Reviewed, UniProtKB/Swiss-Prot O43272 (PROD_HUMAN)

Names and origin

Protein names

Recommended name:
    Proline dehydrogenase, mitochondrial
    EC=1.5.99.8
Alternative name(s):
    Proline oxidase
    Proline oxidase 2
    p53-induced gene 6 protein

Gene names

Name:	PRODH
Synonyms:	PIG6, POX2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts proline to delta-1-pyrroline-5-carboxylate.
Catalytic activity	L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor. 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 TP53-induced apoptosis. Ref.7
Involvement in disease	Defects in PRODH are the cause of hyperprolinemia type 1 [MIM:239500]. It is a disorder characterized by elevated serum proline levels. May be involved in the psychiatric and behavioral phenotypes associated with the 22q11 velocardiofacial and DiGeorge syndrome. Ref.8 Defects in PRODH may be associated with susceptibility to schizophrenia 4 (SCZD4) [MIM:600850]. Schizophrenia [MIM:181500] is a psychosis, a disorder of thought and sense of self. 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. No objective biological test for schizophrenia exists. Schizophrenia is a common disorder with a lifetime prevalence of approximately 1%. It is highly heritable but the genetics are complex. A subset of schizophrenia patients present hyperprolinemia type 1. Ref.9
Sequence similarities	Belongs to the proline oxidase family.

Ontologies

Keywords
Biological process	Proline metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from electronic annotation. Source: InterPro induction of apoptosis by oxidative stress Ref.7 Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	proline dehydrogenase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43272-1) 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: O43272-2) The sequence of this isoform differs from the canonical sequence as follows:      1-24: Missing.
Isoform 3 (identifier: O43272-3) The sequence of this isoform differs from the canonical sequence as follows:      1-75: Missing.
Isoform 4 (identifier: O43272-4) The sequence of this isoform differs from the canonical sequence as follows:      1-11: MLEFVMREWKK → MALRRALPAL...LARHEQLLYV
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Natural variant	8	1	P → L
	Natural variant	19	1	Q → P Moderate reduction of enzymatic activity. dbSNP rs2008720.
	Natural variant	30	1	P → S
	Natural variant	58	1	A → T
Isoform 5 (identifier: O43272-5) The sequence of this isoform differs from the canonical sequence as follows:      1-271: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 516		Proline dehydrogenase, mitochondrial		PRO_0000025800
Natural variations
	Alternative sequence	1 – 271	271	Missing in isoform 5.		VSP_021846
	Alternative sequence	1 – 75	75	Missing in isoform 3.		VSP_021847
	Alternative sequence	1 – 24	24	Missing in isoform 2.		VSP_021848
	Alternative sequence	1 – 11	11	MLEFVMREWKK → MALRRALPALRPCIPRFVQL STAPASREQPAAGPAAVPGG GSATAVRPPVPAVDFGNAQE AYRSRRTWELARSLLVLRLC AWPALLARHEQLLYV in isoform 4.		VSP_021849
	Natural variant	83	1	A → V Associated with susceptibility to SCZD4; moderate reduction of enzymatic activity. Ref.3		VAR_029563
	Natural variant	101	1	R → Q No effect on enzymatic activity. Ref.3		VAR_029564
	Natural variant	101	1	R → W Moderate reduction of enzymatic activity. dbSNP rs4819756. Ref.3		VAR_029565
	Natural variant	191	1	T → N Ref.11		VAR_029874
	Natural variant	205	1	L → M Can be associated with hyperprolinemia type 1 in a subset of schizophrenia patients; no effect on enzymatic activity. Ref.3 Ref.8		VAR_029566
	Natural variant	322	1	P → L Associated with susceptibility to SCZD4; strongly reduced enzymatic activity. dbSNP rs3970555. Ref.3 Ref.9		VAR_029567
	Natural variant	342	1	D → N Moderate reduction of enzymatic activity. Ref.3		VAR_029568
	Natural variant	343	1	V → M Associated with susceptibility to SCZD4; moderate reduction of enzymatic activity. dbSNP rs2238731. Ref.3 Ref.9		VAR_029569
	Natural variant	347	1	R → H Associated with hyperprolinemia type 1 in a subset of schizophrenia patients; moderate reduction of enzymatic activity. dbSNP rs2904552. Ref.3 Ref.8 Ref.11		VAR_029570
	Natural variant	357	1	L → P in hyperprolinemia type 1; associated with susceptibility to SCZD4; strongly reduced enzymatic activity. dbSNP rs2904551. Ref.3 Ref.8 Ref.9		VAR_029571
	Natural variant	360	1	G → D Ref.11		VAR_029875
	Natural variant	369	1	R → C Associated with susceptibility to SCZD4; can be associated with hyperprolinemia type 1 in a subset of schizophrenia patients; strongly reduced enzymatic activity. dbSNP rs3970559. Ref.3 Ref.8 Ref.9		VAR_029572
	Natural variant	371	1	A → S Can be associated with hyperprolinemia type 1 in a subset of schizophrenia patients; no effect on enzymatic activity. dbSNP rs1807467. Ref.3 Ref.8		VAR_029573
	Natural variant	382	1	T → M Associated with susceptibility to SCZD4; strongly reduced affinity for FAD and enzymatic activity. dbSNP rs2870984. Ref.3 Ref.9		VAR_029574
	Natural variant	388	1	A → T Associated with susceptibility to SCZD4; no effect on enzymatic activity. dbSNP rs2870983. Ref.3 Ref.8 Ref.9		VAR_029575
	Natural variant	404	1	N → S in a breast cancer sample; somatic mutation. Ref.10		VAR_036566
	Natural variant	437	1	Q → E Strongly reduced enzymatic activity. Ref.3 Ref.8 Ref.9 Ref.6		VAR_029576
	Natural variant	437	1	Q → R Associated with susceptibility to SCZD4; can be associated with hyperprolinemia type 1 in a subset of schizophrenia patients; enhanced enzymatic activity. dbSNP rs450046. Ref.3 Ref.8 Ref.9 Ref.6		VAR_029577
Experimental info
	Sequence conflict	60	1	Y → F in AAH94736. Ref.6
	Sequence conflict	80	1	T → S in AAB88789. Ref.1
	Sequence conflict	259	1	P → H in AAH68260. Ref.6
	Sequence conflict	263	1	R → G in AAF21464. Ref.3
	Sequence conflict	371 – 372	2	AE → Q in AAC39529. Ref.7
	Sequence conflict	487	1	L → F in BAD92709. Ref.4
	Sequence conflict	512	1	F → L in AAH68260. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: E5E72B3C595B4596	FASTA	516	59,231
	10 20 30 40 50 60 MLEFVMREWK KSRKLLGQRL FNKLMKMTFY GHFVAGEDQE SIQPLLRHYR AFGVSAILDY 70 80 90 100 110 120 GVEEDLSPEE AEHKEMESCT SAAERDGSGT NKRDKQYQAH RAFGDRRNGV ISARTYFYAN 130 140 150 160 170 180 EAKCDSHMET FLRCIEASGR VSDDGFIAIK LTALGRPQFL LQFSEVLAKW RCFFHQMAVE 190 200 210 220 230 240 QGQAGLAAMD TKLEVAVLQE SVAKLGIASR AEIEDWFTAE TLGVSGTMDL LDWSSLIDSR 250 260 270 280 290 300 TKLSKHLVVP NAQTGQLEPL LSRFTEEEEL QMTRMLQRMD VLAKKATEMG VRLMVDAEQT 310 320 330 340 350 360 YFQPAISRLT LEMQRKFNVE KPLIFNTYQC YLKDAYDNVT LDVELARREG WCFGAKLVRG 370 380 390 400 410 420 AYLAQERARA AEIGYEDPIN PTYEATNAMY HRCLDYVLEE LKHNAKAKVM VASHNEDTVR 430 440 450 460 470 480 FALRRMEELG LHPADHQVYF GQLLGMCDQI SFPLGQAGYP VYKYVPYGPV MEVLPYLSRR 490 500 510 ALENSSLMKG THRERQLLWL ELLRRLRTGN LFHRPA
	Isoform 2. Checksum: BE51A3277E264431	FASTA	492	56,197
	10 20 30 40 50 60 MKMTFYGHFV AGEDQESIQP LLRHYRAFGV SAILDYGVEE DLSPEEAEHK EMESCTSAAE 70 80 90 100 110 120 RDGSGTNKRD KQYQAHRAFG DRRNGVISAR TYFYANEAKC DSHMETFLRC IEASGRVSDD 130 140 150 160 170 180 GFIAIKLTAL GRPQFLLQFS EVLAKWRCFF HQMAVEQGQA GLAAMDTKLE VAVLQESVAK 190 200 210 220 230 240 LGIASRAEIE DWFTAETLGV SGTMDLLDWS SLIDSRTKLS KHLVVPNAQT GQLEPLLSRF 250 260 270 280 290 300 TEEEELQMTR MLQRMDVLAK KATEMGVRLM VDAEQTYFQP AISRLTLEMQ RKFNVEKPLI 310 320 330 340 350 360 FNTYQCYLKD AYDNVTLDVE LARREGWCFG AKLVRGAYLA QERARAAEIG YEDPINPTYE 370 380 390 400 410 420 ATNAMYHRCL DYVLEELKHN AKAKVMVASH NEDTVRFALR RMEELGLHPA DHQVYFGQLL 430 440 450 460 470 480 GMCDQISFPL GQAGYPVYKY VPYGPVMEVL PYLSRRALEN SSLMKGTHRE RQLLWLELLR 490 RLRTGNLFHR PA
	Isoform 3. Checksum: 8BFF87F57590E0F0	FASTA	441	50,344
	10 20 30 40 50 60 MESCTSAAER DGSGTNKRDK QYQAHRAFGD RRNGVISART YFYANEAKCD SHMETFLRCI 70 80 90 100 110 120 EASGRVSDDG FIAIKLTALG RPQFLLQFSE VLAKWRCFFH QMAVEQGQAG LAAMDTKLEV 130 140 150 160 170 180 AVLQESVAKL GIASRAEIED WFTAETLGVS GTMDLLDWSS LIDSRTKLSK HLVVPNAQTG 190 200 210 220 230 240 QLEPLLSRFT EEEELQMTRM LQRMDVLAKK ATEMGVRLMV DAEQTYFQPA ISRLTLEMQR 250 260 270 280 290 300 KFNVEKPLIF NTYQCYLKDA YDNVTLDVEL ARREGWCFGA KLVRGAYLAQ ERARAAEIGY 310 320 330 340 350 360 EDPINPTYEA TNAMYHRCLD YVLEELKHNA KAKVMVASHN EDTVRFALRR MEELGLHPAD 370 380 390 400 410 420 HQVYFGQLLG MCDQISFPLG QAGYPVYKYV PYGPVMEVLP YLSRRALENS SLMKGTHRER 430 440 QLLWLELLRR LRTGNLFHRP A
	Isoform 4. Checksum: 249E98A0A5BB8027	FASTA	600	68,002
	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
	Isoform 5. Checksum: D25D16C277B0B738	FASTA	245	28,517
	10 20 30 40 50 60 MTRMLQRMDV LAKKATEMGV RLMVDAEQTY FQPAISRLTL EMQRKFNVEK PLIFNTYQCY 70 80 90 100 110 120 LKDAYDNVTL DVELARREGW CFGAKLVRGA YLAQERARAA EIGYEDPINP TYEATNAMYH 130 140 150 160 170 180 RCLDYVLEEL KHNAKAKVMV ASHNEDTVRF ALRRMEELGL HPADHQVYFG QLLGMCDQIS 190 200 210 220 230 240 FPLGQAGYPV YKYVPYGPVM EVLPYLSRRA LENSSLMKGT HRERQLLWLE LLRRLRTGNL FHRPA

References

	« Hide 'large scale' referencesShow '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: 9385373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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: 10192398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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: 15662599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ENZYME ACTIVITY, COFACTOR, VARIANTS VAL-83 AND ARG-437, CHARACTERIZATION OF VARIANTS VAL-83; TRP-101; GLN-101; MET-205; LEU-322; ASN-342; MET-343; HIS-347; PRO-357; CYS-369; SER-371; MET-382; THR-388; ARG-437 AND GLU-437. Tissue: Kidney.
[4]	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] (ISOFORM 5). Tissue: Brain.
[5]	"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. , 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: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT ARG-437. 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: 9305847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 360-455, 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: 12217952] [Abstract] Cited for: VARIANTS MET-205; HIS-347; PRO-357; CYS-369; SER-371; THR-388 AND ARG-437, INVOLVEMENT IN SCHIZOPHRENIA-LINKED HYPERPROLINEMIA TYPE 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: 11891283] [Abstract] Cited for: VARIANTS LEU-322; MET-343; PRO-357; CYS-369; MET-382; THR-388 AND ARG-437, 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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-404.
[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. , 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: 17135275] [Abstract] Cited for: VARIANTS ASN-191; HIS-347 AND ASP-360.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	U82381 mRNA. Translation: AAB88789.1. AF120278 mRNA. Translation: AAD24775.1. U79754 mRNA. Translation: AAF21464.1. AB209472 mRNA. Translation: BAD92709.1. Different initiation. AC007326 Genomic DNA. No translation available. BC068260 mRNA. Translation: AAH68260.1. Different initiation. BC094736 mRNA. Translation: AAH94736.1. Different initiation. BC118597 mRNA. Translation: AAI18598.1. BC121809 mRNA. Translation: AAI21810.1. AF010310 mRNA. Translation: AAC39529.1. Different termination.
IPI	IPI00383798. IPI00432511. IPI00747489. IPI00816398. IPI00816668.
RefSeq	NP_057419.3.
UniGene	Hs.517352
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	O43272.
Genome annotation databases
Ensembl	ENSG00000100033. Homo sapiens. [Contig view]
GeneID	5625.
KEGG	hsa:5625.
Organism-specific databases
GeneCards	GC22M017274.
HGNC	HGNC:9453. PRODH.
MIM	181500. phenotype. 239500. phenotype. 600850. phenotype. 606810. gene.
Orphanet	419. Hyperprolinaemia type I. 3140. Schizophrenia.
PharmGKB	PA33801.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O43272.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11427.
BRENDA	1.5.99.8. 247.
Reactome	REACT_13. Metabolism of amino acids.
Gene expression databases
ArrayExpress	O43272.
Bgee	O43272.
GermOnline	ENSG00000100033. Homo sapiens.
Family and domain databases
InterPro	IPR002872. Proline_DH. IPR015659. Proline_oxidase. [Graphical view]
PANTHER	PTHR13914. Proline_oxidase. 1 hit.
Pfam	PF01619. Pro_dh. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00172. L-Proline.
NextBio	21864.
SOURCE	Search...

Entry information

Entry name

PROD_HUMAN

Accession

Primary (citable) accession number: O43272
Secondary accession number(s): A6NF53 , O14680, Q0P507, Q147W8, Q504W1, Q59FI8, Q6NV86, Q9UF13

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 12, 2006
Last modified:	June 16, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)