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Protein

Di-N-acetylchitobiase

Gene

CTBS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Di-N-acetylchitobiase (EC:3.2.1.-)
Gene namesi
Name:CTBS
Synonyms:CTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2496. CTBS.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: GO_Central
  • extracellular space Source: UniProtKB
  • lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26997.

Polymorphism and mutation databases

BioMutaiCTBS.
DMDMi399376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838By similarityAdd
BLAST
Chaini39 – 385347Di-N-acetylchitobiasePRO_0000011961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ01459.
PaxDbiQ01459.
PeptideAtlasiQ01459.
PRIDEiQ01459.

PTM databases

PhosphoSiteiQ01459.

Expressioni

Gene expression databases

BgeeiQ01459.
CleanExiHS_CTBS.
ExpressionAtlasiQ01459. baseline and differential.
GenevisibleiQ01459. HS.

Organism-specific databases

HPAiCAB017043.
HPA023594.
HPA048810.

Interactioni

Protein-protein interaction databases

BioGridi107868. 4 interactions.
IntActiQ01459. 3 interactions.
STRINGi9606.ENSP00000359664.

Structurei

3D structure databases

ProteinModelPortaliQ01459.
SMRiQ01459. Positions 115-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3858.
GeneTreeiENSGT00390000012891.
HOGENOMiHOG000007829.
HOVERGENiHBG005486.
InParanoidiQ01459.
KOiK12310.
OMAiDEQSQIW.
OrthoDBiEOG7ZGX3G.
PhylomeDBiQ01459.
TreeFamiTF332677.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPQLRRWR LVSSPPSGVP GLALLALLAL LALRLAAGTD CPCPEPELCR
60 70 80 90 100
PIRHHPDFEV FVFDVGQKTW KSYDWSQITT VATFGKYDSE LMCYAHSKGA
110 120 130 140 150
RVVLKGDVSL KDIIDPAFRA SWIAQKLNLA KTQYMDGINI DIEQEVNCLS
160 170 180 190 200
PEYDALTALV KETTDSFHRE IEGSQVTFDV AWSPKNIDRR CYNYTGIADA
210 220 230 240 250
CDFLFVMSYD EQSQIWSECI AAANAPYNQT LTGYNDYIKM SINPKKLVMG
260 270 280 290 300
VPWYGYDYTC LNLSEDHVCT IAKVPFRGAP CSDAAGRQVP YKTIMKQINS
310 320 330 340 350
SISGNLWDKD QRAPYYNYKD PAGHFHQVWY DNPQSISLKA TYIQNYRLRG
360 370 380
IGMWNANCLD YSGDAVAKQQ TEEMWEVLKP KLLQR
Length:385
Mass (Da):43,760
Last modified:July 1, 1993 - v1
Checksum:i0A9D14C8B26B52EE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741V → I.
Corresponds to variant rs15911 [ dbSNP | Ensembl ].
VAR_049197
Natural varianti310 – 3101D → Y.
Corresponds to variant rs3768249 [ dbSNP | Ensembl ].
VAR_020160

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95767 mRNA. Translation: AAA35684.1.
AF085706
, AF085700, AF085701, AF085702, AF085703, AF085704, AF085705 Genomic DNA. Translation: AAC35852.1.
AL359762 Genomic DNA. Translation: CAH70207.1.
CH471097 Genomic DNA. Translation: EAW73232.1.
CH471097 Genomic DNA. Translation: EAW73233.1.
BC126333 mRNA. Translation: AAI26334.1.
BC126335 mRNA. Translation: AAI26336.1.
CCDSiCCDS698.1.
PIRiA44102.
RefSeqiNP_004379.1. NM_004388.2.
UniGeneiHs.513557.

Genome annotation databases

EnsembliENST00000370630; ENSP00000359664; ENSG00000117151.
GeneIDi1486.
KEGGihsa:1486.
UCSCiuc001dka.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95767 mRNA. Translation: AAA35684.1.
AF085706
, AF085700, AF085701, AF085702, AF085703, AF085704, AF085705 Genomic DNA. Translation: AAC35852.1.
AL359762 Genomic DNA. Translation: CAH70207.1.
CH471097 Genomic DNA. Translation: EAW73232.1.
CH471097 Genomic DNA. Translation: EAW73233.1.
BC126333 mRNA. Translation: AAI26334.1.
BC126335 mRNA. Translation: AAI26336.1.
CCDSiCCDS698.1.
PIRiA44102.
RefSeqiNP_004379.1. NM_004388.2.
UniGeneiHs.513557.

3D structure databases

ProteinModelPortaliQ01459.
SMRiQ01459. Positions 115-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107868. 4 interactions.
IntActiQ01459. 3 interactions.
STRINGi9606.ENSP00000359664.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteiQ01459.

Polymorphism and mutation databases

BioMutaiCTBS.
DMDMi399376.

Proteomic databases

MaxQBiQ01459.
PaxDbiQ01459.
PeptideAtlasiQ01459.
PRIDEiQ01459.

Protocols and materials databases

DNASUi1486.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370630; ENSP00000359664; ENSG00000117151.
GeneIDi1486.
KEGGihsa:1486.
UCSCiuc001dka.2. human.

Organism-specific databases

CTDi1486.
GeneCardsiGC01M085018.
HGNCiHGNC:2496. CTBS.
HPAiCAB017043.
HPA023594.
HPA048810.
MIMi600873. gene.
neXtProtiNX_Q01459.
PharmGKBiPA26997.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3858.
GeneTreeiENSGT00390000012891.
HOGENOMiHOG000007829.
HOVERGENiHBG005486.
InParanoidiQ01459.
KOiK12310.
OMAiDEQSQIW.
OrthoDBiEOG7ZGX3G.
PhylomeDBiQ01459.
TreeFamiTF332677.

Miscellaneous databases

GeneWikiiCTBS.
GenomeRNAii1486.
NextBioi6101.
PROiQ01459.
SOURCEiSearch...

Gene expression databases

BgeeiQ01459.
CleanExiHS_CTBS.
ExpressionAtlasiQ01459. baseline and differential.
GenevisibleiQ01459. HS.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the cDNA sequence encoding the lysosomal glycosidase di-N-acetylchitobiase."
    Fisher K.J., Aronson N.N. Jr.
    J. Biol. Chem. 267:19607-19616(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Structure of the human gene for lysosomal di-N-acetylchitobiase."
    Liu B., Ahmad W., Aronson N.N. Jr.
    Glycobiology 9:589-593(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
    , 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].
  4. 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].
    Tissue: Brain.
  6. "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-299.
    Tissue: Liver.

Entry informationi

Entry nameiDIAC_HUMAN
AccessioniPrimary (citable) accession number: Q01459
Secondary accession number(s): Q5VX50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 24, 2015
This is version 129 of the entry and version 1 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.