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Reviewed, UniProtKB/Swiss-Prot Q96C36 (P5CR2_HUMAN)

Last modified November 25, 2008. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyrroline-5-carboxylate reductase 2
      Short name=P5C reductase 2
      Short name=P5CR 2
    EC=1.5.1.2
Gene names
Name: PYCR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H.

Pathway

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

Subunit structure

Homodecamer; composed of 5 homodimers By similarity.

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Ontologies

Keywords

   Biological processAmino-acid biosynthesis
Proline biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

pyrroline-5-carboxylate reductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 320319Pyrroline-5-carboxylate reductase 2
PRO_0000187317

Amino acid modifications

Modified residue21N-acetylserine

Experimental info

Sequence conflict131Y → N in AAP97169. Ref.1
Sequence conflict23 – 242GI → AF in AAP97169. Ref.1
Sequence conflict72 – 732PH → HI in AAP97169. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96C36-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9348455A64CCE722

FASTA32033,637
        10         20         30         40         50         60 
MSVGFIGAGQ LAYALARGFT AAGILSAHKI IASSPEMNLP TVSALRKMGV NLTRSNKETV 

        70         80         90        100        110        120 
KHSDVLFLAV KPHIIPFILD EIGADVQARH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC 

       130        140        150        160        170        180 
MTNTPVVVQE GATVYATGTH ALVEDGQLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY 

       190        200        210        220        230        240 
AFMALDALAD GGVKMGLPRR LAIQLGAQAL LGAAKMLLDS EQHPCQLKDN VCSPGGATIH 

       250        260        270        280        290        300 
ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKISPA ALKKTLLDRV KLESPTVSTL 

       310        320 
TPSSPGKLLT RSLALGGKKD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a new human cDNA homologous to human pyrroline 5-carboxylate reductase mRNA."
Yue P., Yu L., Zhao S.Y.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix and Skin.
[4]Bienvenut W.V., Heiserich L., Gottlieb E., Zebisch A., Kolch W.
Submitted (OCT-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
Tissue: Colon carcinoma.

Cross-references

Sequence databases

AF087859 mRNA. Translation: AAP97169.1.
AL117348 Genomic DNA. Translation: CAI21802.1.
BC014868 mRNA. Translation: AAH14868.1.
BC020553 mRNA. Translation: AAH20553.1.
RefSeqNP_037460.2.
UniGeneHs.654718

3D structure databases

SMRQ96C36. Positions 1-275.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96C36.

PTM databases

PhosphoSiteQ96C36.

Genome annotation databases

EnsemblENSG00000143811. Homo sapiens. [Contig view]
GeneID29920.
KEGGhsa:29920.

Organism-specific databases

H-InvDBHIX0001639.
HGNCHGNC:30262. PYCR2.
PharmGKBPA134881955.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ96C36.

Gene expression databases

ArrayExpressQ96C36.
CleanExHS_PYCR2.
GermOnlineENSG00000143811. Homo sapiens.

Family and domain databases

InterProIPR016040. NAD(P)-bd.
IPR004455. NADP_OxRdtase_F420.
IPR000304. P5CR.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11645. P5CR. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
TIGRFAMsTIGR00112. proC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00172. L-Proline.
DB00157. NADH.
NextBio52520.

Entry information

Entry nameP5CR2_HUMAN
AccessionPrimary (citable) accession number: Q96C36
Secondary accession number(s): Q7Z515, Q9Y5J4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: December 1, 2001
Last modified: November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents