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Q9HAB8 (PPCS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphopantothenate--cysteine ligase

EC=6.3.2.5
Alternative name(s):
Phosphopantothenoylcysteine synthetase
Short name=PPC synthetase
Gene names
Name:PPCS
Synonyms:COAB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. Ref.4 Ref.8

Catalytic activity

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

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.

Subunit structure

Homodimer. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the PPC synthetase family.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HAB8-1)

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.
Isoform 2 (identifier: Q9HAB8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 311310Phosphopantothenate--cysteine ligase
PRO_0000182040

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.7

Natural variations

Alternative sequence1 – 173173Missing in isoform 2.
VSP_045796

Secondary structure

.................................................. 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: D3B337D3250D7170

FASTA31134,005
        10         20         30         40         50         60 
MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE ARPVRFLDNF 

        70         80         90        100        110        120 
SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT WLSALRPSGP ALSGLLSLEA 

       130        140        150        160        170        180 
EENALPGFAE ALRSYQEAAA AGTFLAVEFT TLADYLHLLQ AAAQALNPLG PSAMFYLAAA 

       190        200        210        220        230        240 
VSDFYVPVSE MPEHKIQSSG GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI 

       250        260        270        280        290        300 
NRARKALEIY QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ 

       310 
SRHTAFIGDR N 

« Hide

Isoform 2 [UniParc].

Checksum: 67B9F972DCC2B60F
Show »

FASTA13815,645

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41311.1. [Q9HAB8-1]
CCDS41312.1. [Q9HAB8-2]
RefSeqNP_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]
UniGeneHs.706662.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9OX-ray2.30A/B1-311[»]
ProteinModelPortalQ9HAB8.
SMRQ9HAB8. Positions 7-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122833. 2 interactions.
IntActQ9HAB8. 1 interaction.
STRING9606.ENSP00000361642.

PTM databases

PhosphoSiteQ9HAB8.

Polymorphism databases

DMDM47117318.

Proteomic databases

MaxQBQ9HAB8.
PaxDbQ9HAB8.
PRIDEQ9HAB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372561; ENSP00000361642; ENSG00000127125. [Q9HAB8-1]
ENST00000372562; ENSP00000361643; ENSG00000127125. [Q9HAB8-2]
ENST00000455780; ENSP00000389893; ENSG00000127125. [Q9HAB8-2]
GeneID79717.
KEGGhsa:79717.
UCSCuc001chk.3. human.
uc001chl.3. human. [Q9HAB8-1]

Organism-specific databases

CTD79717.
GeneCardsGC01P042921.
HGNCHGNC:25686. PPCS.
HPAHPA031361.
MIM609853. gene.
neXtProtNX_Q9HAB8.
PharmGKBPA142671158.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0452.
HOGENOMHOG000194726.
HOVERGENHBG049438.
InParanoidQ9HAB8.
KOK01922.
OMARSAFPYA.
OrthoDBEOG7TTQ82.
PhylomeDBQ9HAB8.
TreeFamTF105615.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00241; UER00353.

Gene expression databases

ArrayExpressQ9HAB8.
BgeeQ9HAB8.
CleanExHS_PPCS.
GenevestigatorQ9HAB8.

Family and domain databases

Gene3D3.40.50.10300. 1 hit.
InterProIPR007085. DNA/pantothenate-metab_flavo_C.
[Graphical view]
PfamPF04127. DFP. 2 hits.
[Graphical view]
SUPFAMSSF102645. SSF102645. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9HAB8.
GeneWikiPhosphopantothenate%E2%80%94cysteine_ligase.
GenomeRNAi79717.
NextBio69059.
PROQ9HAB8.
SOURCESearch...

Entry information

Entry namePPCS_HUMAN
AccessionPrimary (citable) accession number: Q9HAB8
Secondary accession number(s): Q3KQT2, Q5VVM0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 119 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM