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Q86T65 (DAAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disheveled-associated activator of morphogenesis 2
Gene names
Name:DAAM2
Synonyms:KIAA0381
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1068 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Tissue specificity

Expressed in most tissues examined.

Sequence similarities

Belongs to the formin homology family.

Contains 1 DAD (diaphanous autoregulatory) domain.

Contains 1 FH1 (formin homology 1) domain.

Contains 1 FH2 (formin homology 2) domain.

Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Sequence caution

The sequence BAA20835.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

   Molecular functionRho GTPase binding

Inferred from electronic annotation. Source: InterPro

actin binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10681068Disheveled-associated activator of morphogenesis 2
PRO_0000194909

Regions

Domain40 – 416377GBD/FH3
Domain518 – 59477FH1
Domain595 – 994400FH2
Domain1016 – 104833DAD
Coiled coil434 – 51683 Potential
Compositional bias518 – 60487Pro-rich

Natural variations

Natural variant1051R → H.
Corresponds to variant rs6919807 [ dbSNP | Ensembl ].
VAR_055805
Natural variant6171R → H.
Corresponds to variant rs34699846 [ dbSNP | Ensembl ].
VAR_055806

Experimental info

Sequence conflict4141R → W in CAD89973. Ref.3
Sequence conflict8941Missing in CAD89973. Ref.3
Sequence conflict9011Q → R in CAD89973. Ref.3
Sequence conflict10031R → W in CAD89973. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q86T65 [UniParc].

Last modified April 26, 2005. Version 3.
Checksum: 90B071DD1BC13F9A

FASTA1,068123,499
        10         20         30         40         50         60 
MAPRKRSHHG LGFLCCFGGS DIPEINLRDN HPLQFMEFSS PIPNAEELNI RFAELVDELD 

        70         80         90        100        110        120 
LTDKNREAMF ALPPEKKWQI YCSKKKEQED PNKLATSWPD YYIDRINSMA AMQSLYAFDE 

       130        140        150        160        170        180 
EETEMRNQVV EDLKTALRTQ PMRFVTRFIE LEGLTCLLNF LRSMDHATCE SRIHTSLIGC 

       190        200        210        220        230        240 
IKALMNNSQG RAHVLAQPEA ISTIAQSLRT ENSKTKVAVL EILGAVCLVP GGHKKVLQAM 

       250        260        270        280        290        300 
LHYQVYAAER TRFQTLLNEL DRSLGRYRDE VNLKTAIMSF INAVLNAGAG EDNLEFRLHL 

       310        320        330        340        350        360 
RYEFLMLGIQ PVIDKLRQHE NAILDKHLDF FEMVRNEDDL ELARRFDMVH IDTKSASQMF 

       370        380        390        400        410        420 
ELIHKKLKYT EAYPCLLSVL HHCLQMPYKR NGGYFQQWQL LDRILQQIVL QDERGVDPDL 

       430        440        450        460        470        480 
APLENFNVKN IVNMLINENE VKQWRDQAEK FRKEHMELVS RLERKERECE TKTLEKEEMM 

       490        500        510        520        530        540 
RTLNKMKDKL ARESQELRQA RGQVAELVAQ LSELSTGPVS SPPPPGGPLT LSSSMTTNDL 

       550        560        570        580        590        600 
PPPPPPLPFA CCPPPPPPPL PPGGPPTPPG APPCLGMGLP LPQDPYPSSD VPLRKKRVPQ 

       610        620        630        640        650        660 
PSHPLKSFNW VKLNEERVPG TVWNEIDDMQ VFRILDLEDF EKMFSAYQRH QKELGSTEDI 

       670        680        690        700        710        720 
YLASRKVKEL SVIDGRRAQN CIILLSKLKL SNEEIRQAIL KMDEQEDLAK DMLEQLLKFI 

       730        740        750        760        770        780 
PEKSDIDLLE EHKHEIERMA RADRFLYEMS RIDHYQQRLQ ALFFKKKFQE RLAEAKPKVE 

       790        800        810        820        830        840 
AILLASRELV RSKRLRQMLE VILAIGNFMN KGQRGGAYGF RVASLNKIAD TKSSIDRNIS 

       850        860        870        880        890        900 
LLHYLIMILE KHFPDILNMP SELQHLPEAA KVNLAELEKE VGNLRRGLRA VEVELEYQRR 

       910        920        930        940        950        960 
QVREPSDKFV PVMSDFITVS SFSFSELEDQ LNEARDKFAK ALMHFGEHDS KMQPDEFFGI 

       970        980        990       1000       1010       1020 
FDTFLQAFSE ARQDLEAMRR RKEEEERRAR MEAMLKEQRE RERWQRQRKV LAAGSSLEEG 

      1030       1040       1050       1060 
GEFDDLVSAL RSGEVFDKDL CKLKRSRKRS GSQALEVTRE RAINRLNY 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spinal cord.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002379 mRNA. Translation: BAA20835.2. Different initiation.
AL833083 mRNA. Translation: CAD89973.1.
AL590999, AL136089, AL357412 Genomic DNA. Translation: CAI16176.2.
AL136089, AL357412, AL590999 Genomic DNA. Translation: CAI20010.2.
AL357412, AL136089, AL590999 Genomic DNA. Translation: CAI23288.2.
IPIIPI00514893.
RefSeqNP_001188356.1. NM_001201427.1.
NP_056160.2. NM_015345.3.
UniGeneHs.357128.
Hs.718492.

3D structure databases

ProteinModelPortalQ86T65.
SMRQ86T65. Positions 48-420, 590-1038.
ModBaseSearch...

Protein-protein interaction databases

IntActQ86T65. 1 interaction.
STRINGQ86T65.

PTM databases

PhosphoSiteQ86T65.

Polymorphism databases

DMDM62906888.

Proteomic databases

PRIDEQ86T65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274867; ENSP00000274867; ENSG00000146122.
ENST00000398904; ENSP00000381876; ENSG00000146122.
GeneID23500.
KEGGhsa:23500.
UCSCuc003oow.1. human.

Organism-specific databases

CTD23500.
GeneCardsGC06P039807.
H-InvDBHIX0005854.
HGNCHGNC:18143. DAAM2.
MIM606627. gene.
neXtProtNX_Q86T65.
PharmGKBPA27130.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05304.
GeneTreeENSGT00600000084372.
HOGENOMHBG357301.
HOVERGENHBG101333.
InParanoidQ86T65.
OMAIMILEKH.
OrthoDBEOG4MKNFH.
PhylomeDBQ86T65.

Gene expression databases

ArrayExpressQ86T65.
BgeeQ86T65.
CleanExHS_DAAM2.
GenevestigatorQ86T65.
GermOnlineENSG00000146122. Homo sapiens.

Family and domain databases

InterProIPR003104. Actin-bd_FH2/DRF_autoreg.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR010472. Drf_FH3.
IPR010473. Drf_GTPase-bd.
IPR015425. FH2_actin-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 2 hits.
KOK04512.
PfamPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
SSF101447. FH2_actin_bd. 1 hit.
PROSITEPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio45877.
SOURCESearch...

Entry information

Entry nameDAAM2_HUMAN
AccessionPrimary (citable) accession number: Q86T65
Secondary accession number(s): Q5T4T8 expand/collapse secondary AC list , Q5T4U0, Q9NQI5, Q9Y4G0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 86 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

Human chromosome 6

Human chromosome 6: 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