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P32322 (P5CR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyrroline-5-carboxylate reductase 1, mitochondrial

Short name=P5C reductase 1
Short name=P5CR 1
EC=1.5.1.2
Gene names
Name:PYCR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length319 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. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress. Ref.11 Ref.14

Catalytic activity

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H. Ref.14

Enzyme regulation

Subject to competitive inhibition by the reaction product proline. Subject to competitive inhibition by stearoyl coenzyme A. Ref.14

Pathway

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

Subunit structure

Homodecamer; composed of 5 homodimers. Ref.14

Subcellular location

Mitochondrion Ref.11.

Involvement in disease

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. Ref.11 Ref.16

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. Ref.11 Ref.17

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.151 mM for NAD+ Ref.14

KM=3.06 mM for NADP+

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-848624,EBI-848624

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32322-1)

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.
Isoform 2 (identifier: P32322-2)

The sequence of this isoform differs from the canonical sequence as follows:
     290-319: VKLDSPAGTALSPSGHTKLLPRSLAPAGKD → DHLPLELGSPEGLHPLLLQYQLARAPS
Isoform 3 (identifier: P32322-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGGGRRVGRDEPVPSVGALGQGSPDSM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 319318Pyrroline-5-carboxylate reductase 1, mitochondrial
PRO_0000187314

Regions

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

Sites

Binding site341NADP; via carbonyl oxygen
Binding site561NADP

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.9 Ref.10

Natural variations

Alternative sequence11M → MVGGGRRVGRDEPVPSVGAL GQGSPDSM in isoform 3.
VSP_054616
Alternative sequence290 – 31930VKLDS…PAGKD → DHLPLELGSPEGLHPLLLQY QLARAPS in isoform 2.
VSP_044507
Natural variant1191R → G in ARCL2B. Ref.11
VAR_059068
Natural variant1191R → H in ARCL2B. Ref.11
Corresponds to variant rs121918377 [ dbSNP | Ensembl ].
VAR_059069
Natural variant1791A → T in ARCL2B. Ref.11
VAR_059070
Natural variant1891A → V. Ref.11
VAR_059071
Natural variant2061G → R in ARCL2B. Ref.11
Corresponds to variant rs121918375 [ dbSNP | Ensembl ].
VAR_059072
Natural variant2061G → W in ARCL2B. Ref.11
VAR_059073
Natural variant2481G → E in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient. Ref.17
Corresponds to variant rs281875319 [ dbSNP | Ensembl ].
VAR_067600
Natural variant2511R → H in ARCL3B. Ref.11
VAR_059074
Natural variant2571A → T in ARCL3B. Ref.11
Corresponds to variant rs281875318 [ dbSNP | Ensembl ].
VAR_059075
Natural variant2661R → Q in ARCL2B; may cause skipping of exon 6. Ref.16
VAR_059076
Natural variant2971G → R. Ref.17
VAR_067601

Experimental info

Mutagenesis2211E → A: Reduced enzyme activity. Ref.14
Sequence conflict1551S → T in AAA36407. Ref.1
Sequence conflict3171G → S in CAG46568. Ref.4

Secondary structure

................................................. 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: 9E8C4DED0638EFC5

FASTA31933,361
        10         20         30         40         50         60 
MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV 

        70         80         90        100        110        120 
QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC 

       130        140        150        160        170        180 
MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY 

       190        200        210        220        230        240 
AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH 

       250        260        270        280        290        300 
ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL 

       310 
SPSGHTKLLP RSLAPAGKD 

« Hide

Isoform 2 [UniParc].

Checksum: 65C247E391225ED6
Show »

FASTA31633,341
Isoform 3 [UniParc].

Checksum: 25E6A7FEBBB34A3E
Show »

FASTA34635,981

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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].
[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]"Mutations in PYCR1 cause cutis laxa with progeroid features."
Reversade B., Escande-Beillard N., Dimopoulou A., Fischer B., Chng S.C., Li Y., Shboul M., Tham P.-Y., Kayserili H., Al-Gazali L., Shahwan M., Brancati F., Lee H., O'Connor B.D., Schmidt-von Kegler M., Merriman B., Nelson S.F., Masri A. expand/collapse author list , Alkazaleh F., Guerra D., Ferrari P., Nanda A., Rajab A., Markie D., Gray M., Nelson J., Grix A., Sommer A., Savarirayan R., Janecke A.R., Steichen E., Sillence D., Hausser I., Budde B., Nuernberg G., Nuernberg P., Seemann P., Kunkel D., Zambruno G., Dallapiccola B., Schuelke M., Robertson S., Hamamy H., Wollnik B., Van Maldergem L., Mundlos S., Kornak U.
Nat. Genet. 41:1016-1021(2009) [PubMed] [Europe PMC] [Abstract]
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]"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]"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]"Mutation in pyrroline-5-carboxylate reductase 1 gene in families with cutis laxa type 2."
Guernsey D.L., Jiang H., Evans S.C., Ferguson M., Matsuoka M., Nightingale M., Rideout A.L., Provost S., Bedard K., Orr A., Dube M.-P., Ludman M., Samuels M.E.
Am. J. Hum. Genet. 85:120-129(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11794.1. [P32322-2]
CCDS11795.1. [P32322-1]
PIRA41770.
RefSeqNP_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]
UniGeneHs.163451.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP32322.
SMRP32322. Positions 1-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111789. 14 interactions.
IntActP32322. 5 interactions.
STRING9606.ENSP00000328858.

Chemistry

DrugBankDB00172. L-Proline.
DB00157. NADH.

PTM databases

PhosphoSiteP32322.

Polymorphism databases

DMDM60416434.

Proteomic databases

MaxQBP32322.
PaxDbP32322.
PRIDEP32322.

Protocols and materials databases

DNASU5831.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329875; ENSP00000328858; ENSG00000183010. [P32322-1]
ENST00000337943; ENSP00000336579; ENSG00000183010. [P32322-2]
ENST00000402252; ENSP00000384949; ENSG00000183010.
GeneID5831.
KEGGhsa:5831.
UCSCuc002kcp.3. human. [P32322-2]
uc002kcr.1. human. [P32322-1]

Organism-specific databases

CTD5831.
GeneCardsGC17M079890.
HGNCHGNC:9721. PYCR1.
HPAHPA047660.
MIM179035. gene.
612940. phenotype.
614438. phenotype.
neXtProtNX_P32322.
Orphanet357064. Autosomal recessive cutis laxa type 2B.
2078. Geroderma osteodysplastica.
293633. PYCR1-related DeBarsy syndrome.
PharmGKBPA34064.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0345.
HOGENOMHOG000230247.
HOVERGENHBG053399.
InParanoidP32322.
KOK00286.
OrthoDBEOG7N0C5N.
PhylomeDBP32322.

Enzyme and pathway databases

BioCycMetaCyc:HS06848-MONOMER.
BRENDA1.5.1.2. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP32322.
UniPathwayUPA00098; UER00361.

Gene expression databases

ArrayExpressP32322.
BgeeP32322.
CleanExHS_PYCR1.
GenevestigatorP32322.

Family and domain databases

Gene3D1.10.3730.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR029036. P5CR_dimer.
IPR028939. ProC_N.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
PANTHERPTHR11645. PTHR11645. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
PF14748. P5CR_dimer. 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

EvolutionaryTraceP32322.
GeneWikiPYCR1.
GenomeRNAi5831.
NextBio22720.
PROP32322.
SOURCESearch...

Entry information

Entry nameP5CR1_HUMAN
AccessionPrimary (citable) accession number: P32322
Secondary accession number(s): A6NFM2 expand/collapse secondary AC list , B4DMU0, Q6FHI4, Q96DI6, Q9HBQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 139 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM