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Protein

Pyrroline-5-carboxylate reductase 1, mitochondrial

Gene

PYCR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress.2 Publications

Catalytic activityi

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

Enzyme regulationi

Subject to competitive inhibition by the reaction product proline. Subject to competitive inhibition by stearoyl coenzyme A.1 Publication

Kineticsi

  1. KM=0.151 mM for NAD+1 Publication
  2. KM=3.06 mM for NADP+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341NADP; via carbonyl oxygen1 Publication
    Binding sitei56 – 561NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 116NADP1 Publication
    Nucleotide bindingi69 – 724NADP1 Publication
    Nucleotide bindingi95 – 973NADP1 Publication

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • pyrroline-5-carboxylate reductase activity Source: UniProtKB

    GO - Biological processi

    • cellular amino acid biosynthetic process Source: Reactome
    • cellular nitrogen compound metabolic process Source: Reactome
    • cellular response to oxidative stress Source: UniProtKB
    • L-proline biosynthetic process Source: UniProtKB-UniPathway
    • negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
    • proline biosynthetic process Source: UniProtKB
    • regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis, Stress response

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06848-MONOMER.
    BRENDAi1.5.1.2. 2681.
    ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP32322.
    UniPathwayiUPA00098; UER00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroline-5-carboxylate reductase 1, mitochondrial (EC:1.5.1.2)
    Short name:
    P5C reductase 1
    Short name:
    P5CR 1
    Gene namesi
    Name:PYCR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9721. PYCR1.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Cutis laxa, autosomal recessive, 2B (ARCL2B)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Patients do not manifest metabolic abnormalities.

    See also OMIM:612940
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191R → G in ARCL2B. 1 Publication
    VAR_059068
    Natural varianti119 – 1191R → H in ARCL2B. 1 Publication
    Corresponds to variant rs121918377 [ dbSNP | Ensembl ].
    VAR_059069
    Natural varianti179 – 1791A → T in ARCL2B. 1 Publication
    VAR_059070
    Natural varianti206 – 2061G → R in ARCL2B. 1 Publication
    Corresponds to variant rs121918375 [ dbSNP | Ensembl ].
    VAR_059072
    Natural varianti206 – 2061G → W in ARCL2B. 1 Publication
    VAR_059073
    Natural varianti266 – 2661R → Q in ARCL2B; may cause skipping of exon 6. 1 Publication
    VAR_059076
    Cutis laxa, autosomal recessive, 3B (ARCL3B)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa.

    See also OMIM:614438
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti248 – 2481G → E in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient. 1 Publication
    Corresponds to variant rs281875319 [ dbSNP | Ensembl ].
    VAR_067600
    Natural varianti251 – 2511R → H in ARCL3B. 1 Publication
    VAR_059074
    Natural varianti257 – 2571A → T in ARCL3B. 1 Publication
    Corresponds to variant rs281875318 [ dbSNP | Ensembl ].
    VAR_059075

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2211E → A: Reduced enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612940. phenotype.
    614438. phenotype.
    Orphaneti357064. Autosomal recessive cutis laxa type 2B.
    2078. Geroderma osteodysplastica.
    293633. PYCR1-related De Barsy syndrome.
    PharmGKBiPA34064.

    Chemistry

    DrugBankiDB00172. L-Proline.

    Polymorphism and mutation databases

    BioMutaiPYCR1.
    DMDMi60416434.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 319318Pyrroline-5-carboxylate reductase 1, mitochondrialPRO_0000187314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP32322.
    PaxDbiP32322.
    PRIDEiP32322.

    PTM databases

    PhosphoSiteiP32322.

    Expressioni

    Gene expression databases

    BgeeiP32322.
    CleanExiHS_PYCR1.
    ExpressionAtlasiP32322. baseline and differential.
    GenevestigatoriP32322.

    Organism-specific databases

    HPAiHPA047660.

    Interactioni

    Subunit structurei

    Homodecamer; composed of 5 homodimers.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-848624,EBI-848624
    PARK7Q994975EBI-848624,EBI-1164361

    Protein-protein interaction databases

    BioGridi111789. 21 interactions.
    IntActiP32322. 7 interactions.
    STRINGi9606.ENSP00000328858.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75Combined sources
    Helixi10 – 2112Combined sources
    Helixi27 – 293Combined sources
    Beta strandi30 – 334Combined sources
    Helixi40 – 489Combined sources
    Beta strandi51 – 544Combined sources
    Helixi56 – 627Combined sources
    Beta strandi64 – 685Combined sources
    Helixi72 – 743Combined sources
    Helixi75 – 828Combined sources
    Helixi83 – 853Combined sources
    Beta strandi91 – 944Combined sources
    Helixi101 – 1099Combined sources
    Beta strandi112 – 1143Combined sources
    Beta strandi116 – 1216Combined sources
    Helixi124 – 1285Combined sources
    Beta strandi131 – 1377Combined sources
    Helixi143 – 15412Combined sources
    Beta strandi157 – 1615Combined sources
    Helixi164 – 1663Combined sources
    Helixi167 – 1737Combined sources
    Turni174 – 1763Combined sources
    Helixi177 – 19418Combined sources
    Helixi199 – 21921Combined sources
    Helixi224 – 2318Combined sources
    Helixi237 – 24711Combined sources
    Helixi250 – 27021Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GERX-ray3.10A/B/C/D/E1-319[»]
    2GR9X-ray3.10A/B/C/D/E1-275[»]
    2GRAX-ray3.10A/B/C/D/E1-275[»]
    2IZZX-ray1.95A/B/C/D/E1-300[»]
    ProteinModelPortaliP32322.
    SMRiP32322. Positions 1-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32322.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0345.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiP32322.
    KOiK00286.
    OMAiRTFNEHQ.
    OrthoDBiEOG7N0C5N.
    PhylomeDBiP32322.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P32322-1) [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
    MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV
    60 70 80 90 100
    KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT
    110 120 130 140 150
    ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME
    160 170 180 190 200
    QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR
    210 220 230 240 250
    LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF
    260 270 280 290 300
    RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL
    310
    SPSGHTKLLP RSLAPAGKD
    Length:319
    Mass (Da):33,361
    Last modified:March 1, 2005 - v2
    Checksum:i9E8C4DED0638EFC5
    GO
    Isoform 2 (identifier: P32322-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         290-319: VKLDSPAGTALSPSGHTKLLPRSLAPAGKD → DHLPLELGSPEGLHPLLLQYQLARAPS

    Show »
    Length:316
    Mass (Da):33,341
    Checksum:i65C247E391225ED6
    GO
    Isoform 3 (identifier: P32322-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVGGGRRVGRDEPVPSVGALGQGSPDSM

    Note: No experimental confirmation available.

    Show »
    Length:346
    Mass (Da):35,981
    Checksum:i25E6A7FEBBB34A3E
    GO

    Sequence cautioni

    The sequence AAG17242.1 differs from that shown. Reason: Frameshift at position 214. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551S → T in AAA36407 (PubMed:1730675).Curated
    Sequence conflicti317 – 3171G → S in CAG46568 (Ref. 4) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191R → G in ARCL2B. 1 Publication
    VAR_059068
    Natural varianti119 – 1191R → H in ARCL2B. 1 Publication
    Corresponds to variant rs121918377 [ dbSNP | Ensembl ].
    VAR_059069
    Natural varianti179 – 1791A → T in ARCL2B. 1 Publication
    VAR_059070
    Natural varianti189 – 1891A → V.1 Publication
    VAR_059071
    Natural varianti206 – 2061G → R in ARCL2B. 1 Publication
    Corresponds to variant rs121918375 [ dbSNP | Ensembl ].
    VAR_059072
    Natural varianti206 – 2061G → W in ARCL2B. 1 Publication
    VAR_059073
    Natural varianti248 – 2481G → E in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient. 1 Publication
    Corresponds to variant rs281875319 [ dbSNP | Ensembl ].
    VAR_067600
    Natural varianti251 – 2511R → H in ARCL3B. 1 Publication
    VAR_059074
    Natural varianti257 – 2571A → T in ARCL3B. 1 Publication
    Corresponds to variant rs281875318 [ dbSNP | Ensembl ].
    VAR_059075
    Natural varianti266 – 2661R → Q in ARCL2B; may cause skipping of exon 6. 1 Publication
    VAR_059076
    Natural varianti297 – 2971G → R.1 Publication
    VAR_067601

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MVGGGRRVGRDEPVPSVGAL GQGSPDSM in isoform 3. 1 PublicationVSP_054616
    Alternative sequencei290 – 31930VKLDS…PAGKD → DHLPLELGSPEGLHPLLLQY QLARAPS in isoform 2. 1 PublicationVSP_044507Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77836 mRNA. Translation: AAA36407.1.
    AF218000 mRNA. Translation: AAG17242.1. Frameshift.
    AK297627 mRNA. Translation: BAG60002.1.
    CR541769 mRNA. Translation: CAG46568.1.
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89724.1.
    BC001504 mRNA. Translation: AAH01504.1.
    BC071842 mRNA. Translation: AAH71842.1.
    CCDSiCCDS11794.1. [P32322-2]
    CCDS11795.1. [P32322-1]
    CCDS62366.1. [P32322-3]
    PIRiA41770.
    RefSeqiNP_001269209.1. NM_001282280.1. [P32322-1]
    NP_001269210.1. NM_001282281.1. [P32322-3]
    NP_008838.2. NM_006907.3. [P32322-1]
    NP_722546.1. NM_153824.2. [P32322-2]
    XP_005256438.1. XM_005256381.1. [P32322-1]
    UniGeneiHs.163451.

    Genome annotation databases

    EnsembliENST00000329875; ENSP00000328858; ENSG00000183010. [P32322-1]
    ENST00000337943; ENSP00000336579; ENSG00000183010. [P32322-2]
    ENST00000402252; ENSP00000384949; ENSG00000183010. [P32322-3]
    ENST00000619204; ENSP00000479793; ENSG00000183010. [P32322-1]
    GeneIDi5831.
    KEGGihsa:5831.
    UCSCiuc002kcp.3. human. [P32322-2]
    uc002kcr.1. human. [P32322-1]
    uc010wvd.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mendelian genes pyrroline-5-carboxylate reductase 1 (PYCR1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77836 mRNA. Translation: AAA36407.1.
    AF218000 mRNA. Translation: AAG17242.1. Frameshift.
    AK297627 mRNA. Translation: BAG60002.1.
    CR541769 mRNA. Translation: CAG46568.1.
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89724.1.
    BC001504 mRNA. Translation: AAH01504.1.
    BC071842 mRNA. Translation: AAH71842.1.
    CCDSiCCDS11794.1. [P32322-2]
    CCDS11795.1. [P32322-1]
    CCDS62366.1. [P32322-3]
    PIRiA41770.
    RefSeqiNP_001269209.1. NM_001282280.1. [P32322-1]
    NP_001269210.1. NM_001282281.1. [P32322-3]
    NP_008838.2. NM_006907.3. [P32322-1]
    NP_722546.1. NM_153824.2. [P32322-2]
    XP_005256438.1. XM_005256381.1. [P32322-1]
    UniGeneiHs.163451.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GERX-ray3.10A/B/C/D/E1-319[»]
    2GR9X-ray3.10A/B/C/D/E1-275[»]
    2GRAX-ray3.10A/B/C/D/E1-275[»]
    2IZZX-ray1.95A/B/C/D/E1-300[»]
    ProteinModelPortaliP32322.
    SMRiP32322. Positions 1-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111789. 21 interactions.
    IntActiP32322. 7 interactions.
    STRINGi9606.ENSP00000328858.

    Chemistry

    DrugBankiDB00172. L-Proline.

    PTM databases

    PhosphoSiteiP32322.

    Polymorphism and mutation databases

    BioMutaiPYCR1.
    DMDMi60416434.

    Proteomic databases

    MaxQBiP32322.
    PaxDbiP32322.
    PRIDEiP32322.

    Protocols and materials databases

    DNASUi5831.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000329875; ENSP00000328858; ENSG00000183010. [P32322-1]
    ENST00000337943; ENSP00000336579; ENSG00000183010. [P32322-2]
    ENST00000402252; ENSP00000384949; ENSG00000183010. [P32322-3]
    ENST00000619204; ENSP00000479793; ENSG00000183010. [P32322-1]
    GeneIDi5831.
    KEGGihsa:5831.
    UCSCiuc002kcp.3. human. [P32322-2]
    uc002kcr.1. human. [P32322-1]
    uc010wvd.1. human.

    Organism-specific databases

    CTDi5831.
    GeneCardsiGC17M079890.
    HGNCiHGNC:9721. PYCR1.
    HPAiHPA047660.
    MIMi179035. gene.
    612940. phenotype.
    614438. phenotype.
    neXtProtiNX_P32322.
    Orphaneti357064. Autosomal recessive cutis laxa type 2B.
    2078. Geroderma osteodysplastica.
    293633. PYCR1-related De Barsy syndrome.
    PharmGKBiPA34064.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0345.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiP32322.
    KOiK00286.
    OMAiRTFNEHQ.
    OrthoDBiEOG7N0C5N.
    PhylomeDBiP32322.

    Enzyme and pathway databases

    UniPathwayiUPA00098; UER00361.
    BioCyciMetaCyc:HS06848-MONOMER.
    BRENDAi1.5.1.2. 2681.
    ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP32322.

    Miscellaneous databases

    EvolutionaryTraceiP32322.
    GeneWikiiPYCR1.
    GenomeRNAii5831.
    NextBioi22720.
    PROiP32322.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP32322.
    CleanExiHS_PYCR1.
    ExpressionAtlasiP32322. baseline and differential.
    GenevestigatoriP32322.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae."
      Dougherty K.M., Brandriss M.C., Valle D.
      J. Biol. Chem. 267:871-875(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Novel Human cDNA clones with function of inhibiting cancer cell growth."
      Gu J.R., Wan D.F., Zhao X.T., Zhou X.M., Jiang H.Q., Zhang P.P., Qin W.X., Huang Y., Qiu X.K., Qian L.F., He L.P., Li H.N., Yu Y., Yu J., Han L.H.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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.
      , 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 3).
      Tissue: Brain.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Lymph and Placenta.
    8. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17 AND 205-215, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-46; 130-147; 205-215 AND 252-264, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANTS ARCL2B GLY-119; HIS-119; THR-179; TRP-206 AND ARG-206, VARIANTS ARCL3B HIS-251 AND THR-257, VARIANT VAL-189.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of human pyrroline-5-carboxylate reductase."
      Meng Z., Lou Z., Liu Z., Li M., Zhao X., Bartlam M., Rao Z.
      J. Mol. Biol. 359:1364-1377(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH NAD; NADP AND SUBSTRATE ANALOG GLU, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-221, SUBUNIT.
    15. "Crystal structure of human pyrroline-5-carboxylate reductase."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-300 IN COMPLEX WITH NAD.
    16. Cited for: VARIANT ARCL2B GLN-266.
    17. "Compound heterozygous mutations in PYCR1 further expand the phenotypic spectrum of De Barsy syndrome."
      Lin D.S., Chang J.H., Liu H.L., Wei C.H., Yeung C.Y., Ho C.S., Shu C.H., Chiang M.F., Chuang C.K., Huang Y.W., Wu T.Y., Jian Y.R., Huang Z.D., Lin S.P.
      Am. J. Med. Genet. A 155:3095-3099(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARCL3B GLU-248, VARIANT ARG-297.

    Entry informationi

    Entry nameiP5CR1_HUMAN
    AccessioniPrimary (citable) accession number: P32322
    Secondary accession number(s): A6NFM2
    , B4DMU0, Q6FHI4, Q96DI6, Q9HBQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: March 1, 2005
    Last modified: April 29, 2015
    This is version 146 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3

    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 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.