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O60610

- DIAP1_HUMAN

UniProt

O60610 - DIAP1_HUMAN

Protein

Protein diaphanous homolog 1

Gene

DIAPH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    GO - Molecular functioni

    1. ion channel binding Source: BHF-UCL
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. receptor binding Source: ProtInc

    GO - Biological processi

    1. actin filament polymerization Source: Ensembl
    2. cellular response to histamine Source: BHF-UCL
    3. cytoskeleton organization Source: UniProtKB
    4. neuron projection development Source: Ensembl
    5. positive regulation of cell migration Source: Ensembl
    6. protein localization to microtubule Source: BHF-UCL
    7. regulation of cell shape Source: UniProtKB
    8. regulation of microtubule-based process Source: UniProtKB
    9. regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    10. sensory perception of sound Source: ProtInc

    Keywords - Biological processi

    Hearing

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein diaphanous homolog 1
    Alternative name(s):
    Diaphanous-related formin-1
    Short name:
    DRF1
    Gene namesi
    Name:DIAPH1
    Synonyms:DIAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2876. DIAPH1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. mitotic spindle Source: BHF-UCL
    3. neuron projection Source: Ensembl
    4. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Deafness, Non-syndromic deafness

    Organism-specific databases

    MIMi124900. phenotype.
    Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    PharmGKBiPA27333.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12721272Protein diaphanous homolog 1PRO_0000194893Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei22 – 221Phosphoserine3 Publications
    Cross-linki486 – 486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei1057 – 10571N6-acetyllysine1 Publication
    Modified residuei1103 – 11031N6-acetyllysine1 Publication
    Modified residuei1121 – 11211PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO60610.
    PaxDbiO60610.
    PRIDEiO60610.

    2D gel databases

    OGPiO60610.

    PTM databases

    PhosphoSiteiO60610.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO60610.
    BgeeiO60610.
    CleanExiHS_DIAPH1.
    GenevestigatoriO60610.

    Organism-specific databases

    HPAiHPA004916.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORFQ9Q2G42EBI-3959709,EBI-6248094From a different organism.
    PPM1FP495933EBI-3959709,EBI-719945
    RHOAP615863EBI-3959709,EBI-446668

    Protein-protein interaction databases

    BioGridi108073. 29 interactions.
    IntActiO60610. 19 interactions.
    MINTiMINT-1198324.
    STRINGi9606.ENSP00000381565.

    Structurei

    3D structure databases

    ProteinModelPortaliO60610.
    SMRiO60610. Positions 92-461, 762-1215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 449366GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini583 – 764182FH1Add
    BLAST
    Domaini769 – 1171403FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1194 – 122229DADPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili468 – 572105Sequence AnalysisAdd
    BLAST
    Coiled coili1039 – 1196158Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1213 – 12164Arg/Lys-rich (basic)

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
    Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
    Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG149898.
    HOGENOMiHOG000293231.
    HOVERGENiHBG051357.
    KOiK05740.
    PhylomeDBiO60610.
    TreeFamiTF315383.

    Family and domain databases

    InterProiIPR016024. 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]
    PANTHERiPTHR23213:SF17. PTHR23213:SF17. 1 hit.
    PfamiPF06345. 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]
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60610-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFT LKRLMADELE     50
    RFTSMRIKKE KEKPNSAHRN SSASYGDDPT AQSLQDVSDE QVLVLFEQML 100
    LDMNLNEEKQ QPLREKDIII KREMVSQYLY TSKAGMSQKE SSKSAMMYIQ 150
    ELRSGLRDMP LLSCLESLRV SLNNNPVSWV QTFGAEGLAS LLDILKRLHD 200
    EKEETAGSYD SRNKHEIIRC LKAFMNNKFG IKTMLETEEG ILLLVRAMDP 250
    AVPNMMIDAA KLLSALCILP QPEDMNERVL EAMTERAEMD EVERFQPLLD 300
    GLKSGTTIAL KVGCLQLINA LITPAEELDF RVHIRSELMR LGLHQVLQDL 350
    REIENEDMRV QLNVFDEQGE EDSYDLKGRL DDIRMEMDDF NEVFQILLNT 400
    VKDSKAEPHF LSILQHLLLV RNDYEARPQY YKLIEECISQ IVLHKNGADP 450
    DFKCRHLQIE IEGLIDQMID KTKVEKSEAK AAELEKKLDS ELTARHELQV 500
    EMKKMESDFE QKLQDLQGEK DALHSEKQQI ATEKQDLEAE VSQLTGEVAK 550
    LTKELEDAKK EMASLSAAAI TVPPSVPSRA PVPPAPPLPG DSGTIIPPPP 600
    APGDSTTPPP PPPPPPPPPP LPGGVCISSP PSLPGGTAIS PPPPLSGDAT 650
    IPPPPPLPEG VGIPSPSSLP GGTAIPPPPP LPGSARIPPP PPPLPGSAGI 700
    PPPPPPLPGE AGMPPPPPPL PGGPGIPPPP PFPGGPGIPP PPPGMGMPPP 750
    PPFGFGVPAA PVLPFGLTPK KLYKPEVQLR RPNWSKLVAE DLSQDCFWTK 800
    VKEDRFENNE LFAKLTLTFS AQTKTSKAKK DQEGGEEKKS VQKKKVKELK 850
    VLDSKTAQNL SIFLGSFRMP YQEIKNVILE VNEAVLTESM IQNLIKQMPE 900
    PEQLKMLSEL KDEYDDLAES EQFGVVMGTV PRLRPRLNAI LFKLQFSEQV 950
    ENIKPEIVSV TAACEELRKS ESFSNLLEIT LLVGNYMNAG SRNAGAFGFN 1000
    ISFLCKLRDT KSTDQKMTLL HFLAELCEND YPDVLKFPDE LAHVEKASRV 1050
    SAENLQKNLD QMKKQISDVE RDVQNFPAAT DEKDKFVEKM TSFVKDAQEQ 1100
    YNKLRMMHSN METLYKELGE YFLFDPKKLS VEEFFMDLHN FRNMFLQAVK 1150
    ENQKRRETEE KMRRAKLAKE KAEKERLEKQ QKREQLIDMN AEGDETGVMD 1200
    SLLEALQSGA AFRRKRGPRQ ANRKAGCAVT SLLASELTKD DAMAAVPAKV 1250
    SKNSETFPTI LEEAKELVGR AS 1272
    Length:1,272
    Mass (Da):141,347
    Last modified:November 25, 2008 - v2
    Checksum:i9C8273DE4748564F
    GO
    Isoform 2 (identifier: O60610-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-48: Missing.
         621-632: Missing.
         826-828: Missing.

    Show »
    Length:1,248
    Mass (Da):138,907
    Checksum:i7F17EB0B99DB3519
    GO
    Isoform 3 (identifier: O60610-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-48: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,263
    Mass (Da):140,289
    Checksum:i394E98CBBB2DDA4D
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131G → E in AAC05373. (PubMed:9360932)Curated
    Sequence conflicti609 – 6091Missing in AAI17258. (PubMed:15489334)Curated
    Sequence conflicti1156 – 11561R → A AA sequence (PubMed:7737110)Curated
    Sequence conflicti1157 – 11571E → K in AAC05373. (PubMed:9360932)Curated
    Sequence conflicti1157 – 11571E → K AA sequence (PubMed:7737110)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei40 – 489Missing in isoform 2 and isoform 3. 4 PublicationsVSP_035870
    Alternative sequencei621 – 63212Missing in isoform 2. 3 PublicationsVSP_035871Add
    BLAST
    Alternative sequencei826 – 8283Missing in isoform 2. 3 PublicationsVSP_035872

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43373.1. [O60610-3]
    CCDS43374.1. [O60610-1]
    RefSeqiNP_001073280.1. NM_001079812.2. [O60610-3]
    NP_005210.3. NM_005219.4. [O60610-1]
    UniGeneiHs.529451.

    Genome annotation databases

    EnsembliENST00000389057; ENSP00000373709; ENSG00000131504. [O60610-3]
    ENST00000398557; ENSP00000381565; ENSG00000131504. [O60610-1]
    GeneIDi1729.
    KEGGihsa:1729.
    UCSCiuc003llb.4. human. [O60610-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Hereditary hearing loss homepage

    Gene page

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS43373.1. [O60610-3 ]
    CCDS43374.1. [O60610-1 ]
    RefSeqi NP_001073280.1. NM_001079812.2. [O60610-3 ]
    NP_005210.3. NM_005219.4. [O60610-1 ]
    UniGenei Hs.529451.

    3D structure databases

    ProteinModelPortali O60610.
    SMRi O60610. Positions 92-461, 762-1215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108073. 29 interactions.
    IntActi O60610. 19 interactions.
    MINTi MINT-1198324.
    STRINGi 9606.ENSP00000381565.

    PTM databases

    PhosphoSitei O60610.

    2D gel databases

    OGPi O60610.

    Proteomic databases

    MaxQBi O60610.
    PaxDbi O60610.
    PRIDEi O60610.

    Protocols and materials databases

    DNASUi 1729.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389057 ; ENSP00000373709 ; ENSG00000131504 . [O60610-3 ]
    ENST00000398557 ; ENSP00000381565 ; ENSG00000131504 . [O60610-1 ]
    GeneIDi 1729.
    KEGGi hsa:1729.
    UCSCi uc003llb.4. human. [O60610-1 ]

    Organism-specific databases

    CTDi 1729.
    GeneCardsi GC05M140875.
    GeneReviewsi DIAPH1.
    HGNCi HGNC:2876. DIAPH1.
    HPAi HPA004916.
    MIMi 124900. phenotype.
    602121. gene.
    neXtProti NX_O60610.
    Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    PharmGKBi PA27333.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149898.
    HOGENOMi HOG000293231.
    HOVERGENi HBG051357.
    KOi K05740.
    PhylomeDBi O60610.
    TreeFami TF315383.

    Miscellaneous databases

    ChiTaRSi DIAPH1. human.
    GeneWikii DIAPH1.
    GenomeRNAii 1729.
    NextBioi 6997.
    PROi O60610.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60610.
    Bgeei O60610.
    CleanExi HS_DIAPH1.
    Genevestigatori O60610.

    Family and domain databases

    InterProi IPR016024. 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 ]
    PANTHERi PTHR23213:SF17. PTHR23213:SF17. 1 hit.
    Pfami 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 ]
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      Tissue: Mammary cancer.
    9. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDIAP1_HUMAN
    AccessioniPrimary (citable) accession number: O60610
    Secondary accession number(s): A6NF18
    , B7ZKW2, E9PEZ2, Q17RN4, Q59FH8, Q9UC76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3