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Protein

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Gene

Ngly1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.3 Publications

Catalytic activityi

Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by Z-VAD-fmk, a well-known caspase inhibitor, which inhibits enzyme activity through covalent binding of the carbohydrate to the single Cys-306 residue.1 Publication

Kineticsi

  1. KM=114 µM for fetuin glycopeptide I1 Publication
  1. Vmax=0.0964 nmol/min/mg enzyme with fetuin glycopeptide I as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi247 – 2471Zinc
Metal bindingi250 – 2501Zinc
Metal bindingi280 – 2801Zinc
Metal bindingi283 – 2831Zinc
Active sitei306 – 3061Nucleophile
Active sitei333 – 3331
Active sitei350 – 3501

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity Source: MGI

GO - Biological processi

  • glycoprotein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.52. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Short name:
mPNGase
Alternative name(s):
N-glycanase 1
Peptide:N-glycanase
Gene namesi
Name:Ngly1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1913276. Ngly1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411N → P: Abolishes interaction with VCP. 1 Publication
Mutagenesisi58 – 581N → A: Does not affect the interaction with VCP. 1 Publication
Mutagenesisi79 – 802GF → AA: Abolishes interaction with VCP. 1 Publication
Mutagenesisi306 – 3061C → A: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 651650Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidasePRO_0000248973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JI78.
MaxQBiQ9JI78.
PaxDbiQ9JI78.
PRIDEiQ9JI78.

PTM databases

iPTMnetiQ9JI78.
PhosphoSiteiQ9JI78.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest level in testis.2 Publications

Gene expression databases

BgeeiQ9JI78.
CleanExiMM_NGLY1.
GenevisibleiQ9JI78. MM.

Interactioni

Subunit structurei

Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with the proteasome components RAD23B and PSMC1. Interacts with directly with VCP. Interacts with DERL1, bringing it close to the endoplasmic reticulum membrane. Interacts with SAKS1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AmfrQ9R0495EBI-3648128,EBI-3648125
RAD23AP547252EBI-3648128,EBI-746453From a different organism.
VcpQ018533EBI-3648128,EBI-80597

Protein-protein interaction databases

BioGridi208478. 7 interactions.
DIPiDIP-41155N.
IntActiQ9JI78. 5 interactions.
MINTiMINT-214719.
STRINGi10090.ENSMUSP00000022310.

Structurei

Secondary structure

1
651
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 206Combined sources
Helixi25 – 4319Combined sources
Beta strandi45 – 473Combined sources
Helixi49 – 524Combined sources
Beta strandi53 – 553Combined sources
Helixi59 – 646Combined sources
Turni65 – 673Combined sources
Helixi71 – 788Combined sources
Beta strandi84 – 885Combined sources
Helixi95 – 10915Combined sources
Helixi167 – 18014Combined sources
Helixi181 – 1833Combined sources
Helixi185 – 19410Combined sources
Helixi197 – 21115Combined sources
Helixi223 – 23614Combined sources
Turni248 – 2503Combined sources
Beta strandi255 – 2617Combined sources
Helixi266 – 2694Combined sources
Beta strandi275 – 2806Combined sources
Turni281 – 2844Combined sources
Beta strandi285 – 2906Combined sources
Helixi295 – 3017Combined sources
Beta strandi303 – 3053Combined sources
Helixi306 – 31914Combined sources
Beta strandi324 – 3296Combined sources
Turni330 – 3323Combined sources
Beta strandi333 – 3408Combined sources
Turni341 – 3444Combined sources
Beta strandi345 – 3506Combined sources
Turni351 – 3544Combined sources
Beta strandi355 – 3573Combined sources
Helixi359 – 3613Combined sources
Turni362 – 3654Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi381 – 3833Combined sources
Helixi385 – 3884Combined sources
Helixi392 – 3987Combined sources
Helixi404 – 41916Combined sources
Helixi424 – 44118Combined sources
Beta strandi458 – 4625Combined sources
Helixi482 – 4876Combined sources
Beta strandi489 – 4957Combined sources
Turni496 – 4994Combined sources
Beta strandi500 – 5034Combined sources
Helixi504 – 5063Combined sources
Beta strandi509 – 5135Combined sources
Helixi514 – 5174Combined sources
Beta strandi519 – 52911Combined sources
Turni530 – 5334Combined sources
Beta strandi534 – 5396Combined sources
Beta strandi544 – 55310Combined sources
Helixi555 – 5573Combined sources
Beta strandi559 – 5679Combined sources
Beta strandi569 – 5724Combined sources
Beta strandi577 – 5837Combined sources
Beta strandi588 – 5914Combined sources
Beta strandi598 – 6003Combined sources
Turni602 – 6054Combined sources
Beta strandi607 – 61610Combined sources
Helixi620 – 6256Combined sources
Beta strandi626 – 6338Combined sources
Beta strandi641 – 65010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5UNMR-A1-119[»]
2F4MX-ray1.85A164-450[»]
2F4OX-ray2.26A164-450[»]
2G9FX-ray1.90A451-651[»]
2G9GX-ray2.00A451-651[»]
2HPJX-ray1.70A12-110[»]
2HPLX-ray1.80A12-111[»]
2I74X-ray1.75A/B471-651[»]
ProteinModelPortaliQ9JI78.
SMRiQ9JI78. Positions 12-110, 164-450, 472-651.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JI78.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 9162PUBAdd
BLAST
Domaini451 – 651201PAWPROSITE-ProRule annotationAdd
BLAST

Domaini

The PUB domain mediates the interaction with VCP.1 Publication

Sequence similaritiesi

Belongs to the transglutaminase-like superfamily. PNGase family.PROSITE-ProRule annotation
Contains 1 PAW domain.PROSITE-ProRule annotation
Contains 1 PUB (PUG) domain.Curated

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
GeneTreeiENSGT00390000006540.
HOGENOMiHOG000247069.
HOVERGENiHBG082026.
InParanoidiQ9JI78.
KOiK01456.
OMAiRVEDHYC.
OrthoDBiEOG780RMR.
PhylomeDBiQ9JI78.
TreeFamiTF315254.

Family and domain databases

InterProiIPR008979. Galactose-bd-like.
IPR006588. Peptide_N_glycanase_PAW_dom.
IPR018997. PUB_domain.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF04721. PAW. 1 hit.
PF09409. PUB. 1 hit.
PF01841. Transglut_core. 1 hit.
[Graphical view]
SMARTiSM00613. PAW. 1 hit.
SM00580. PUG. 1 hit.
SM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS51398. PAW. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JI78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATLGSSS SSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPSDEK
60 70 80 90 100
YRSIRIGNTA FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK
110 120 130 140 150
IRDLIAIERS SRLDGSSKKV QFSQHPAAAK LPLEQSEDPA GLIRHSGNQT
160 170 180 190 200
GQLPSLPSAP MVVGDSTILK VLQSNIQHVQ LYENPVLQEK ALTCIPVSEL
210 220 230 240 250
KRKAQEKLFR ARKLDKGTNV SDEDFLLLEL LHWFKEEFFR WVNNIVCSKC
260 270 280 290 300
GGETRSRDEA LLPNDDELKW GAKNVENHYC DACQLSNRFP RYNNPEKLLE
310 320 330 340 350
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD
360 370 380 390 400
ACEDVCDKPL LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHDEVMSRRT
410 420 430 440 450
KVKEELLRET INGLNKQRQL SLSESRRKEL LQRIIVELVE FISPKTPRPG
460 470 480 490 500
ELGGRVSGSL AWRVARGETG LERKEILFIP SENEKISKQF HLRYDIVRDR
510 520 530 540 550
YIRVSDNNIN ISGWENGVWK MESIFRKVEK DWNMVYLARK EGSSFAYISW
560 570 580 590 600
KFECGSAGLK VDTVSIRTSS QSFESGSVRW KLRSETAQVN LLGDKNLRSY
610 620 630 640 650
NDFSGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDSGEN GLEIIITFND

L
Length:651
Mass (Da):74,275
Last modified:September 5, 2006 - v2
Checksum:iF9D7A35726482F81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti509 – 5091I → T in AAF74723 (PubMed:10831608).Curated
Sequence conflicti509 – 5091I → T in AAP03060 (PubMed:12711318).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250927 mRNA. Translation: AAF74723.1.
AY225417 Genomic DNA. Translation: AAP03060.1.
AK003279 mRNA. Translation: BAB22686.1.
AK028248 mRNA. Translation: BAC25839.1.
BC028961 mRNA. Translation: AAH28961.1.
CCDSiCCDS26832.1.
RefSeqiNP_067479.2. NM_021504.3.
UniGeneiMm.258381.

Genome annotation databases

EnsembliENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785.
GeneIDi59007.
KEGGimmu:59007.
UCSCiuc007sgz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250927 mRNA. Translation: AAF74723.1.
AY225417 Genomic DNA. Translation: AAP03060.1.
AK003279 mRNA. Translation: BAB22686.1.
AK028248 mRNA. Translation: BAC25839.1.
BC028961 mRNA. Translation: AAH28961.1.
CCDSiCCDS26832.1.
RefSeqiNP_067479.2. NM_021504.3.
UniGeneiMm.258381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5UNMR-A1-119[»]
2F4MX-ray1.85A164-450[»]
2F4OX-ray2.26A164-450[»]
2G9FX-ray1.90A451-651[»]
2G9GX-ray2.00A451-651[»]
2HPJX-ray1.70A12-110[»]
2HPLX-ray1.80A12-111[»]
2I74X-ray1.75A/B471-651[»]
ProteinModelPortaliQ9JI78.
SMRiQ9JI78. Positions 12-110, 164-450, 472-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208478. 7 interactions.
DIPiDIP-41155N.
IntActiQ9JI78. 5 interactions.
MINTiMINT-214719.
STRINGi10090.ENSMUSP00000022310.

PTM databases

iPTMnetiQ9JI78.
PhosphoSiteiQ9JI78.

Proteomic databases

EPDiQ9JI78.
MaxQBiQ9JI78.
PaxDbiQ9JI78.
PRIDEiQ9JI78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785.
GeneIDi59007.
KEGGimmu:59007.
UCSCiuc007sgz.1. mouse.

Organism-specific databases

CTDi55768.
MGIiMGI:1913276. Ngly1.

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
GeneTreeiENSGT00390000006540.
HOGENOMiHOG000247069.
HOVERGENiHBG082026.
InParanoidiQ9JI78.
KOiK01456.
OMAiRVEDHYC.
OrthoDBiEOG780RMR.
PhylomeDBiQ9JI78.
TreeFamiTF315254.

Enzyme and pathway databases

BRENDAi3.5.1.52. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9JI78.
NextBioi314538.
PROiQ9JI78.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JI78.
CleanExiMM_NGLY1.
GenevisibleiQ9JI78. MM.

Family and domain databases

InterProiIPR008979. Galactose-bd-like.
IPR006588. Peptide_N_glycanase_PAW_dom.
IPR018997. PUB_domain.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF04721. PAW. 1 hit.
PF09409. PUB. 1 hit.
PF01841. Transglut_core. 1 hit.
[Graphical view]
SMARTiSM00613. PAW. 1 hit.
SM00580. PUG. 1 hit.
SM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS51398. PAW. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase."
    Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.
    J. Cell Biol. 149:1039-1052(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Ngly1, a mouse gene encoding a deglycosylating enzyme implicated in proteasomal degradation: expression, genomic organization, and chromosomal mapping."
    Suzuki T., Kwofie M.A., Lennarz W.J.
    Biochem. Biophys. Res. Commun. 304:326-332(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  4. "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: Eye.
  5. "Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation."
    Suzuki T., Seko A., Kitajima K., Inoue Y., Inoue S.
    J. Biol. Chem. 269:17611-17618(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation."
    Park H., Suzuki T., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:11163-11168(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAD23B; PSMC1 AND SAKS1.
  7. "A role for N-glycanase in the cytosolic turnover of glycoproteins."
    Hirsch C., Blom D., Ploegh H.L.
    EMBO J. 22:1036-1046(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-306.
  8. "Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover."
    Misaghi S., Pacold M.E., Blom D., Ploegh H.L., Korbel G.A.
    Chem. Biol. 11:1677-1687(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins."
    Katiyar S., Li G., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD23B AND PSMC1.
  10. "The retrotranslocation protein derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum."
    Katiyar S., Joshi S., Lennarz W.J.
    Mol. Biol. Cell 16:4584-4594(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DERL1.
  11. "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome."
    Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMC1; RAD23B AND VCP.
  12. Erratum
    Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006)
  13. "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor."
    Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMFR; PSMC1; SAKS1; RAD23B AND VCP, DOMAIN, MUTAGENESIS OF ASN-41; ASN-58 AND 79-GLY-PHE-80.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  15. "Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways."
    Zhao G., Zhou X., Wang L., Li G., Kisker C., Lennarz W.J., Schindelin H.
    J. Biol. Chem. 281:13751-13761(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 164-450 IN COMPLEX WITH RAD23 AND Z-VAD-FMK, COFACTOR, ZINC-BINDING.

Entry informationi

Entry nameiNGLY1_MOUSE
AccessioniPrimary (citable) accession number: Q9JI78
Secondary accession number(s): Q8K113, Q9CTK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.