Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HAB8

- PPCS_HUMAN

UniProt

Q9HAB8 - PPCS_HUMAN

(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)

Protein

Phosphopantothenate--cysteine ligase

Gene

PPCS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9HAB8.
CleanExiHS_PPCS.
ExpressionAtlasiQ9HAB8. baseline and differential.
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.
GeneTreeiENSGT00390000015263.
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

        10         20         30         40         50
MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE
60 70 80 90 100
ARPVRFLDNF SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT
110 120 130 140 150
WLSALRPSGP ALSGLLSLEA EENALPGFAE ALRSYQEAAA AGTFLAVEFT
160 170 180 190 200
TLADYLHLLQ AAAQALNPLG PSAMFYLAAA VSDFYVPVSE MPEHKIQSSG
210 220 230 240 250
GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI NRARKALEIY
260 270 280 290 300
QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ
310
SRHTAFIGDR N
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.
GeneTreei ENSGT00390000015263.
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

Bgeei Q9HAB8.
CleanExi HS_PPCS.
ExpressionAtlasi Q9HAB8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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