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Q01459

- DIAC_HUMAN

UniProt

Q01459 - DIAC_HUMAN

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Protein

Di-N-acetylchitobiase

Gene

CTBS

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chitinase activity Source: Ensembl

GO - Biological processi

  1. chitin catabolic process Source: Ensembl
  2. oligosaccharide catabolic process Source: Ensembl
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:2496. CTBS.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. extracellular vesicular exosome Source: UniProt
  3. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26997.

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.
GenevestigatoriQ01459.

Organism-specific databases

HPAiCAB017043.
HPA023594.
HPA048810.

Interactioni

Protein-protein interaction databases

BioGridi107868. 2 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.

Polymorphism databases

DMDMi399376.

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 .
CCDSi CCDS698.1.
PIRi A44102.
RefSeqi NP_004379.1. NM_004388.2.
UniGenei Hs.513557.

3D structure databases

ProteinModelPortali Q01459.
SMRi Q01459. Positions 115-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107868. 2 interactions.
IntActi Q01459. 3 interactions.
STRINGi 9606.ENSP00000359664.

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSitei Q01459.

Polymorphism databases

DMDMi 399376.

Proteomic databases

MaxQBi Q01459.
PaxDbi Q01459.
PeptideAtlasi Q01459.
PRIDEi Q01459.

Protocols and materials databases

DNASUi 1486.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370630 ; ENSP00000359664 ; ENSG00000117151 .
GeneIDi 1486.
KEGGi hsa:1486.
UCSCi uc001dka.2. human.

Organism-specific databases

CTDi 1486.
GeneCardsi GC01M085018.
HGNCi HGNC:2496. CTBS.
HPAi CAB017043.
HPA023594.
HPA048810.
MIMi 600873. gene.
neXtProti NX_Q01459.
PharmGKBi PA26997.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3858.
GeneTreei ENSGT00390000012891.
HOGENOMi HOG000007829.
HOVERGENi HBG005486.
InParanoidi Q01459.
KOi K12310.
OMAi DEQSQIW.
OrthoDBi EOG7ZGX3G.
PhylomeDBi Q01459.
TreeFami TF332677.

Miscellaneous databases

GeneWikii CTBS.
GenomeRNAii 1486.
NextBioi 6101.
PROi Q01459.
SOURCEi Search...

Gene expression databases

Bgeei Q01459.
CleanExi HS_CTBS.
ExpressionAtlasi Q01459. baseline and differential.
Genevestigatori Q01459.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SMARTi SM00636. Glyco_18. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
PROSITEi PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 124 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