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Q9Y4D1 (DAAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Disheveled-associated activator of morphogenesis 1
Gene names
Name:DAAM1
Synonyms:KIAA0666
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1078 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. Ref.7 Ref.8

Subunit structure

Homodimer. Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds specifically to GTP-bound CDC42 and RHOA. Ref.7 Ref.8

Subcellular location

Cytoplasm. Note: Perinuclear. Ref.7

Tissue specificity

Expressed in all tissues examined.

Domain

The C-terminal DAD domain may participate in intramolecular interactions with the N-terminus.

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 BAA31641.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC04230.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandActin-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular functionRho GTPase binding

Inferred from electronic annotation. Source: InterPro

actin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4D1-1)

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.
Isoform 2 (identifier: Q9Y4D1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     656-665: Missing.
Isoform 3 (identifier: Q9Y4D1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     788-818: Missing.
     888-916: NMTELDKEISTLRSGLKAVETELEYQKSQ → KSWNIRSLSPHSPEISLCLLSASSSQ
     917-1078: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10781078Disheveled-associated activator of morphogenesis 1
PRO_0000194907

Regions

Domain45 – 420376GBD/FH3
Domain528 – 59972FH1
Domain600 – 1009410FH2
Domain1027 – 105832DAD
Region693 – 70210Actin-binding
Coiled coil437 – 52690 Potential
Compositional bias528 – 59366Pro-rich

Natural variations

Alternative sequence656 – 66510Missing in isoform 2.
VSP_008000
Alternative sequence788 – 81831Missing in isoform 3.
VSP_008001
Alternative sequence888 – 91629NMTEL…YQKSQ → KSWNIRSLSPHSPEISLCLL SASSSQ in isoform 3.
VSP_008002
Alternative sequence917 – 1078162Missing in isoform 3.
VSP_008003

Experimental info

Mutagenesis6981I → A: Abolishes actin-binding. Ref.8
Sequence conflict9401S → F in AAH24781. Ref.3

Secondary structure

..................................................... 1078
Helix Strand Turn

Details...

Sequences

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

Last modified August 15, 2003. Version 2.
Checksum: E82D9892390254B6

FASTA1,078123,473
        10         20         30         40         50         60 
MAPRKRGGRG ISFIFCCFRN NDHPEITYRL RNDSNFALQT MEPALPMPPV EELDVMFSEL 

        70         80         90        100        110        120 
VDELDLTDKH REAMFALPAE KKWQIYCSKK KDQEENKGAT SWPEFYIDQL NSMAARKSLL 

       130        140        150        160        170        180 
ALEKEEEEER SKTIESLKTA LRTKPMRFVT RFIDLDGLSC ILNFLKTMDY ETSESRIHTS 

       190        200        210        220        230        240 
LIGCIKALMN NSQGRAHVLA HSESINVIAQ SLSTENIKTK VAVLEILGAV CLVPGGHKKV 

       250        260        270        280        290        300 
LQAMLHYQKY ASERTRFQTL INDLDKSTGR YRDEVSLKTA IMSFINAVLS QGAGVESLDF 

       310        320        330        340        350        360 
RLHLRYEFLM LGIQPVIDKL REHENSTLDR HLDFFEMLRN EDELEFAKRF ELVHIDTKSA 

       370        380        390        400        410        420 
TQMFELTRKR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ 

       430        440        450        460        470        480 
DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK 

       490        500        510        520        530        540 
EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELSR RAVCASIPGG PSPGAPGGPF 

       550        560        570        580        590        600 
PSSVPGSLLP PPPPPPLPGG MLPPPPPPLP PGGPPPPPGP PPLGAIMPPP GAPMGLALKK 

       610        620        630        640        650        660 
KSIPQPTNAL KSFNWSKLPE NKLEGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQDFFV 

       670        680        690        700        710        720 
NSNSKQKEAD AIDDTLSSKL KVKELSVIDG RRAQNCNILL SRLKLSNDEI KRAILTMDEQ 

       730        740        750        760        770        780 
EDLPKDMLEQ LLKFVPEKSD IDLLEEHKHE LDRMAKADRF LFEMSRINHY QQRLQSLYFK 

       790        800        810        820        830        840 
KKFAERVAEV KPKVEAIRSG SEEVFRSGAL KQLLEVVLAF GNYMNKGQRG NAYGFKISSL 

       850        860        870        880        890        900 
NKIADTKSSI DKNITLLHYL ITIVENKYPS VLNLNEELRD IPQAAKVNMT ELDKEISTLR 

       910        920        930        940        950        960 
SGLKAVETEL EYQKSQPPQP GDKFVSVVSQ FITVASFSFS DVEDLLAEAK DLFTKAVKHF 

       970        980        990       1000       1010       1020 
GEEAGKIQPD EFFGIFDQFL QAVSEAKQEN ENMRKKKEEE ERRARMEAQL KEQRERERKM 

      1030       1040       1050       1060       1070 
RKAKENSEES GEFDDLVSAL RSGEVFDKDL SKLKRNRKRI TNQMTDSSRE RPITKLNF 

« Hide

Isoform 2 [UniParc].

Checksum: C58B1A7445080313
Show »

FASTA1,068122,306
Isoform 3 [UniParc].

Checksum: 1BB2D1876B212852
Show »

FASTA882100,745

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta and Uterus.
[4]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497 (ISOFORM 1).
Tissue: Fetal brain.
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 706-1078 (ISOFORM 3).
Tissue: Thymus.
[6]"Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1."
Habas R., Kato Y., He X.
Cell 107:843-854(2001) [PubMed: 11779461] [Abstract]
Cited for: CHARACTERIZATION.
[7]"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
Aspenstroem P., Richnau N., Johansson A.-S.
Exp. Cell Res. 312:2180-2194(2006) [PubMed: 16630611] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ABL1; BTK; CDC42; CIP4; ENDOPHILIN; FNBP1; FNBP1L; RHOA; SPECTRIN AND SRC, SUBCELLULAR LOCATION.
[8]"Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly."
Lu J., Meng W., Poy F., Maiti S., Goode B.L., Eck M.J.
J. Mol. Biol. 369:1258-1269(2007) [PubMed: 17482208] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 596-1078, SUBUNIT, MUTAGENESIS OF ILE-698, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014566 mRNA. Translation: BAA31641.1. Different initiation.
AL133502 Genomic DNA. No translation available.
BC024781 mRNA. Translation: AAH24781.1.
BC038428 mRNA. Translation: AAH38428.1.
BC064999 mRNA. Translation: AAH64999.1.
BX247986 mRNA. Translation: CAD62320.1.
AK093813 mRNA. Translation: BAC04230.1. Different initiation.
IPIIPI00337800.
IPI00337801.
IPI00337802.
RefSeqNP_055807.1. NM_014992.1.
UniGeneHs.654934.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J1DX-ray2.55G596-1078[»]
2Z6EX-ray2.80A/B/C/D594-1012[»]
ProteinModelPortalQ9Y4D1.
SMRQ9Y4D1. Positions 53-424, 594-1048.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29641N.
IntActQ9Y4D1. 4 interactions.
MINTMINT-1180756.
STRINGQ9Y4D1.

PTM databases

PhosphoSiteQ9Y4D1.

Polymorphism databases

DMDM34098767.

Proteomic databases

PRIDEQ9Y4D1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351081; ENSP00000247170; ENSG00000100592.
ENST00000395125; ENSP00000378557; ENSG00000100592.
GeneID23002.
KEGGhsa:23002.
UCSCuc001xdz.1. human.
uc001xea.1. human.

Organism-specific databases

CTD23002.
GeneCardsGC14P059655.
H-InvDBHIX0011701.
HGNCHGNC:18142. DAAM1.
HPAHPA026605.
MIM606626. gene.
neXtProtNX_Q9Y4D1.
PharmGKBPA27129.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06028.
GeneTreeENSGT00600000084372.
HOGENOMHBG357301.
HOVERGENHBG101333.
InParanoidQ9Y4D1.
OMAPMGLALK.
OrthoDBEOG4RBQHV.
PhylomeDBQ9Y4D1.

Gene expression databases

ArrayExpressQ9Y4D1.
BgeeQ9Y4D1.
CleanExHS_DAAM1.
GenevestigatorQ9Y4D1.
GermOnlineENSG00000100592. 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. 1 hit.
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

NextBio43908.
SOURCESearch...

Entry information

Entry nameDAAM1_HUMAN
AccessionPrimary (citable) accession number: Q9Y4D1
Secondary accession number(s): Q86U34, Q8N1Z8, Q8TB39
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: January 25, 2012
This is version 101 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 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families