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Q9NSV4 (DIAP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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:
Protein diaphanous homolog 3
Alternative name(s):
Diaphanous-related formin-3
Short name=DRF3
MDia2
Gene names
Name:DIAPH3
Synonyms:DIAP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to GTP-bound form of Rho and to profilin. Acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. It is required for cytokinesis, stress fiber formation, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics By similarity.

Subcellular location

Cytoplasmcytosol. Note: During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis. Ref.9 Ref.10

Developmental stage

Increased expression in S phase and mitotic cells; levels decrease as cells enter in G0/G1 phase due to proteasomal degradation (at protein level). Ref.10

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

Auditory neuropathy, autosomal dominant, 1 (AUNA1) [MIM:609129]: A form of sensorineural hearing loss with absent or severely abnormal auditory brainstem response, in the presence of normal cochlear outer hair cell function and normal otoacoustic emissions. Auditory neuropathies result from a lesion in the area including the inner hair cells, connections between the inner hair cells and the cochlear branch of the auditory nerve, the auditory nerve itself and auditory pathways of the brainstem.
Note: The disease is caused by mutations affecting the gene represented in this entry. A disease-causing mutation in the conserved 5'-UTR leads to increased protein expression (Ref.11). Ref.11

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 AAW73254.1 differs from that shown. Reason: Frameshift at position 1147.

Ontologies

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9NSV4-3)

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 1 (identifier: Q9NSV4-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.
     1107-1112: ENQKVQ → GNKPYL
     1113-1193: Missing.
Isoform 2 (identifier: Q9NSV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.
     913-956: VSVETLEKNL...DKFVTKMSRF → GLCLFKKHFM...HSVFIPNISF
     957-1193: Missing.
Isoform 4 (identifier: Q9NSV4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     61-71: Missing.
Isoform 5 (identifier: Q9NSV4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     61-71: Missing.
     131-165: Missing.
Isoform 6 (identifier: Q9NSV4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     61-71: Missing.
     72-130: Missing.
Isoform 7 (identifier: Q9NSV4-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1107-1112: ENQKVQ → GNKPYL
     1113-1193: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11931193Protein diaphanous homolog 3
PRO_0000194897

Regions

Domain114 – 476363GBD/FH3
Domain561 – 63171FH1
Domain636 – 1034399FH2
Domain1057 – 108731DAD
Coiled coil497 – 55458 Potential
Coiled coil1013 – 105644 Potential
Compositional bias561 – 63676Pro-rich

Amino acid modifications

Modified residue6241Phosphoserine Ref.12
Cross-link139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Natural variations

Alternative sequence1 – 263263Missing in isoform 1 and isoform 2.
VSP_015958
Alternative sequence61 – 7111Missing in isoform 4, isoform 5 and isoform 6.
VSP_027774
Alternative sequence72 – 13059Missing in isoform 6.
VSP_027775
Alternative sequence131 – 16535Missing in isoform 5.
VSP_027776
Alternative sequence913 – 95644VSVET…KMSRF → GLCLFKKHFMALIFSAKRLK IIPFICMYFPLSHSVFIPNI SF in isoform 2.
VSP_001574
Alternative sequence957 – 1193237Missing in isoform 2.
VSP_001575
Alternative sequence1107 – 11126ENQKVQ → GNKPYL in isoform 7 and isoform 1.
VSP_027777
Alternative sequence1113 – 119381Missing in isoform 7 and isoform 1.
VSP_027778
Natural variant3631N → S.
Corresponds to variant rs36084898 [ dbSNP | Ensembl ].
VAR_049097
Natural variant7731F → L.
Corresponds to variant rs35579086 [ dbSNP | Ensembl ].
VAR_049098
Natural variant10411E → G.
Corresponds to variant rs7491389 [ dbSNP | Ensembl ].
VAR_049099

Experimental info

Sequence conflict551E → G in BAE96352. Ref.3
Sequence conflict1281K → R in BAC03793. Ref.7
Sequence conflict2741A → V in AAH34952. Ref.6
Sequence conflict3301L → P in BAE96351. Ref.3
Sequence conflict5881P → L in BAC03793. Ref.7
Sequence conflict6131P → L in BAE96351. Ref.3
Sequence conflict6691N → K in CAE46204. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified September 11, 2007. Version 4.
Checksum: ABCA4E859873F9E7

FASTA1,193136,926
        10         20         30         40         50         60 
MERHQPRLHH PAQGSAAGTP YPSSASLRGC RESKMPRRKG PQHPPPPSGP EEPGEKRPKF 

        70         80         90        100        110        120 
HLNIRTLTDD MLDKFASIRI PGSKKERPPL PNLKTAFASS DCSAAPLEMM ENFPKPLSEN 

       130        140        150        160        170        180 
ELLELFEKMM EDMNLNEDKK APLREKDFSI KKEMVMQYIN TASKTGSLKR SRQISPQEFI 

       190        200        210        220        230        240 
HELKMGSADE RLVTCLESLR VSLTSNPVSW VESFGHEGLG LLLDILEKLI SGKIQEKVVK 

       250        260        270        280        290        300 
KNQHKVIQCL KALMNTQYGL ERIMSEERSL SLLAKAVDPR HPNMMTDVVK LLSAVCIVGE 

       310        320        330        340        350        360 
ESILEEVLEA LTSAGEEKKI DRFFCIVEGL RHNSVQLQVA CMQLINALVT SPDDLDFRLH 

       370        380        390        400        410        420 
IRNEFMRCGL KEILPNLKCI KNDGLDIQLK VFDEHKEEDL FELSHRLEDI RAELDEAYDV 

       430        440        450        460        470        480 
YNMVWSTVKE TRAEGYFISI LQHLLLIRND YFIRQQYFKL IDECVSQIVL HRDGMDPDFT 

       490        500        510        520        530        540 
YRKRLDLDLT QFVDICIDQA KLEEFEEKAS ELYKKFEKEF TDHQETQAEL QKKEAKINEL 

       550        560        570        580        590        600 
QAELQAFKSQ FGALPADCNI PLPPSKEGGT GHSALPPPPP LPSGGGVPPP PPPPPPPPLP 

       610        620        630        640        650        660 
GMRMPFSGPV PPPPPLGFLG GQNSPPLPIL PFGLKPKKEF KPEISMRRLN WLKIRPHEMT 

       670        680        690        700        710        720 
ENCFWIKVNE NKYENVDLLC KLENTFCCQQ KERREEEDIE EKKSIKKKIK ELKFLDSKIA 

       730        740        750        760        770        780 
QNLSIFLSSF RVPYEEIRMM ILEVDETRLA ESMIQNLIKH LPDQEQLNSL SQFKSEYSNL 

       790        800        810        820        830        840 
CEPEQFVVVM SNVKRLRPRL SAILFKLQFE EQVNNIKPDI MAVSTACEEI KKSKSFSKLL 

       850        860        870        880        890        900 
ELVLLMGNYM NAGSRNAQTF GFNLSSLCKL KDTKSADQKT TLLHFLVEIC EEKYPDILNF 

       910        920        930        940        950        960 
VDDLEPLDKA SKVSVETLEK NLRQMGRQLQ QLEKELETFP PPEDLHDKFV TKMSRFVISA 

       970        980        990       1000       1010       1020 
KEQYETLSKL HENMEKLYQS IIGYYAIDVK KVSVEDFLTD LNNFRTTFMQ AIKENIKKRE 

      1030       1040       1050       1060       1070       1080 
AEEKEKRVRI AKELAERERL ERQQKKKRLL EMKTEGDETG VMDNLLEALQ SGAAFRDRRK 

      1090       1100       1110       1120       1130       1140 
RTPMPKDVRQ SLSPMSQRPV LKVCNHENQK VQLTEGSRSH YNINCNSTRT PVAKELNYNL 

      1150       1160       1170       1180       1190 
DTHTSTGRIK AAEKKEACNV ESNRKKETEL LGSFSKNESV PEVEALLARL RAL 

« Hide

Isoform 1 [UniParc].

Checksum: 5CE99DEE93AC833C
Show »

FASTA84998,140
Isoform 2 [UniParc].

Checksum: CDFF84D86D4B66DF
Show »

FASTA69179,445
Isoform 4 [UniParc].

Checksum: 9169ACD33B8FB00D
Show »

FASTA1,182135,615
Isoform 5 [UniParc].

Checksum: 4286EEB6F00A3F01
Show »

FASTA1,147131,487
Isoform 6 [UniParc].

Checksum: 4623CCC9C5D433C6
Show »

FASTA1,123128,994
Isoform 7 [UniParc].

Checksum: DCB5192396280A30
Show »

FASTA1,112127,856

References

« Hide 'large scale' references
[1]"Homo sapiens diaphanous homolog 3 (DIAPH3) mRNA."
Mao M., Ward T., Schimmack G., Linsley P.S.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]"Identification and analysis of DIAPH3 as an EGF-dependent lipid raft complex in LNCaP prostate cancer cells."
Khoury J., Freeman M.R.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
[3]"Control of mitotic spindle orientation by mDia-mediated actin fibers."
Yasuda S., Narumiya S.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-669 (ISOFORM 3).
Tissue: Testis.
[5]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Testis.
[7]"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 1-699 (ISOFORM 3).
Tissue: Mesangial cell.
[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-139.
Tissue: Mammary cancer.
[9]"Filopodia formation induced by active mDia2/Drf3."
Block J., Stradal T.E., Hanisch J., Geffers R., Kostler S.A., Urban E., Small J.V., Rottner K., Faix J.
J. Microsc. 231:506-517(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division."
DeWard A.D., Alberts A.S.
J. Biol. Chem. 284:20061-20069(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, DEVELOPMENTAL STAGE.
[11]"Increased activity of Diaphanous homolog 3 (DIAPH3)/diaphanous causes hearing defects in humans with auditory neuropathy and in Drosophila."
Schoen C.J., Emery S.B., Thorne M.C., Ammana H.R., Sliwerska E., Arnett J., Hortsch M., Hannan F., Burmeister M., Lesperance M.M.
Proc. Natl. Acad. Sci. U.S.A. 107:13396-13401(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AUNA1.
[12]"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-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY750055 mRNA. Translation: AAW73254.1. Frameshift.
AY818645 mRNA. Translation: AAW78862.1.
AB244756 mRNA. Translation: BAE96350.1.
AB244757 mRNA. Translation: BAE96351.1.
AB244758 mRNA. Translation: BAE96352.1.
AL137718 mRNA. Translation: CAB70890.1.
BX649186 mRNA. Translation: CAE46204.1.
AL354829 expand/collapse EMBL AC list , AL356502, AL359266, AL390878 Genomic DNA. Translation: CAI39756.2.
AL354829, AL356502, AL390878 Genomic DNA. Translation: CAI39757.2.
AL354829 expand/collapse EMBL AC list , AL356502, AL359266, AL390878 Genomic DNA. Translation: CAM14265.1.
AL354829 expand/collapse EMBL AC list , AL356502, AL359266, AL390878 Genomic DNA. Translation: CAM14266.1.
AL354829 expand/collapse EMBL AC list , AL356502, AL359266, AL390878 Genomic DNA. Translation: CAM14267.1.
AL356502 expand/collapse EMBL AC list , AL354829, AL359266, AL390878 Genomic DNA. Translation: CAI14102.2.
AL356502, AL354829, AL390878 Genomic DNA. Translation: CAM19398.1.
AL356502 expand/collapse EMBL AC list , AL354829, AL359266, AL390878 Genomic DNA. Translation: CAM19399.1.
AL356502 expand/collapse EMBL AC list , AL354829, AL359266, AL390878 Genomic DNA. Translation: CAM19400.1.
AL356502 expand/collapse EMBL AC list , AL354829, AL359266, AL390878 Genomic DNA. Translation: CAM19401.1.
AL359266 expand/collapse EMBL AC list , AL354829, AL356502, AL390878 Genomic DNA. Translation: CAM15403.1.
AL359266 expand/collapse EMBL AC list , AL354829, AL356502, AL390878 Genomic DNA. Translation: CAM15404.1.
AL359266 expand/collapse EMBL AC list , AL354829, AL356502, AL390878 Genomic DNA. Translation: CAM15405.1.
AL359266 expand/collapse EMBL AC list , AL354829, AL356502, AL390878 Genomic DNA. Translation: CAM15406.1.
AL390878 expand/collapse EMBL AC list , AL354829, AL356502, AL359266 Genomic DNA. Translation: CAI14158.2.
AL390878, AL354829, AL356502 Genomic DNA. Translation: CAM19738.1.
AL390878 expand/collapse EMBL AC list , AL354829, AL356502, AL359266 Genomic DNA. Translation: CAM19739.1.
AL390878 expand/collapse EMBL AC list , AL354829, AL356502, AL359266 Genomic DNA. Translation: CAM19740.1.
AL390878 expand/collapse EMBL AC list , AL354829, AL356502, AL359266 Genomic DNA. Translation: CAM19741.1.
BC034952 mRNA. Translation: AAH34952.1.
BC048963 mRNA. Translation: AAH48963.1.
BC068504 mRNA. Translation: AAH68504.1.
AK092024 mRNA. Translation: BAC03793.1.
RefSeqNP_001035982.1. NM_001042517.1.
NP_001245295.1. NM_001258366.1.
NP_001245296.1. NM_001258367.1.
NP_001245297.1. NM_001258368.1.
NP_001245298.1. NM_001258369.1.
NP_001245299.1. NM_001258370.1.
NP_112194.2. NM_030932.3.
UniGeneHs.283127.

3D structure databases

ProteinModelPortalQ9NSV4.
SMRQ9NSV4. Positions 710-1030.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123559. 13 interactions.
IntActQ9NSV4. 5 interactions.
MINTMINT-1195088.

PTM databases

PhosphoSiteQ9NSV4.

Polymorphism databases

DMDM158520000.

Proteomic databases

PaxDbQ9NSV4.
PRIDEQ9NSV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267215; ENSP00000267215; ENSG00000139734. [Q9NSV4-7]
ENST00000377908; ENSP00000367141; ENSG00000139734. [Q9NSV4-4]
ENST00000400319; ENSP00000383173; ENSG00000139734. [Q9NSV4-6]
ENST00000400320; ENSP00000383174; ENSG00000139734. [Q9NSV4-5]
ENST00000400324; ENSP00000383178; ENSG00000139734. [Q9NSV4-3]
GeneID81624.
KEGGhsa:81624.
UCSCuc001vht.4. human. [Q9NSV4-3]
uc001vhu.3. human. [Q9NSV4-1]
uc001vhv.4. human. [Q9NSV4-2]
uc001vhw.2. human. [Q9NSV4-4]
uc010aed.2. human. [Q9NSV4-5]
uc010aee.2. human. [Q9NSV4-6]
uc031qlw.1. human. [Q9NSV4-7]

Organism-specific databases

CTD81624.
GeneCardsGC13M060239.
H-InvDBHIX0037336.
HGNCHGNC:15480. DIAPH3.
HPAHPA004917.
HPA032151.
HPA032152.
MIM609129. phenotype.
614567. gene.
neXtProtNX_Q9NSV4.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBPA27335.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149898.
HOVERGENHBG051357.
InParanoidQ9NSV4.
KOK05745.
OMAKQMGRQL.
OrthoDBEOG7G1V5D.
PhylomeDBQ9NSV4.
TreeFamTF315383.

Gene expression databases

ArrayExpressQ9NSV4.
BgeeQ9NSV4.
CleanExHS_DIAPH3.
GenevestigatorQ9NSV4.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027654. Formin_DIAPH3.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERPTHR23213:SF16. PTHR23213:SF16. 1 hit.
PfamPF06345. Drf_DAD. 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

ChiTaRSDIAPH3. human.
GenomeRNAi81624.
NextBio71996.
PROQ9NSV4.
SOURCESearch...

Entry information

Entry nameDIAP3_HUMAN
AccessionPrimary (citable) accession number: Q9NSV4
Secondary accession number(s): A2A3B8 expand/collapse secondary AC list , A2A3B9, A2A3C0, Q18P99, Q18PA0, Q18PA1, Q2KPB6, Q3ZK23, Q5JTP8, Q5T2S7, Q5XKF6, Q6MZF0, Q6NUP0, Q86VS4, Q8NAV4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 4 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 13

Human chromosome 13: entries, gene names and cross-references to MIM