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Q9HAB8

- PPCS_HUMAN

UniProt

Q9HAB8 - PPCS_HUMAN

Protein

Phosphopantothenate--cysteine ligase

Gene

PPCS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine.2 Publications

    Catalytic activityi

    CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.

    Pathwayi

    GO - Molecular functioni

    1. phosphopantothenate--cysteine ligase activity Source: UniProtKB

    GO - Biological processi

    1. coenzyme A biosynthetic process Source: UniProtKB
    2. coenzyme biosynthetic process Source: Reactome
    3. pantothenate metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Enzyme and pathway databases

    ReactomeiREACT_11218. Coenzyme A biosynthesis.
    UniPathwayiUPA00241; UER00353.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphopantothenate--cysteine ligase (EC:6.3.2.5)
    Alternative name(s):
    Phosphopantothenoylcysteine synthetase
    Short name:
    PPC synthetase
    Gene namesi
    Name:PPCS
    Synonyms:COAB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25686. PPCS.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671158.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 311310Phosphopantothenate--cysteine ligasePRO_0000182040Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9HAB8.
    PaxDbiQ9HAB8.
    PRIDEiQ9HAB8.

    PTM databases

    PhosphoSiteiQ9HAB8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HAB8.
    BgeeiQ9HAB8.
    CleanExiHS_PPCS.
    GenevestigatoriQ9HAB8.

    Organism-specific databases

    HPAiHPA031361.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi122833. 2 interactions.
    IntActiQ9HAB8. 1 interaction.
    STRINGi9606.ENSP00000361642.

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 3214
    Beta strandi37 – 448
    Beta strandi46 – 527
    Beta strandi54 – 596
    Helixi64 – 7512
    Beta strandi79 – 857
    Helixi93 – 953
    Helixi98 – 1047
    Beta strandi114 – 1218
    Turni122 – 1243
    Helixi128 – 14114
    Beta strandi144 – 1496
    Helixi152 – 16615
    Helixi167 – 1726
    Beta strandi173 – 1775
    Beta strandi183 – 1853
    Beta strandi203 – 2064
    Helixi211 – 2144
    Helixi218 – 2203
    Beta strandi225 – 2317
    Helixi236 – 25015
    Beta strandi253 – 2586
    Beta strandi267 – 2715
    Beta strandi274 – 2785
    Helixi282 – 2865
    Helixi291 – 30616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P9OX-ray2.30A/B1-311[»]
    ProteinModelPortaliQ9HAB8.
    SMRiQ9HAB8. Positions 7-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HAB8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPC synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0452.
    HOGENOMiHOG000194726.
    HOVERGENiHBG049438.
    InParanoidiQ9HAB8.
    KOiK01922.
    OMAiRSAFPYA.
    OrthoDBiEOG7TTQ82.
    PhylomeDBiQ9HAB8.
    TreeFamiTF105615.

    Family and domain databases

    Gene3Di3.40.50.10300. 1 hit.
    InterProiIPR007085. DNA/pantothenate-metab_flavo_C.
    [Graphical view]
    PfamiPF04127. DFP. 2 hits.
    [Graphical view]
    SUPFAMiSSF102645. SSF102645. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HAB8-1) [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

    MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE    50
    ARPVRFLDNF SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT 100
    WLSALRPSGP ALSGLLSLEA EENALPGFAE ALRSYQEAAA AGTFLAVEFT 150
    TLADYLHLLQ AAAQALNPLG PSAMFYLAAA VSDFYVPVSE MPEHKIQSSG 200
    GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI NRARKALEIY 250
    QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ 300
    SRHTAFIGDR N 311
    Length:311
    Mass (Da):34,005
    Last modified:May 10, 2004 - v2
    Checksum:iD3B337D3250D7170
    GO
    Isoform 2 (identifier: Q9HAB8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-173: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:138
    Mass (Da):15,645
    Checksum:i67B9F972DCC2B60F
    GO

    Sequence cautioni

    The sequence BAB13931.1 differs from that shown. Reason: Frameshift at position 282.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 173173Missing in isoform 2. 1 PublicationVSP_045796Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021900 mRNA. Translation: BAB13931.1. Frameshift.
    AL445669 Genomic DNA. Translation: CAH70748.1.
    AL445669 Genomic DNA. Translation: CAH70749.1.
    BC012383 mRNA. No translation available.
    BC104938 mRNA. Translation: AAI04939.1.
    BC106064 mRNA. Translation: AAI06065.1.
    BC112015 mRNA. Translation: AAI12016.1.
    CCDSiCCDS41311.1. [Q9HAB8-1]
    CCDS41312.1. [Q9HAB8-2]
    RefSeqiNP_001070915.1. NM_001077447.2. [Q9HAB8-2]
    NP_001274435.1. NM_001287506.1. [Q9HAB8-2]
    NP_001274437.1. NM_001287508.1. [Q9HAB8-2]
    NP_001274438.1. NM_001287509.1. [Q9HAB8-2]
    NP_001274439.1. NM_001287510.1. [Q9HAB8-2]
    NP_001274440.1. NM_001287511.1.
    NP_078940.2. NM_024664.3. [Q9HAB8-1]
    UniGeneiHs.706662.

    Genome annotation databases

    EnsembliENST00000372561; ENSP00000361642; ENSG00000127125. [Q9HAB8-1]
    ENST00000372562; ENSP00000361643; ENSG00000127125. [Q9HAB8-2]
    GeneIDi79717.
    KEGGihsa:79717.
    UCSCiuc001chk.3. human.
    uc001chl.3. human. [Q9HAB8-1]

    Polymorphism databases

    DMDMi47117318.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021900 mRNA. Translation: BAB13931.1 . Frameshift.
    AL445669 Genomic DNA. Translation: CAH70748.1 .
    AL445669 Genomic DNA. Translation: CAH70749.1 .
    BC012383 mRNA. No translation available.
    BC104938 mRNA. Translation: AAI04939.1 .
    BC106064 mRNA. Translation: AAI06065.1 .
    BC112015 mRNA. Translation: AAI12016.1 .
    CCDSi CCDS41311.1. [Q9HAB8-1 ]
    CCDS41312.1. [Q9HAB8-2 ]
    RefSeqi NP_001070915.1. NM_001077447.2. [Q9HAB8-2 ]
    NP_001274435.1. NM_001287506.1. [Q9HAB8-2 ]
    NP_001274437.1. NM_001287508.1. [Q9HAB8-2 ]
    NP_001274438.1. NM_001287509.1. [Q9HAB8-2 ]
    NP_001274439.1. NM_001287510.1. [Q9HAB8-2 ]
    NP_001274440.1. NM_001287511.1.
    NP_078940.2. NM_024664.3. [Q9HAB8-1 ]
    UniGenei Hs.706662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P9O X-ray 2.30 A/B 1-311 [» ]
    ProteinModelPortali Q9HAB8.
    SMRi Q9HAB8. Positions 7-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122833. 2 interactions.
    IntActi Q9HAB8. 1 interaction.
    STRINGi 9606.ENSP00000361642.

    PTM databases

    PhosphoSitei Q9HAB8.

    Polymorphism databases

    DMDMi 47117318.

    Proteomic databases

    MaxQBi Q9HAB8.
    PaxDbi Q9HAB8.
    PRIDEi Q9HAB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372561 ; ENSP00000361642 ; ENSG00000127125 . [Q9HAB8-1 ]
    ENST00000372562 ; ENSP00000361643 ; ENSG00000127125 . [Q9HAB8-2 ]
    GeneIDi 79717.
    KEGGi hsa:79717.
    UCSCi uc001chk.3. human.
    uc001chl.3. human. [Q9HAB8-1 ]

    Organism-specific databases

    CTDi 79717.
    GeneCardsi GC01P042921.
    HGNCi HGNC:25686. PPCS.
    HPAi HPA031361.
    MIMi 609853. gene.
    neXtProti NX_Q9HAB8.
    PharmGKBi PA142671158.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0452.
    HOGENOMi HOG000194726.
    HOVERGENi HBG049438.
    InParanoidi Q9HAB8.
    KOi K01922.
    OMAi RSAFPYA.
    OrthoDBi EOG7TTQ82.
    PhylomeDBi Q9HAB8.
    TreeFami TF105615.

    Enzyme and pathway databases

    UniPathwayi UPA00241 ; UER00353 .
    Reactomei REACT_11218. Coenzyme A biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9HAB8.
    GeneWikii Phosphopantothenate%E2%80%94cysteine_ligase.
    GenomeRNAii 79717.
    NextBioi 69059.
    PROi Q9HAB8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAB8.
    Bgeei Q9HAB8.
    CleanExi HS_PPCS.
    Genevestigatori Q9HAB8.

    Family and domain databases

    Gene3Di 3.40.50.10300. 1 hit.
    InterProi IPR007085. DNA/pantothenate-metab_flavo_C.
    [Graphical view ]
    Pfami PF04127. DFP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF102645. SSF102645. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
      Tissue: Embryo.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2).
      Tissue: Brain, Ovary tumor and Uterus.
    4. "Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics."
      Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A., de Crecy-Lagard V., Osterman A.
      J. Biol. Chem. 277:21431-21439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution."
      Manoj N., Strauss E., Begley T.P., Ealick S.E.
      Structure 11:927-936(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, HOMODIMERIZATION.

    Entry informationi

    Entry nameiPPCS_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAB8
    Secondary accession number(s): Q3KQT2, Q5VVM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 121 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

    Miscellaneous

    The mammalian enzyme has a preference for ATP over CTP, in contrast to the E.coli ortholog.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3