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P43251

- BTD_HUMAN

UniProt

P43251 - BTD_HUMAN

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Protein

Biotinidase

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

Functioni

Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.

Catalytic activityi

Biotin amide + H2O = biotin + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 1121Proton acceptorPROSITE-ProRule annotations
Active sitei212 – 2121Proton donorPROSITE-ProRule annotations
Active sitei245 – 2451NucleophilePROSITE-ProRule annotations

GO - Molecular functioni

  1. biotin carboxylase activity Source: ProtInc
  2. biotinidase activity Source: UniProtKB-EC

GO - Biological processi

  1. biotin metabolic process Source: Reactome
  2. central nervous system development Source: ProtInc
  3. epidermis development Source: ProtInc
  4. small molecule metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiREACT_11153. Biotin transport and metabolism.
SABIO-RKP43251.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotinidase (EC:3.5.1.12)
Short name:
Biotinase
Gene namesi
Name:BTD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Organism-specific databases

HGNCiHGNC:1122. BTD.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrial matrix Source: Reactome
  6. nucleolus Source: Ensembl
  7. perikaryon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Biotinidase deficiency (BTD deficiency) [MIM:253260]: A juvenile form of multiple carboxylase deficiency, an autosomal recessive disorder of biotin metabolism, characterized by ketoacidosis, hyperammonemia, excretion of abnormal organic acid metabolites, and dermatitis. Biotinidase deficiency is characterized by seizures, hypotonia, skin rash, alopecia, ataxia, hearing loss, and optic atrophy. If untreated, symptoms usually become progressively worse, and coma and death may occur.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281F → V in BTD deficiency. 1 Publication
VAR_005113
Natural varianti171 – 1711A → T in BTD deficiency. 2 Publications
Corresponds to variant rs13073139 [ dbSNP | Ensembl ].
VAR_005114
Natural varianti228 – 2281D → Y in BTD deficiency. 1 Publication
VAR_005115
Natural varianti323 – 3231H → R in BTD deficiency; partial. 1 Publication
VAR_005116
Natural varianti444 – 4441D → H in BTD deficiency; profound and partial; 52% decrease in activity. 2 Publications
Corresponds to variant rs13078881 [ dbSNP | Ensembl ].
VAR_005117
Natural varianti451 – 4511G → D in BTD deficiency; partial. 1 Publication
VAR_005118
Natural varianti456 – 4561Q → H in BTD deficiency. 1 Publication
Corresponds to variant rs80338685 [ dbSNP | Ensembl ].
VAR_005119
Natural varianti532 – 5321T → M in BTD deficiency. 1 Publication
Corresponds to variant rs104893688 [ dbSNP | Ensembl ].
VAR_005120
Natural varianti538 – 5381R → C in BTD deficiency. 2 Publications
VAR_005121

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi253260. phenotype.
Orphaneti79241. Biotinidase deficiency.
PharmGKBiPA25443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Add
BLAST
Chaini42 – 543502BiotinidasePRO_0000019707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)2 Publications
Glycosylationi150 – 1501N-linked (GlcNAc...) (complex)3 Publications
Glycosylationi203 – 2031N-linked (GlcNAc...)1 Publication
Glycosylationi349 – 3491N-linked (GlcNAc...)2 Publications
Glycosylationi402 – 4021N-linked (GlcNAc...)2 Publications
Glycosylationi489 – 4891N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP43251.
PaxDbiP43251.
PRIDEiP43251.

PTM databases

PhosphoSiteiP43251.

Expressioni

Gene expression databases

ArrayExpressiP43251.
BgeeiP43251.
CleanExiHS_BTD.
GenevestigatoriP43251.

Organism-specific databases

HPAiHPA052275.

Interactioni

Protein-protein interaction databases

BioGridi107151. 1 interaction.
IntActiP43251. 1 interaction.
STRINGi9606.ENSP00000306477.

Structurei

3D structure databases

ProteinModelPortaliP43251.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 363307CN hydrolasePROSITE-ProRule annotationsAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotations

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG270742.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiP43251.
KOiK01435.
PhylomeDBiP43251.
TreeFamiTF323645.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERiPTHR10609. PTHR10609. 1 hit.
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFiPIRSF011861. Biotinidase. 1 hit.
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P43251-1) [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

MAHAHIQGGR RAKSRFVVCI MSGARSKLAL FLCGCYVVAL GAHTGEESVA    50
DHHEAEYYVA AVYEHPSILS LNPLALISRQ EALELMNQNL DIYEQQVMTA 100
AQKDVQIIVF PEDGIHGFNF TRTSIYPFLD FMPSPQVVRW NPCLEPHRFN 150
DTEVLQRLSC MAIRGDMFLV ANLGTKEPCH SSDPRCPKDG RYQFNTNVVF 200
SNNGTLVDRY RKHNLYFEAA FDVPLKVDLI TFDTPFAGRF GIFTCFDILF 250
FDPAIRVLRD YKVKHVVYPT AWMNQLPLLA AIEIQKAFAV AFGINVLAAN 300
VHHPVLGMTG SGIHTPLESF WYHDMENPKS HLIIAQVAKN PVGLIGAENA 350
TGETDPSHSK FLKILSGDPY CEKDAQEVHC DEATKWNVNA PPTFHSEMMY 400
DNFTLVPVWG KEGYLHVCSN GLCCYLLYER PTLSKELYAL GVFDGLHTVH 450
GTYYIQVCAL VRCGGLGFDT CGQEITEATG IFEFHLWGNF STSYIFPLFL 500
TSGMTLEVPD QLGWENDHYF LRKSRLSSGL VTAALYGRLY ERD 543
Length:543
Mass (Da):61,133
Last modified:April 14, 2009 - v2
Checksum:i1A999893A0784944
GO
Isoform 2 (identifier: P43251-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MAHAHIQGGRRAKS → MARKETQLIIKMNHLA

Note: No experimental confirmation available.

Show »
Length:545
Mass (Da):61,510
Checksum:iBD12F620C4FF7EE9
GO
Isoform 3 (identifier: P43251-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MAHAHIQGGRRAK → MPEGGGTSRRLLPMQ

Note: No experimental confirmation available.

Show »
Length:545
Mass (Da):61,330
Checksum:iAC348AE5C8DF373C
GO
Isoform 4 (identifier: P43251-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: No experimental confirmation available.

Show »
Length:523
Mass (Da):58,913
Checksum:i62ED4E8FACA8020D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281F → V in BTD deficiency. 1 Publication
VAR_005113
Natural varianti171 – 1711A → T in BTD deficiency. 2 Publications
Corresponds to variant rs13073139 [ dbSNP | Ensembl ].
VAR_005114
Natural varianti228 – 2281D → Y in BTD deficiency. 1 Publication
VAR_005115
Natural varianti323 – 3231H → R in BTD deficiency; partial. 1 Publication
VAR_005116
Natural varianti391 – 3911P → S.
Corresponds to variant rs35034250 [ dbSNP | Ensembl ].
VAR_056238
Natural varianti444 – 4441D → H in BTD deficiency; profound and partial; 52% decrease in activity. 2 Publications
Corresponds to variant rs13078881 [ dbSNP | Ensembl ].
VAR_005117
Natural varianti451 – 4511G → D in BTD deficiency; partial. 1 Publication
VAR_005118
Natural varianti456 – 4561Q → H in BTD deficiency. 1 Publication
Corresponds to variant rs80338685 [ dbSNP | Ensembl ].
VAR_005119
Natural varianti532 – 5321T → M in BTD deficiency. 1 Publication
Corresponds to variant rs104893688 [ dbSNP | Ensembl ].
VAR_005120
Natural varianti538 – 5381R → C in BTD deficiency. 2 Publications
VAR_005121

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform 4. 1 PublicationVSP_055921Add
BLAST
Alternative sequencei1 – 1414MAHAH…RRAKS → MARKETQLIIKMNHLA in isoform 2. 1 PublicationVSP_054925Add
BLAST
Alternative sequencei1 – 1313MAHAH…GRRAK → MPEGGGTSRRLLPMQ in isoform 3. 1 PublicationVSP_054926Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti379 – 3791H → Y in BAH13565. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03274 mRNA. Translation: AAC04318.1.
AF018631, AF018630 Genomic DNA. Translation: AAC21679.1.
AK294301 mRNA. Translation: BAG57582.1.
AK297033 mRNA. Translation: BAG59561.1.
AK301838 mRNA. Translation: BAH13565.1.
AK313252 mRNA. Translation: BAG36062.1.
AC027129 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64254.1.
BC012099 mRNA. Translation: AAH12099.1.
CCDSiCCDS2628.1. [P43251-1]
CCDS63563.1. [P43251-3]
CCDS63564.1. [P43251-2]
PIRiA54362.
RefSeqiNP_000051.1. NM_000060.3. [P43251-1]
NP_001268652.1. NM_001281723.1. [P43251-3]
NP_001268653.1. NM_001281724.1.
NP_001268654.1. NM_001281725.1.
XP_005265474.1. XM_005265417.2.
XP_006713377.1. XM_006713314.1.
XP_006713378.1. XM_006713315.1.
UniGeneiHs.517830.

Genome annotation databases

EnsembliENST00000303498; ENSP00000306477; ENSG00000169814. [P43251-1]
ENST00000383778; ENSP00000373288; ENSG00000169814.
ENST00000437172; ENSP00000400995; ENSG00000169814. [P43251-2]
ENST00000449107; ENSP00000388212; ENSG00000169814. [P43251-3]
GeneIDi686.
KEGGihsa:686.
UCSCiuc003cah.3. human. [P43251-1]

Polymorphism databases

DMDMi226693503.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03274 mRNA. Translation: AAC04318.1 .
AF018631 , AF018630 Genomic DNA. Translation: AAC21679.1 .
AK294301 mRNA. Translation: BAG57582.1 .
AK297033 mRNA. Translation: BAG59561.1 .
AK301838 mRNA. Translation: BAH13565.1 .
AK313252 mRNA. Translation: BAG36062.1 .
AC027129 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64254.1 .
BC012099 mRNA. Translation: AAH12099.1 .
CCDSi CCDS2628.1. [P43251-1 ]
CCDS63563.1. [P43251-3 ]
CCDS63564.1. [P43251-2 ]
PIRi A54362.
RefSeqi NP_000051.1. NM_000060.3. [P43251-1 ]
NP_001268652.1. NM_001281723.1. [P43251-3 ]
NP_001268653.1. NM_001281724.1.
NP_001268654.1. NM_001281725.1.
XP_005265474.1. XM_005265417.2.
XP_006713377.1. XM_006713314.1.
XP_006713378.1. XM_006713315.1.
UniGenei Hs.517830.

3D structure databases

ProteinModelPortali P43251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107151. 1 interaction.
IntActi P43251. 1 interaction.
STRINGi 9606.ENSP00000306477.

PTM databases

PhosphoSitei P43251.

Polymorphism databases

DMDMi 226693503.

Proteomic databases

MaxQBi P43251.
PaxDbi P43251.
PRIDEi P43251.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303498 ; ENSP00000306477 ; ENSG00000169814 . [P43251-1 ]
ENST00000383778 ; ENSP00000373288 ; ENSG00000169814 .
ENST00000437172 ; ENSP00000400995 ; ENSG00000169814 . [P43251-2 ]
ENST00000449107 ; ENSP00000388212 ; ENSG00000169814 . [P43251-3 ]
GeneIDi 686.
KEGGi hsa:686.
UCSCi uc003cah.3. human. [P43251-1 ]

Organism-specific databases

CTDi 686.
GeneCardsi GC03P015621.
GeneReviewsi BTD.
HGNCi HGNC:1122. BTD.
HPAi HPA052275.
MIMi 253260. phenotype.
609019. gene.
neXtProti NX_P43251.
Orphaneti 79241. Biotinidase deficiency.
PharmGKBi PA25443.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270742.
HOGENOMi HOG000007627.
HOVERGENi HBG003996.
InParanoidi P43251.
KOi K01435.
PhylomeDBi P43251.
TreeFami TF323645.

Enzyme and pathway databases

Reactomei REACT_11153. Biotin transport and metabolism.
SABIO-RK P43251.

Miscellaneous databases

GenomeRNAii 686.
NextBioi 2824.
PROi P43251.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43251.
Bgeei P43251.
CleanExi HS_BTD.
Genevestigatori P43251.

Family and domain databases

Gene3Di 3.60.110.10. 1 hit.
InterProi IPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view ]
PANTHERi PTHR10609. PTHR10609. 1 hit.
Pfami PF00795. CN_hydrolase. 1 hit.
[Graphical view ]
PIRSFi PIRSF011861. Biotinidase. 1 hit.
SUPFAMi SSF56317. SSF56317. 1 hit.
PROSITEi PS50263. CN_HYDROLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human serum biotinidase. cDNA cloning, sequence, and characterization."
    Cole H., Reynolds T.R., Lockyer J.M., Buck G.A., Denson T., Spence J.E., Hymes J., Wolf B.
    J. Biol. Chem. 269:6566-6570(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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; 2; 3 AND 4).
    Tissue: Amygdala, Pericardium and Umbilical cord blood.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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] (ISOFORM 1).
    Tissue: Kidney.
  7. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-203; ASN-349 AND ASN-402.
    Tissue: Plasma.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-349 AND ASN-402.
    Tissue: Liver.
  9. Cited for: GLYCOSYLATION AT ASN-150.
  10. "Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of profound biotinidase deficiency in symptomatic children."
    Pomponio R.J., Norrgard K.J., Hymes J., Reynolds T.R., Buck G.A., Baumgartner R., Suormala T., Wolf B.
    Hum. Genet. 99:506-512(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BTD DEFICIENCY CYS-538.
  11. "Partial biotinidase deficiency is usually due to the D444H mutation in the biotinidase gene."
    Swango K.L., Demirkol M., Huener G., Pronicka E., Sykut-Cegielska J., Schulze A., Mayatepek E., Wolf B.
    Hum. Genet. 102:571-575(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS BTD DEFICIENCY VAL-128; THR-171; TYR-228; ARG-323; HIS-444; ASP-451; HIS-456; MET-532 AND CYS-538.
  12. "Double mutation (A171T and D444H) is a common cause of profound biotinidase deficiency in children ascertained by newborn screening in the United States."
    Norrgard K.J., Pomponio R.J., Swango K.L., Hymes J., Reynolds T., Buck G.A., Wolf B.
    Hum. Mutat. 11:410-410(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS BTD DEFICIENCY THR-171 AND HIS-444.

Entry informationi

Entry nameiBTD_HUMAN
AccessioniPrimary (citable) accession number: P43251
Secondary accession number(s): A6NHF2
, B2R865, B4DFX1, B4DLJ9, B7Z7C9, F8W1Q3, Q96EM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 14, 2009
Last modified: October 1, 2014
This is version 130 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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