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O60610 (DIAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein diaphanous homolog 1
Alternative name(s):
Diaphanous-related formin-1
Short name=DRF1
Gene names
Name:DIAPH1
Synonyms:DIAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration By similarity. Has neurite outgrowth promoting activity By similarity. In hear cells, it may play a role in the regulation of actin polymerization in hair cells. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. Ref.12 Ref.14

Subunit structure

Homodimer. Interacts with the GTP-bound form of RHOA. Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC. Interacts with SCAI By similarity. Interacts with DCAF7, via FH2 domain. Interacts with NCDN By similarity. Ref.6

Subcellular location

Cell membrane. Cell projectionruffle membrane. Cytoplasmcytoskeleton. Note: Membrane ruffles, especially at the tip of ruffles, of motile cells.

Tissue specificity

Expressed in brain, heart, placenta, lung, kidney, pancreas, liver, skeletal muscle and cochlea.

Domain

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments By similarity.

Involvement in disease

Deafness, autosomal dominant, 1 (DFNA1) [MIM:124900]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the formin homology family. Diaphanous subfamily.

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 BAB14533.1 differs from that shown. Reason: Intron retention.

The sequence BAD92719.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHearing
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Non-syndromic deafness
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament polymerization

Inferred from electronic annotation. Source: Ensembl

cellular response to histamine

Inferred from mutant phenotype PubMed 15123714. Source: BHF-UCL

cytoskeleton organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

protein localization to microtubule

Inferred from mutant phenotype PubMed 15123714. Source: BHF-UCL

regulation of cell shape

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of microtubule-based process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

regulation of release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 15123714. Source: BHF-UCL

sensory perception of sound

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle

Inferred from direct assay PubMed 15123714. Source: BHF-UCL

neuron projection

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionion channel binding

Inferred from physical interaction PubMed 15123714. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

receptor binding

Non-traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G42EBI-3959709,EBI-6248094From a different organism.
PPM1FP495933EBI-3959709,EBI-719945
RHOAP615863EBI-3959709,EBI-446668

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60610-1)

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: O60610-2)

The sequence of this isoform differs from the canonical sequence as follows:
     40-48: Missing.
     621-632: Missing.
     826-828: Missing.
Isoform 3 (identifier: O60610-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-48: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12721272Protein diaphanous homolog 1
PRO_0000194893

Regions

Domain84 – 449366GBD/FH3
Domain583 – 764182FH1
Domain769 – 1171403FH2
Domain1194 – 122229DAD
Coiled coil468 – 572105 Potential
Coiled coil1039 – 1196158 Potential
Compositional bias1213 – 12164Arg/Lys-rich (basic)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16 Ref.17
Modified residue221Phosphoserine Ref.9 Ref.10 Ref.13
Modified residue10571N6-acetyllysine Ref.11
Modified residue11031N6-acetyllysine Ref.11
Modified residue11211Phosphotyrosine By similarity
Cross-link486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Natural variations

Alternative sequence40 – 489Missing in isoform 2 and isoform 3.
VSP_035870
Alternative sequence621 – 63212Missing in isoform 2.
VSP_035871
Alternative sequence826 – 8283Missing in isoform 2.
VSP_035872

Experimental info

Sequence conflict131G → E in AAC05373. Ref.1
Sequence conflict6091Missing in AAI17258. Ref.4
Sequence conflict11561R → A AA sequence Ref.7
Sequence conflict11571E → K in AAC05373. Ref.1
Sequence conflict11571E → K AA sequence Ref.7

Sequences

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

Last modified November 25, 2008. Version 2.
Checksum: 9C8273DE4748564F

FASTA1,272141,347
        10         20         30         40         50         60 
MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFT LKRLMADELE RFTSMRIKKE 

        70         80         90        100        110        120 
KEKPNSAHRN SSASYGDDPT AQSLQDVSDE QVLVLFEQML LDMNLNEEKQ QPLREKDIII 

       130        140        150        160        170        180 
KREMVSQYLY TSKAGMSQKE SSKSAMMYIQ ELRSGLRDMP LLSCLESLRV SLNNNPVSWV 

       190        200        210        220        230        240 
QTFGAEGLAS LLDILKRLHD EKEETAGSYD SRNKHEIIRC LKAFMNNKFG IKTMLETEEG 

       250        260        270        280        290        300 
ILLLVRAMDP AVPNMMIDAA KLLSALCILP QPEDMNERVL EAMTERAEMD EVERFQPLLD 

       310        320        330        340        350        360 
GLKSGTTIAL KVGCLQLINA LITPAEELDF RVHIRSELMR LGLHQVLQDL REIENEDMRV 

       370        380        390        400        410        420 
QLNVFDEQGE EDSYDLKGRL DDIRMEMDDF NEVFQILLNT VKDSKAEPHF LSILQHLLLV 

       430        440        450        460        470        480 
RNDYEARPQY YKLIEECISQ IVLHKNGADP DFKCRHLQIE IEGLIDQMID KTKVEKSEAK 

       490        500        510        520        530        540 
AAELEKKLDS ELTARHELQV EMKKMESDFE QKLQDLQGEK DALHSEKQQI ATEKQDLEAE 

       550        560        570        580        590        600 
VSQLTGEVAK LTKELEDAKK EMASLSAAAI TVPPSVPSRA PVPPAPPLPG DSGTIIPPPP 

       610        620        630        640        650        660 
APGDSTTPPP PPPPPPPPPP LPGGVCISSP PSLPGGTAIS PPPPLSGDAT IPPPPPLPEG 

       670        680        690        700        710        720 
VGIPSPSSLP GGTAIPPPPP LPGSARIPPP PPPLPGSAGI PPPPPPLPGE AGMPPPPPPL 

       730        740        750        760        770        780 
PGGPGIPPPP PFPGGPGIPP PPPGMGMPPP PPFGFGVPAA PVLPFGLTPK KLYKPEVQLR 

       790        800        810        820        830        840 
RPNWSKLVAE DLSQDCFWTK VKEDRFENNE LFAKLTLTFS AQTKTSKAKK DQEGGEEKKS 

       850        860        870        880        890        900 
VQKKKVKELK VLDSKTAQNL SIFLGSFRMP YQEIKNVILE VNEAVLTESM IQNLIKQMPE 

       910        920        930        940        950        960 
PEQLKMLSEL KDEYDDLAES EQFGVVMGTV PRLRPRLNAI LFKLQFSEQV ENIKPEIVSV 

       970        980        990       1000       1010       1020 
TAACEELRKS ESFSNLLEIT LLVGNYMNAG SRNAGAFGFN ISFLCKLRDT KSTDQKMTLL 

      1030       1040       1050       1060       1070       1080 
HFLAELCEND YPDVLKFPDE LAHVEKASRV SAENLQKNLD QMKKQISDVE RDVQNFPAAT 

      1090       1100       1110       1120       1130       1140 
DEKDKFVEKM TSFVKDAQEQ YNKLRMMHSN METLYKELGE YFLFDPKKLS VEEFFMDLHN 

      1150       1160       1170       1180       1190       1200 
FRNMFLQAVK ENQKRRETEE KMRRAKLAKE KAEKERLEKQ QKREQLIDMN AEGDETGVMD 

      1210       1220       1230       1240       1250       1260 
SLLEALQSGA AFRRKRGPRQ ANRKAGCAVT SLLASELTKD DAMAAVPAKV SKNSETFPTI 

      1270 
LEEAKELVGR AS 

« Hide

Isoform 2 [UniParc].

Checksum: 7F17EB0B99DB3519
Show »

FASTA1,248138,907
Isoform 3 [UniParc].

Checksum: 394E98CBBB2DDA4D
Show »

FASTA1,263140,289

References

« Hide 'large scale' references
[1]"Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous."
Lynch E.D., Lee M.K., Morrow J.E., Welcsh P.L., Leon P.E., King M.-C.
Science 278:1315-1318(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 1 AND 3).
Tissue: Heart and Lung.
[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] OF 227-841 (ISOFORM 2).
Tissue: Ovarian carcinoma.
[6]"HAN11 binds mDia1 and controls GLI1 transcriptional activity."
Morita K., Lo Celso C., Spencer-Dene B., Zouboulis C.C., Watt F.M.
J. Dermatol. Sci. 44:11-20(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 560-580 AND 855-869, INTERACTION WITH DCAF7.
[7]"The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins."
Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B.M., Walter U.
EMBO J. 14:1583-1589(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 742-801 AND 1145-1169.
Tissue: Platelet.
[8]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-486.
Tissue: Mammary cancer.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1057 AND LYS-1103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF051782 mRNA. Translation: AAC05373.1.
AB209482 mRNA. Translation: BAD92719.1. Different initiation.
AC008781 Genomic DNA. No translation available.
BC117257 mRNA. Translation: AAI17258.1.
BC143413 mRNA. Translation: AAI43414.1.
AK023345 mRNA. Translation: BAB14533.1. Sequence problems.
RefSeqNP_001073280.1. NM_001079812.2.
NP_005210.3. NM_005219.4.
UniGeneHs.529451.

3D structure databases

ProteinModelPortalO60610.
SMRO60610. Positions 92-461, 762-1215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108073. 27 interactions.
IntActO60610. 18 interactions.
MINTMINT-1198324.
STRING9606.ENSP00000381565.

PTM databases

PhosphoSiteO60610.

2D gel databases

OGPO60610.

Proteomic databases

PaxDbO60610.
PRIDEO60610.

Protocols and materials databases

DNASU1729.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389057; ENSP00000373709; ENSG00000131504. [O60610-3]
ENST00000398557; ENSP00000381565; ENSG00000131504. [O60610-1]
GeneID1729.
KEGGhsa:1729.
UCSCuc003llb.4. human. [O60610-1]

Organism-specific databases

CTD1729.
GeneCardsGC05M140875.
HGNCHGNC:2876. DIAPH1.
HPAHPA004916.
MIM124900. phenotype.
602121. gene.
neXtProtNX_O60610.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBPA27333.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149898.
HOGENOMHOG000293231.
HOVERGENHBG051357.
KOK05740.
PhylomeDBO60610.
TreeFamTF315383.

Gene expression databases

ArrayExpressO60610.
BgeeO60610.
CleanExHS_DIAPH1.
GenevestigatorO60610.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027653. Formin_Diaph1.
IPR009408. Formin_homology_1.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERPTHR23213:SF17. PTHR23213:SF17. 1 hit.
PfamPF06345. Drf_DAD. 1 hit.
PF06346. Drf_FH1. 1 hit.
PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDIAPH1. human.
GeneWikiDIAPH1.
GenomeRNAi1729.
NextBio6997.
PROO60610.
SOURCESearch...

Entry information

Entry nameDIAP1_HUMAN
AccessionPrimary (citable) accession number: O60610
Secondary accession number(s): A6NF18 expand/collapse secondary AC list , B7ZKW2, E9PEZ2, Q17RN4, Q59FH8, Q9UC76
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 140 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM