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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.4 Publications

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.1 Publication
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.1 Publication

Enzyme regulationi

Isoform Short: Inhibited by L-ornithine with a Ki of approximately 0.25 mm. Isoform Long: 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: L-proline biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Delta-1-pyrroline-5-carboxylate synthase (ALDH18A1)
  2. Delta-1-pyrroline-5-carboxylate synthase (ALDH18A1)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei117SubstrateBy similarity1
Binding sitei223SubstrateBy similarity1
Binding sitei246Substrate; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi266 – 267ATPBy similarity2
Nucleotide bindingi305 – 311ATPBy similarity7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • delta1-pyrroline-5-carboxylate synthetase activity Source: Reactome
  • glutamate 5-kinase activity Source: UniProtKB
  • glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cellular amino acid biosynthetic 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

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.
ZFISH:HS00730-MONOMER.
ReactomeiR-HSA-70614. 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:2.7.2.111 Publication)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
Gamma-glutamyl phosphate reductase (EC:1.2.1.411 Publication)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9722. ALDH18A1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • mitochondrial inner membrane Source: Reactome
  • mitochondrion Source: UniProtKB

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 3A (ARCL3A)4 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_03848284R → Q in ARCL3A; reduction of activity. 1 PublicationCorresponds to variant rs121434582dbSNPEnsembl.1
Natural variantiVAR_07588493G → R in ARCL3A. 1 Publication1
Natural variantiVAR_051792299T → I in ARCL3A. 3 PublicationsCorresponds to variant rs2275272dbSNPEnsembl.1
Natural variantiVAR_075896782Y → C in ARCL3A. 1 PublicationCorresponds to variant rs774047299dbSNPEnsembl.1
Natural variantiVAR_058006784H → Y in ARCL3A; does not affect proline and ornithine biosynthetic activity. 1 PublicationCorresponds to variant rs121434583dbSNPEnsembl.1
Cutis laxa, autosomal dominant, 3 (ADCL3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of cutis laxa, a connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. ADCL3 patients manifest thin skin with visible veins and wrinkles, cataract or corneal clouding, moderate intellectual disability, muscular hypotonia with brisk muscle reflexes, clenched fingers, and pre- and postnatal growth retardation.
See also OMIM:616603
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075887138R → L in ADCL3. 1 Publication1
Natural variantiVAR_075888138R → Q in ADCL3. 1 Publication1
Natural variantiVAR_075889138R → W in ADCL3; no effect on protein abundance; altered sub-mitochondrial distribution; decreased proline biosynthetic process. 1 Publication1
Spastic paraplegia 9A, autosomal dominant (SPG9A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG9A patients have gait difficulties, motor neuropathy, and dysarthria. Additional variable features include cerebellar signs, cataract, pes cavus, and urinary urgency.
See also OMIM:601162
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075885120V → A in SPG9A. 1 Publication1
Natural variantiVAR_075890243V → L in SPG9A; decreased protein abundance; no effect on localization to the mitochondrion; altered homohexamerization; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process. 1 Publication1
Natural variantiVAR_075891252R → Q in SPG9A; altered homohexamerization; no effect on localization to the mitochondrion; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process. 2 Publications1
Natural variantiVAR_075893652S → F in SPG9A. 1 Publication1
Natural variantiVAR_075894665R → L in SPG9A. 1 Publication1
Spastic paraplegia 9B, autosomal recessive (SPG9B)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG9B is a complex form characterized by delayed psychomotor development, intellectual disability, and severe motor impairment. Dysmorphic facial features, tremor, and urinary incontinence are variably observed in SPG9B patients.
See also OMIM:616586
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075886128R → H in SPG9B. 1 PublicationCorresponds to variant rs768323248dbSNPEnsembl.1
Natural variantiVAR_075892637L → P in SPG9B. 1 Publication1
Natural variantiVAR_075895715D → H in SPG9B. 1 PublicationCorresponds to variant rs752669339dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Mental retardation, Neurodegeneration

Organism-specific databases

DisGeNETi5832.
MalaCardsiALDH18A1.
MIMi219150. phenotype.
601162. phenotype.
616586. phenotype.
616603. phenotype.
OpenTargetsiENSG00000059573.
Orphaneti35664. ALDH18A1-related De Barsy syndrome.
PharmGKBiPA34065.

Polymorphism and mutation databases

BioMutaiALDH18A1.
DMDMi6226882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001097691 – 795Delta-1-pyrroline-5-carboxylate synthaseAdd BLAST795

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei311N6-succinyllysineBy similarity1
Modified residuei347N6-succinyllysineBy similarity1
Modified residuei550N6-succinyllysineBy similarity1

Proteomic databases

EPDiP54886.
MaxQBiP54886.
PaxDbiP54886.
PeptideAtlasiP54886.
PRIDEiP54886.

PTM databases

iPTMnetiP54886.
PhosphoSitePlusiP54886.
SwissPalmiP54886.

Expressioni

Gene expression databases

BgeeiENSG00000059573.
CleanExiHS_ALDH18A1.
GenevisibleiP54886. HS.

Organism-specific databases

HPAiHPA008333.
HPA012604.

Interactioni

Subunit structurei

Homohexamer or homotetramer.2 Publications

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111790. 37 interactors.
IntActiP54886. 21 interactors.
MINTiMINT-3020614.
STRINGi9606.ENSP00000360268.

Structurei

Secondary structure

1795
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi363 – 379Combined sources17
Helixi382 – 398Combined sources17
Helixi400 – 414Combined sources15
Turni415 – 417Combined sources3
Helixi420 – 424Combined sources5
Helixi430 – 446Combined sources17
Beta strandi454 – 461Combined sources8
Beta strandi464 – 472Combined sources9
Beta strandi475 – 482Combined sources8
Helixi486 – 497Combined sources12
Beta strandi500 – 504Combined sources5
Helixi507 – 509Combined sources3
Helixi510 – 525Combined sources16
Turni526 – 528Combined sources3
Helixi530 – 532Combined sources3
Beta strandi533 – 535Combined sources3
Beta strandi553 – 559Combined sources7
Helixi561 – 570Combined sources10
Beta strandi572 – 574Combined sources3
Beta strandi584 – 588Combined sources5
Turni594 – 596Combined sources3
Helixi597 – 606Combined sources10
Beta strandi614 – 621Combined sources8
Helixi622 – 624Combined sources3
Helixi628 – 639Combined sources12
Beta strandi643 – 646Combined sources4
Helixi648 – 651Combined sources4
Beta strandi670 – 680Combined sources11
Helixi681 – 691Combined sources11
Beta strandi694 – 700Combined sources7
Helixi704 – 713Combined sources10
Beta strandi716 – 723Combined sources8
Helixi725 – 727Combined sources3
Turni730 – 734Combined sources5
Beta strandi745 – 747Combined sources3
Helixi754 – 757Combined sources4
Beta strandi758 – 765Combined sources8
Helixi771 – 774Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H5GX-ray2.25A/B362-795[»]
ProteinModelPortaliP54886.
SMRiP54886.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54886.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 361Glutamate 5-kinaseAdd BLAST361
Regioni362 – 795Gamma-glutamyl phosphate reductaseAdd BLAST434

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

eggNOGiKOG1154. Eukaryota.
KOG4165. Eukaryota.
COG0014. LUCA.
COG0263. LUCA.
GeneTreeiENSGT00500000044903.
HOVERGENiHBG007911.
InParanoidiP54886.
KOiK12657.
OMAiLLPWVQS.
OrthoDBiEOG091G02MP.
PhylomeDBiP54886.
TreeFamiTF314372.

Family and domain databases

CDDicd07079. ALDH_F18-19_ProA-GPR. 1 hit.
Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA. 1 hit.
MF_00456. ProB. 1 hit.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAH13064 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87E → K in BAG35201 (PubMed:14702039).Curated1
Sequence conflicti126R → T in CAA64224 (PubMed:8761662).Curated1
Sequence conflicti266S → P in CAA64224 (PubMed:8761662).Curated1
Sequence conflicti299T → P in CAA64224 (PubMed:8761662).Curated1
Sequence conflicti305 – 307MGG → NGC in CAA64224 (PubMed:8761662).Curated3
Sequence conflicti314 – 315AA → ST in CAA64224 (PubMed:8761662).Curated2
Sequence conflicti487 – 493LPQVAAL → PTPGGSF in CAA64224 (PubMed:8761662).Curated7

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03848284R → Q in ARCL3A; reduction of activity. 1 PublicationCorresponds to variant rs121434582dbSNPEnsembl.1
Natural variantiVAR_07588493G → R in ARCL3A. 1 Publication1
Natural variantiVAR_075885120V → A in SPG9A. 1 Publication1
Natural variantiVAR_075886128R → H in SPG9B. 1 PublicationCorresponds to variant rs768323248dbSNPEnsembl.1
Natural variantiVAR_075887138R → L in ADCL3. 1 Publication1
Natural variantiVAR_075888138R → Q in ADCL3. 1 Publication1
Natural variantiVAR_075889138R → W in ADCL3; no effect on protein abundance; altered sub-mitochondrial distribution; decreased proline biosynthetic process. 1 Publication1
Natural variantiVAR_075890243V → L in SPG9A; decreased protein abundance; no effect on localization to the mitochondrion; altered homohexamerization; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process. 1 Publication1
Natural variantiVAR_075891252R → Q in SPG9A; altered homohexamerization; no effect on localization to the mitochondrion; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process. 2 Publications1
Natural variantiVAR_051792299T → I in ARCL3A. 3 PublicationsCorresponds to variant rs2275272dbSNPEnsembl.1
Natural variantiVAR_051793372S → Y.1 PublicationCorresponds to variant rs3765571dbSNPEnsembl.1
Natural variantiVAR_075892637L → P in SPG9B. 1 Publication1
Natural variantiVAR_075893652S → F in SPG9A. 1 Publication1
Natural variantiVAR_075894665R → L in SPG9A. 1 Publication1
Natural variantiVAR_075895715D → H in SPG9B. 1 PublicationCorresponds to variant rs752669339dbSNPEnsembl.1
Natural variantiVAR_075896782Y → C in ARCL3A. 1 PublicationCorresponds to variant rs774047299dbSNPEnsembl.1
Natural variantiVAR_058006784H → Y in ARCL3A; does not affect proline and ornithine biosynthetic activity. 1 PublicationCorresponds to variant rs121434583dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005215239 – 240Missing in isoform Short. 2 Publications2

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_001310341.1. NM_001323412.1.
NP_001310342.1. NM_001323413.1. [P54886-1]
NP_001310343.1. NM_001323414.1. [P54886-1]
NP_001310344.1. NM_001323415.1. [P54886-2]
NP_001310345.1. NM_001323416.1.
NP_001310348.1. NM_001323419.1.
NP_002851.2. NM_002860.3. [P54886-1]
UniGeneiHs.500645.

Genome annotation databases

EnsembliENST00000371221; ENSP00000360265; ENSG00000059573. [P54886-2]
ENST00000371224; ENSP00000360268; ENSG00000059573. [P54886-1]
GeneIDi5832.
KEGGihsa:5832.
UCSCiuc001kky.4. 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_001310341.1. NM_001323412.1.
NP_001310342.1. NM_001323413.1. [P54886-1]
NP_001310343.1. NM_001323414.1. [P54886-1]
NP_001310344.1. NM_001323415.1. [P54886-2]
NP_001310345.1. NM_001323416.1.
NP_001310348.1. NM_001323419.1.
NP_002851.2. NM_002860.3. [P54886-1]
UniGeneiHs.500645.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H5GX-ray2.25A/B362-795[»]
ProteinModelPortaliP54886.
SMRiP54886.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111790. 37 interactors.
IntActiP54886. 21 interactors.
MINTiMINT-3020614.
STRINGi9606.ENSP00000360268.

PTM databases

iPTMnetiP54886.
PhosphoSitePlusiP54886.
SwissPalmiP54886.

Polymorphism and mutation databases

BioMutaiALDH18A1.
DMDMi6226882.

Proteomic databases

EPDiP54886.
MaxQBiP54886.
PaxDbiP54886.
PeptideAtlasiP54886.
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.4. human. [P54886-1]

Organism-specific databases

CTDi5832.
DisGeNETi5832.
GeneCardsiALDH18A1.
HGNCiHGNC:9722. ALDH18A1.
HPAiHPA008333.
HPA012604.
MalaCardsiALDH18A1.
MIMi138250. gene.
219150. phenotype.
601162. phenotype.
616586. phenotype.
616603. phenotype.
neXtProtiNX_P54886.
OpenTargetsiENSG00000059573.
Orphaneti35664. ALDH18A1-related De Barsy syndrome.
PharmGKBiPA34065.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1154. Eukaryota.
KOG4165. Eukaryota.
COG0014. LUCA.
COG0263. LUCA.
GeneTreeiENSGT00500000044903.
HOVERGENiHBG007911.
InParanoidiP54886.
KOiK12657.
OMAiLLPWVQS.
OrthoDBiEOG091G02MP.
PhylomeDBiP54886.
TreeFamiTF314372.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.
BioCyciMetaCyc:HS00730-MONOMER.
ZFISH:HS00730-MONOMER.
ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000059573.
CleanExiHS_ALDH18A1.
GenevisibleiP54886. HS.

Family and domain databases

CDDicd07079. ALDH_F18-19_ProA-GPR. 1 hit.
Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA. 1 hit.
MF_00456. ProB. 1 hit.
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...

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: November 2, 2016
This is version 178 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

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 one 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.