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Protein

Delta-1-pyrroline-5-carboxylate synthase

Gene

ALDH18A1

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

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

  • ATP binding Source: UniProtKB-KW
  • glutamate 5-kinase activity Source: UniProtKB
  • glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB
  • NADP binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cellular amino acid biosynthetic process Source: Reactome
  • cellular nitrogen compound metabolic process Source: Reactome
  • citrulline biosynthetic process Source: UniProtKB
  • glutamate metabolic process Source: UniProtKB
  • L-proline biosynthetic process Source: UniProtKB-UniPathway
  • ornithine biosynthetic process Source: UniProtKB
  • proline biosynthetic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9722. ALDH18A1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 3A (ARCL3A)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:219150
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.

Polymorphism and mutation databases

BioMutaiALDH18A1.
DMDMi6226882.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-1210304,EBI-741181
CMTM5Q96DZ93EBI-1210304,EBI-2548702

Protein-protein interaction databases

BioGridi111790. 33 interactions.
IntActiP54886. 12 interactions.
MINTiMINT-3020614.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5GX-ray2.25A/B362-795[»]
ProteinModelPortaliP54886.
SMRiP54886. Positions 64-351, 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.
GeneTreeiENSGT00500000044903.
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.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR000965. GPR_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT
60 70 80 90 100
VPLSRTHGKS FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE
110 120 130 140 150
QVSVLQNQGR EMMLVTSGAV AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE
160 170 180 190 200
MAIPVLEARA CAAAGQSGLM ALYEAMFTQY SICAAQILVT NLDFHDEQKR
210 220 230 240 250
RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV ISVKDNDSLA
260 270 280 290 300
ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
310 320 330 340 350
SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG
360 370 380 390 400
TFFSEVKPAG PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR
410 420 430 440 450
DEILLANKKD LEEAEGRLAA PLLKRLSLST SKLNSLAIGL RQIAASSQDS
460 470 480 490 500
VGRVLRRTRI AKNLELEQVT VPIGVLLVIF ESRPDCLPQV AALAIASGNG
510 520 530 540 550
LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE EVEDLCRLDK
560 570 580 590 600
MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
610 620 630 640 650
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF
660 670 680 690 700
ASYLTFSPSE VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV
710 720 730 740 750
TEDENTAEFF LQHVDSACVF WNASTRFSDG YRFGLGAEVG ISTSRIHARG
760 770 780 790
PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL KYLHENLPIP QRNTN
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. Curated
The sequence BAH13064.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5GX-ray2.25A/B362-795[»]
ProteinModelPortaliP54886.
SMRiP54886. Positions 64-351, 362-794.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111790. 33 interactions.
IntActiP54886. 12 interactions.
MINTiMINT-3020614.

PTM databases

PhosphoSiteiP54886.

Polymorphism and mutation databases

BioMutaiALDH18A1.
DMDMi6226882.

Proteomic databases

MaxQBiP54886.
PaxDbiP54886.
PRIDEiP54886.

Protocols and materials databases

DNASUi5832.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5832.
GeneCardsiGC10M097355.
HGNCiHGNC:9722. ALDH18A1.
HPAiHPA008333.
HPA012604.
MIMi138250. gene.
219150. phenotype.
neXtProtiNX_P54886.
Orphaneti35664. ALDH18A1-related De Barsy syndrome.
PharmGKBiPA34065.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0014.
GeneTreeiENSGT00500000044903.
HOVERGENiHBG007911.
InParanoidiP54886.
KOiK12657.
OMAiLLPWVQS.
OrthoDBiEOG7WX07N.
PhylomeDBiP54886.
TreeFamiTF314372.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiALDH18A1. human.
EvolutionaryTraceiP54886.
GeneWikiiAldehyde_dehydrogenase_18_family,_member_A1.
GenomeRNAii5832.
NextBioi22726.
PROiP54886.
SOURCEiSearch...

Gene expression databases

BgeeiP54886.
CleanExiHS_ALDH18A1.
GenevestigatoriP54886.

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.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR000965. GPR_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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.
  10. "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.
  11. "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: May 27, 2015
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.