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P32322

- P5CR1_HUMAN

UniProt

P32322 - P5CR1_HUMAN

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Protein

Pyrroline-5-carboxylate reductase 1, mitochondrial

Gene
PYCR1
Organism
Homo sapiens (Human)
Status
Reviewed - 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+

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. pyrroline-5-carboxylate reductase activity Source: UniProtKB

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. cellular response to oxidative stress Source: UniProtKB
  4. L-proline biosynthetic process Source: UniProtKB-UniPathway
  5. proline biosynthetic process Source: UniProtKB
  6. 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: Chromosome 17

Organism-specific databases

HGNCiHGNC:9721. PYCR1.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 2B (ARCL2B) [MIM:612940]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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) [MIM:614438]: A disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 DeBarsy syndrome.
PharmGKBiPA34064.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 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

ArrayExpressiP32322.
BgeeiP32322.
CleanExiHS_PYCR1.
GenevestigatoriP32322.

Organism-specific databases

HPAiHPA047660.

Interactioni

Subunit structurei

Homodecamer; composed of 5 homodimers.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111789. 16 interactions.
IntActiP32322. 6 interactions.
STRINGi9606.ENSP00000328858.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP32322.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0345.
HOGENOMiHOG000230247.
HOVERGENiHBG053399.
InParanoidiP32322.
KOiK00286.
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. Align

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

MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV    50
KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT 100
ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME 150
QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR 200
LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF 250
RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL 300
SPSGHTKLLP RSLAPAGKD 319
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.

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. VSP_054616
Alternative sequencei290 – 31930VKLDS…PAGKD → DHLPLELGSPEGLHPLLLQY QLARAPS in isoform 2. VSP_044507Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551S → T in AAA36407. 1 Publication
Sequence conflicti317 – 3171G → S in CAG46568. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi5831.
KEGGihsa:5831.
UCSCiuc002kcp.3. human. [P32322-2]
uc002kcr.1. human. [P32322-1]

Polymorphism databases

DMDMi60416434.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11794.1. [P32322-2 ]
CCDS11795.1. [P32322-1 ]
CCDS62366.1. [P32322-3 ]
PIRi A41770.
RefSeqi NP_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 ]
UniGenei Hs.163451.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GER X-ray 3.10 A/B/C/D/E 1-319 [» ]
2GR9 X-ray 3.10 A/B/C/D/E 1-275 [» ]
2GRA X-ray 3.10 A/B/C/D/E 1-275 [» ]
2IZZ X-ray 1.95 A/B/C/D/E 1-300 [» ]
ProteinModelPortali P32322.
SMRi P32322. Positions 1-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111789. 16 interactions.
IntActi P32322. 6 interactions.
STRINGi 9606.ENSP00000328858.

Chemistry

DrugBanki DB00172. L-Proline.
DB00157. NADH.

PTM databases

PhosphoSitei P32322.

Polymorphism databases

DMDMi 60416434.

Proteomic databases

MaxQBi P32322.
PaxDbi P32322.
PRIDEi P32322.

Protocols and materials databases

DNASUi 5831.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329875 ; ENSP00000328858 ; ENSG00000183010 . [P32322-1 ]
ENST00000337943 ; ENSP00000336579 ; ENSG00000183010 . [P32322-2 ]
ENST00000402252 ; ENSP00000384949 ; ENSG00000183010 .
GeneIDi 5831.
KEGGi hsa:5831.
UCSCi uc002kcp.3. human. [P32322-2 ]
uc002kcr.1. human. [P32322-1 ]

Organism-specific databases

CTDi 5831.
GeneCardsi GC17M079890.
HGNCi HGNC:9721. PYCR1.
HPAi HPA047660.
MIMi 179035. gene.
612940. phenotype.
614438. phenotype.
neXtProti NX_P32322.
Orphaneti 357064. Autosomal recessive cutis laxa type 2B.
2078. Geroderma osteodysplastica.
293633. PYCR1-related DeBarsy syndrome.
PharmGKBi PA34064.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0345.
HOGENOMi HOG000230247.
HOVERGENi HBG053399.
InParanoidi P32322.
KOi K00286.
OrthoDBi EOG7N0C5N.
PhylomeDBi P32322.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00361 .
BioCyci MetaCyc:HS06848-MONOMER.
BRENDAi 1.5.1.2. 2681.
Reactomei REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RK P32322.

Miscellaneous databases

EvolutionaryTracei P32322.
GeneWikii PYCR1.
GenomeRNAii 5831.
NextBioi 22720.
PROi P32322.
SOURCEi Search...

Gene expression databases

ArrayExpressi P32322.
Bgeei P32322.
CleanExi HS_PYCR1.
Genevestigatori P32322.

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

« 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].
  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: September 3, 2014
This is version 140 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

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