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Q8NFI3 (ENASE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic endo-beta-N-acetylglucosaminidase

Short name=ENGase
EC=3.2.1.96
Gene names
Name:ENGASE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length743 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol. Ref.1

Catalytic activity

Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

Subcellular location

Cytoplasmcytosol By similarity.

Tissue specificity

Widely expressed. Expressed at higher level in thymus and spleen. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 85 family.

Contains 1 BRCT domain.

Sequence caution

The sequence AAH24213.2 differs from that shown. Reason: Frameshift at position 694.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionGlycosidase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NFI3-1)

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.
Isoform 2 (identifier: Q8NFI3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     364-377: GWVYECLEKKDFFQ → SCSVFPGVGNLLCC
     378-743: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NFI3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     347-406: SLELIRKHGF...SLPFVTSFCL → VGGGFRPRAS...CPAPAKLCPH
     407-743: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 743743Cytosolic endo-beta-N-acetylglucosaminidase
PRO_0000328867

Regions

Domain291 – 38393BRCT

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue661Phosphoserine Ref.6

Natural variations

Alternative sequence347 – 40660SLELI…TSFCL → VGGGFRPRASGPVPPLGPHF LMDLPFPSAPQRNDSSCSSQ SGDPVALRNRCPAPAKLCPH in isoform 3.
VSP_032835
Alternative sequence364 – 37714GWVYE…KDFFQ → SCSVFPGVGNLLCC in isoform 2.
VSP_032836
Alternative sequence378 – 743366Missing in isoform 2.
VSP_032837
Alternative sequence407 – 743337Missing in isoform 3.
VSP_032838
Natural variant5961S → N. Ref.5
Corresponds to variant rs4789879 [ dbSNP | Ensembl ].
VAR_060188
Natural variant7311E → K.
Corresponds to variant rs11871357 [ dbSNP | Ensembl ].
VAR_060189

Experimental info

Sequence conflict1521F → L in BAB15158. Ref.2
Sequence conflict2241T → A in CAH56405. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 384DA533AE549FC5

FASTA74383,987
        10         20         30         40         50         60 
MEAAAVTVTR SATRRRRRQL QGLAAPEAGT QEEQEDQEPR PRRRRPGRSI KDEEEETVFR 

        70         80         90        100        110        120 
EVVSFSPDPL PVRYYDKDTT KPISFYLSSL EELLAWKPRL EDGFNVALEP LACRQPPLSS 

       130        140        150        160        170        180 
QRPRTLLCHD MMGGYLDDRF IQGSVVQTPY AFYHWQCIDV FVYFSHHTVT IPPVGWTNTA 

       190        200        210        220        230        240 
HRHGVCVLGT FITEWNEGGR LCEAFLAGDE RSYQAVADRL VQITQFFRFD GWLINIENSL 

       250        260        270        280        290        300 
SLAAVGNMPP FLRYLTTQLH RQVPGGLVLW YDSVVQSGQL KWQDELNQHN RVFFDSCDGF 

       310        320        330        340        350        360 
FTNYNWREEH LERMLGQAGE RRADVYVGVD VFARGNVVGG RFDTDKSLEL IRKHGFSVAL 

       370        380        390        400        410        420 
FAPGWVYECL EKKDFFQNQD KFWGRLERYL PTHSICSLPF VTSFCLGMGA RRVCYGQEEA 

       430        440        450        460        470        480 
VGPWYHLSAQ EIQPLFGEHR LGGDGRGWVR THCCLEDAWH GGSSLLVRGV IPPEVGNVAV 

       490        500        510        520        530        540 
RLFSLQAPVP PKIYLSMVYK LEGPTDVTVA LELTTGDAGS CHIGGISVLN AETSSRHSLR 

       550        560        570        580        590        600 
PLRVPPTKLA RWVGRCGRQL SGGWVQHCYE VSLRGCLLLD LLVCFSRPPG SREEESFTCR 

       610        620        630        640        650        660 
LGEIQVVDAA SLLAPLPQVQ AVTISHIRWQ PSASEREGPP ALLQLSCTLH WSFLLSQVRC 

       670        680        690        700        710        720 
FRIHCWGGMS DDSPGRELPR PEMPMFLGLA FATQYRIVDL LVEAAGPGQD RRMEFLVEPV 

       730        740 
PKEGFRVPQA EWGRAVLLYS APA 

« Hide

Isoform 2 [UniParc].

Checksum: A60D0AE20C2EDD79
Show »

FASTA37743,107
Isoform 3 [UniParc].

Checksum: 4EB91EC292C1A61A
Show »

FASTA40646,090

References

« Hide 'large scale' references
[1]"Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol."
Suzuki T., Yano K., Sugimoto S., Kitajima K., Lennarz W.J., Inoue S., Inoue Y., Emori Y.
Proc. Natl. Acad. Sci. U.S.A. 99:9691-9696(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Hepatoma.
[3]Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-680 (ISOFORM 3).
Tissue: Testis.
[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] OF 486-743 (ISOFORM 1), VARIANT ASN-596.
Tissue: Skin.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF512564 mRNA. Translation: AAM80487.1.
AK025518 mRNA. Translation: BAB15158.1.
CH471099 Genomic DNA. Translation: EAW89562.1.
AL110283 mRNA. Translation: CAH56405.1.
BC024213 mRNA. Translation: AAH24213.2. Frameshift.
CCDSCCDS42394.1. [Q8NFI3-1]
RefSeqNP_001036038.1. NM_001042573.2. [Q8NFI3-1]
UniGeneHs.29288.

3D structure databases

ProteinModelPortalQ8NFI3.
SMRQ8NFI3. Positions 91-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122283. 1 interaction.
IntActQ8NFI3. 2 interactions.
STRING9606.ENSP00000300682.

Chemistry

BindingDBQ8NFI3.
ChEMBLCHEMBL5172.

Protein family/group databases

CAZyGH85. Glycoside Hydrolase Family 85.

PTM databases

PhosphoSiteQ8NFI3.

Polymorphism databases

DMDM74715557.

Proteomic databases

MaxQBQ8NFI3.
PaxDbQ8NFI3.
PeptideAtlasQ8NFI3.
PRIDEQ8NFI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000579016; ENSP00000462333; ENSG00000167280. [Q8NFI3-1]
GeneID64772.
KEGGhsa:64772.
UCSCuc002jwu.1. human. [Q8NFI3-3]
uc002jwv.4. human. [Q8NFI3-1]

Organism-specific databases

CTD64772.
GeneCardsGC17P077071.
HGNCHGNC:24622. ENGASE.
HPAHPA021551.
MIM611898. gene.
neXtProtNX_Q8NFI3.
PharmGKBPA164719123.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4724.
HOGENOMHOG000082678.
HOVERGENHBG107848.
InParanoidQ8NFI3.
KOK01227.
OMAPTKLARW.
OrthoDBEOG7KQ218.
PhylomeDBQ8NFI3.
TreeFamTF314391.

Gene expression databases

ArrayExpressQ8NFI3.
BgeeQ8NFI3.
GenevestigatorQ8NFI3.

Family and domain databases

InterProIPR001357. BRCT_dom.
IPR005201. Glyco_hydro_85.
[Graphical view]
PfamPF03644. Glyco_hydro_85. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENGASE. human.
GenomeRNAi64772.
NextBio66783.
PROQ8NFI3.
SOURCESearch...

Entry information

Entry nameENASE_HUMAN
AccessionPrimary (citable) accession number: Q8NFI3
Secondary accession number(s): Q659F0, Q8TB86, Q9H6U4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 83 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 17

Human chromosome 17: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries