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O14874

- BCKD_HUMAN

UniProt

O14874 - BCKD_HUMAN

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Protein
[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
Gene
BCKDK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate.

GO - Molecular functioni

  1. ATP binding Source: HGNC
  2. [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity Source: UniProtKB-EC
  3. kinase activity Source: HGNC
  4. protein binding Source: IntAct
  5. protein serine/threonine kinase activity Source: HGNC

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: HGNC
  2. cellular amino acid catabolic process Source: UniProtKB
  3. phosphorylation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:BCKDK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:16902. BCKDK.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  2. mitochondrion Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD) [MIM:614923]: A metabolic disorder characterized by autism, epilepsy, intellectual disability, and reduced branched-chain amino acids.
Note: The disease is caused by mutations affecting the gene represented in this entry. A diet enriched in branched amino acids (BCAAs) allows to normalize plasma BCAA levels. This suggests that it may be possible to treat patients with mutations in BCKDK with BCAA supplementation.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241R → P in BCKDKD. 1 Publication
VAR_069037

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614923. phenotype.
Orphaneti308410. Autism-epilepsy syndrome due to branched chain ketoacid dehydrogenase kinase deficiency.
PharmGKBiPA134899581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion By similarity
Add
BLAST
Chaini31 – 412382[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
PRO_0000023452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by autocatalysis By similarity
Modified residuei192 – 1921N6-acetyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication

Post-translational modificationi

Autophosphorylated By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14874.
PaxDbiO14874.
PRIDEiO14874.

PTM databases

PhosphoSiteiO14874.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiO14874.
BgeeiO14874.
CleanExiHS_BCKDK.
GenevestigatoriO14874.

Organism-specific databases

HPAiHPA017995.
HPA056067.

Interactioni

Subunit structurei

Monomer By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX22EBI-1046765,EBI-6863741From a different organism.
STAT3P407632EBI-1046765,EBI-518675

Protein-protein interaction databases

BioGridi115583. 15 interactions.
IntActiO14874. 5 interactions.
MINTiMINT-2998419.
STRINGi9606.ENSP00000219794.

Structurei

3D structure databases

ProteinModelPortaliO14874.
SMRiO14874. Positions 68-408.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 404246Histidine kinase
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000164315.
HOVERGENiHBG004829.
InParanoidiO14874.
KOiK00905.
OMAiTIANNDV.
OrthoDBiEOG7TQV0S.
PhylomeDBiO14874.
TreeFamiTF331303.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14874-1) [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

MILASVLRSG PGGGLPLRPL LGPALALRAR STSATDTHHV EMARERSKTV    50
TSFYNQSAID AAAEKPSVRL TPTMMLYAGR SQDGSHLLKS ARYLQQELPV 100
RIAHRIKGFR CLPFIIGCNP TILHVHELYI RAFQKLTDFP PIKDQADEAQ 150
YCQLVRQLLD DHKDVVTLLA EGLRESRKHI EDEKLVRYFL DKTLTSRLGI 200
RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR LCEHKYGNAP 250
RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI 300
TIANNDVDLI IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRISPLFG 350
HLDMHSGAQS GPMHGFGFGL PTSRAYAEYL GGSLQLQSLQ GIGTDVYLRL 400
RHIDGREESF RI 412
Length:412
Mass (Da):46,360
Last modified:June 6, 2002 - v2
Checksum:iAC97CF5D151FEFB4
GO
Isoform 2 (identifier: O14874-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     282-311: Missing.
     366-412: Missing.

Note: No experimental confirmation available.

Show »
Length:335
Mass (Da):37,768
Checksum:iB66E1F96C0718C57
GO
Isoform 3 (identifier: O14874-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     366-412: Missing.

Note: No experimental confirmation available.

Show »
Length:365
Mass (Da):41,090
Checksum:i8702A3E7E94341DC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241R → P in BCKDKD. 1 Publication
VAR_069037

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei282 – 31130Missing in isoform 2.
VSP_054604Add
BLAST
Alternative sequencei366 – 41247Missing in isoform 2 and isoform 3.
VSP_054605Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31L → P in AK130145. 1 Publication
Sequence conflicti114 – 1141F → S in AK130145. 1 Publication
Sequence conflicti218 – 2181V → F in AAB82714. 1 Publication
Sequence conflicti227 – 2271P → S in AK130145. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026548 mRNA. Translation: AAB82714.1.
AK130145 mRNA. No translation available.
CR542093 mRNA. Translation: CAG46890.1.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52160.1.
CH471192 Genomic DNA. Translation: EAW52161.1.
CH471192 Genomic DNA. Translation: EAW52163.1.
BC007363 mRNA. Translation: AAH07363.1.
BC009872 mRNA. Translation: AAH09872.1.
CCDSiCCDS10705.1. [O14874-1]
CCDS45467.1. [O14874-3]
CCDS61917.1. [O14874-2]
RefSeqiNP_001116429.1. NM_001122957.2. [O14874-3]
NP_001258855.1. NM_001271926.1. [O14874-2]
NP_005872.2. NM_005881.3. [O14874-1]
UniGeneiHs.513520.

Genome annotation databases

EnsembliENST00000219794; ENSP00000219794; ENSG00000103507.
ENST00000287507; ENSP00000287507; ENSG00000103507.
ENST00000394950; ENSP00000378404; ENSG00000103507.
ENST00000394951; ENSP00000378405; ENSG00000103507.
GeneIDi10295.
KEGGihsa:10295.
UCSCiuc002eav.5. human. [O14874-1]
uc010cai.4. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

The silence within - Issue 147 of March 2013

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026548 mRNA. Translation: AAB82714.1 .
AK130145 mRNA. No translation available.
CR542093 mRNA. Translation: CAG46890.1 .
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52160.1 .
CH471192 Genomic DNA. Translation: EAW52161.1 .
CH471192 Genomic DNA. Translation: EAW52163.1 .
BC007363 mRNA. Translation: AAH07363.1 .
BC009872 mRNA. Translation: AAH09872.1 .
CCDSi CCDS10705.1. [O14874-1 ]
CCDS45467.1. [O14874-3 ]
CCDS61917.1. [O14874-2 ]
RefSeqi NP_001116429.1. NM_001122957.2. [O14874-3 ]
NP_001258855.1. NM_001271926.1. [O14874-2 ]
NP_005872.2. NM_005881.3. [O14874-1 ]
UniGenei Hs.513520.

3D structure databases

ProteinModelPortali O14874.
SMRi O14874. Positions 68-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115583. 15 interactions.
IntActi O14874. 5 interactions.
MINTi MINT-2998419.
STRINGi 9606.ENSP00000219794.

PTM databases

PhosphoSitei O14874.

Proteomic databases

MaxQBi O14874.
PaxDbi O14874.
PRIDEi O14874.

Protocols and materials databases

DNASUi 10295.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219794 ; ENSP00000219794 ; ENSG00000103507 .
ENST00000287507 ; ENSP00000287507 ; ENSG00000103507 .
ENST00000394950 ; ENSP00000378404 ; ENSG00000103507 .
ENST00000394951 ; ENSP00000378405 ; ENSG00000103507 .
GeneIDi 10295.
KEGGi hsa:10295.
UCSCi uc002eav.5. human. [O14874-1 ]
uc010cai.4. human.

Organism-specific databases

CTDi 10295.
GeneCardsi GC16P031117.
HGNCi HGNC:16902. BCKDK.
HPAi HPA017995.
HPA056067.
MIMi 614901. gene.
614923. phenotype.
neXtProti NX_O14874.
Orphaneti 308410. Autism-epilepsy syndrome due to branched chain ketoacid dehydrogenase kinase deficiency.
PharmGKBi PA134899581.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0642.
HOGENOMi HOG000164315.
HOVERGENi HBG004829.
InParanoidi O14874.
KOi K00905.
OMAi TIANNDV.
OrthoDBi EOG7TQV0S.
PhylomeDBi O14874.
TreeFami TF331303.

Miscellaneous databases

GeneWikii BCKDK.
GenomeRNAii 10295.
NextBioi 39014.
PROi O14874.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14874.
Bgeei O14874.
CleanExi HS_BCKDK.
Genevestigatori O14874.

Family and domain databases

Gene3Di 1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProi IPR018955. BCDHK/PDK_N.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view ]
Pfami PF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view ]
PRINTSi PR00344. BCTRLSENSOR.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEi PS50109. HIS_KIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Chuang J.C., Cox R.P., Chuang D.T.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORM 3).
  3. "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] (ISOFORM 1).
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung and Placenta.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-192 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANT BCKDKD PRO-224.

Entry informationi

Entry nameiBCKD_HUMAN
AccessioniPrimary (citable) accession number: O14874
Secondary accession number(s): A8MY43
, Q6FGL4, Q96G95, Q96IN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 6, 2002
Last modified: September 3, 2014
This is version 136 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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