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Q96C36

- P5CR2_HUMAN

UniProt

Q96C36 - P5CR2_HUMAN

Protein

Pyrroline-5-carboxylate reductase 2

Gene

PYCR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H.2 Publications

    Enzyme regulationi

    Subject to competitive inhibition by NADP. Not inhibited by proline.2 Publications

    Kineticsi

    1. KM=0.64 mM for NADH1 Publication
    2. KM=0.04 mM for NADPH1 Publication
    3. KM=1.49 mM for pyrroline-5-carboxylate (in the presence of NADH)1 Publication
    4. KM=0.23 mM for pyrroline-5-carboxylate (in the presence of NADPH)1 Publication

    Vmax=28.5 µmol/min/µg enzyme (in the presence of NADH)1 Publication

    Vmax=3.7 µmol/min/µg enzyme (in the presence of NADPH)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341NADP; via carbonyl oxygenBy similarity
    Binding sitei56 – 561NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 116NADPBy similarity
    Nucleotide bindingi69 – 724NADPBy similarity
    Nucleotide bindingi95 – 973NADPBy similarity

    GO - Molecular functioni

    1. pyrroline-5-carboxylate reductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-proline biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    SABIO-RKQ96C36.
    UniPathwayiUPA00098; UER00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroline-5-carboxylate reductase 2 (EC:1.5.1.2)
    Short name:
    P5C reductase 2
    Short name:
    P5CR 2
    Gene namesi
    Name:PYCR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30262. PYCR2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134881955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 320319Pyrroline-5-carboxylate reductase 2PRO_0000187317Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei304 – 3041Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96C36.
    PaxDbiQ96C36.
    PRIDEiQ96C36.

    PTM databases

    PhosphoSiteiQ96C36.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ96C36.
    BgeeiQ96C36.
    CleanExiHS_PYCR2.
    GenevestigatoriQ96C36.

    Organism-specific databases

    HPAiHPA056873.

    Interactioni

    Subunit structurei

    Homodecamer; composed of 5 homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi118962. 12 interactions.
    IntActiQ96C36. 8 interactions.
    MINTiMINT-1150827.
    STRINGi9606.ENSP00000342502.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96C36.
    SMRiQ96C36. Positions 1-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0345.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiQ96C36.
    KOiK00286.
    OMAiASCENAD.
    OrthoDBiEOG7N0C5N.
    PhylomeDBiQ96C36.

    Family and domain databases

    Gene3Di1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_01925. P5C_reductase.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view]
    PANTHERiPTHR11645. PTHR11645. 1 hit.
    PfamiPF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00112. proC. 1 hit.
    PROSITEiPS00521. P5CR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96C36-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVGFIGAGQ LAYALARGFT AAGILSAHKI IASSPEMNLP TVSALRKMGV    50
    NLTRSNKETV KHSDVLFLAV KPHIIPFILD EIGADVQARH IVVSCAAGVT 100
    ISSVEKKLMA FQPAPKVIRC MTNTPVVVQE GATVYATGTH ALVEDGQLLE 150
    QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY AFMALDALAD GGVKMGLPRR 200
    LAIQLGAQAL LGAAKMLLDS EQHPCQLKDN VCSPGGATIH ALHFLESGGF 250
    RSLLINAVEA SCIRTRELQS MADQEKISPA ALKKTLLDRV KLESPTVSTL 300
    TPSSPGKLLT RSLALGGKKD 320
    Length:320
    Mass (Da):33,637
    Last modified:December 1, 2001 - v1
    Checksum:i9348455A64CCE722
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131Y → N in AAP97169. 1 PublicationCurated
    Sequence conflicti23 – 242GI → AF in AAP97169. 1 PublicationCurated
    Sequence conflicti72 – 732PH → HI in AAP97169. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31043.1.
    RefSeqiNP_001258610.1. NM_001271681.1.
    NP_037460.2. NM_013328.3.
    UniGeneiHs.654718.

    Genome annotation databases

    EnsembliENST00000343818; ENSP00000342502; ENSG00000143811.
    GeneIDi29920.
    KEGGihsa:29920.
    UCSCiuc001hpq.4. human.

    Polymorphism databases

    DMDMi60390642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31043.1.
    RefSeqi NP_001258610.1. NM_001271681.1.
    NP_037460.2. NM_013328.3.
    UniGenei Hs.654718.

    3D structure databases

    ProteinModelPortali Q96C36.
    SMRi Q96C36. Positions 1-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118962. 12 interactions.
    IntActi Q96C36. 8 interactions.
    MINTi MINT-1150827.
    STRINGi 9606.ENSP00000342502.

    Chemistry

    DrugBanki DB00172. L-Proline.
    DB00157. NADH.

    PTM databases

    PhosphoSitei Q96C36.

    Polymorphism databases

    DMDMi 60390642.

    Proteomic databases

    MaxQBi Q96C36.
    PaxDbi Q96C36.
    PRIDEi Q96C36.

    Protocols and materials databases

    DNASUi 29920.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343818 ; ENSP00000342502 ; ENSG00000143811 .
    GeneIDi 29920.
    KEGGi hsa:29920.
    UCSCi uc001hpq.4. human.

    Organism-specific databases

    CTDi 29920.
    GeneCardsi GC01M226107.
    H-InvDB HIX0200217.
    HGNCi HGNC:30262. PYCR2.
    HPAi HPA056873.
    neXtProti NX_Q96C36.
    PharmGKBi PA134881955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0345.
    HOGENOMi HOG000230247.
    HOVERGENi HBG053399.
    InParanoidi Q96C36.
    KOi K00286.
    OMAi ASCENAD.
    OrthoDBi EOG7N0C5N.
    PhylomeDBi Q96C36.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00361 .
    SABIO-RK Q96C36.

    Miscellaneous databases

    GenomeRNAii 29920.
    NextBioi 52520.
    PROi Q96C36.

    Gene expression databases

    ArrayExpressi Q96C36.
    Bgeei Q96C36.
    CleanExi HS_PYCR2.
    Genevestigatori Q96C36.

    Family and domain databases

    Gene3Di 1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_01925. P5C_reductase.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view ]
    PANTHERi PTHR11645. PTHR11645. 1 hit.
    Pfami PF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00112. proC. 1 hit.
    PROSITEi PS00521. P5CR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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].

    Entry informationi

    Entry nameiP5CR2_HUMAN
    AccessioniPrimary (citable) accession number: Q96C36
    Secondary accession number(s): A8K798, Q7Z515, Q9Y5J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3