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P54886 (P5CS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-1-pyrroline-5-carboxylate synthase

Short name=P5CS
Alternative name(s):
Aldehyde dehydrogenase family 18 member A1

Including the following 2 domains:

  1. Glutamate 5-kinase
    Short name=GK
    EC=2.7.2.11
    Alternative name(s):
    Gamma-glutamyl kinase
  2. Gamma-glutamyl phosphate reductase
    Short name=GPR
    EC=1.2.1.41
    Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
Gene names
Name:ALDH18A1
Synonyms:GSAS, P5CS, PYCS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. Ref.2 Ref.9

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. Ref.2 Ref.9

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. Ref.2 Ref.9

Enzyme regulation

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. Ref.2

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Subcellular location

Mitochondrion inner membrane.

Involvement in disease

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. Ref.9 Ref.10

Sequence similarities

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.

Sequence caution

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

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   LigandATP-binding
NADP
Nucleotide-binding
   Molecular functionKinase
Oxidoreductase
Transferase
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

citrulline biosynthetic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

glutamate metabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

ornithine biosynthetic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

proline biosynthetic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

mitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate 5-kinase activity

Inferred from direct assay Ref.9. Source: UniProtKB

glutamate-5-semialdehyde dehydrogenase activity

Inferred from direct assay Ref.9. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P54886-1)

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.
Isoform Short (identifier: P54886-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Delta-1-pyrroline-5-carboxylate synthase
PRO_0000109769

Regions

Nucleotide binding266 – 2672ATP By similarity
Nucleotide binding305 – 3117ATP By similarity
Region1 – 361361Glutamate 5-kinase
Region362 – 795434Gamma-glutamyl phosphate reductase

Sites

Binding site1171Substrate By similarity
Binding site2231Substrate By similarity
Binding site2461Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue3111N6-succinyllysine By similarity
Modified residue3471N6-succinyllysine By similarity
Modified residue5501N6-succinyllysine By similarity

Natural variations

Alternative sequence239 – 2402Missing in isoform Short.
VSP_005215
Natural variant841R → Q in ARCL3A; reduction of activity. Ref.9
VAR_038482
Natural variant2991T → I. Ref.3 Ref.6
Corresponds to variant rs2275272 [ dbSNP | Ensembl ].
VAR_051792
Natural variant3721S → Y. Ref.6
Corresponds to variant rs3765571 [ dbSNP | Ensembl ].
VAR_051793
Natural variant7841H → Y in ARCL3A; does not affect proline and ornithine biosynthetic activity. Ref.10
VAR_058006

Experimental info

Sequence conflict871E → K in BAG35201. Ref.3
Sequence conflict1261R → T in CAA64224. Ref.1
Sequence conflict2661S → P in CAA64224. Ref.1
Sequence conflict2991T → P in CAA64224. Ref.1
Sequence conflict305 – 3073MGG → NGC in CAA64224. Ref.1
Sequence conflict314 – 3152AA → ST in CAA64224. Ref.1
Sequence conflict487 – 4937LPQVAAL → PTPGGSF in CAA64224. Ref.1

Secondary structure

..................................................................... 795
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 8BF27EF2A8FB2D79

FASTA79587,302
        10         20         30         40         50         60 
MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS 

        70         80         90        100        110        120 
FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV 

       130        140        150        160        170        180 
AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY 

       190        200        210        220        230        240 
SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV 

       250        260        270        280        290        300 
ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK 

       310        320        330        340        350        360 
SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG 

       370        380        390        400        410        420 
PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR DEILLANKKD LEEAEGRLAA 

       430        440        450        460        470        480 
PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF 

       490        500        510        520        530        540 
ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE 

       550        560        570        580        590        600 
EVEDLCRLDK MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL 

       610        620        630        640        650        660 
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE 

       670        680        690        700        710        720 
VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV TEDENTAEFF LQHVDSACVF 

       730        740        750        760        770        780 
WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL 

       790 
KYLHENLPIP QRNTN 

« Hide

Isoform Short [UniParc].

Checksum: 550F0B435805C0CA
Show »

FASTA79387,089

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001017423.1. NM_001017423.1.
NP_002851.2. NM_002860.3.
UniGeneHs.500645.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5GX-ray2.25A/B362-795[»]
ProteinModelPortalP54886.
SMRP54886. Positions 70-353, 362-794.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111790. 23 interactions.
IntActP54886. 10 interactions.
MINTMINT-3020614.

Chemistry

DrugBankDB00142. L-Glutamic Acid.

PTM databases

PhosphoSiteP54886.

Polymorphism databases

DMDM6226882.

Proteomic databases

PaxDbP54886.
PRIDEP54886.

Protocols and materials databases

DNASU5832.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371221; ENSP00000360265; ENSG00000059573. [P54886-2]
ENST00000371224; ENSP00000360268; ENSG00000059573. [P54886-1]
GeneID5832.
KEGGhsa:5832.
UCSCuc001kky.3. human. [P54886-2]
uc001kkz.3. human. [P54886-1]

Organism-specific databases

CTD5832.
GeneCardsGC10M097355.
HGNCHGNC:9722. ALDH18A1.
HPAHPA008333.
HPA012604.
MIM138250. gene.
219150. phenotype.
neXtProtNX_P54886.
Orphanet35664. ALDH18A1-related De Barsy syndrome.
PharmGKBPA34065.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0014.
HOVERGENHBG007911.
InParanoidP54886.
KOK12657.
OMALLPWVQS.
OrthoDBEOG7WX07N.
PhylomeDBP54886.
TreeFamTF314372.

Enzyme and pathway databases

BioCycMetaCyc:HS00730-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00098; UER00359.
UPA00098; UER00360.

Gene expression databases

BgeeP54886.
CleanExHS_ALDH18A1.
GenevestigatorP54886.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
InterProIPR016161. 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]
PfamPF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036429. P5C_syn. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH18A1. human.
EvolutionaryTraceP54886.
GeneWikiAldehyde_dehydrogenase_18_family,_member_A1.
GenomeRNAi5832.
NextBio22726.
PROP54886.
SOURCESearch...

Entry information

Entry nameP5CS_HUMAN
AccessionPrimary (citable) accession number: P54886
Secondary accession number(s): B2R5Q4 expand/collapse secondary AC list , B7Z350, B7Z5X8, B7ZLP1, D3DR44, O95952, Q3KQU2, Q5T566, Q5T567, Q9UM72
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM