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P26440

- IVD_HUMAN

UniProt

P26440 - IVD_HUMAN

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Protein

Isovaleryl-CoA dehydrogenase, mitochondrial

Gene

IVD

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

Functioni

Catalytic activityi

Isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FAD1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711Substrate; via carbonyl oxygen
Binding sitei274 – 2741Substrate
Active sitei283 – 2831Proton acceptor1 Publication
Binding sitei309 – 3091FAD1 Publication
Binding sitei320 – 3201FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 17110FAD1 Publication
Nucleotide bindingi195 – 1973FAD1 Publication
Nucleotide bindingi377 – 3815FAD1 Publication
Nucleotide bindingi406 – 4083FAD1 Publication

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. isovaleryl-CoA dehydrogenase activity Source: BHF-UCL

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. leucine catabolic process Source: BHF-UCL
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKP26440.
UniPathwayiUPA00363; UER00860.

Names & Taxonomyi

Protein namesi
Recommended name:
Isovaleryl-CoA dehydrogenase, mitochondrial (EC:1.3.8.4)
Short name:
IVD
Gene namesi
Name:IVD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6186. IVD.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Isovaleric acidemia (IVA) [MIM:243500]: A metabolic disorder characterized by retarded psychomotor development, a peculiar odor resembling sweaty feet, an aversion to dietary protein, and pernicious vomiting, leading to acidosis and coma. The acute neonatal form leads to massive metabolic acidosis from the first days of life and rapid death.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421L → P in IVA. 1 Publication
VAR_000423
Natural varianti50 – 501R → P in IVA. 1 Publication
VAR_015960
Natural varianti69 – 691D → N in IVA. 1 Publication
VAR_015961
Natural varianti94 – 941A → G in IVA. 1 Publication
VAR_070061
Natural varianti120 – 1201G → R in IVA. 2 Publications
Corresponds to variant rs142761835 [ dbSNP | Ensembl ].
VAR_070062
Natural varianti196 – 1961I → M in IVA. 1 Publication
VAR_070063
Natural varianti199 – 1991G → V in IVA. 1 Publication
VAR_000424
Natural varianti276 – 2761L → P in IVA. 1 Publication
VAR_070064
Natural varianti311 – 3111A → V in IVA. 1 Publication
Corresponds to variant rs28940889 [ dbSNP | Ensembl ].
VAR_015962
Natural varianti357 – 3571C → R in IVA. 1 Publication
VAR_015963
Natural varianti371 – 3711V → A in IVA. 1 Publication
VAR_015964
Natural varianti392 – 3921R → C in IVA. 1 Publication
VAR_015965
Natural varianti400 – 4001Y → C in IVA. 1 Publication
VAR_070065
Natural varianti411 – 4111R → L in IVA. 1 Publication
VAR_015966

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi283 – 2831E → D: Residual activity. 1 Publication
Mutagenesisi283 – 2831E → G or Q: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi243500. phenotype.
Orphaneti33. Isovaleric acidemia.
PharmGKBiPA29984.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion2 PublicationsAdd
BLAST
Chaini30 – 423394Isovaleryl-CoA dehydrogenase, mitochondrialPRO_0000000531Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
Modified residuei238 – 2381N6-acetyllysineBy similarity
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei315 – 3151N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP26440.
PaxDbiP26440.
PRIDEiP26440.

2D gel databases

REPRODUCTION-2DPAGEIPI00645805.
UCD-2DPAGEP26440.

PTM databases

PhosphoSiteiP26440.

Expressioni

Gene expression databases

BgeeiP26440.
CleanExiHS_IVD.
ExpressionAtlasiP26440. baseline and differential.
GenevestigatoriP26440.

Organism-specific databases

HPAiHPA041391.
HPA044250.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi109916. 7 interactions.
IntActiP26440. 1 interaction.
STRINGi9606.ENSP00000249760.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 403Combined sources
Helixi44 – 6017Combined sources
Turni61 – 644Combined sources
Helixi65 – 717Combined sources
Helixi77 – 8711Combined sources
Turni90 – 934Combined sources
Helixi96 – 983Combined sources
Helixi105 – 11814Combined sources
Helixi120 – 13011Combined sources
Turni131 – 1333Combined sources
Helixi134 – 1407Combined sources
Helixi143 – 15412Combined sources
Beta strandi160 – 1634Combined sources
Beta strandi169 – 1724Combined sources
Helixi173 – 1753Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi184 – 19714Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2119Combined sources
Helixi218 – 2214Combined sources
Beta strandi222 – 2287Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi250 – 26112Combined sources
Helixi262 – 2643Combined sources
Beta strandi265 – 2673Combined sources
Helixi272 – 28716Combined sources
Helixi289 – 30618Combined sources
Helixi316 – 3183Combined sources
Helixi320 – 34829Combined sources
Helixi354 – 37926Combined sources
Helixi380 – 3845Combined sources
Helixi390 – 39910Combined sources
Turni400 – 4045Combined sources
Helixi407 – 41913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVHX-ray2.60A/B/C/D30-423[»]
ProteinModelPortaliP26440.
SMRiP26440. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26440.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2202Substrate binding
Regioni281 – 2844Substrate binding
Regioni404 – 4052Substrate binding

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP26440.
KOiK00253.
OMAiFPNQLWP.
OrthoDBiEOG74FF0S.
PhylomeDBiP26440.
TreeFamiTF105050.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26440-1) [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
MATATRLLGW RVASWRLRPP LAGFVSQRAH SLLPVDDAIN GLSEEQRQLR
60 70 80 90 100
QTMAKFLQEH LAPKAQEIDR SNEFKNLREF WKQLGNLGVL GITAPVQYGG
110 120 130 140 150
SGLGYLEHVL VMEEISRASG AVGLSYGAHS NLCINQLVRN GNEAQKEKYL
160 170 180 190 200
PKLISGEYIG ALAMSEPNAG SDVVSMKLKA EKKGNHYILN GNKFWITNGP
210 220 230 240 250
DADVLIVYAK TDLAAVPASR GITAFIVEKG MPGFSTSKKL DKLGMRGSNT
260 270 280 290 300
CELIFEDCKI PAANILGHEN KGVYVLMSGL DLERLVLAGG PLGLMQAVLD
310 320 330 340 350
HTIPYLHVRE AFGQKIGHFQ LMQGKMADMY TRLMACRQYV YNVAKACDEG
360 370 380 390 400
HCTAKDCAGV ILYSAECATQ VALDGIQCFG GNGYINDFPM GRFLRDAKLY
410 420
EIGAGTSEVR RLVIGRAFNA DFH
Length:423
Mass (Da):46,319
Last modified:August 1, 1992 - v1
Checksum:i121AF14C7F1FA13D
GO
Isoform 2 (identifier: P26440-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-78: Missing.

Note: No experimental confirmation available.

Show »
Length:393
Mass (Da):42,724
Checksum:i6C75C436286F2617
GO

Sequence cautioni

The sequence BAG53799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW92413.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW92414.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW92415.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101W → C in AAP35809. 1 PublicationCurated
Sequence conflicti10 – 101W → C in AAH17202. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421L → P in IVA. 1 Publication
VAR_000423
Natural varianti50 – 501R → P in IVA. 1 Publication
VAR_015960
Natural varianti69 – 691D → N in IVA. 1 Publication
VAR_015961
Natural varianti94 – 941A → G in IVA. 1 Publication
VAR_070061
Natural varianti120 – 1201G → R in IVA. 2 Publications
Corresponds to variant rs142761835 [ dbSNP | Ensembl ].
VAR_070062
Natural varianti196 – 1961I → M in IVA. 1 Publication
VAR_070063
Natural varianti199 – 1991G → V in IVA. 1 Publication
VAR_000424
Natural varianti276 – 2761L → P in IVA. 1 Publication
VAR_070064
Natural varianti311 – 3111A → V in IVA. 1 Publication
Corresponds to variant rs28940889 [ dbSNP | Ensembl ].
VAR_015962
Natural varianti357 – 3571C → R in IVA. 1 Publication
VAR_015963
Natural varianti371 – 3711V → A in IVA. 1 Publication
VAR_015964
Natural varianti392 – 3921R → C in IVA. 1 Publication
VAR_015965
Natural varianti400 – 4001Y → C in IVA. 1 Publication
VAR_070065
Natural varianti411 – 4111R → L in IVA. 1 Publication
VAR_015966

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 7830Missing in isoform 2. 1 PublicationVSP_045193Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34192 mRNA. Translation: AAA52711.1.
AF191218
, AF191214, AF191215, AF191216, AF191217 Genomic DNA. Translation: AAF20182.1.
BT007145 mRNA. Translation: AAP35809.1.
AK122922 mRNA. Translation: BAG53799.1. Different initiation.
AK315296 mRNA. Translation: BAG37702.1.
AC013356 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92413.1. Sequence problems.
CH471125 Genomic DNA. Translation: EAW92414.1. Sequence problems.
CH471125 Genomic DNA. Translation: EAW92415.1. Sequence problems.
BC017202 mRNA. Translation: AAH17202.1.
AF038318 Genomic DNA. Translation: AAB92584.1.
PIRiA37033.
RefSeqiNP_001152980.1. NM_001159508.1.
NP_002216.2. NM_002225.3.
UniGeneiHs.513646.

Genome annotation databases

EnsembliENST00000479013; ENSP00000417990; ENSG00000128928.
GeneIDi3712.
KEGGihsa:3712.
UCSCiuc001zlq.2. human.
uc001zls.3. human.

Polymorphism databases

DMDMi125051.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34192 mRNA. Translation: AAA52711.1 .
AF191218
, AF191214 , AF191215 , AF191216 , AF191217 Genomic DNA. Translation: AAF20182.1 .
BT007145 mRNA. Translation: AAP35809.1 .
AK122922 mRNA. Translation: BAG53799.1 . Different initiation.
AK315296 mRNA. Translation: BAG37702.1 .
AC013356 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92413.1 . Sequence problems.
CH471125 Genomic DNA. Translation: EAW92414.1 . Sequence problems.
CH471125 Genomic DNA. Translation: EAW92415.1 . Sequence problems.
BC017202 mRNA. Translation: AAH17202.1 .
AF038318 Genomic DNA. Translation: AAB92584.1 .
PIRi A37033.
RefSeqi NP_001152980.1. NM_001159508.1.
NP_002216.2. NM_002225.3.
UniGenei Hs.513646.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IVH X-ray 2.60 A/B/C/D 30-423 [» ]
ProteinModelPortali P26440.
SMRi P26440. Positions 35-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109916. 7 interactions.
IntActi P26440. 1 interaction.
STRINGi 9606.ENSP00000249760.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSitei P26440.

Polymorphism databases

DMDMi 125051.

2D gel databases

REPRODUCTION-2DPAGE IPI00645805.
UCD-2DPAGE P26440.

Proteomic databases

MaxQBi P26440.
PaxDbi P26440.
PRIDEi P26440.

Protocols and materials databases

DNASUi 3712.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000479013 ; ENSP00000417990 ; ENSG00000128928 .
GeneIDi 3712.
KEGGi hsa:3712.
UCSCi uc001zlq.2. human.
uc001zls.3. human.

Organism-specific databases

CTDi 3712.
GeneCardsi GC15P040697.
HGNCi HGNC:6186. IVD.
HPAi HPA041391.
HPA044250.
MIMi 243500. phenotype.
607036. gene.
neXtProti NX_P26440.
Orphaneti 33. Isovaleric acidemia.
PharmGKBi PA29984.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00760000119007.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi P26440.
KOi K00253.
OMAi FPNQLWP.
OrthoDBi EOG74FF0S.
PhylomeDBi P26440.
TreeFami TF105050.

Enzyme and pathway databases

UniPathwayi UPA00363 ; UER00860 .
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK P26440.

Miscellaneous databases

ChiTaRSi IVD. human.
EvolutionaryTracei P26440.
GenomeRNAii 3712.
NextBioi 14547.
PROi P26440.
SOURCEi Search...

Gene expression databases

Bgeei P26440.
CleanExi HS_IVD.
ExpressionAtlasi P26440. baseline and differential.
Genevestigatori P26440.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts."
    Matsubara Y., Ito M., Glassberg R., Satyabhama S., Ikeda Y., Tanaka K.
    J. Clin. Invest. 85:1058-1064(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Exon skipping in IVD RNA processing in isovaleric acidemia caused by point mutations in the coding region of the IVD gene."
    Vockley J., Rogan P.K., Anderson B.D., Willard J., Seelan R.S., Smith D.I., Liu W.
    Am. J. Hum. Genet. 66:356-367(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Pericardium and Testis.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(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: Brain.
  8. "Structural organization of the human isovaleryl-CoA dehydrogenase gene."
    Parimoo B., Tanaka K.
    Genomics 15:582-590(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-423.
  9. "The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors."
    Vockley J., Nagao M., Parimoo B., Tanaka K.
    J. Biol. Chem. 267:2494-2501(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
  10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-47.
    Tissue: Platelet.
  11. "Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase."
    Mohsen A.W., Vockley J.
    Biochemistry 34:10146-10152(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, MUTAGENESIS OF GLU-283.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure of human isovaleryl-CoA dehydrogenase at 2.6-A resolution: structural basis for substrate specificity."
    Tiffany K.A., Roberts D.L., Wang M., Paschke R., Mohsen A.W., Vockley J., Kim J.-J.P.
    Biochemistry 36:8455-8464(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 30-423 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, COFACTOR.
  15. "Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia."
    Vockley J., Parimoo B., Tanaka K.
    Am. J. Hum. Genet. 49:147-157(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IVA PRO-42 AND VAL-199.
  16. "Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia."
    Mohsen A.-W.A., Anderson B.D., Volchenboum S.L., Battaile K.P., Tiffany K.A., Roberts D.L., Kim J.-J.P., Vockley J.
    Biochemistry 37:10325-10335(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IVA PRO-50; ASN-69; VAL-311; ARG-357; ALA-371; CYS-392 AND LEU-411.
  17. "Phenotypic and mutation spectrums of Thai patients with isovaleric acidemia."
    Vatanavicharn N., Liammongkolkul S., Sakamoto O., Sathienkijkanchai A., Wasant P.
    Pediatr. Int. 53:990-994(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IVA GLY-94; ARG-120; PRO-276 AND CYS-400.
  18. "Clinical variability of isovaleric acidemia in a genetically homogeneous population."
    Dercksen M., Duran M., Ijlst L., Mienie L.J., Reinecke C.J., Ruiter J.P., Waterham H.R., Wanders R.J.
    J. Inherit. Metab. Dis. 35:1021-1029(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT IVA ARG-120.
  19. "Two novel isovaleryl-CoA dehydrogenase gene mutations in a Chinese infant."
    Bei F., Sun J.H., Yu Y.G., Jia J., Zheng Z.J., Fu Q.H., Cai W.
    Gene 524:396-400(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT IVA MET-196.

Entry informationi

Entry nameiIVD_HUMAN
AccessioniPrimary (citable) accession number: P26440
Secondary accession number(s): B2RCV5
, B3KVI7, J3KR54, Q53XZ9, Q96AF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 163 of the entry and version 1 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 15
    Human chromosome 15: 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