Q01459 (DIAC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Di-N-acetylchitobiase
EC=3.2.1.-

Gene names

Name:	CTBS
Synonyms:	CTB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chitin catabolic process Inferred from electronic annotation. Source: Compara oligosaccharide catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chitinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38	By similarity
	Chain	39 – 385	347	Di-N-acetylchitobiase		PRO_0000011961
Sites
	Active site	143	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	193	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Glycosylation	299	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Natural variant	274	1	V → I. Corresponds to variant rs15911 [ dbSNP | Ensembl ].		VAR_049197
	Natural variant	310	1	D → Y. Corresponds to variant rs3768249 [ dbSNP | Ensembl ].		VAR_020160

Sequences

	Sequence		Length	Mass (Da)
	Q01459 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 0A9D14C8B26B52EE	FASTA	385	43,760
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00007778.
PIR	A44102.
RefSeq	NP_004379.1. NM_004388.2.
UniGene	Hs.513557.
3D structure databases
ProteinModelPortal	Q01459.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01459. 3 interactions.
STRING	9606.ENSP00000359664.
Protein family/group databases
CAZy	GH18. Glycoside Hydrolase Family 18.
PTM databases
PhosphoSite	Q01459.
Polymorphism databases
DMDM	399376.
Proteomic databases
PaxDb	Q01459.
PeptideAtlas	Q01459.
PRIDE	Q01459.
Protocols and materials databases
DNASU	1486.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370630; ENSP00000359664; ENSG00000117151.
GeneID	1486.
KEGG	hsa:1486.
UCSC	uc001dka.2. human.
Organism-specific databases
CTD	1486.
GeneCards	GC01M085018.
HGNC	HGNC:2496. CTBS.
HPA	CAB017043. HPA023594.
MIM	600873. gene.
neXtProt	NX_Q01459.
PharmGKB	PA26997.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3858.
HOGENOM	HOG000007829.
HOVERGEN	HBG005486.
InParanoid	Q01459.
KO	K12310.
OMA	DEQSQIW.
OrthoDB	EOG480HWR.
PhylomeDB	Q01459.
Gene expression databases
ArrayExpress	Q01459.
Bgee	Q01459.
CleanEx	HS_CTBS.
Genevestigator	Q01459.
GermOnline	ENSG00000117151. Homo sapiens.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR011583. Chitinase_II. IPR001223. Glyco_hydro18cat. IPR001579. Glyco_hydro_18_chit_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00704. Glyco_hydro_18. 1 hit. [Graphical view]
SMART	SM00636. Glyco_18. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1486.
NextBio	6101.
SOURCE	Search...

Entry information

Entry name

DIAC_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.