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Q01459 (DIAC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Di-N-acetylchitobiase

EC=3.2.1.-
Gene names
Name:CTBS
Synonyms:CTB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from electronic annotation. Source: Ensembl

oligosaccharide catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 By similarity
Chain39 – 385347Di-N-acetylchitobiase
PRO_0000011961

Sites

Active site1431Proton donor By similarity

Amino acid modifications

Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant2741V → I.
Corresponds to variant rs15911 [ dbSNP | Ensembl ].
VAR_049197
Natural variant3101D → Y.
Corresponds to variant rs3768249 [ dbSNP | Ensembl ].
VAR_020160

Sequences

Sequence LengthMass (Da)Tools
Q01459 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 0A9D14C8B26B52EE

FASTA38543,760
        10         20         30         40         50         60 
MSRPQLRRWR LVSSPPSGVP GLALLALLAL LALRLAAGTD CPCPEPELCR PIRHHPDFEV 

        70         80         90        100        110        120 
FVFDVGQKTW KSYDWSQITT VATFGKYDSE LMCYAHSKGA RVVLKGDVSL KDIIDPAFRA 

       130        140        150        160        170        180 
SWIAQKLNLA KTQYMDGINI DIEQEVNCLS PEYDALTALV KETTDSFHRE IEGSQVTFDV 

       190        200        210        220        230        240 
AWSPKNIDRR CYNYTGIADA CDFLFVMSYD EQSQIWSECI AAANAPYNQT LTGYNDYIKM 

       250        260        270        280        290        300 
SINPKKLVMG VPWYGYDYTC LNLSEDHVCT IAKVPFRGAP CSDAAGRQVP YKTIMKQINS 

       310        320        330        340        350        360 
SISGNLWDKD QRAPYYNYKD PAGHFHQVWY DNPQSISLKA TYIQNYRLRG IGMWNANCLD 

       370        380 
YSGDAVAKQQ TEEMWEVLKP KLLQR 

« Hide

References

« Hide 'large scale' references
[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. 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].
[4]Mural R.J., Istrail S., Sutton 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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95767 mRNA. Translation: AAA35684.1.
AF085706 expand/collapse EMBL AC list , 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.
CCDSCCDS698.1.
PIRA44102.
RefSeqNP_004379.1. NM_004388.2.
UniGeneHs.513557.

3D structure databases

ProteinModelPortalQ01459.
SMRQ01459. Positions 116-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107868. 2 interactions.
IntActQ01459. 3 interactions.
STRING9606.ENSP00000359664.

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteQ01459.

Polymorphism databases

DMDM399376.

Proteomic databases

MaxQBQ01459.
PaxDbQ01459.
PeptideAtlasQ01459.
PRIDEQ01459.

Protocols and materials databases

DNASU1486.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370630; ENSP00000359664; ENSG00000117151.
GeneID1486.
KEGGhsa:1486.
UCSCuc001dka.2. human.

Organism-specific databases

CTD1486.
GeneCardsGC01M085018.
HGNCHGNC:2496. CTBS.
HPACAB017043.
HPA023594.
HPA048810.
MIM600873. gene.
neXtProtNX_Q01459.
PharmGKBPA26997.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3858.
HOGENOMHOG000007829.
HOVERGENHBG005486.
InParanoidQ01459.
KOK12310.
OMADEQSQIW.
OrthoDBEOG7ZGX3G.
PhylomeDBQ01459.
TreeFamTF332677.

Gene expression databases

ArrayExpressQ01459.
BgeeQ01459.
CleanExHS_CTBS.
GenevestigatorQ01459.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCTBS.
GenomeRNAi1486.
NextBio6101.
PROQ01459.
SOURCESearch...

Entry information

Entry nameDIAC_HUMAN
AccessionPrimary (citable) accession number: Q01459
Secondary accession number(s): Q5VX50
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 121 of the entry and version 1 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

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries