O60610 (DIAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein diaphanous homolog 1

Alternative name(s):
Diaphanous-related formin-1
Short name=DRF1

Gene names

Name:	DIAPH1
Synonyms:	DIAP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1272 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › ruffle membrane. Cytoplasm › cytoskeleton. 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 process	Hearing
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Disease	Deafness Non-syndromic deafness
Domain	Coiled coil Repeat
Ligand	Actin-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin filament polymerization Inferred from electronic annotation. Source: Compara 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: Compara 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_component	cytoplasm 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: Compara ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	receptor binding Non-traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORF	Q9Q2G4	2	EBI-3959709,EBI-6248094	From a different organism.
RHOA	P61586	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1272	1272	Protein diaphanous homolog 1		PRO_0000194893
Regions
	Domain	84 – 449	366	GBD/FH3
	Domain	583 – 764	182	FH1
	Domain	769 – 1171	403	FH2
	Domain	1194 – 1222	29	DAD
	Coiled coil	468 – 572	105	Potential
	Coiled coil	1039 – 1196	158	Potential
	Compositional bias	1213 – 1216	4	Arg/Lys-rich (basic)
Amino acid modifications
	Modified residue	22	1	Phosphoserine Ref.9 Ref.10 Ref.13
	Modified residue	1057	1	N6-acetyllysine Ref.11
	Modified residue	1103	1	N6-acetyllysine Ref.11
	Modified residue	1121	1	Phosphotyrosine By similarity
	Cross-link	486		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Natural variations
	Alternative sequence	40 – 48	9	Missing in isoform 2 and isoform 3.		VSP_035870
	Alternative sequence	621 – 632	12	Missing in isoform 2.		VSP_035871
	Alternative sequence	826 – 828	3	Missing in isoform 2.		VSP_035872
Experimental info
	Sequence conflict	13	1	G → E in AAC05373. Ref.1
	Sequence conflict	609	1	Missing in AAI17258. Ref.4
	Sequence conflict	1156	1	R → A AA sequence Ref.7
	Sequence conflict	1157	1	E → K in AAC05373. Ref.1
	Sequence conflict	1157	1	E → K AA sequence Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 9C8273DE4748564F	FASTA	1,272	141,347
	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
	Isoform 2 [UniParc]. Checksum: 7F17EB0B99DB3519	FASTA	1,248	138,907
	10 20 30 40 50 60 MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFL ERFTSMRIKK EKEKPNSAHR 70 80 90 100 110 120 NSSASYGDDP TAQSLQDVSD EQVLVLFEQM LLDMNLNEEK QQPLREKDII IKREMVSQYL 130 140 150 160 170 180 YTSKAGMSQK ESSKSAMMYI QELRSGLRDM PLLSCLESLR VSLNNNPVSW VQTFGAEGLA 190 200 210 220 230 240 SLLDILKRLH DEKEETAGSY DSRNKHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD 250 260 270 280 290 300 PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTTIA 310 320 330 340 350 360 LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQD LREIENEDMR VQLNVFDEQG 370 380 390 400 410 420 EEDSYDLKGR LDDIRMEMDD FNEVFQILLN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ 430 440 450 460 470 480 YYKLIEECIS QIVLHKNGAD PDFKCRHLQI EIEGLIDQMI DKTKVEKSEA KAAELEKKLD 490 500 510 520 530 540 SELTARHELQ VEMKKMESDF EQKLQDLQGE KDALHSEKQQ IATEKQDLEA EVSQLTGEVA 550 560 570 580 590 600 KLTKELEDAK KEMASLSAAA ITVPPSVPSR APVPPAPPLP GDSGTIIPPP PAPGDSTTPP 610 620 630 640 650 660 PPPPPPPPPP PLPGGTAISP PPPLSGDATI PPPPPLPEGV GIPSPSSLPG GTAIPPPPPL 670 680 690 700 710 720 PGSARIPPPP PPLPGSAGIP PPPPPLPGEA GMPPPPPPLP GGPGIPPPPP FPGGPGIPPP 730 740 750 760 770 780 PPGMGMPPPP PFGFGVPAAP VLPFGLTPKK LYKPEVQLRR PNWSKLVAED LSQDCFWTKV 790 800 810 820 830 840 KEDRFENNEL FAKLTLTFSA QTKTKKDQEG GEEKKSVQKK KVKELKVLDS KTAQNLSIFL 850 860 870 880 890 900 GSFRMPYQEI KNVILEVNEA VLTESMIQNL IKQMPEPEQL KMLSELKDEY DDLAESEQFG 910 920 930 940 950 960 VVMGTVPRLR PRLNAILFKL QFSEQVENIK PEIVSVTAAC EELRKSESFS NLLEITLLVG 970 980 990 1000 1010 1020 NYMNAGSRNA GAFGFNISFL CKLRDTKSTD QKMTLLHFLA ELCENDYPDV LKFPDELAHV 1030 1040 1050 1060 1070 1080 EKASRVSAEN LQKNLDQMKK QISDVERDVQ NFPAATDEKD KFVEKMTSFV KDAQEQYNKL 1090 1100 1110 1120 1130 1140 RMMHSNMETL YKELGEYFLF DPKKLSVEEF FMDLHNFRNM FLQAVKENQK RRETEEKMRR 1150 1160 1170 1180 1190 1200 AKLAKEKAEK ERLEKQQKRE QLIDMNAEGD ETGVMDSLLE ALQSGAAFRR KRGPRQANRK 1210 1220 1230 1240 AGCAVTSLLA SELTKDDAMA AVPAKVSKNS ETFPTILEEA KELVGRAS
	Isoform 3 [UniParc]. Checksum: 394E98CBBB2DDA4D	FASTA	1,263	140,289
	10 20 30 40 50 60 MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFL ERFTSMRIKK EKEKPNSAHR 70 80 90 100 110 120 NSSASYGDDP TAQSLQDVSD EQVLVLFEQM LLDMNLNEEK QQPLREKDII IKREMVSQYL 130 140 150 160 170 180 YTSKAGMSQK ESSKSAMMYI QELRSGLRDM PLLSCLESLR VSLNNNPVSW VQTFGAEGLA 190 200 210 220 230 240 SLLDILKRLH DEKEETAGSY DSRNKHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD 250 260 270 280 290 300 PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTTIA 310 320 330 340 350 360 LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQD LREIENEDMR VQLNVFDEQG 370 380 390 400 410 420 EEDSYDLKGR LDDIRMEMDD FNEVFQILLN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ 430 440 450 460 470 480 YYKLIEECIS QIVLHKNGAD PDFKCRHLQI EIEGLIDQMI DKTKVEKSEA KAAELEKKLD 490 500 510 520 530 540 SELTARHELQ VEMKKMESDF EQKLQDLQGE KDALHSEKQQ IATEKQDLEA EVSQLTGEVA 550 560 570 580 590 600 KLTKELEDAK KEMASLSAAA ITVPPSVPSR APVPPAPPLP GDSGTIIPPP PAPGDSTTPP 610 620 630 640 650 660 PPPPPPPPPP PLPGGVCISS PPSLPGGTAI SPPPPLSGDA TIPPPPPLPE GVGIPSPSSL 670 680 690 700 710 720 PGGTAIPPPP PLPGSARIPP PPPPLPGSAG IPPPPPPLPG EAGMPPPPPP LPGGPGIPPP 730 740 750 760 770 780 PPFPGGPGIP PPPPGMGMPP PPPFGFGVPA APVLPFGLTP KKLYKPEVQL RRPNWSKLVA 790 800 810 820 830 840 EDLSQDCFWT KVKEDRFENN ELFAKLTLTF SAQTKTSKAK KDQEGGEEKK SVQKKKVKEL 850 860 870 880 890 900 KVLDSKTAQN LSIFLGSFRM PYQEIKNVIL EVNEAVLTES MIQNLIKQMP EPEQLKMLSE 910 920 930 940 950 960 LKDEYDDLAE SEQFGVVMGT VPRLRPRLNA ILFKLQFSEQ VENIKPEIVS VTAACEELRK 970 980 990 1000 1010 1020 SESFSNLLEI TLLVGNYMNA GSRNAGAFGF NISFLCKLRD TKSTDQKMTL LHFLAELCEN 1030 1040 1050 1060 1070 1080 DYPDVLKFPD ELAHVEKASR VSAENLQKNL DQMKKQISDV ERDVQNFPAA TDEKDKFVEK 1090 1100 1110 1120 1130 1140 MTSFVKDAQE QYNKLRMMHS NMETLYKELG EYFLFDPKKL SVEEFFMDLH NFRNMFLQAV 1150 1160 1170 1180 1190 1200 KENQKRRETE EKMRRAKLAK EKAEKERLEK QQKREQLIDM NAEGDETGVM DSLLEALQSG 1210 1220 1230 1240 1250 1260 AAFRRKRGPR QANRKAGCAV TSLLASELTK DDAMAAVPAK VSKNSETFPT ILEEAKELVG RAS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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].
+	Additional computationally mapped references.

Web resources

Hereditary hearing loss homepage

Gene page

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.
IPI	IPI00852685. IPI00884341. IPI01009439.
RefSeq	NP_001073280.1. NM_001079812.2. NP_005210.3. NM_005219.4.
UniGene	Hs.529451.
3D structure databases
ProteinModelPortal	O60610.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60610. 12 interactions.
MINT	MINT-1198324.
STRING	9606.ENSP00000381565.
PTM databases
PhosphoSite	O60610.
2D gel databases
OGP	O60610.
Proteomic databases
PaxDb	O60610.
PRIDE	O60610.
Protocols and materials databases
DNASU	1729.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389057; ENSP00000373709; ENSG00000131504. ENST00000398557; ENSP00000381565; ENSG00000131504.
GeneID	1729.
KEGG	hsa:1729.
UCSC	uc003llb.4. human.
Organism-specific databases
CTD	1729.
GeneCards	GC05M140875.
HGNC	HGNC:2876. DIAPH1.
HPA	HPA004916.
MIM	124900. phenotype. 602121. gene.
neXtProt	NX_O60610.
Orphanet	90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKB	PA27333.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG149898.
HOGENOM	HOG000293231.
HOVERGEN	HBG051357.
KO	K05740.
Gene expression databases
ArrayExpress	O60610.
Bgee	O60610.
CleanEx	HS_DIAPH1.
Genevestigator	O60610.
GermOnline	ENSG00000131504. Homo sapiens.
Family and domain databases
InterPro	IPR003104. Actin-bd_FH2/DRF_autoreg. IPR016024. ARM-type_fold. IPR014767. Diaphanous_autoregulatory. IPR010465. Drf_DAD. IPR010472. Drf_FH3. IPR010473. Drf_GTPase-bd. IPR015425. FH2_actin-bd. IPR009408. Formin_homology_1. IPR014768. GTPase-bd/formin_homology_3. [Graphical view]
Pfam	PF06345. 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]
SMART	SM00498. FH2. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF101447. FH2_actin_bd. 1 hit.
PROSITE	PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DIAPH1. human.
GenomeRNAi	1729.
NextBio	6997.
SOURCE	Search...

Entry information

Entry name

DIAP1_HUMAN

Accession

Primary (citable) accession number: O60610
Secondary accession number(s): A6NF18 , B7ZKW2, E9PEZ2, Q17RN4, Q59FH8, Q9UC76

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.