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Q9NRN7 (ADPPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AASDHPPT
ORF Names:CGI-80, HAH-P, HSPC223, x0005
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.11 Ref.16

Catalytic activity

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

Cofactor

Binds 1 magnesium ion. Ref.11 Ref.16

Subunit structure

Monomer. Interacts with FASN. Ref.11

Subcellular location

Cytoplasm Ref.11.

Tissue specificity

Detected in heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. Ref.1 Ref.11

Sequence similarities

Belongs to the P-Pant transferase superfamily. AcpS family.

Biophysicochemical properties

Kinetic parameters:

KM=0.44 mM for magnesium Ref.16

KM=0.025 mM for coenzyme A

Sequence caution

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
PRO_0000175736

Regions

Region86 – 916Coenzyme A binding
Region108 – 1114Coenzyme A binding
Region181 – 1855Coenzyme A binding

Sites

Metal binding1291Magnesium
Metal binding1811Magnesium
Binding site471Coenzyme A

Amino acid modifications

Modified residue2581Phosphoserine Ref.12 Ref.13 Ref.14

Experimental info

Mutagenesis471R → A: Reduces affinity for magnesium 7-fold, and enzyme activity 2-fold. Ref.16
Mutagenesis861R → A: Reduces affinity for magnesium and coenzyme A, and reduces enzyme activity 7-fold. Ref.16
Mutagenesis1111H → A: Reduces affinity for magnesium 75-fold, and enzyme activity 150-fold. Ref.16
Mutagenesis1121Q → E: Reduces affinity for magnesium 200-fold and abolishes enzyme activity; when associated with Q-181. Ref.16
Mutagenesis1291D → A: Reduces affinity for magnesium 10-fold, and enzyme activity 30000-fold. Ref.16
Mutagenesis1811E → A: Reduces affinity for magnesium 40-fold, and enzyme activity 32000-fold. Ref.16
Mutagenesis1811E → Q: Reduces affinity for magnesium 20-fold, and enzyme activity 6500-fold. Ref.16
Mutagenesis1851K → A: Reduces enzyme activity 2000-fold, with only minor change in the affinity for magnesium and coenzyme A. Ref.16
Sequence conflict136 – 1416PGRGSI → FQVVVQF in AAG49439. Ref.4
Sequence conflict307 – 3093TKS → YKVMMIP in AAG49439. Ref.4

Secondary structure

.......................................................... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NRN7 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: 6263E302600FDDED

FASTA30935,776
        10         20         30         40         50         60 
MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ FVFARDAKAA 

        70         80         90        100        110        120 
MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN PYPNFNFNIS HQGDYAVLAA 

       130        140        150        160        170        180 
EPELQVGIDI MKTSFPGRGS IPEFFHIMKR KFTNKEWETI RSFKDEWTQL DMFYRNWALK 

       190        200        210        220        230        240 
ESFIKAIGVG LGFELQRLEF DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF 

       250        260        270        280        290        300 
VAVALRKPDG SRHQDVPSQD DSKPTQRQFT ILNFNDLMSS AVPMTPEDPS FWDCFCFTEE 


IPIRNGTKS 

« Hide

References

« Hide 'large scale' references
[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], 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].
[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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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. expand/collapse author list , 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].
Tissue: Tongue.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Urinary bladder and Uterus.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-309.
Tissue: Kidney.
[10]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.
[11]"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.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CH471065 Genomic DNA. Translation: EAW67078.1.
BC015470 mRNA. Translation: AAH15470.1.
BC016728 mRNA. Translation: AAH16728.1.
AL050073 mRNA. Translation: CAB43257.1.
PIRT08733.
RefSeqNP_056238.2. NM_015423.2.
UniGeneHs.524009.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BYDX-ray2.00A14-309[»]
2C43X-ray1.93A14-309[»]
2CG5X-ray2.70A14-309[»]
ProteinModelPortalQ9NRN7.
SMRQ9NRN7. Positions 14-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121927. 16 interactions.
IntActQ9NRN7. 6 interactions.
MINTMINT-5005661.
STRING9606.ENSP00000278618.

PTM databases

PhosphoSiteQ9NRN7.

Polymorphism databases

DMDM81170356.

Proteomic databases

PaxDbQ9NRN7.
PeptideAtlasQ9NRN7.
PRIDEQ9NRN7.

Protocols and materials databases

DNASU60496.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278618; ENSP00000278618; ENSG00000149313.
GeneID60496.
KEGGhsa:60496.
UCSCuc001pjc.1. human.

Organism-specific databases

CTD60496.
GeneCardsGC11P105982.
HGNCHGNC:14235. AASDHPPT.
HPAHPA026687.
MIM607756. gene.
neXtProtNX_Q9NRN7.
PharmGKBPA24368.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2091.
HOGENOMHOG000265195.
HOVERGENHBG080822.
InParanoidQ9NRN7.
KOK06133.
OMASPRGKPY.
PhylomeDBQ9NRN7.
TreeFamTF313753.

Enzyme and pathway databases

BioCycMetaCyc:HS14278-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9NRN7.

Gene expression databases

ArrayExpressQ9NRN7.
BgeeQ9NRN7.
CleanExHS_AASDHPPT.
GenevestigatorQ9NRN7.

Family and domain databases

Gene3D3.90.470.20. 2 hits.
InterProIPR008278. 4-PPantetheinyl_Trfase_SF.
[Graphical view]
PfamPF01648. ACPS. 1 hit.
[Graphical view]
SUPFAMSSF56214. SSF56214. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ9NRN7.
GeneWikiAASDHPPT.
GenomeRNAi60496.
NextBio65403.
PROQ9NRN7.
SOURCESearch...

Entry information

Entry nameADPPT_HUMAN
AccessionPrimary (citable) accession number: Q9NRN7
Secondary accession number(s): B2R6D1 expand/collapse secondary AC list , Q9C068, Q9P0Q3, Q9UG80, Q9Y389
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM