Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NRN7

- ADPPT_HUMAN

UniProt

Q9NRN7 - ADPPT_HUMAN

Protein

L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase

Gene

AASDHPPT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (08 Nov 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.3 Publications

    Catalytic activityi

    CoA-[4'-phosphopantetheine] + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].

    Cofactori

    Binds 1 magnesium ion.2 Publications

    Kineticsi

    1. KM=0.44 mM for magnesium1 Publication
    2. KM=0.025 mM for coenzyme A1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471Coenzyme A
    Metal bindingi129 – 1291Magnesium
    Metal bindingi181 – 1811Magnesium

    GO - Molecular functioni

    1. holo-[acyl-carrier-protein] synthase activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. macromolecule biosynthetic process Source: InterPro
    2. pantothenate metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome
    4. vitamin metabolic process Source: Reactome
    5. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS14278-MONOMER.
    ReactomeiREACT_11172. Vitamin B5 (pantothenate) metabolism.
    SABIO-RKQ9NRN7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC:2.7.8.-)
    Alternative name(s):
    4'-phosphopantetheinyl transferase
    Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase
    Short name:
    AASD-PPT
    LYS5 ortholog
    Gene namesi
    ORF Names:CGI-80, HAH-P, HSPC223, x0005
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14235. AASDHPPT.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471R → A: Reduces affinity for magnesium 7-fold, and enzyme activity 2-fold. 1 Publication
    Mutagenesisi86 – 861R → A: Reduces affinity for magnesium and coenzyme A, and reduces enzyme activity 7-fold. 1 Publication
    Mutagenesisi111 – 1111H → A: Reduces affinity for magnesium 75-fold, and enzyme activity 150-fold. 1 Publication
    Mutagenesisi112 – 1121Q → E: Reduces affinity for magnesium 200-fold and abolishes enzyme activity; when associated with Q-181. 1 Publication
    Mutagenesisi129 – 1291D → A: Reduces affinity for magnesium 10-fold, and enzyme activity 30000-fold. 1 Publication
    Mutagenesisi181 – 1811E → A: Reduces affinity for magnesium 40-fold, and enzyme activity 32000-fold. 1 Publication
    Mutagenesisi181 – 1811E → Q: Reduces affinity for magnesium 20-fold, and enzyme activity 6500-fold. 1 Publication
    Mutagenesisi185 – 1851K → A: Reduces enzyme activity 2000-fold, with only minor change in the affinity for magnesium and coenzyme A. 1 Publication

    Organism-specific databases

    PharmGKBiPA24368.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferasePRO_0000175736Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei258 – 2581Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRN7.
    PaxDbiQ9NRN7.
    PeptideAtlasiQ9NRN7.
    PRIDEiQ9NRN7.

    PTM databases

    PhosphoSiteiQ9NRN7.

    Expressioni

    Tissue specificityi

    Detected in heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ9NRN7.
    BgeeiQ9NRN7.
    CleanExiHS_AASDHPPT.
    GenevestigatoriQ9NRN7.

    Organism-specific databases

    HPAiHPA026687.

    Interactioni

    Subunit structurei

    Monomer. Interacts with FASN.1 Publication

    Protein-protein interaction databases

    BioGridi121927. 16 interactions.
    IntActiQ9NRN7. 6 interactions.
    MINTiMINT-5005661.
    STRINGi9606.ENSP00000278618.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 215
    Helixi23 – 253
    Helixi30 – 389
    Helixi42 – 498
    Helixi54 – 7421
    Helixi79 – 813
    Beta strandi84 – 863
    Beta strandi92 – 943
    Beta strandi102 – 1043
    Beta strandi106 – 1127
    Beta strandi115 – 13218
    Beta strandi137 – 1393
    Helixi141 – 1477
    Helixi149 – 1513
    Helixi154 – 1607
    Beta strandi163 – 1653
    Helixi166 – 18722
    Helixi190 – 1923
    Helixi195 – 1973
    Beta strandi198 – 2014
    Beta strandi203 – 2064
    Beta strandi217 – 2204
    Beta strandi228 – 2369
    Beta strandi239 – 2468
    Beta strandi270 – 2723
    Helixi274 – 2774
    Turni278 – 2803
    Helixi289 – 2913
    Helixi298 – 3003
    Turni305 – 3073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BYDX-ray2.00A14-309[»]
    2C43X-ray1.93A14-309[»]
    2CG5X-ray2.70A14-309[»]
    ProteinModelPortaliQ9NRN7.
    SMRiQ9NRN7. Positions 14-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NRN7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni86 – 916Coenzyme A binding
    Regioni108 – 1114Coenzyme A binding
    Regioni181 – 1855Coenzyme A binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2091.
    HOGENOMiHOG000265195.
    HOVERGENiHBG080822.
    InParanoidiQ9NRN7.
    KOiK06133.
    OMAiSPRGKPY.
    PhylomeDBiQ9NRN7.
    TreeFamiTF313753.

    Family and domain databases

    Gene3Di3.90.470.20. 2 hits.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    [Graphical view]
    PfamiPF01648. ACPS. 1 hit.
    [Graphical view]
    SUPFAMiSSF56214. SSF56214. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRN7-1) [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

    MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ    50
    FVFARDAKAA MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN 100
    PYPNFNFNIS HQGDYAVLAA EPELQVGIDI MKTSFPGRGS IPEFFHIMKR 150
    KFTNKEWETI RSFKDEWTQL DMFYRNWALK ESFIKAIGVG LGFELQRLEF 200
    DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF VAVALRKPDG 250
    SRHQDVPSQD DSKPTQRQFT ILNFNDLMSS AVPMTPEDPS FWDCFCFTEE 300
    IPIRNGTKS 309
    Length:309
    Mass (Da):35,776
    Last modified:November 8, 2005 - v2
    Checksum:i6263E302600FDDED
    GO
    Isoform 2 (identifier: Q9NRN7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-138: R → T
         139-309: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:138
    Mass (Da):15,574
    Checksum:iEBB854D6A68B6AAC
    GO

    Sequence cautioni

    The sequence AAD34075.1 differs from that shown. Reason: Frameshift at positions 34 and 63.
    The sequence AAF86879.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1416PGRGSI → FQVVVQF in AAG49439. (PubMed:10931946)Curated
    Sequence conflicti307 – 3093TKS → YKVMMIP in AAG49439. (PubMed:10931946)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei138 – 1381R → T in isoform 2. 1 PublicationVSP_055783
    Alternative sequencei139 – 309171Missing in isoform 2. 1 PublicationVSP_055784Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302110 mRNA. Translation: AAG30872.1.
    AF151838 mRNA. Translation: AAD34075.1. Frameshift.
    AF151057 mRNA. Translation: AAF36143.1.
    AF136978 mRNA. Translation: AAG49439.1.
    AF201943 mRNA. Translation: AAF86879.1. Different initiation.
    AK312529 mRNA. Translation: BAG35428.1.
    AK293362 mRNA. Translation: BAG56878.1.
    AP001001 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67078.1.
    BC015470 mRNA. Translation: AAH15470.1.
    BC016728 mRNA. Translation: AAH16728.1.
    AL050073 mRNA. Translation: CAB43257.1.
    CCDSiCCDS31664.1.
    PIRiT08733.
    RefSeqiNP_056238.2. NM_015423.2.
    UniGeneiHs.524009.

    Genome annotation databases

    EnsembliENST00000278618; ENSP00000278618; ENSG00000149313. [Q9NRN7-1]
    ENST00000525660; ENSP00000437144; ENSG00000149313. [Q9NRN7-2]
    GeneIDi60496.
    KEGGihsa:60496.
    UCSCiuc001pjc.1. human.

    Polymorphism databases

    DMDMi81170356.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302110 mRNA. Translation: AAG30872.1 .
    AF151838 mRNA. Translation: AAD34075.1 . Frameshift.
    AF151057 mRNA. Translation: AAF36143.1 .
    AF136978 mRNA. Translation: AAG49439.1 .
    AF201943 mRNA. Translation: AAF86879.1 . Different initiation.
    AK312529 mRNA. Translation: BAG35428.1 .
    AK293362 mRNA. Translation: BAG56878.1 .
    AP001001 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67078.1 .
    BC015470 mRNA. Translation: AAH15470.1 .
    BC016728 mRNA. Translation: AAH16728.1 .
    AL050073 mRNA. Translation: CAB43257.1 .
    CCDSi CCDS31664.1.
    PIRi T08733.
    RefSeqi NP_056238.2. NM_015423.2.
    UniGenei Hs.524009.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BYD X-ray 2.00 A 14-309 [» ]
    2C43 X-ray 1.93 A 14-309 [» ]
    2CG5 X-ray 2.70 A 14-309 [» ]
    ProteinModelPortali Q9NRN7.
    SMRi Q9NRN7. Positions 14-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121927. 16 interactions.
    IntActi Q9NRN7. 6 interactions.
    MINTi MINT-5005661.
    STRINGi 9606.ENSP00000278618.

    PTM databases

    PhosphoSitei Q9NRN7.

    Polymorphism databases

    DMDMi 81170356.

    Proteomic databases

    MaxQBi Q9NRN7.
    PaxDbi Q9NRN7.
    PeptideAtlasi Q9NRN7.
    PRIDEi Q9NRN7.

    Protocols and materials databases

    DNASUi 60496.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278618 ; ENSP00000278618 ; ENSG00000149313 . [Q9NRN7-1 ]
    ENST00000525660 ; ENSP00000437144 ; ENSG00000149313 . [Q9NRN7-2 ]
    GeneIDi 60496.
    KEGGi hsa:60496.
    UCSCi uc001pjc.1. human.

    Organism-specific databases

    CTDi 60496.
    GeneCardsi GC11P105982.
    HGNCi HGNC:14235. AASDHPPT.
    HPAi HPA026687.
    MIMi 607756. gene.
    neXtProti NX_Q9NRN7.
    PharmGKBi PA24368.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2091.
    HOGENOMi HOG000265195.
    HOVERGENi HBG080822.
    InParanoidi Q9NRN7.
    KOi K06133.
    OMAi SPRGKPY.
    PhylomeDBi Q9NRN7.
    TreeFami TF313753.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS14278-MONOMER.
    Reactomei REACT_11172. Vitamin B5 (pantothenate) metabolism.
    SABIO-RK Q9NRN7.

    Miscellaneous databases

    EvolutionaryTracei Q9NRN7.
    GeneWikii AASDHPPT.
    GenomeRNAii 60496.
    NextBioi 65403.
    PROi Q9NRN7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRN7.
    Bgeei Q9NRN7.
    CleanExi HS_AASDHPPT.
    Genevestigatori Q9NRN7.

    Family and domain databases

    Gene3Di 3.90.470.20. 2 hits.
    InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
    [Graphical view ]
    Pfami PF01648. ACPS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56214. SSF56214. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene."
      Praphanphoj V., Sacksteder K.A., Gould S.J., Thomas G.H., Geraghty M.T.
      Mol. Genet. Metab. 72:336-342(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    5. "Novel genes expressed in human dendritic cell."
      Li N., Peng Y., Li Y., Gu W., Han Z., Fu G., Chen Z.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Dendritic cell.
    6. "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 1 AND 2).
      Tissue: Tongue and Urinary bladder.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Urinary bladder and Uterus.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-309 (ISOFORM 1).
      Tissue: Kidney.
    11. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 235-246, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    12. "Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity."
      Joshi A.K., Zhang L., Rangan V.S., Smith S.
      J. Biol. Chem. 278:33142-33149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Mechanism and substrate recognition of human holo ACP synthase."
      Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S., Oppermann U.
      Chem. Biol. 14:1243-1253(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 14-309 IN COMPLEXES WITH COENZYME A; MAGNESIUM IONS AND FASN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF ARG-47; ARG-86; HIS-111; GLN-112; ASP-129; GLU-181 AND LYS-185.

    Entry informationi

    Entry nameiADPPT_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRN7
    Secondary accession number(s): B2R6D1
    , B4DDW7, Q9C068, Q9P0Q3, Q9UG80, Q9Y389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 103 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3