ADPPT_HUMAN
ID ADPPT_HUMAN Reviewed; 309 AA.
AC Q9NRN7; B2R6D1; B4DDW7; Q9C068; Q9P0Q3; Q9UG80; Q9Y389;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE EC=2.7.8.7 {ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563, ECO:0000269|PubMed:19933275, ECO:0000269|PubMed:21238436};
DE AltName: Full=4'-phosphopantetheinyl transferase;
DE AltName: Full=Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE Short=AASD-PPT;
DE AltName: Full=LYS5 ortholog;
GN Name=AASDHPPT; ORFNames=CGI-80, HAH-P, HSPC223, x0005;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11286508; DOI=10.1006/mgme.2000.3138;
RA Praphanphoj V., Sacksteder K.A., Gould S.J., Thomas G.H., Geraghty M.T.;
RT "Identification of the alpha-aminoadipic semialdehyde dehydrogenase-
RT phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5
RT gene.";
RL Mol. Genet. Metab. 72:336-342(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Li N., Peng Y., Li Y., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Tongue, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-309 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP PROTEIN SEQUENCE OF 235-246, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=12815048; DOI=10.1074/jbc.m305459200;
RA Joshi A.K., Zhang L., Rangan V.S., Smith S.;
RT "Cloning, expression, and characterization of a human 4'-
RT phosphopantetheinyl transferase with broad substrate specificity.";
RL J. Biol. Chem. 278:33142-33149(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19933275; DOI=10.1074/jbc.m109.080556;
RA Strickland K.C., Hoeferlin L.A., Oleinik N.V., Krupenko N.I.,
RA Krupenko S.A.;
RT "Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates
RT 10-formyltetrahydrofolate dehydrogenase.";
RL J. Biol. Chem. 285:1627-1633(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21238436; DOI=10.1016/j.cbi.2011.01.008;
RA Strickland K.C., Krupenko N.I., Dubard M.E., Hu C.J., Tsybovsky Y.,
RA Krupenko S.A.;
RT "Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate
RT dehydrogenase.";
RL Chem. Biol. Interact. 191:129-136(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 14-309 IN COMPLEXES WITH COENZYME
RP A; MAGNESIUM IONS AND FASN, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF ARG-47; ARG-86;
RP HIS-111; GLN-112; ASP-129; GLU-181 AND LYS-185.
RX PubMed=18022563; DOI=10.1016/j.chembiol.2007.10.013;
RA Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S.,
RA Oppermann U.;
RT "Mechanism and substrate recognition of human holo ACP synthase.";
RL Chem. Biol. 14:1243-1253(2007).
CC -!- FUNCTION: Catalyzes the post-translational modification of target
CC proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine
CC moiety from coenzyme A, regardless of whether the CoA is presented in
CC the free thiol form or as an acetyl thioester, to a serine residue of a
CC broad range of acceptors including the acyl carrier domain of FASN.
CC {ECO:0000269|PubMed:11286508, ECO:0000269|PubMed:12815048,
CC ECO:0000269|PubMed:18022563, ECO:0000269|PubMed:19933275,
CC ECO:0000269|PubMed:21238436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563,
CC ECO:0000269|PubMed:19933275, ECO:0000269|PubMed:21238436};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12069;
CC Evidence={ECO:0000269|PubMed:19933275, ECO:0000269|PubMed:21238436};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + apo-[ACP] = acetyl-[ACP] + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:46564, Rhea:RHEA-COMP:9621,
CC Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58343, ChEBI:CHEBI:78446;
CC Evidence={ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46565;
CC Evidence={ECO:0000305|PubMed:12815048};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:12815048,
CC ECO:0000269|PubMed:18022563};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 mM for magnesium {ECO:0000269|PubMed:18022563};
CC KM=0.025 mM for coenzyme A {ECO:0000269|PubMed:18022563};
CC pH dependence:
CC Optimum pH is 6-10. {ECO:0000269|PubMed:12815048};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12815048}.
CC -!- INTERACTION:
CC Q9NRN7; O43186: CRX; NbExp=3; IntAct=EBI-740884, EBI-748171;
CC Q9NRN7; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-740884, EBI-2349927;
CC Q9NRN7; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-740884, EBI-747107;
CC Q9NRN7; Q12933: TRAF2; NbExp=7; IntAct=EBI-740884, EBI-355744;
CC Q9NRN7; Q9UPT9: USP22; NbExp=6; IntAct=EBI-740884, EBI-723510;
CC Q9NRN7; Q9UPT9-2: USP22; NbExp=11; IntAct=EBI-740884, EBI-12074414;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12815048}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRN7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRN7-2; Sequence=VSP_055783, VSP_055784;
CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, placenta,
CC testis, brain, pancreas, liver and kidney.
CC {ECO:0000269|PubMed:11286508, ECO:0000269|PubMed:12815048}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34075.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF86879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF302110; AAG30872.1; -; mRNA.
DR EMBL; AF151838; AAD34075.1; ALT_FRAME; mRNA.
DR EMBL; AF151057; AAF36143.1; -; mRNA.
DR EMBL; AF136978; AAG49439.1; -; mRNA.
DR EMBL; AF201943; AAF86879.1; ALT_INIT; mRNA.
DR EMBL; AK312529; BAG35428.1; -; mRNA.
DR EMBL; AK293362; BAG56878.1; -; mRNA.
DR EMBL; AP001001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67078.1; -; Genomic_DNA.
DR EMBL; BC015470; AAH15470.1; -; mRNA.
DR EMBL; BC016728; AAH16728.1; -; mRNA.
DR EMBL; AL050073; CAB43257.1; -; mRNA.
DR CCDS; CCDS31664.1; -. [Q9NRN7-1]
DR PIR; T08733; T08733.
DR RefSeq; NP_056238.2; NM_015423.2. [Q9NRN7-1]
DR PDB; 2BYD; X-ray; 2.00 A; A=14-309.
DR PDB; 2C43; X-ray; 1.93 A; A=14-309.
DR PDB; 2CG5; X-ray; 2.70 A; A=14-309.
DR PDBsum; 2BYD; -.
DR PDBsum; 2C43; -.
DR PDBsum; 2CG5; -.
DR AlphaFoldDB; Q9NRN7; -.
DR SMR; Q9NRN7; -.
DR BioGRID; 121927; 60.
DR IntAct; Q9NRN7; 25.
DR MINT; Q9NRN7; -.
DR STRING; 9606.ENSP00000278618; -.
DR ChEMBL; CHEMBL3137295; -.
DR SwissLipids; SLP:000001260; -.
DR iPTMnet; Q9NRN7; -.
DR PhosphoSitePlus; Q9NRN7; -.
DR SwissPalm; Q9NRN7; -.
DR BioMuta; AASDHPPT; -.
DR DMDM; 81170356; -.
DR EPD; Q9NRN7; -.
DR jPOST; Q9NRN7; -.
DR MassIVE; Q9NRN7; -.
DR MaxQB; Q9NRN7; -.
DR PaxDb; Q9NRN7; -.
DR PeptideAtlas; Q9NRN7; -.
DR PRIDE; Q9NRN7; -.
DR ProteomicsDB; 3900; -.
DR ProteomicsDB; 82396; -. [Q9NRN7-1]
DR Antibodypedia; 18138; 221 antibodies from 26 providers.
DR DNASU; 60496; -.
DR Ensembl; ENST00000278618.9; ENSP00000278618.4; ENSG00000149313.11. [Q9NRN7-1]
DR Ensembl; ENST00000525660.1; ENSP00000437144.1; ENSG00000149313.11. [Q9NRN7-2]
DR GeneID; 60496; -.
DR KEGG; hsa:60496; -.
DR MANE-Select; ENST00000278618.9; ENSP00000278618.4; NM_015423.3; NP_056238.2.
DR UCSC; uc001pjc.2; human. [Q9NRN7-1]
DR CTD; 60496; -.
DR DisGeNET; 60496; -.
DR GeneCards; AASDHPPT; -.
DR HGNC; HGNC:14235; AASDHPPT.
DR HPA; ENSG00000149313; Low tissue specificity.
DR MIM; 607756; gene.
DR neXtProt; NX_Q9NRN7; -.
DR OpenTargets; ENSG00000149313; -.
DR PharmGKB; PA24368; -.
DR VEuPathDB; HostDB:ENSG00000149313; -.
DR eggNOG; KOG0945; Eukaryota.
DR GeneTree; ENSGT00390000004663; -.
DR HOGENOM; CLU_1854476_0_0_1; -.
DR InParanoid; Q9NRN7; -.
DR OMA; IPWSEIR; -.
DR OrthoDB; 960416at2759; -.
DR PhylomeDB; Q9NRN7; -.
DR TreeFam; TF313753; -.
DR BioCyc; MetaCyc:HS14278-MON; -.
DR BRENDA; 2.7.8.7; 2681.
DR PathwayCommons; Q9NRN7; -.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR SABIO-RK; Q9NRN7; -.
DR SignaLink; Q9NRN7; -.
DR BioGRID-ORCS; 60496; 311 hits in 1056 CRISPR screens.
DR ChiTaRS; AASDHPPT; human.
DR EvolutionaryTrace; Q9NRN7; -.
DR GeneWiki; AASDHPPT; -.
DR GenomeRNAi; 60496; -.
DR Pharos; Q9NRN7; Tbio.
DR PRO; PR:Q9NRN7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NRN7; protein.
DR Bgee; ENSG00000149313; Expressed in cortical plate and 208 other tissues.
DR ExpressionAtlas; Q9NRN7; baseline and differential.
DR Genevisible; Q9NRN7; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IMP:UniProtKB.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR GO; GO:0051604; P:protein maturation; IDA:UniProtKB.
DR Gene3D; 3.90.470.20; -; 2.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175736"
FT BINDING 47
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43, ECO:0007744|PDB:2CG5"
FT BINDING 86..91
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43, ECO:0007744|PDB:2CG5"
FT BINDING 108..111
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43, ECO:0007744|PDB:2CG5"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43"
FT BINDING 181..185
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43, ECO:0007744|PDB:2CG5"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18022563,
FT ECO:0007744|PDB:2C43"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 138
FT /note="R -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055783"
FT VAR_SEQ 139..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055784"
FT MUTAGEN 47
FT /note="R->A: Reduces affinity for magnesium by 7-fold, and
FT holo-[acyl-carrier-protein] synthase activity by 2-fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 86
FT /note="R->A: Reduces affinity for magnesium and coenzyme A,
FT and reduces holo-[acyl-carrier-protein] synthase activity
FT by 7-fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 111
FT /note="H->A: Reduces affinity for magnesium by 75-fold, and
FT holo-[acyl-carrier-protein] synthase activity by 150-fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 112
FT /note="Q->E: Reduces affinity for magnesium by 200-fold and
FT abolishes holo-[acyl-carrier-protein] synthase activity;
FT when associated with Q-181."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 129
FT /note="D->A: Reduces affinity for magnesium by 10-fold, and
FT holo-[acyl-carrier-protein] synthase activity by 30000-
FT fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 181
FT /note="E->A: Reduces affinity for magnesium by 40-fold, and
FT holo-[acyl-carrier-protein] synthase activity by 32000-
FT fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 181
FT /note="E->Q: Reduces affinity for magnesium by 20-fold, and
FT holo-[acyl-carrier-protein] synthase activity by 6500-
FT fold."
FT /evidence="ECO:0000269|PubMed:18022563"
FT MUTAGEN 185
FT /note="K->A: Reduces holo-[acyl-carrier-protein] synthase
FT activity by 2000-fold, with only minor change in the
FT affinity for magnesium and coenzyme A."
FT /evidence="ECO:0000269|PubMed:18022563"
FT CONFLICT 136..141
FT /note="PGRGSI -> FQVVVQF (in Ref. 4; AAG49439)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..309
FT /note="TKS -> YKVMMIP (in Ref. 4; AAG49439)"
FT /evidence="ECO:0000305"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 115..132
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 166..187
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2BYD"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2BYD"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2C43"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2C43"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2C43"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2C43"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2BYD"
SQ SEQUENCE 309 AA; 35776 MW; 6263E302600FDDED CRC64;
MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ FVFARDAKAA
MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN PYPNFNFNIS HQGDYAVLAA
EPELQVGIDI MKTSFPGRGS IPEFFHIMKR KFTNKEWETI RSFKDEWTQL DMFYRNWALK
ESFIKAIGVG LGFELQRLEF DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF
VAVALRKPDG SRHQDVPSQD DSKPTQRQFT ILNFNDLMSS AVPMTPEDPS FWDCFCFTEE
IPIRNGTKS
