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O60610

- DIAP1_HUMAN

UniProt

O60610 - DIAP1_HUMAN

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Protein

Protein diaphanous homolog 1

Gene
DIAPH1, DIAP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 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
Complete GO annotation...

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
Complete GO annotation...

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 – 11211Phosphotyrosine By 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.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 449366GBD/FH3Add
BLAST
Domaini583 – 764182FH1Add
BLAST
Domaini769 – 1171403FH2Add
BLAST
Domaini1194 – 122229DADAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili468 – 572105 Reviewed predictionAdd
BLAST
Coiled coili1039 – 1196158 Reviewed predictionAdd
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.

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei40 – 489Missing in isoform 2 and isoform 3. VSP_035870
Alternative sequencei621 – 63212Missing in isoform 2. VSP_035871Add
BLAST
Alternative sequencei826 – 8283Missing in isoform 2. VSP_035872

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131G → E in AAC05373. 1 Publication
Sequence conflicti609 – 6091Missing in AAI17258. 1 Publication
Sequence conflicti1156 – 11561R → A AA sequence 1 Publication
Sequence conflicti1157 – 11571E → K in AAC05373. 1 Publication
Sequence conflicti1157 – 11571E → K AA sequence 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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