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P54886

- P5CS_HUMAN

UniProt

P54886 - P5CS_HUMAN

Protein

Delta-1-pyrroline-5-carboxylate synthase

Gene

ALDH18A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine.2 Publications

    Catalytic activityi

    ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
    L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

    Enzyme regulationi

    Isoform Short is inhibited by L-ornithine with a Ki of approximately 0.25 mm. Isoform Long is insensitive to ornithine inhibition. This is due to the two amino acid insert which abolishes feedback inhibition of P5CS activity by L-ornithine.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171SubstrateBy similarity
    Binding sitei223 – 2231SubstrateBy similarity
    Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi266 – 2672ATPBy similarity
    Nucleotide bindingi305 – 3117ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate 5-kinase activity Source: UniProtKB
    3. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. citrulline biosynthetic process Source: UniProtKB
    4. glutamate metabolic process Source: UniProtKB
    5. L-proline biosynthetic process Source: UniProtKB-UniPathway
    6. ornithine biosynthetic process Source: UniProtKB
    7. proline biosynthetic process Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    ATP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00730-MONOMER.
    ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
    UniPathwayiUPA00098; UER00359.
    UPA00098; UER00360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate synthase
    Short name:
    P5CS
    Alternative name(s):
    Aldehyde dehydrogenase family 18 member A1
    Including the following 2 domains:
    Glutamate 5-kinase (EC:2.7.2.11)
    Short name:
    GK
    Alternative name(s):
    Gamma-glutamyl kinase
    Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
    Short name:
    GPR
    Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
    Gene namesi
    Name:ALDH18A1
    Synonyms:GSAS, P5CS, PYCS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9722. ALDH18A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Cutis laxa, autosomal recessive, 3A (ARCL3A) [MIM:219150]: A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti84 – 841R → Q in ARCL3A; reduction of activity. 1 Publication
    VAR_038482
    Natural varianti784 – 7841H → Y in ARCL3A; does not affect proline and ornithine biosynthetic activity. 1 Publication
    VAR_058006

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi219150. phenotype.
    Orphaneti35664. ALDH18A1-related De Barsy syndrome.
    PharmGKBiPA34065.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 795795Delta-1-pyrroline-5-carboxylate synthasePRO_0000109769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei311 – 3111N6-succinyllysineBy similarity
    Modified residuei347 – 3471N6-succinyllysineBy similarity
    Modified residuei550 – 5501N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiP54886.
    PaxDbiP54886.
    PRIDEiP54886.

    PTM databases

    PhosphoSiteiP54886.

    Expressioni

    Gene expression databases

    BgeeiP54886.
    CleanExiHS_ALDH18A1.
    GenevestigatoriP54886.

    Organism-specific databases

    HPAiHPA008333.
    HPA012604.

    Interactioni

    Protein-protein interaction databases

    BioGridi111790. 24 interactions.
    IntActiP54886. 10 interactions.
    MINTiMINT-3020614.

    Structurei

    Secondary structure

    1
    795
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi363 – 37917
    Helixi382 – 39817
    Helixi400 – 41415
    Turni415 – 4173
    Helixi420 – 4245
    Helixi430 – 44617
    Beta strandi454 – 4618
    Beta strandi464 – 4729
    Beta strandi475 – 4828
    Helixi486 – 49712
    Beta strandi500 – 5045
    Helixi507 – 5093
    Helixi510 – 52516
    Turni526 – 5283
    Helixi530 – 5323
    Beta strandi533 – 5353
    Beta strandi553 – 5597
    Helixi561 – 57010
    Beta strandi572 – 5743
    Beta strandi584 – 5885
    Turni594 – 5963
    Helixi597 – 60610
    Beta strandi614 – 6218
    Helixi622 – 6243
    Helixi628 – 63912
    Beta strandi643 – 6464
    Helixi648 – 6514
    Beta strandi670 – 68011
    Helixi681 – 69111
    Beta strandi694 – 7007
    Helixi704 – 71310
    Beta strandi716 – 7238
    Helixi725 – 7273
    Turni730 – 7345
    Beta strandi745 – 7473
    Helixi754 – 7574
    Beta strandi758 – 7658
    Helixi771 – 7744

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H5GX-ray2.25A/B362-795[»]
    ProteinModelPortaliP54886.
    SMRiP54886. Positions 70-353, 362-794.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54886.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 361361Glutamate 5-kinaseAdd
    BLAST
    Regioni362 – 795434Gamma-glutamyl phosphate reductaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate 5-kinase family.Curated
    In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0014.
    HOVERGENiHBG007911.
    InParanoidiP54886.
    KOiK12657.
    OMAiLLPWVQS.
    OrthoDBiEOG7WX07N.
    PhylomeDBiP54886.
    TreeFamiTF314372.

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPiMF_00412. ProA.
    MF_00456. ProB.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR001057. Glu/AcGlu_kinase.
    IPR019797. Glutamate_5-kinase_CS.
    IPR005766. P5_carboxy_syn.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF00171. Aldedh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036429. P5C_syn. 1 hit.
    PRINTSiPR00474. GLU5KINASE.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    SSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01092. P5CS. 1 hit.
    TIGR00407. proA. 1 hit.
    PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
    PS01223. PROA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P54886-1) [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

    MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT    50
    VPLSRTHGKS FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE 100
    QVSVLQNQGR EMMLVTSGAV AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE 150
    MAIPVLEARA CAAAGQSGLM ALYEAMFTQY SICAAQILVT NLDFHDEQKR 200
    RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV ISVKDNDSLA 250
    ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK 300
    SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG 350
    TFFSEVKPAG PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR 400
    DEILLANKKD LEEAEGRLAA PLLKRLSLST SKLNSLAIGL RQIAASSQDS 450
    VGRVLRRTRI AKNLELEQVT VPIGVLLVIF ESRPDCLPQV AALAIASGNG 500
    LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE EVEDLCRLDK 550
    MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL 600
    VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF 650
    ASYLTFSPSE VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV 700
    TEDENTAEFF LQHVDSACVF WNASTRFSDG YRFGLGAEVG ISTSRIHARG 750
    PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL KYLHENLPIP QRNTN 795
    Length:795
    Mass (Da):87,302
    Last modified:May 30, 2000 - v2
    Checksum:i8BF27EF2A8FB2D79
    GO
    Isoform Short (identifier: P54886-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         239-240: Missing.

    Show »
    Length:793
    Mass (Da):87,089
    Checksum:i550F0B435805C0CA
    GO

    Sequence cautioni

    The sequence BAH12086.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAH13064.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871E → K in BAG35201. (PubMed:14702039)Curated
    Sequence conflicti126 – 1261R → T in CAA64224. (PubMed:8761662)Curated
    Sequence conflicti266 – 2661S → P in CAA64224. (PubMed:8761662)Curated
    Sequence conflicti299 – 2991T → P in CAA64224. (PubMed:8761662)Curated
    Sequence conflicti305 – 3073MGG → NGC in CAA64224. (PubMed:8761662)Curated
    Sequence conflicti314 – 3152AA → ST in CAA64224. (PubMed:8761662)Curated
    Sequence conflicti487 – 4937LPQVAAL → PTPGGSF in CAA64224. (PubMed:8761662)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti84 – 841R → Q in ARCL3A; reduction of activity. 1 Publication
    VAR_038482
    Natural varianti299 – 2991T → I.2 Publications
    Corresponds to variant rs2275272 [ dbSNP | Ensembl ].
    VAR_051792
    Natural varianti372 – 3721S → Y.1 Publication
    Corresponds to variant rs3765571 [ dbSNP | Ensembl ].
    VAR_051793
    Natural varianti784 – 7841H → Y in ARCL3A; does not affect proline and ornithine biosynthetic activity. 1 Publication
    VAR_058006

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei239 – 2402Missing in isoform Short. 2 PublicationsVSP_005215

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94453 mRNA. Translation: CAA64224.1.
    U76542 mRNA. Translation: AAD17454.1.
    U68758 mRNA. Translation: AAD00169.1.
    AK295487 mRNA. Translation: BAH12086.1. Different initiation.
    AK299557 mRNA. Translation: BAH13064.1. Different initiation.
    AK312271 mRNA. Translation: BAG35201.1.
    AL356632 Genomic DNA. Translation: CAI16765.1.
    AL356632 Genomic DNA. Translation: CAI16766.1.
    CH471066 Genomic DNA. Translation: EAW49995.1.
    CH471066 Genomic DNA. Translation: EAW49994.1.
    CH471066 Genomic DNA. Translation: EAW49996.1.
    CH471066 Genomic DNA. Translation: EAW49997.1.
    BC106054 mRNA. Translation: AAI06055.1.
    BC117240 mRNA. Translation: AAI17241.1.
    BC117242 mRNA. Translation: AAI17243.1.
    BC143930 mRNA. Translation: AAI43931.1.
    CCDSiCCDS31257.1. [P54886-2]
    CCDS7443.1. [P54886-1]
    RefSeqiNP_001017423.1. NM_001017423.1. [P54886-2]
    NP_002851.2. NM_002860.3. [P54886-1]
    XP_006717996.1. XM_006717933.1. [P54886-1]
    UniGeneiHs.500645.

    Genome annotation databases

    EnsembliENST00000371221; ENSP00000360265; ENSG00000059573. [P54886-2]
    ENST00000371224; ENSP00000360268; ENSG00000059573. [P54886-1]
    GeneIDi5832.
    KEGGihsa:5832.
    UCSCiuc001kky.3. human. [P54886-2]
    uc001kkz.3. human. [P54886-1]

    Polymorphism databases

    DMDMi6226882.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94453 mRNA. Translation: CAA64224.1 .
    U76542 mRNA. Translation: AAD17454.1 .
    U68758 mRNA. Translation: AAD00169.1 .
    AK295487 mRNA. Translation: BAH12086.1 . Different initiation.
    AK299557 mRNA. Translation: BAH13064.1 . Different initiation.
    AK312271 mRNA. Translation: BAG35201.1 .
    AL356632 Genomic DNA. Translation: CAI16765.1 .
    AL356632 Genomic DNA. Translation: CAI16766.1 .
    CH471066 Genomic DNA. Translation: EAW49995.1 .
    CH471066 Genomic DNA. Translation: EAW49994.1 .
    CH471066 Genomic DNA. Translation: EAW49996.1 .
    CH471066 Genomic DNA. Translation: EAW49997.1 .
    BC106054 mRNA. Translation: AAI06055.1 .
    BC117240 mRNA. Translation: AAI17241.1 .
    BC117242 mRNA. Translation: AAI17243.1 .
    BC143930 mRNA. Translation: AAI43931.1 .
    CCDSi CCDS31257.1. [P54886-2 ]
    CCDS7443.1. [P54886-1 ]
    RefSeqi NP_001017423.1. NM_001017423.1. [P54886-2 ]
    NP_002851.2. NM_002860.3. [P54886-1 ]
    XP_006717996.1. XM_006717933.1. [P54886-1 ]
    UniGenei Hs.500645.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H5G X-ray 2.25 A/B 362-795 [» ]
    ProteinModelPortali P54886.
    SMRi P54886. Positions 70-353, 362-794.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111790. 24 interactions.
    IntActi P54886. 10 interactions.
    MINTi MINT-3020614.

    Chemistry

    DrugBanki DB00142. L-Glutamic Acid.

    PTM databases

    PhosphoSitei P54886.

    Polymorphism databases

    DMDMi 6226882.

    Proteomic databases

    MaxQBi P54886.
    PaxDbi P54886.
    PRIDEi P54886.

    Protocols and materials databases

    DNASUi 5832.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371221 ; ENSP00000360265 ; ENSG00000059573 . [P54886-2 ]
    ENST00000371224 ; ENSP00000360268 ; ENSG00000059573 . [P54886-1 ]
    GeneIDi 5832.
    KEGGi hsa:5832.
    UCSCi uc001kky.3. human. [P54886-2 ]
    uc001kkz.3. human. [P54886-1 ]

    Organism-specific databases

    CTDi 5832.
    GeneCardsi GC10M097355.
    HGNCi HGNC:9722. ALDH18A1.
    HPAi HPA008333.
    HPA012604.
    MIMi 138250. gene.
    219150. phenotype.
    neXtProti NX_P54886.
    Orphaneti 35664. ALDH18A1-related De Barsy syndrome.
    PharmGKBi PA34065.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0014.
    HOVERGENi HBG007911.
    InParanoidi P54886.
    KOi K12657.
    OMAi LLPWVQS.
    OrthoDBi EOG7WX07N.
    PhylomeDBi P54886.
    TreeFami TF314372.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00359 .
    UPA00098 ; UER00360 .
    BioCyci MetaCyc:HS00730-MONOMER.
    Reactomei REACT_238. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    ChiTaRSi ALDH18A1. human.
    EvolutionaryTracei P54886.
    GeneWikii Aldehyde_dehydrogenase_18_family,_member_A1.
    GenomeRNAii 5832.
    NextBioi 22726.
    PROi P54886.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54886.
    CleanExi HS_ALDH18A1.
    Genevestigatori P54886.

    Family and domain databases

    Gene3Di 3.40.1160.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPi MF_00412. ProA.
    MF_00456. ProB.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR001057. Glu/AcGlu_kinase.
    IPR019797. Glutamate_5-kinase_CS.
    IPR005766. P5_carboxy_syn.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF00171. Aldedh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036429. P5C_syn. 1 hit.
    PRINTSi PR00474. GLU5KINASE.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01092. P5CS. 1 hit.
    TIGR00407. proA. 1 hit.
    PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
    PS01223. PROA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis."
      Aral B., Schlenzig J.S., Liu G., Kamoun P.
      C. R. Acad. Sci. III, Sci. Vie 319:171-178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Kidney.
    2. "Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition."
      Hu C.A., Lin W.-W., Obie C., Valle D.
      J. Biol. Chem. 274:6754-6762(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, ENZYME REGULATION.
      Tissue: Small intestine.
    3. "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 LONG), VARIANT ILE-299.
      Tissue: Brain and Hippocampus.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 LONG AND SHORT), VARIANTS ILE-299 AND TYR-372.
      Tissue: Brain and Uterus.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Crystal structure of human pyrroline-5-carboxylate synthetase."
      Structural genomics consortium (SGC)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 362-795.
    9. "Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase."
      Baumgartner M.R., Hu C.A., Almashanu S., Steel G., Obie C., Aral B., Rabier D., Kamoun P., Saudubray J.-M., Valle D.
      Hum. Mol. Genet. 9:2853-2858(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARCL3A GLN-84, CHARACTERIZATION OF VARIANT ARCL3A GLN-84, FUNCTION, CATALYTIC ACTIVITY.
    10. "A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome."
      Bicknell L.S., Pitt J., Aftimos S., Ramadas R., Maw M.A., Robertson S.P.
      Eur. J. Hum. Genet. 16:1176-1186(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARCL3A TYR-784, CHARACTERIZATION OF VARIANT ARCL3A TYR-784.

    Entry informationi

    Entry nameiP5CS_HUMAN
    AccessioniPrimary (citable) accession number: P54886
    Secondary accession number(s): B2R5Q4
    , B7Z350, B7Z5X8, B7ZLP1, D3DR44, O95952, Q3KQU2, Q5T566, Q5T567, Q9UM72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 156 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3