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O43272 (PROD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline dehydrogenase 1, mitochondrial

EC=1.5.5.2
Alternative name(s):
Proline oxidase
Proline oxidase 2
p53-induced gene 6 protein
Gene names
Name:PRODH
Synonyms:PIG6, POX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts proline to delta-1-pyrroline-5-carboxylate.

Catalytic activity

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol. Ref.3

Cofactor

FAD. Ref.3

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Expressed in lung, skeletal muscle and brain, to a lesser extent in heart and kidney, and weakly in liver, placenta and pancreas.

Induction

During p53/TP53-induced apoptosis. Ref.7

Involvement in disease

Hyperprolinemia 1 (HP-1) [MIM:239500]: Characterized by elevated serum proline levels. May be involved in the psychiatric and behavioral phenotypes associated with the 22q11 velocardiofacial and DiGeorge syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Schizophrenia 4 (SCZD4) [MIM:600850]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the proline oxidase family.

Sequence caution

The sequence AAC39529.1 differs from that shown. Reason: Frameshift at positions 540, 563, 568, 577, 580 and 582.

The sequence AAH68260.1 differs from that shown. Reason: Frameshift at position 123.

The sequence AAH94736.1 differs from that shown. Reason: Frameshift at position 40.

The sequence AAH94736.1 differs from that shown. Reason: Artifact. Missing internal sequence that doesn't correspond to an exon-intron boundary.

The sequence BAD92709.1 differs from that shown. Reason: Intron retention. Includes intronic sequence at the 5' end.

Ontologies

Keywords
   Biological processProline metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Schizophrenia
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process4-hydroxyproline catabolic process

Traceable author statement PubMed 21998747. Source: BHF-UCL

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glutamate biosynthetic process

Inferred from electronic annotation. Source: InterPro

intrinsic apoptotic signaling pathway in response to oxidative stress

Non-traceable author statement Ref.7. Source: UniProtKB

proline catabolic process

Traceable author statement. Source: Reactome

proline catabolic process to glutamate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

proline metabolic process

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionFAD binding

Inferred from direct assay Ref.3. Source: UniProtKB

amino acid binding

Inferred from electronic annotation. Source: Ensembl

proline dehydrogenase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43272-4)

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: O43272-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Isoform 3 (identifier: O43272-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
     85-95: LLARHEQLLYV → MLEFVMREWKK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 600Proline dehydrogenase 1, mitochondrialPRO_0000025800

Amino acid modifications

Modified residue3681N6-acetyllysine By similarity
Modified residue4861N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 108108Missing in isoform 2.
VSP_021848
Alternative sequence1 – 8484Missing in isoform 3.
VSP_040848
Alternative sequence85 – 9511LLARHEQLLYV → MLEFVMREWKK in isoform 3.
VSP_040849
Natural variant81P → L.
VAR_064883
Natural variant191Q → P Moderate reduction of enzymatic activity.
Corresponds to variant rs2008720 [ dbSNP | Ensembl ].
VAR_064884
Natural variant301P → S.
VAR_064885
Natural variant581A → T.
VAR_064886
Natural variant1671A → V Associated with susceptibility to SCZD4; moderate reduction of enzymatic activity. Ref.3
VAR_029563
Natural variant1851R → Q No effect on enzymatic activity. Ref.3
VAR_029564
Natural variant1851R → W Moderate reduction of enzymatic activity. Ref.3
Corresponds to variant rs4819756 [ dbSNP | Ensembl ].
VAR_029565
Natural variant2751T → N. Ref.11
VAR_029874
Natural variant2891L → M Can be associated with HP-1 in a subset of schizophrenia patients; no effect on enzymatic activity. Ref.3 Ref.8
VAR_029566
Natural variant4061P → L Associated with susceptibility to SCZD4; strongly reduced enzymatic activity. Ref.3 Ref.9
Corresponds to variant rs3970555 [ dbSNP | Ensembl ].
VAR_029567
Natural variant4261D → N Moderate reduction of enzymatic activity. Ref.3
VAR_029568
Natural variant4271V → M Associated with susceptibility to SCZD4; moderate reduction of enzymatic activity. Ref.3 Ref.9
Corresponds to variant rs2238731 [ dbSNP | Ensembl ].
VAR_029569
Natural variant4311R → H Associated with HP-1 in a subset of schizophrenia patients; moderate reduction of enzymatic activity. Ref.3 Ref.8 Ref.11
Corresponds to variant rs2904552 [ dbSNP | Ensembl ].
VAR_029570
Natural variant4411L → P in HP-1; associated with susceptibility to SCZD4; strongly reduced enzymatic activity. Ref.3 Ref.8 Ref.9
Corresponds to variant rs2904551 [ dbSNP | Ensembl ].
VAR_029571
Natural variant4441G → D. Ref.11
VAR_029875
Natural variant4531R → C Associated with susceptibility to SCZD4; can be associated with HP-1 in a subset of schizophrenia patients; strongly reduced enzymatic activity. Ref.3 Ref.8 Ref.9
Corresponds to variant rs3970559 [ dbSNP | Ensembl ].
VAR_029572
Natural variant4551A → S Can be associated with HP-1 in a subset of schizophrenia patients; no effect on enzymatic activity. Ref.3 Ref.8
Corresponds to variant rs1807467 [ dbSNP | Ensembl ].
VAR_029573
Natural variant4661T → M Associated with susceptibility to SCZD4; strongly reduced affinity for FAD and enzymatic activity. Ref.3 Ref.9
Corresponds to variant rs2870984 [ dbSNP | Ensembl ].
VAR_029574
Natural variant4721A → T Associated with susceptibility to SCZD4; no effect on enzymatic activity. Ref.3 Ref.8 Ref.9
Corresponds to variant rs2870983 [ dbSNP | Ensembl ].
VAR_029575
Natural variant4881N → S in a breast cancer sample; somatic mutation. Ref.10
VAR_036566
Natural variant5211Q → E Strongly reduced enzymatic activity. Ref.3
VAR_029576
Natural variant5211Q → R Associated with susceptibility to SCZD4; can be associated with HP-1 in a subset of schizophrenia patients; enhanced enzymatic activity. Ref.3 Ref.5 Ref.8 Ref.9
Corresponds to variant rs450046 [ dbSNP | Ensembl ].
VAR_029577

Experimental info

Sequence conflict1441Y → F in AAH94736. Ref.5
Sequence conflict1641T → S in AAB88789. Ref.1
Sequence conflict3431P → H in AAH68260. Ref.5
Sequence conflict3471R → G in AAF21464. Ref.3
Sequence conflict455 – 4562AE → Q in AAC39529. Ref.7
Sequence conflict5711L → F in BAD92709. Ref.6
Sequence conflict5881R → K in AAC39529. Ref.7
Sequence conflict5961F → L in AAH68260. Ref.5

Sequences

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

Last modified April 5, 2011. Version 3.
Checksum: 249E98A0A5BB8027

FASTA60068,002
        10         20         30         40         50         60 
MALRRALPAL RPCIPRFVQL STAPASREQP AAGPAAVPGG GSATAVRPPV PAVDFGNAQE 

        70         80         90        100        110        120 
AYRSRRTWEL ARSLLVLRLC AWPALLARHE QLLYVSRKLL GQRLFNKLMK MTFYGHFVAG 

       130        140        150        160        170        180 
EDQESIQPLL RHYRAFGVSA ILDYGVEEDL SPEEAEHKEM ESCTSAAERD GSGTNKRDKQ 

       190        200        210        220        230        240 
YQAHRAFGDR RNGVISARTY FYANEAKCDS HMETFLRCIE ASGRVSDDGF IAIKLTALGR 

       250        260        270        280        290        300 
PQFLLQFSEV LAKWRCFFHQ MAVEQGQAGL AAMDTKLEVA VLQESVAKLG IASRAEIEDW 

       310        320        330        340        350        360 
FTAETLGVSG TMDLLDWSSL IDSRTKLSKH LVVPNAQTGQ LEPLLSRFTE EEELQMTRML 

       370        380        390        400        410        420 
QRMDVLAKKA TEMGVRLMVD AEQTYFQPAI SRLTLEMQRK FNVEKPLIFN TYQCYLKDAY 

       430        440        450        460        470        480 
DNVTLDVELA RREGWCFGAK LVRGAYLAQE RARAAEIGYE DPINPTYEAT NAMYHRCLDY 

       490        500        510        520        530        540 
VLEELKHNAK AKVMVASHNE DTVRFALRRM EELGLHPADH QVYFGQLLGM CDQISFPLGQ 

       550        560        570        580        590        600 
AGYPVYKYVP YGPVMEVLPY LSRRALENSS LMKGTHRERQ LLWLELLRRL RTGNLFHRPA 

« Hide

Isoform 2 [UniParc].

Checksum: BE51A3277E264431
Show »

FASTA49256,197
Isoform 3 [UniParc].

Checksum: E5E72B3C595B4596
Show »

FASTA51659,231

References

« Hide 'large scale' references
[1]"A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia."
Campbell H.D., Webb G.C., Young I.G.
Hum. Genet. 101:69-74(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Brain.
[2]"The gene encoding proline dehydrogenase modulates sensorimotor gating in mice."
Gogos J.A., Santha M., Takacs Z., Beck K.D., Luine V., Lucas L.R., Nadler J.V., Karayiorgou M.
Nat. Genet. 21:434-439(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Cerebellum and Kidney.
[3]"Functional consequences of PRODH missense mutations."
Bender H.-U., Almashanu S., Steel G., Hu C.-A., Lin W.-W., Willis A., Pulver A., Valle D.
Am. J. Hum. Genet. 76:409-420(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, COFACTOR, VARIANTS VAL-167 AND ARG-521, CHARACTERIZATION OF VARIANTS VAL-167; TRP-185; GLN-185; MET-289; LEU-406; ASN-426; MET-427; HIS-431; PRO-441; CYS-453; SER-455; MET-466; THR-472; ARG-521 AND GLU-521.
Tissue: Kidney.
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2), VARIANT ARG-521.
Tissue: Brain.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-600 (ISOFORMS 1/2/3).
Tissue: Brain.
[7]"A model for p53-induced apoptosis."
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.
Nature 389:300-306(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 444-600, INDUCTION BY TP53.
[8]"PRODH mutations and hyperprolinemia in a subset of schizophrenic patients."
Jacquet H., Raux G., Thibaut F., Hecketsweiler B., Houy E., Demilly C., Haouzir S., Allio G., Fouldrin G., Drouin V., Bou J., Petit M., Campion D., Frebourg T.
Hum. Mol. Genet. 11:2243-2249(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-289; HIS-431; PRO-441; CYS-453; SER-455; THR-472 AND ARG-521, INVOLVEMENT IN HP-1.
[9]"Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual pattern and increases susceptibility to schizophrenia."
Liu H., Heath S.C., Sobin C., Roos J.L., Galke B.L., Blundell M.L., Lenane M., Robertson B., Wijsman E.M., Rapoport J.L., Gogos J.A., Karayiorgou M.
Proc. Natl. Acad. Sci. U.S.A. 99:3717-3722(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-406; MET-427; PRO-441; CYS-453; MET-466; THR-472 AND ARG-521, INVOLVEMENT IN SCZD4.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-488.
[11]"Involvement of hyperprolinemia in cognitive and psychiatric features of the 22q11 deletion syndrome."
Raux G., Bumsel E., Hecketsweiler B., van Amelsvoort T., Zinkstok J., Manouvrier-Hanu S., Fantini C., Breviere G.-M.M., Di Rosa G., Pustorino G., Vogels A., Swillen A., Legallic S., Bou J., Opolczynski G., Drouin-Garraud V., Lemarchand M., Philip N. expand/collapse author list , Gerard-Desplanches A., Carlier M., Philippe A., Nolen M.C., Heron D., Sarda P., Lacombe D., Coizet C., Alembik Y., Layet V., Afenjar A., Hannequin D., Demily C., Petit M., Thibaut F., Frebourg T., Campion D.
Hum. Mol. Genet. 16:83-91(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-275; HIS-431 AND ASP-444.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82381 mRNA. Translation: AAB88789.1.
AF120278 mRNA. Translation: AAD24775.1.
U79754 mRNA. Translation: AAF21464.1.
AC007326 Genomic DNA. No translation available.
BC068260 mRNA. Translation: AAH68260.1. Frameshift.
BC094736 mRNA. Translation: AAH94736.1. Sequence problems.
BC118597 mRNA. Translation: AAI18598.1.
BC121809 mRNA. Translation: AAI21810.1.
AB209472 mRNA. Translation: BAD92709.1. Sequence problems.
AF010310 mRNA. Translation: AAC39529.1. Frameshift.
CCDSCCDS13754.1. [O43272-4]
CCDS56223.1. [O43272-2]
RefSeqNP_001182155.1. NM_001195226.1. [O43272-2]
NP_057419.4. NM_016335.4.
UniGeneHs.517352.

3D structure databases

ProteinModelPortalO43272.
SMRO43272. Positions 350-570.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00172. L-Proline.

PTM databases

PhosphoSiteO43272.

Proteomic databases

MaxQBO43272.
PaxDbO43272.
PRIDEO43272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357068; ENSP00000349577; ENSG00000100033.
GeneID5625.
KEGGhsa:5625.
UCSCuc002zok.4. human. [O43272-4]

Organism-specific databases

CTD5625.
GeneCardsGC22M018900.
HGNCHGNC:9453. PRODH.
HPAHPA020361.
MIM181500. phenotype.
239500. phenotype.
600850. phenotype.
606810. gene.
neXtProtNX_O43272.
Orphanet419. Hyperprolinemia type 1.
3140. Schizophrenia.
PharmGKBPA33801.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0506.
HOVERGENHBG008262.
InParanoidO43272.
KOK00318.
OrthoDBEOG7K9K2J.
PhylomeDBO43272.
TreeFamTF313544.

Enzyme and pathway databases

BioCycMetaCyc:HS01958-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00261; UER00373.

Gene expression databases

ArrayExpressO43272.
BgeeO43272.
GenevestigatorO43272.

Family and domain databases

Gene3D3.20.20.220. 3 hits.
InterProIPR029041. FAD-linked_oxidoreductase-like.
IPR002872. Proline_DH.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERPTHR13914. PTHR13914. 1 hit.
PfamPF01619. Pro_dh. 1 hit.
[Graphical view]
SUPFAMSSF51730. SSF51730. 3 hits.
ProtoNetSearch...

Other

ChiTaRSPRODH. human.
GeneWikiProline_oxidase.
GenomeRNAi5625.
NextBio21864.
PROO43272.
SOURCESearch...

Entry information

Entry namePROD_HUMAN
AccessionPrimary (citable) accession number: O43272
Secondary accession number(s): A6NF53 expand/collapse secondary AC list , O14680, Q0P507, Q147W8, Q504W1, Q59FI8, Q6NV86, Q9UF13
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 5, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 22

Human chromosome 22: entries, gene names and cross-references to MIM