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O75689

- ADAP1_HUMAN

UniProt

O75689 - ADAP1_HUMAN

Protein

Arf-GAP with dual PH domain-containing protein 1

Gene

ADAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    GTPase-activating protein for the ADP ribosylation factor family Probable. Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).1 Publication1 PublicationCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri21 – 4424C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: UniProtKB
    2. inositol 1,3,4,5 tetrakisphosphate binding Source: UniProtKB
    3. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
    4. protein binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. positive regulation of GTPase activity Source: GOC
    3. regulation of ARF GTPase activity Source: InterPro
    4. regulation of GTPase activity Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arf-GAP with dual PH domain-containing protein 1
    Alternative name(s):
    Centaurin-alpha-1
    Short name:
    Cnt-a1
    Putative MAPK-activating protein PM25
    Gene namesi
    Name:ADAP1
    Synonyms:CENTA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:16486. ADAP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211C → A: Loss of GTPase-activating activity. 1 Publication
    Mutagenesisi24 – 241C → A: Loss of GTPase-activating activity. 1 Publication
    Mutagenesisi149 – 1491R → C: 40-45% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-273. 2 Publications
    Mutagenesisi273 – 2731R → C: 70% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-149. 2 Publications

    Organism-specific databases

    PharmGKBiPA26404.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 374374Arf-GAP with dual PH domain-containing protein 1PRO_0000074205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine; by PKC1 Publication
    Modified residuei272 – 2721N6-acetyllysine1 Publication
    Modified residuei276 – 2761Phosphothreonine; by PKC1 Publication

    Post-translational modificationi

    Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75689.
    PaxDbiO75689.
    PRIDEiO75689.

    PTM databases

    PhosphoSiteiO75689.

    Expressioni

    Tissue specificityi

    Expressed at highest levels in brain and at lower levels in peripheral blood leukocytes.1 Publication

    Gene expression databases

    BgeeiO75689.
    CleanExiHS_ADAP1.
    GenevestigatoriO75689.

    Organism-specific databases

    HPAiHPA007033.
    HPA012049.

    Interactioni

    Subunit structurei

    Interacts with PRKCA, PRKCI and PRKCZ. Interacts with the N-terminal region of PRKD1.1 Publication

    Protein-protein interaction databases

    BioGridi116222. 13 interactions.
    DIPiDIP-41731N.
    IntActiO75689. 5 interactions.
    MINTiMINT-193767.
    STRINGi9606.ENSP00000265846.

    Structurei

    Secondary structure

    1
    374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Helixi16 – 183
    Turni22 – 243
    Beta strandi31 – 333
    Turni34 – 374
    Beta strandi38 – 403
    Helixi42 – 498
    Turni52 – 543
    Beta strandi57 – 593
    Turni60 – 623
    Helixi67 – 759
    Helixi78 – 858
    Turni86 – 883
    Helixi102 – 11312
    Turni117 – 1193
    Helixi121 – 1244
    Helixi125 – 1284
    Beta strandi129 – 13911
    Beta strandi141 – 1433
    Beta strandi146 – 1549
    Turni155 – 1584
    Beta strandi159 – 1635
    Beta strandi165 – 1673
    Beta strandi172 – 1765
    Helixi177 – 1793
    Beta strandi180 – 1845
    Helixi186 – 1894
    Beta strandi195 – 2017
    Beta strandi204 – 2118
    Helixi215 – 23622
    Beta strandi237 – 2404
    Helixi242 – 2454
    Helixi246 – 2483
    Beta strandi254 – 2618
    Beta strandi271 – 2788
    Beta strandi281 – 2877
    Beta strandi294 – 2985
    Helixi302 – 3043
    Beta strandi307 – 3115
    Beta strandi323 – 3286
    Beta strandi333 – 3408
    Helixi341 – 35616
    Helixi363 – 3697

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FEHX-ray1.90A3-370[»]
    3FM8X-ray2.30C/D1-374[»]
    3LJUX-ray1.70X3-370[»]
    3MDBX-ray2.95C/D1-374[»]
    ProteinModelPortaliO75689.
    SMRiO75689. Positions 2-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75689.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 126120Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini129 – 230102PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini252 – 356105PH 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri21 – 4424C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    HOGENOMiHOG000006719.
    HOVERGENiHBG050888.
    InParanoidiO75689.
    OrthoDBiEOG71K62W.
    PhylomeDBiO75689.
    TreeFamiTF324540.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR001164. ArfGAP.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF01412. ArfGap. 1 hit.
    [Graphical view]
    PRINTSiPR00405. REVINTRACTNG.
    SMARTiSM00105. ArfGap. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view]
    PROSITEiPS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75689-1) [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

    MAKERRRAVL ELLQRPGNAR CADCGAPDPD WASYTLGVFI CLSCSGIHRN    50
    IPQVSKVKSV RLDAWEEAQV EFMASHGNDA ARARFESKVP SFYYRPTPSD 100
    CQLLREQWIR AKYERQEFIY PEKQEPYSAG YREGFLWKRG RDNGQFLSRK 150
    FVLTEREGAL KYFNRNDAKE PKAVMKIEHL NATFQPAKIG HPHGLQVTYL 200
    KDNSTRNIFI YHEDGKEIVD WFNALRAARF HYLQVAFPGA GDADLVPKLS 250
    RNYLKEGYME KTGPKQTEGF RKRWFTMDDR RLMYFKDPLD AFARGEVFIG 300
    SKESGYTVLH GFPPSTQGHH WPHGITIVTP DRKFLFACET ESDQREWVAA 350
    FQKAVDRPML PQEYAVEAHF KHKP 374
    Length:374
    Mass (Da):43,395
    Last modified:November 25, 2008 - v2
    Checksum:i38547281FB09D9B9
    GO
    Isoform 2 (identifier: O75689-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MAKERRRAVLELLQRPGNARCADCGAP → MFQFVFSRVYCINPARRKWKEFEKMLGCAEEGHASLGR

    Show »
    Length:385
    Mass (Da):44,936
    Checksum:i67ACBB2A85819D46
    GO
    Isoform 3 (identifier: O75689-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Show »
    Length:302
    Mass (Da):35,353
    Checksum:i8197A42910488E1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151G → R in BAG52556. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411G → S.4 Publications
    Corresponds to variant rs10256887 [ dbSNP | Ensembl ].
    VAR_047470

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 3. 1 PublicationVSP_054793Add
    BLAST
    Alternative sequencei1 – 2727MAKER…DCGAP → MFQFVFSRVYCINPARRKWK EFEKMLGCAEEGHASLGR in isoform 2. 1 PublicationVSP_054794Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006422 mRNA. Translation: CAA07024.1.
    AF082324 mRNA. Translation: AAD11414.1.
    AB097049 mRNA. Translation: BAC77402.1.
    AK300999 mRNA. Translation: BAG62618.1.
    AC073957 Genomic DNA. No translation available.
    AK092471 mRNA. Translation: BAG52556.1.
    CH236965 Genomic DNA. Translation: EAL23709.1.
    CH471144 Genomic DNA. Translation: EAW87183.1.
    CH471144 Genomic DNA. Translation: EAW87184.1.
    BC033747 mRNA. Translation: AAH33747.1.
    CCDSiCCDS5318.1. [O75689-1]
    CCDS64576.1. [O75689-3]
    CCDS64577.1. [O75689-2]
    PIRiJC7091.
    RefSeqiNP_001271237.1. NM_001284308.1.
    NP_001271238.1. NM_001284309.1.
    NP_001271239.1. NM_001284310.1.
    NP_001271240.1. NM_001284311.1.
    NP_006860.1. NM_006869.3.
    UniGeneiHs.602573.

    Genome annotation databases

    EnsembliENST00000265846; ENSP00000265846; ENSG00000105963. [O75689-1]
    ENST00000449296; ENSP00000407267; ENSG00000105963. [O75689-3]
    ENST00000539900; ENSP00000442682; ENSG00000105963. [O75689-2]
    GeneIDi11033.
    KEGGihsa:11033.
    UCSCiuc003sjm.4. human. [O75689-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006422 mRNA. Translation: CAA07024.1 .
    AF082324 mRNA. Translation: AAD11414.1 .
    AB097049 mRNA. Translation: BAC77402.1 .
    AK300999 mRNA. Translation: BAG62618.1 .
    AC073957 Genomic DNA. No translation available.
    AK092471 mRNA. Translation: BAG52556.1 .
    CH236965 Genomic DNA. Translation: EAL23709.1 .
    CH471144 Genomic DNA. Translation: EAW87183.1 .
    CH471144 Genomic DNA. Translation: EAW87184.1 .
    BC033747 mRNA. Translation: AAH33747.1 .
    CCDSi CCDS5318.1. [O75689-1 ]
    CCDS64576.1. [O75689-3 ]
    CCDS64577.1. [O75689-2 ]
    PIRi JC7091.
    RefSeqi NP_001271237.1. NM_001284308.1.
    NP_001271238.1. NM_001284309.1.
    NP_001271239.1. NM_001284310.1.
    NP_001271240.1. NM_001284311.1.
    NP_006860.1. NM_006869.3.
    UniGenei Hs.602573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FEH X-ray 1.90 A 3-370 [» ]
    3FM8 X-ray 2.30 C/D 1-374 [» ]
    3LJU X-ray 1.70 X 3-370 [» ]
    3MDB X-ray 2.95 C/D 1-374 [» ]
    ProteinModelPortali O75689.
    SMRi O75689. Positions 2-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116222. 13 interactions.
    DIPi DIP-41731N.
    IntActi O75689. 5 interactions.
    MINTi MINT-193767.
    STRINGi 9606.ENSP00000265846.

    PTM databases

    PhosphoSitei O75689.

    Proteomic databases

    MaxQBi O75689.
    PaxDbi O75689.
    PRIDEi O75689.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265846 ; ENSP00000265846 ; ENSG00000105963 . [O75689-1 ]
    ENST00000449296 ; ENSP00000407267 ; ENSG00000105963 . [O75689-3 ]
    ENST00000539900 ; ENSP00000442682 ; ENSG00000105963 . [O75689-2 ]
    GeneIDi 11033.
    KEGGi hsa:11033.
    UCSCi uc003sjm.4. human. [O75689-1 ]

    Organism-specific databases

    CTDi 11033.
    GeneCardsi GC07M000905.
    HGNCi HGNC:16486. ADAP1.
    HPAi HPA007033.
    HPA012049.
    MIMi 608114. gene.
    neXtProti NX_O75689.
    PharmGKBi PA26404.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000006719.
    HOVERGENi HBG050888.
    InParanoidi O75689.
    OrthoDBi EOG71K62W.
    PhylomeDBi O75689.
    TreeFami TF324540.

    Miscellaneous databases

    ChiTaRSi ADAP1. human.
    EvolutionaryTracei O75689.
    GeneWikii Centaurin,_alpha_1.
    GenomeRNAii 11033.
    NextBioi 35469618.
    PROi O75689.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75689.
    CleanExi HS_ADAP1.
    Genevestigatori O75689.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR001164. ArfGAP.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF01412. ArfGap. 1 hit.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00105. ArfGap. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view ]
    PROSITEi PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional characterization of a human homologue of centaurin-alpha."
      Venkateswarlu K., Cullen P.J.
      Biochem. Biophys. Res. Commun. 262:237-244(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-149 AND ARG-273.
      Tissue: Blood1 Publication.
    2. "Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1."
      Venkateswarlu K., Oatey P.B., Tavare J.M., Jackson T.R., Cullen P.J.
      Biochem. J. 340:359-363(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-21; CYS-24; ARG-149 AND ARG-273, VARIANT SER-241.
      Tissue: Peripheral bloodImported.
    3. "Molecular identification of a high-affinity Ins(1,3,4,5)tetrakisphosphate/phosphatidylinositol(3,4, 5)trisphosphate binding protein from human brain, p42IP4."
      Horstmeyer A., Reiser G.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-241.
      Tissue: BrainImported.
    4. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
      Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
      Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-241.
      Tissue: Lung fibroblast.
    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] (ISOFORMS 2 AND 3).
      Tissue: Small intestine.
    6. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT SER-241.
      Tissue: BrainImported.
    9. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
      Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
      Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCA; PRKCI; PRKCZ AND PRKD1, PHOSPHORYLATION AT SER-87 AND THR-276.
    10. "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-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of full length centaurin alpha-1."
      Structural genomics consortium (SGC)
      Submitted (DEC-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-370.

    Entry informationi

    Entry nameiADAP1_HUMAN
    AccessioniPrimary (citable) accession number: O75689
    Secondary accession number(s): A4D2Q2
    , B3KRZ4, B4DVA6, F6XZ68, H7C2Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 122 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3