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P11182 (ODB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

EC=2.3.1.168
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase complex component E2
Short name=BCKAD-E2
Short name=BCKADE2
Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
Dihydrolipoamide branched chain transacylase
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Gene names
Name:DBT
Synonyms:BCATE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

Catalytic activity

2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry.

Subcellular location

Mitochondrion matrix.

Involvement in disease

Maple syrup urine disease 2 (MSUD2) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence caution

The sequence AAA35589.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA64512.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6161Mitochondrion Potential
Chain62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
PRO_0000020489

Regions

Domain65 – 13874Lipoyl-binding

Sites

Active site4521 Potential
Active site4561 Potential

Amino acid modifications

Modified residue1051N6-lipoyllysine By similarity
Modified residue1331N6-succinyllysine By similarity
Modified residue1961N6-acetyllysine; alternate By similarity
Modified residue1961N6-succinyllysine; alternate By similarity
Modified residue2021N6-acetyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue2501N6-acetyllysine By similarity
Modified residue2611N6-succinyllysine By similarity
Modified residue2891N6-acetyllysine; alternate By similarity
Modified residue2891N6-succinyllysine; alternate By similarity
Modified residue2951N6-acetyllysine Ref.13
Modified residue3041N6-acetyllysine By similarity
Modified residue4351N6-acetyllysine By similarity
Modified residue4401N6-acetyllysine; alternate By similarity
Modified residue4401N6-succinyllysine; alternate By similarity

Natural variations

Natural variant981I → M in MSUD2. Ref.18
VAR_015099
Natural variant2761F → C in MSUD2. Ref.17
VAR_004978
Natural variant3841G → S in MSUD2. Ref.7 Ref.18
Corresponds to variant rs12021720 [ dbSNP | Ensembl ].
VAR_015100

Experimental info

Sequence conflict3211Q → P in AAA64512. Ref.4
Sequence conflict3541L → V in AAA64512. Ref.4

Secondary structure

......................... 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11182 [UniParc].

Last modified July 1, 1993. Version 3.
Checksum: A7CA728C8F33D126

FASTA48253,487
        10         20         30         40         50         60 
MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP HHFLKTTAAL 

        70         80         90        100        110        120 
RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKK 

       130        140        150        160        170        180 
LYYNLDDIAY VGKPLVDIET EALKDSEEDV VETPAVSHDE HTHQEIKGRK TLATPAVRRL 

       190        200        210        220        230        240 
AMENNIKLSE VVGSGKDGRI LKEDILNYLE KQTGAILPPS PKVEIMPPPP KPKDMTVPIL 

       250        260        270        280        290        300 
VSKPPVFTGK DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EIDLTELVKL REELKPIAFA 

       310        320        330        340        350        360 
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT EQGLIVPNVK 

       370        380        390        400        410        420 
NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN IGSIGGTFAK PVIMPPEVAI 

       430        440        450        460        470        480 
GALGSIKAIP RFNQKGEVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD 


LK 

« Hide

References

« Hide 'large scale' references
[1]"The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex."
Lau K.S., Chuang J.L., Herring W.J., Danner D.J., Cox R.P., Chuang D.T.
Biochim. Biophys. Acta 1132:319-321(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure."
Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., Yeaman S.J.
J. Biol. Chem. 263:6165-6168(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase."
Danner D.J., Litwer S., Herring W.J., Pruckler J.
J. Biol. Chem. 264:7742-7746(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex."
Nobukuni Y., Mitsubuchi H., Endo F., Matsuda I.
Biochem. Biophys. Res. Commun. 161:1035-1041(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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].
Tissue: Kidney.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-384.
[8]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].
[9]"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].
Tissue: Skin.
[10]"Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs."
Lau K.S., Griffin T.A., Hu C.-W.C., Chuang D.T.
Biochemistry 27:1972-1981(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-313.
[11]"Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene."
Lau K.S., Herring W.J., Chuang J.L., McKean M., Danner D.J., Cox R.P., Chuang D.T.
J. Biol. Chem. 267:24090-24096(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[12]"Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."
Wynn R.M., Kochi H., Cox R.P., Chuang D.T.
Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-81.
[13]"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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex."
Chang C.-F., Chou H.-T., Chuang J.L., Chuang D.T., Huang T.-H.
J. Biol. Chem. 277:15865-15873(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 62-145.
[16]"Solution structure of the E3-binding domain of dihydrolipoamide branched chain transacylase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 163-220.
[17]"A 17-bp insertion and a Phe215-->Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34."
Fisher C.W., Lau K.S., Fisher C.R., Wynn R.M., Cox R.P., Chuang D.T.
Biochem. Biophys. Res. Commun. 174:804-809(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MSUD2 CYS-276.
[18]"Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex."
Tsuruta M., Mitsubuchi H., Mardy S., Miura Y., Hayashida Y., Kinugasa A., Ishitsu T., Matsuda I., Indo Y.
J. Hum. Genet. 43:91-100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSUD2 MET-98 AND SER-384.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66785 mRNA. Translation: CAA47285.1.
J03208 mRNA. Translation: AAA35589.1. Different initiation.
M27093 mRNA. Translation: AAA64512.1. Different initiation.
BT007372 mRNA. Translation: AAP36036.1.
AL445928 Genomic DNA. Translation: CAH72257.1.
AK313191 mRNA. Translation: BAG36008.1.
CH471097 Genomic DNA. Translation: EAW72963.1.
BC016675 mRNA. Translation: AAH16675.1.
M19301 mRNA. Translation: AAA59200.1. Sequence problems.
X68104 Genomic DNA. Translation: CAA48225.1.
PIRA32422.
RefSeqNP_001909.3. NM_001918.3.
UniGeneHs.709187.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8MNMR-A62-145[»]
1K8ONMR-A62-145[»]
1ZWVNMR-A165-213[»]
2COONMR-A163-220[»]
3RNMX-ray2.40E/F165-213[»]
ProteinModelPortalP11182.
SMRP11182. Positions 62-147, 163-220, 249-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107997. 13 interactions.
IntActP11182. 6 interactions.
MINTMINT-1161634.
STRING9606.ENSP00000359151.

PTM databases

PhosphoSiteP11182.

Polymorphism databases

DMDM400668.

Proteomic databases

PaxDbP11182.
PRIDEP11182.

Protocols and materials databases

DNASU1629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370132; ENSP00000359151; ENSG00000137992.
GeneID1629.
KEGGhsa:1629.
UCSCuc001dta.3. human.

Organism-specific databases

CTD1629.
GeneCardsGC01M100652.
H-InvDBHIX0000815.
HGNCHGNC:2698. DBT.
HPAHPA026481.
HPA026485.
HPA026533.
MIM248600. phenotype.
248610. gene.
neXtProtNX_P11182.
Orphanet268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBPA27167.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281564.
HOVERGENHBG104085.
InParanoidP11182.
KOK09699.
OrthoDBEOG7GFB4W.
PhylomeDBP11182.
TreeFamTF314182.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12007.
BRENDA2.3.1.168. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP11182.
BgeeP11182.
CleanExHS_DBT.
GenevestigatorP11182.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR015761. Lip_Acyl_TA.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR23151:SF11. PTHR23151:SF11. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11182.
GeneWikiDBT_(gene).
GenomeRNAi1629.
NextBio6684.
PROP11182.
SOURCESearch...

Entry information

Entry nameODB2_HUMAN
AccessionPrimary (citable) accession number: P11182
Secondary accession number(s): B2R811, Q5VVL8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 180 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 1

Human chromosome 1: entries, gene names and cross-references to MIM