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P54886

- P5CS_HUMAN

UniProt

P54886 - P5CS_HUMAN

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Protein
Delta-1-pyrroline-5-carboxylate synthase
Gene
ALDH18A1, GSAS, P5CS, PYCS
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.2 Publications

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 – 1171Substrate By similarity
Binding sitei223 – 2231Substrate By similarity
Binding sitei246 – 2461Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2672ATP By similarity
Nucleotide bindingi305 – 3117ATP By 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. L-proline biosynthetic process Source: UniProtKB-UniPathway
  2. cellular amino acid biosynthetic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. citrulline biosynthetic process Source: UniProtKB
  5. glutamate metabolic process Source: UniProtKB
  6. ornithine biosynthetic process Source: UniProtKB
  7. proline biosynthetic process Source: UniProtKB
  8. 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
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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 synthase
PRO_0000109769Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP54886.

Family & Domainsi

Region

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

Sequence similaritiesi

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

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.

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.
VSP_005215

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871E → K in BAG35201. 1 Publication
Sequence conflicti126 – 1261R → T in CAA64224. 1 Publication
Sequence conflicti266 – 2661S → P in CAA64224. 1 Publication
Sequence conflicti299 – 2991T → P in CAA64224. 1 Publication
Sequence conflicti305 – 3073MGG → NGC in CAA64224. 1 Publication
Sequence conflicti314 – 3152AA → ST in CAA64224. 1 Publication
Sequence conflicti487 – 4937LPQVAAL → PTPGGSF in CAA64224. 1 Publication

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

« 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. "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: September 3, 2014
This is version 155 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

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