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Protein

Mannosyl-oligosaccharide glucosidase

Gene

MOGS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the distal alpha 1,2-linked glucose residue from the Glc3Man9GlcNAc2 oligosaccharide precursor in a highly specific manner.

Catalytic activityi

Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc3Man9GlcNAc2.

Pathwayi

GO - Molecular functioni

  1. glucosidase activity Source: ProtInc
  2. mannosyl-oligosaccharide glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. oligosaccharide metabolic process Source: InterPro
  3. post-translational protein modification Source: Reactome
  4. protein folding Source: Reactome
  5. protein N-linked glycosylation Source: ProtInc
  6. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
REACT_267905. Defective MOGS causes MOGS-CDG (CDG-2b).
UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH63. Glycoside Hydrolase Family 63.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide glucosidase (EC:3.2.1.106)
Alternative name(s):
Processing A-glucosidase I
Gene namesi
Name:MOGS
Synonyms:GCS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24862. MOGS.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei39 – 5921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini60 – 837778LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. endoplasmic reticulum membrane Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Type IIb congenital disorder of glycosylation (CDGIIb)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionCharacterized by marked generalized hypotonia and hypomotility of the neonate, dysmorphic features, including a prominent occiput, short palpebral fissures, retrognathia, high arched palate, generalized edema, and hypoplastic genitalia. Symptoms of the infant included hepatomegaly, hypoventilation, feeding problems and seizures. The clinical course was progressive and the infant did not survive more than a few months.

See also OMIM:606056
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti486 – 4861R → T in CDGIIb; loss of activity. 2 Publications
VAR_018966
Natural varianti652 – 6521F → L in CDGIIb; loss of activity. 2 Publications
VAR_018967

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi606056. phenotype.
Orphaneti79330. GCS1-CDG.
PharmGKBiPA164723075.

Polymorphism and mutation databases

BioMutaiMOGS.
DMDMi116242490.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Mannosyl-oligosaccharide glucosidasePRO_0000057710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi657 – 6571N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ13724.
PaxDbiQ13724.
PeptideAtlasiQ13724.
PRIDEiQ13724.

PTM databases

PhosphoSiteiQ13724.

Expressioni

Gene expression databases

BgeeiQ13724.
ExpressionAtlasiQ13724. baseline and differential.
GenevestigatoriQ13724.

Organism-specific databases

HPAiHPA011969.

Interactioni

Protein-protein interaction databases

BioGridi113599. 26 interactions.
IntActiQ13724. 7 interactions.
MINTiMINT-1414631.
STRINGi9606.ENSP00000233616.

Structurei

3D structure databases

ProteinModelPortaliQ13724.
SMRiQ13724. Positions 94-830.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 13762Required for endoplasmic reticulum targetingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 97Endoplasmic reticulum targeting

Sequence similaritiesi

Belongs to the glycosyl hydrolase 63 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305138.
GeneTreeiENSGT00390000017452.
HOGENOMiHOG000201473.
InParanoidiQ13724.
KOiK01228.
OMAiDLRCWIA.
OrthoDBiEOG7XSTD6.
PhylomeDBiQ13724.
TreeFamiTF300749.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR004888. Glycoside_hydrolase_63.
[Graphical view]
PANTHERiPTHR10412:SF1. PTHR10412:SF1. 1 hit.
PfamiPF03200. Glyco_hydro_63. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13724-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV
60 70 80 90 100
LSLALGMSGR WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR
110 120 130 140 150
PHVYFGMKTR SPKPLLTGLM WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF
160 170 180 190 200
HDGLSFGRQH IQDGALRLTT EFVKRPGGQH GGDWSWRVTV EPQDSGTSAL
210 220 230 240 250
PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF RFTLLPPTSP
260 270 280 290 300
GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL
310 320 330 340 350
PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP
360 370 380 390 400
RLAGSLLTQA LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG
410 420 430 440 450
GIGYFYGQGL VLPDIGVEGS EQKVDPALFP PVPLFTAVPS RSFFPRGFLW
460 470 480 490 500
DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA DGWIGREQIL GDEARARVPP
510 520 530 540 550
EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR LHAWFSWLHQ
560 570 580 590 600
SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL
610 620 630 640 650
RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG
660 670 680 690 700
VFADFGNHTK AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR
710 720 730 740 750
LLDPTSSRLG PLLDILADSR HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW
760 770 780 790 800
RGAVWLNVNY LALGALHHYG HLEGPHQARA AKLHGELRAN VVGNVWRQYQ
810 820 830
ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY
Length:837
Mass (Da):91,918
Last modified:October 17, 2006 - v5
Checksum:i11C5B09301B50DEE
GO
Isoform 2 (identifier: Q13724-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Note: Gene prediction based on EST data.

Show »
Length:731
Mass (Da):80,703
Checksum:iB9B38429664731E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti330 – 3301I → F in CAA60683 (PubMed:7635146).Curated
Sequence conflicti389 – 3891V → A in CAA60683 (PubMed:7635146).Curated
Sequence conflicti605 – 6051A → G in CAA60683 (PubMed:7635146).Curated
Sequence conflicti818 – 8181Missing in CAA60683 (PubMed:7635146).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti222 – 2221G → R.
Corresponds to variant rs3213671 [ dbSNP | Ensembl ].
VAR_049233
Natural varianti236 – 2361E → Q.1 Publication
Corresponds to variant rs1063587 [ dbSNP | Ensembl ].
VAR_019361
Natural varianti239 – 2391D → N.1 Publication
Corresponds to variant rs1063588 [ dbSNP | Ensembl ].
VAR_019362
Natural varianti293 – 2931P → S.1 Publication
Corresponds to variant rs2268416 [ dbSNP | Ensembl ].
VAR_049234
Natural varianti486 – 4861R → T in CDGIIb; loss of activity. 2 Publications
VAR_018966
Natural varianti495 – 4951R → P.
Corresponds to variant rs34075781 [ dbSNP | Ensembl ].
VAR_049235
Natural varianti652 – 6521F → L in CDGIIb; loss of activity. 2 Publications
VAR_018967
Natural varianti785 – 7851G → S.
Corresponds to variant rs35533773 [ dbSNP | Ensembl ].
VAR_049236

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform 2. CuratedVSP_046921Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87237 mRNA. Translation: CAA60683.1.
AJ422288 Genomic DNA. Translation: CAD19636.1.
AK292553 mRNA. Translation: BAF85242.1.
AC005041 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99653.1.
BC117252 mRNA. Translation: AAI17253.1.
BC117250 mRNA. Translation: AAI17251.1.
CCDSiCCDS42700.1. [Q13724-1]
CCDS54370.1. [Q13724-2]
PIRiS66258.
RefSeqiNP_001139630.1. NM_001146158.1. [Q13724-2]
NP_006293.2. NM_006302.2. [Q13724-1]
UniGeneiHs.516119.

Genome annotation databases

EnsembliENST00000233616; ENSP00000233616; ENSG00000115275. [Q13724-1]
ENST00000452063; ENSP00000388201; ENSG00000115275. [Q13724-2]
GeneIDi7841.
KEGGihsa:7841.
UCSCiuc010ffh.3. human. [Q13724-1]

Polymorphism and mutation databases

BioMutaiMOGS.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87237 mRNA. Translation: CAA60683.1.
AJ422288 Genomic DNA. Translation: CAD19636.1.
AK292553 mRNA. Translation: BAF85242.1.
AC005041 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99653.1.
BC117252 mRNA. Translation: AAI17253.1.
BC117250 mRNA. Translation: AAI17251.1.
CCDSiCCDS42700.1. [Q13724-1]
CCDS54370.1. [Q13724-2]
PIRiS66258.
RefSeqiNP_001139630.1. NM_001146158.1. [Q13724-2]
NP_006293.2. NM_006302.2. [Q13724-1]
UniGeneiHs.516119.

3D structure databases

ProteinModelPortaliQ13724.
SMRiQ13724. Positions 94-830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113599. 26 interactions.
IntActiQ13724. 7 interactions.
MINTiMINT-1414631.
STRINGi9606.ENSP00000233616.

Chemistry

ChEMBLiCHEMBL4684.

Protein family/group databases

CAZyiGH63. Glycoside Hydrolase Family 63.

PTM databases

PhosphoSiteiQ13724.

Polymorphism and mutation databases

BioMutaiMOGS.
DMDMi116242490.

Proteomic databases

MaxQBiQ13724.
PaxDbiQ13724.
PeptideAtlasiQ13724.
PRIDEiQ13724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233616; ENSP00000233616; ENSG00000115275. [Q13724-1]
ENST00000452063; ENSP00000388201; ENSG00000115275. [Q13724-2]
GeneIDi7841.
KEGGihsa:7841.
UCSCiuc010ffh.3. human. [Q13724-1]

Organism-specific databases

CTDi7841.
GeneCardsiGC02M074688.
GeneReviewsiMOGS.
H-InvDBHIX0002184.
HGNCiHGNC:24862. MOGS.
HPAiHPA011969.
MIMi601336. gene.
606056. phenotype.
neXtProtiNX_Q13724.
Orphaneti79330. GCS1-CDG.
PharmGKBiPA164723075.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG305138.
GeneTreeiENSGT00390000017452.
HOGENOMiHOG000201473.
InParanoidiQ13724.
KOiK01228.
OMAiDLRCWIA.
OrthoDBiEOG7XSTD6.
PhylomeDBiQ13724.
TreeFamiTF300749.

Enzyme and pathway databases

UniPathwayiUPA00280.
ReactomeiREACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
REACT_267905. Defective MOGS causes MOGS-CDG (CDG-2b).

Miscellaneous databases

ChiTaRSiMOGS. human.
GeneWikiiGCS1.
GenomeRNAii7841.
NextBioi30249.
PROiQ13724.
SOURCEiSearch...

Gene expression databases

BgeeiQ13724.
ExpressionAtlasiQ13724. baseline and differential.
GenevestigatoriQ13724.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR004888. Glycoside_hydrolase_63.
[Graphical view]
PANTHERiPTHR10412:SF1. PTHR10412:SF1. 1 hit.
PfamiPF03200. Glyco_hydro_63. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of glucosidase I from human hippocampus."
    Kalz-Fueller B., Bieberich E., Bause E.
    Eur. J. Biochem. 231:344-351(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-236; ASN-239 AND SER-293.
    Tissue: Hippocampus.
  2. Erratum
    Kalz-Fueller B., Bieberich E., Bause E.
    Eur. J. Biochem. 249:912-912(1997)
  3. Voelker C.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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.
    , 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].
    Tissue: Testis.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: VARIANTS CDGIIB THR-486 AND LEU-652.
  11. "Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)."
    Voelker C., De Praeter C.M., Hardt B., Breuer W., Kalz-Fueller B., Van Coster R.N., Bause E.
    Glycobiology 12:473-483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS CDGIIB THR-486 AND LEU-652.

Entry informationi

Entry nameiMOGS_HUMAN
AccessioniPrimary (citable) accession number: Q13724
Secondary accession number(s): A8K938
, F5H6D0, Q17RN9, Q8TCT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 140 of the entry and version 5 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 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.