[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial precursor

Contribute

Send feedback

Read comments (?) or add your own

O14874 (BCKD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
EC=2.7.11.4

Alternative name(s):
Branched-chain alpha-ketoacid dehydrogenase kinase
Short name=BCKD-kinase
Short name=BCKDHKIN

Gene names

Name:

BCKDK

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	412 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	Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex By similarity.
Catalytic activity	ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Ubiquitous.
Post-translational modification	Autophosphorylated By similarity. Ref.5 Ref.6
Sequence similarities	Belongs to the PDK/BCKDK protein kinase family. Contains 1 histidine kinase domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from sequence or structural similarity. Source: HGNC peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial alpha-ketoglutarate dehydrogenase complex Inferred from sequence or structural similarity. Source: HGNC
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: HGNC [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: HGNC two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAT3	P40763	2	EBI-1046765,EBI-518675

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion By similarity

Chain

31 – 412

382

[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial

PRO_0000023452

Regions

Domain

159 – 404

246

Histidine kinase

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

184

N6-acetyllysine Ref.7

Modified residue

192

N6-acetyllysine Ref.7

Modified residue

233

N6-acetyllysine Ref.7

Modified residue

245

N6-acetyllysine Ref.7

Experimental info

Sequence conflict

218

V → F in AAB82714. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O14874 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: AC97CF5D151FEFB4
Show »

FASTA

412

46,360

        10         20         30         40         50         60 
MILASVLRSG PGGGLPLRPL LGPALALRAR STSATDTHHV EMARERSKTV TSFYNQSAID 

        70         80         90        100        110        120 
AAAEKPSVRL TPTMMLYAGR SQDGSHLLKS ARYLQQELPV RIAHRIKGFR CLPFIIGCNP 

       130        140        150        160        170        180 
TILHVHELYI RAFQKLTDFP PIKDQADEAQ YCQLVRQLLD DHKDVVTLLA EGLRESRKHI 

       190        200        210        220        230        240 
EDEKLVRYFL DKTLTSRLGI RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR 

       250        260        270        280        290        300 
LCEHKYGNAP RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI 

       310        320        330        340        350        360 
TIANNDVDLI IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRISPLFG HLDMHSGAQS 

       370        380        390        400        410 
GPMHGFGFGL PTSRAYAEYL GGSLQLQSLQ GIGTDVYLRL RHIDGREESF RI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Chuang J.C., Cox R.P., Chuang D.T. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Placenta.
[5]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-184; LYS-192; LYS-233 AND LYS-245, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF026548 mRNA. Translation: AAB82714.1. CR542093 mRNA. Translation: CAG46890.1. CH471192 Genomic DNA. Translation: EAW52161.1. BC007363 mRNA. Translation: AAH07363.1.
IPI	IPI00298612.
RefSeq	NP_001116429.1. NM_001122957.1. NP_005872.2. NM_005881.2.
UniGene	Hs.513520.
3D structure databases
ProteinModelPortal	O14874.
SMR	O14874. Positions 68-408.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14874. 3 interactions.
MINT	MINT-2998419.
STRING	O14874.
PTM databases
PhosphoSite	O14874.
Proteomic databases
PRIDE	O14874.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219794; ENSP00000219794; ENSG00000103507. ENST00000394951; ENSP00000378405; ENSG00000103507.
GeneID	10295.
KEGG	hsa:10295.
UCSC	uc002eaw.2. human.
Organism-specific databases
CTD	10295.
GeneCards	GC16P031117.
H-InvDB	HIX0012980.
HGNC	HGNC:16902. BCKDK.
HPA	HPA017995.
neXtProt	NX_O14874.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15303.
GeneTree	ENSGT00550000074574.
HOGENOM	HBG281443.
HOVERGEN	HBG004829.
InParanoid	O14874.
OMA	NQSAIDV.
OrthoDB	EOG49ZXPB.
PhylomeDB	O14874.
Gene expression databases
ArrayExpress	O14874.
Bgee	O14874.
CleanEx	HS_BCKDK.
Genevestigator	O14874.
GermOnline	ENSG00000103507. Homo sapiens.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR018955. BCDHK/PDK_N. IPR004358. Sig_transdc_His_kin-like_C. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:1.20.140.20. BCDHK/PDK_N. 1 hit.
KO	K00905.
Pfam	PF10436. BCDHK_Adom3. 1 hit. PF02518. HATPase_c. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF69012. BCDHK/PDK_N. 1 hit.
PROSITE	PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39014.

Entry information

Entry name

BCKD_HUMAN

Accession

Primary (citable) accession number: O14874
Secondary accession number(s): Q6FGL4, Q96IN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 6, 2002
Last modified:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents