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Q8N4T8 (CBR4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Carbonyl reductase family member 4

EC=1.-.-.-
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] reductase
EC=1.1.1.-
Quinone reductase CBR4
Gene names
Name:CBR4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria. The homotetramer may act as NADPH-dependent quinone reductase. Has broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro). Ref.6 Ref.7

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Heterotetramer with HSD17B8; contains two molecules of HSD17B8 and CBR4. Ref.6

Subcellular location

Mitochondrion matrix Ref.6 Ref.7.

Tissue specificity

Detected in liver and kidney (at protein level). Ref.6

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for NADPH

KM=1.6 µM for 9,10-phenanthrenequinone

KM=1.9 µM for 1,4-benzoquinone

pH dependence:

Optimum pH is 6-8.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N4T8-1)

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: Q8N4T8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     180-237: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Carbonyl reductase family member 4
PRO_0000319878

Regions

Nucleotide binding7 – 3125NAD or NADP By similarity

Sites

Active site1481Proton acceptor By similarity
Binding site1351Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8
Modified residue401N6-acetyllysine By similarity
Modified residue961N6-acetyllysine By similarity
Modified residue1951N6-acetyllysine By similarity

Natural variations

Alternative sequence180 – 23758Missing in isoform 2.
VSP_031527
Natural variant701L → M. Ref.1 Ref.2 Ref.5 Ref.9
Corresponds to variant rs2877380 [ dbSNP | Ensembl ].
VAR_039049

Sequences

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

Last modified November 24, 2009. Version 3.
Checksum: 376FF5FA0CB9ABF0

FASTA23725,301
        10         20         30         40         50         60 
MDKVCAVFGG SRGIGRAVAQ LMARKGYRLA VIARNLEGAK AAAGDLGGDH LAFSCDVAKE 

        70         80         90        100        110        120 
HDVQNTFEEL EKHLGRVNFL VNAAGINRDG LLVRTKTEDM VSQLHTNLLG SMLTCKAAMR 

       130        140        150        160        170        180 
TMIQQQGGSI VNVGSIVGLK GNSGQSVYSA SKGGLVGFSR ALAKEVARKK IRVNVVAPGF 

       190        200        210        220        230 
VHTDMTKDLK EEHLKKNIPL GRFGETIEVA HAVVFLLESP YITGHVLVVD GGLQLIL 

« Hide

Isoform 2 [UniParc].

Checksum: 6C43EAF3A2AFCEA0
Show »

FASTA17918,837

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 1 AND 2), VARIANT MET-70.
Tissue: Embryo and Placenta.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-70.
Tissue: Melanoma.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1), VARIANT MET-70.
Tissue: Duodenum and Uterus.
[6]"Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase."
Endo S., Matsunaga T., Kitade Y., Ohno S., Tajima K., El-Kabbani O., Hara A.
Biochem. Biophys. Res. Commun. 377:1326-1330(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
[7]"17beta-Hydroxysteroid dehydrogenase type 8 and carbonyl reductase type 4 assemble as a ketoacyl reductase of human mitochondrial FAS."
Chen Z., Kastaniotis A.J., Miinalainen I.J., Rajaram V., Wierenga R.K., Hiltunen J.K.
FASEB J. 23:3682-3691(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSD17B8.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: VARIANT [LARGE SCALE ANALYSIS] MET-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027337 mRNA. Translation: BAB55045.1.
AK291756 mRNA. Translation: BAF84445.1.
AL833393 mRNA. Translation: CAH10582.1.
AC021151 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04797.1.
BC021973 mRNA. Translation: AAH21973.1.
BC033650 mRNA. Translation: AAH33650.1.
RefSeqNP_116172.2. NM_032783.4.
UniGeneHs.659311.

3D structure databases

ProteinModelPortalQ8N4T8.
SMRQ8N4T8. Positions 3-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124314. 3 interactions.
STRING9606.ENSP00000303525.

PTM databases

PhosphoSiteQ8N4T8.

Polymorphism databases

DMDM269849708.

Proteomic databases

PaxDbQ8N4T8.
PRIDEQ8N4T8.

Protocols and materials databases

DNASU84869.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306193; ENSP00000303525; ENSG00000145439. [Q8N4T8-1]
ENST00000504480; ENSP00000427615; ENSG00000145439. [Q8N4T8-2]
GeneID84869.
KEGGhsa:84869.
UCSCuc003iry.3. human. [Q8N4T8-1]

Organism-specific databases

CTD84869.
GeneCardsGC04M169815.
H-InvDBHIX0004629.
HGNCHGNC:25891. CBR4.
HPAHPA037499.
neXtProtNX_Q8N4T8.
PharmGKBPA144596471.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG002145.
InParanoidQ8N4T8.
KOK11539.
OMATEMIDIN.
PhylomeDBQ8N4T8.
TreeFamTF354265.

Enzyme and pathway databases

SABIO-RKQ8N4T8.
UniPathwayUPA00094.

Gene expression databases

ArrayExpressQ8N4T8.
BgeeQ8N4T8.
CleanExHS_CBR4.
GenevestigatorQ8N4T8.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCBR4. human.
GenomeRNAi84869.
NextBio75151.
PROQ8N4T8.

Entry information

Entry nameCBR4_HUMAN
AccessionPrimary (citable) accession number: Q8N4T8
Secondary accession number(s): Q8WTW8, Q96K93
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 93 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

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 4

Human chromosome 4: entries, gene names and cross-references to MIM