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Q96C36 (P5CR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
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)

Function

Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP+. Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH. Ref.7 Ref.8

Catalytic activity

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H. Ref.7 Ref.8

Enzyme regulation

Subject to competitive inhibition by NADP. Not inhibited by proline. Ref.7 Ref.8

Pathway

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

Subunit structure

Homodecamer; composed of 5 homodimers Probable. Ref.8

Subcellular location

Cytoplasm Ref.8.

Tissue specificity

Detected in erythrocytes (at protein level). Ref.7 Ref.8

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.64 mM for NADH Ref.8

KM=0.04 mM for NADPH

KM=1.49 mM for pyrroline-5-carboxylate (in the presence of NADH)

KM=0.23 mM for pyrroline-5-carboxylate (in the presence of NADPH)

Vmax=28.5 µmol/min/µg enzyme (in the presence of NADH)

Vmax=3.7 µmol/min/µg enzyme (in the presence of NADPH)

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyrroline-5-carboxylate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 320319Pyrroline-5-carboxylate reductase 2
PRO_0000187317

Regions

Nucleotide binding6 – 116NADP By similarity
Nucleotide binding69 – 724NADP By similarity
Nucleotide binding95 – 973NADP By similarity

Sites

Binding site341NADP; via carbonyl oxygen By similarity
Binding site561NADP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue3041Phosphoserine Ref.10 Ref.12 Ref.14

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 [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]"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].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Cervix and Skin.
[6]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[7]"Pyrroline-5-carboxylate reductase in human erythrocytes."
Yeh G.C., Harris S.C., Phang J.M.
J. Clin. Invest. 67:1042-1046(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
[8]"Purified human erythrocyte pyrroline-5-carboxylate reductase. Preferential oxidation of NADPH."
Merrill M.J., Yeh G.C., Phang J.M.
J. Biol. Chem. 264:9352-9358(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087859 mRNA. Translation: AAP97169.1.
AK291913 mRNA. Translation: BAF84602.1.
AL117348 Genomic DNA. Translation: CAI21802.1.
CH471098 Genomic DNA. Translation: EAW69762.1.
BC014868 mRNA. Translation: AAH14868.1.
BC020553 mRNA. Translation: AAH20553.1.
RefSeqNP_001258610.1. NM_001271681.1.
NP_037460.2. NM_013328.3.
UniGeneHs.654718.

3D structure databases

ProteinModelPortalQ96C36.
SMRQ96C36. Positions 1-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118962. 11 interactions.
IntActQ96C36. 7 interactions.
MINTMINT-1150827.
STRING9606.ENSP00000342502.

Chemistry

DrugBankDB00172. L-Proline.
DB00157. NADH.

PTM databases

PhosphoSiteQ96C36.

Polymorphism databases

DMDM60390642.

Proteomic databases

PaxDbQ96C36.
PRIDEQ96C36.

Protocols and materials databases

DNASU29920.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343818; ENSP00000342502; ENSG00000143811.
GeneID29920.
KEGGhsa:29920.
UCSCuc001hpq.4. human.

Organism-specific databases

CTD29920.
GeneCardsGC01M226107.
H-InvDBHIX0200217.
HGNCHGNC:30262. PYCR2.
HPAHPA056873.
neXtProtNX_Q96C36.
PharmGKBPA134881955.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0345.
HOGENOMHOG000230247.
HOVERGENHBG053399.
InParanoidQ96C36.
KOK00286.
OMASRVELLM.
OrthoDBEOG7N0C5N.
PhylomeDBQ96C36.

Enzyme and pathway databases

SABIO-RKQ96C36.
UniPathwayUPA00098; UER00361.

Gene expression databases

ArrayExpressQ96C36.
BgeeQ96C36.
CleanExHS_PYCR2.
GenevestigatorQ96C36.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR028939. ProC_N.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
PANTHERPTHR11645. PTHR11645. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00112. proC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi29920.
NextBio52520.
PROQ96C36.

Entry information

Entry nameP5CR2_HUMAN
AccessionPrimary (citable) accession number: Q96C36
Secondary accession number(s): A8K798, Q7Z515, Q9Y5J4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 108 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 1

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