sites

Site172 – 1732Breakpoint for translocation to form MLL-DAB2IP

Amino acid modifications

Modified residue7021Phosphoserine By similarity
Modified residue9781Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 193193Missing in isoform 3.
VSP_020952
Alternative sequence1 – 124124Missing in isoform 2 and isoform 4.
VSP_020953
Alternative sequence1158 – 118932RYSMQ…NSSNC → SMH in isoform 3 and isoform 4.
VSP_020954
Natural variant591S → F.
Corresponds to variant rs7027492 [ dbSNP | Ensembl ].
VAR_056858

Experimental info

Mutagenesis228 – 2303KKK → AAA: No effect on binding to MAP3K5. Ref.8
Mutagenesis281 – 2844KKKK → AAAA: Significantly reduced binding to MAP3K5. Ref.8
Mutagenesis4131R → L: No effect on binding to MAP3K5. Ref.8
Sequence conflict4821I → T in AAM00371. Ref.1
Sequence conflict9211P → S in AAM00371. Ref.1
Sequence conflict1091 – 10922QQ → HE in AAM00371. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 7494FF05AACF3320

FASTA1,189131,625
        10         20         30         40         50         60 
MSAGGSARKS TGRSSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS RRSLPGSLSE 

        70         80         90        100        110        120 
KSPSMEPSAA TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH SFRHILPGFR SAAAAAADNE 

       130        140        150        160        170        180 
RSHLMPRLKE SRSHESLLSP SSAVEALDLS MEEEVVIKPV HSSILGQDYC FEVTTSSGSK 

       190        200        210        220        230        240 
CFSCRSAAER DKWMENLRRA VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV 

       250        260        270        280        290        300 
LYARTTGKLK TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS 

       310        320        330        340        350        360 
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTITIL PMEMYKEFAE HITNHYLGLC 

       370        380        390        400        410        420 
AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE VDRCGDNEHL IFRENTLATK 

       430        440        450        460        470        480 
AIEEYLKLVG QKYLQDALGE FIKALYESDE NCEVDPSKCS AADLPEHQGN LKMCCELAFC 

       490        500        510        520        530        540 
KIINSYCVFP RELKEVFASW RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ 

       550        560        570        580        590        600 
EYPDDRTART LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET 

       610        620        630        640        650        660 
LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LEQSIVSKLG PLPRILRDVH TALSTPGSGQ 

       670        680        690        700        710        720 
LPGTNDLAST PGSGSSSISA GLQKMVIEND LSGLIDFTRL PSPTPENKDL FFVTRSSGVQ 

       730        740        750        760        770        780 
PSPARSSSYS EANEPDLQMA NGGKSLSMVD LQDARTLDGE AGSPAGPDVL PTDGQAAAAQ 

       790        800        810        820        830        840 
LVAGWPARAT PVNLAGLATV RRAGQTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP 

       850        860        870        880        890        900 
LSPRGLGDSG SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG 

       910        920        930        940        950        960 
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPNLL STLQYPRPSS GTLASASPDW 

       970        980        990       1000       1010       1020 
VGPSTRLRQQ SSSSKGDSPE LKPRAVHKQG PSPVSPNALD RTAAWLLTMN AQLLEDEGLG 

      1030       1040       1050       1060       1070       1080 
PDPPHRDRLR SKDELSQAEK DLAVLQDKLR ISTKKLEEYE TLFKCQEETT QKLVLEYQAR 

      1090       1100       1110       1120       1130       1140 
LEEGEERLRR QQEDKDIQMK GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS 

      1150       1160       1170       1180 
LDAANARLMS ALTQLKERYS MQARNGISPT NPTKLQITEN GEFRNSSNC 

« Hide

Isoform 2 [UniParc].

Checksum: 4787F41F02108AA3
Show »

FASTA1,065117,651
Isoform 3 [UniParc].

Checksum: E69CEB1FB00A2219
Show »

FASTA967106,764
Isoform 4 [UniParc].

Checksum: 1B07D8D3B9DEA76A
Show »

FASTA1,036114,410

References

« Hide 'large scale' references
[1]"Differential regulation of the human gene DAB2IP in normal and malignant prostatic epithelia: cloning and characterization."
Chen H., Pong R.-C., Wang Z., Hsieh J.-T.
Genomics 79:573-581(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
[2]"Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia."
von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S., Falkenburg J.H.F., Kluin P.M., Schuuring E.
Genes Chromosomes Cancer 39:324-334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH MLL.
[3]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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] (ISOFORM 4).
[8]"AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3."
Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.
J. Clin. Invest. 111:1933-1943(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K5, MUTAGENESIS OF 228-LYS--LYS-230; 281-LYS--LYS-284 AND ARG-413.
[9]"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TNFR1; MAP3K5; TRADD; RALBP1 AND TRAF2.
[10]"Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation."
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF367051 mRNA. Translation: AAM00371.1.
AY032952 mRNA. Translation: AAK50336.1.
AB051530 mRNA. Translation: BAB21834.2.
AL365274 Genomic DNA. Translation: CAH72155.3. Sequence problems.
AL365274 Genomic DNA. Translation: CAQ10385.1.
AL365274 Genomic DNA. Translation: CAH72158.1.
CH471090 Genomic DNA. Translation: EAW87503.1.
BC146762 mRNA. Translation: AAI46763.1.
IPIIPI00045600.
IPI00646394.
IPI00789361.
IPI00914911.
RefSeqNP_115941.2. NM_032552.2.
NP_619723.1. NM_138709.1.
UniGeneHs.522378.

3D structure databases

HSSPHSSP built from PDB template 1NF1 based on UniProtKB P21359.
ProteinModelPortalQ5VWQ8.
ModBaseSearch...

Protein-protein interaction databases

IntActQ5VWQ8. 1 interaction.
MINTMINT-268247.
STRING9606.ENSP00000259371.

PTM databases

PhosphoSiteQ5VWQ8.

Polymorphism databases

DMDM116247768.

Proteomic databases

PaxDbQ5VWQ8.
PRIDEQ5VWQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309989; ENSP00000310827; ENSG00000136848.
ENST00000408936; ENSP00000386183; ENSG00000136848.
GeneID153090.
KEGGhsa:153090.
UCSCuc004bln.3. human.

Organism-specific databases

CTD153090.
GeneCardsGC09P124329.
HGNCHGNC:17294. DAB2IP.
HPAHPA036977.
MIM609205. gene.
neXtProtNX_Q5VWQ8.
PharmGKBPA27133.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245428.
HOVERGENHBG006492.
InParanoidQ5VWQ8.
OMACAALEPI.
OrthoDBEOG473PQJ.

Gene expression databases

ArrayExpressQ5VWQ8.
BgeeQ5VWQ8.
CleanExHS_DAB2IP.
GenevestigatorQ5VWQ8.
GermOnlineENSG00000136848. Homo sapiens.

Family and domain databases

Gene3D1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR021887. DUF3498.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF12004. DUF3498. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF48350. Rho_GAP. 1 hit.
PROSITEPS50004. C2. False negative.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAB2IP. human.
GenomeRNAi153090.
NextBio87071.
SOURCESearch...

Entry information

Entry nameDAB2P_HUMAN
AccessionPrimary (citable) accession number: Q5VWQ8
Secondary accession number(s): A6H8V2 expand/collapse secondary AC list , A6NHI9, B0QZB1, Q8TDL2, Q96SE1, Q9C0C0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 87 of the entry and version 2 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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families