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Entry version 111 (13 Feb 2019)
Sequence version 1 (21 Dec 2004)
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Protein

N-acetylglucosamine-1-phosphotransferase subunits alpha/beta

Gene

gnptab

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.By similarity

Miscellaneous

Stealth proteins are part of a protein family that is conserved from bacteria to higher eukaryotes. Family members were first identified in microbes as proteins that help pathogens to elude the host innate immune system. Microbial stealth proteins are most likely involved in the biosynthesis of exopolysaccharides. Stealth proteins are predicted to function as hexose-1-phosphoryltransferases.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi454CalciumPROSITE-ProRule annotation1
Metal bindingi469CalciumPROSITE-ProRule annotation1
Metal bindingi472CalciumPROSITE-ProRule annotation1
Metal bindingi519CalciumPROSITE-ProRule annotation1
Metal bindingi534CalciumPROSITE-ProRule annotation1
Metal bindingi537CalciumPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi983 – 994PROSITE-ProRule annotationAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC:2.7.8.17By similarity)
Alternative name(s):
GlcNAc-1-phosphotransferase subunits alpha/beta
Stealth protein gnptab
UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:gnptab
Synonyms:gnpta
ORF Names:si:ch211-234f20.3, zgc:122985
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7955 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000437 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-030131-4714 gnptab

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei27 – 47HelicalSequence analysisAdd BLAST21
Transmembranei1180 – 1200HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Decreased mannose phosphorylation of lysosomal acid hydrolases, craniofacial and cardiac defects. Impaired development of pectoral fins and otic vesicles. Craniofacial defects are due to changes in the timing and localization of both type II collagen and sox9 expression, suggestive of an accelerated chondrocyte differentiation program. Increased level of active cathepsin K (ctsk) 3 days post-fertilization (dpf) because of abnormal processing and activation, leading to morphologic cartilage defects.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi447C → Y: Partial loss of function due to loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 1 Publication1
Mutagenesisi473C → S: Partial loss of function due to loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 1 Publication1
Mutagenesisi729K → N: Loss of function due to loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002278831 – 893N-acetylglucosamine-1-phosphotransferase subunit alphaAdd BLAST893
ChainiPRO_0000227884894 – 1219N-acetylglucosamine-1-phosphotransferase subunit betaAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi292N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi381N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi443 ↔ 466PROSITE-ProRule annotation
Disulfide bondi457 ↔ 473PROSITE-ProRule annotation
Glycosylationi462N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi508 ↔ 531PROSITE-ProRule annotation
Disulfide bondi522 ↔ 538PROSITE-ProRule annotation
Glycosylationi554N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi610N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi617N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi645N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi696N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi726N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi823N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi974N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1021N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1029N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1094N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The alpha- and beta-subunits are generated by a proteolytic cleavage by mbtps1 protease at the Gln-893-Asp-894 bond.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei893 – 894Cleavage; by mbtps1By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q5RGJ8

PRoteomics IDEntifications database

More...
PRIDEi
Q5RGJ8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000030153 Expressed in 28 organ(s), highest expression level in intestine

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q5RGJ8 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Hexamer of two alpha, two beta and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits.By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7955.ENSDARP00000040444

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q5RGJ8

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q5RGJ8

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati443 – 478LNR 1Add BLAST36
Repeati508 – 538LNR 2Add BLAST31
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini697 – 792DMAP-interactionAdd BLAST96
Domaini970 – 1005EF-handPROSITE-ProRule annotationAdd BLAST36

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The DMAP-interaction domain mediates substrate recognition. It specifically recognizes a conformation-dependent protein determinant present in acid hydrolases.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the stealth family.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IEF9 Eukaryota
ENOG410XYNB LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000006747

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007474

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG057712

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5RGJ8

KEGG Orthology (KO)

More...
KOi
K08239

Database of Orthologous Groups

More...
OrthoDBi
851009at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q5RGJ8

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010506 DMAP1-bd
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR035993 Notch-like_dom_sf
IPR000800 Notch_dom
IPR031358 Stealth_CR1
IPR021520 Stealth_CR2
IPR031357 Stealth_CR3
IPR031356 Stealth_CR4

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06464 DMAP_binding, 1 hit
PF00066 Notch, 2 hits
PF17101 Stealth_CR1, 1 hit
PF11380 Stealth_CR2, 1 hit
PF17102 Stealth_CR3, 1 hit
PF17103 Stealth_CR4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01137 DMAP_binding, 1 hit
SM00004 NL, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF90193 SSF90193, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS50258 LNR, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q5RGJ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLVVNSLLKL LQRQTYTCLS HRYGLYLCFG GLVLMIVSAF QFGEVVVEWS
60 70 80 90 100
RDQYHVLFDS YRDNVAGKSF QTRLCLPMPI DVVYTWVNGT DINLLKDLRA
110 120 130 140 150
VRQRLEEEQK ALRERLGKNG SEITEAPKGR PECLLSHCIM GPVLVLDPAL
160 170 180 190 200
PANITVKELP TLSAAFSSAK ELLQVAKPLH PSSSVTALLF HSHTEAEKAH
210 220 230 240 250
ADALKDLLTH SISRGYLTTD KEAPGLVRMH TLAYLSGFPA SLKETEQLRV
260 270 280 290 300
KLPAVVTSKT KKLQLYSEAS IALLHLNTAQ DFTDLTQQAK KNLTLDGKEL
310 320 330 340 350
TVSSAFLFWD LTAISQSKQD EDVSASRFED NEELRYSLRS IEKHAPWVRH
360 370 380 390 400
IFIVTNGQIP SWLNLDNPRV SVVTHQDIFQ NQTHLPTFSS PAIETHIHRI
410 420 430 440 450
PGLSQKFIYL NDDVMFGKDV WPDDFYSHSK GQKVYLTWPV PNCAEGCPGS
460 470 480 490 500
WIKDGYCDKA CNNSACDWDG GDCQGSSRFG GAGGSVIGGG QPWQFAGGLG
510 520 530 540 550
GLAGMSFCNQ GCANSWLADK FCDQACNVLA CGFDVGDCGQ DNLNQLHRIV
560 570 580 590 600
LRRNQTLYTL PQGELRPYFS FSGLANRVSE AHVADNQVLR HTSVANKWKT
610 620 630 640 650
IHLLLLPGHN ATQIHYNITF QSTDHHDFIM TFSVSVDTRE LPKSNTSTPV
660 670 680 690 700
RDKEEEPKPT VATPEPEVPF EAVPKEKQGP KVREQTHGDV QVPVLNETLL
710 720 730 740 750
PDEVKIELKK LNEKLMSGDI TIKGFNLTKA MLLEPYKEKD QFTLKHEKDK
760 770 780 790 800
EEKQKLSPVA QLQNERAAAR VKREKGENVD QLKPVAPSLV PVQIDDVTTK
810 820 830 840 850
AQSRLFNIEK PHMFHLLSNL KGNLSKERDS DSEGHLRERP TGRRLQFYSD
860 870 880 890 900
SLNRGFLPWE KRKFFQDLME EVNRLQTELQ YTADRTATGR RLQDTFADSL
910 920 930 940 950
RYVNRLLNAQ FGFTSRKVPA HMPHMIDRLI MQELQDTFPQ EFDKTSSHRV
960 970 980 990 1000
RHSEDMQFAF SYFYFLMSAV QQLNISEVFD EIDTDHSGVL SDREIRTLAT
1010 1020 1030 1040 1050
RIHELPLSLQ DLTSLEQMLI NCSKSLPSNL THLHAVSPTQ EAYYDPSMPP
1060 1070 1080 1090 1100
VTKGLVIHCK PITERIHKAF KDQNKYKFEI MGEEEIAFKM IRTNVSHVVG
1110 1120 1130 1140 1150
QLDDIRKNPR KFICLNDNID HIHKDAGTVK AVLRDFYESM FPLPSQFELP
1160 1170 1180 1190 1200
REYRNRFLHM TELQEWRIYR DKLKFWTHCV LVTLVVFTVM SFFAEQLVML
1210
KRWLFPRRRV SKDANPERV
Length:1,219
Mass (Da):138,982
Last modified:December 21, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8073242310E99C90
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G1K2J8G1K2J8_DANRE
N-acetylglucosamine-1-phosphotransf...
gnptab
1,189Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1QEV6F1QEV6_DANRE
N-acetylglucosamine-1-phosphotransf...
gnptab
327Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH92871 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti92I → T in AAH92871 (Ref. 2) Curated1
Sequence conflicti100A → V in AAH92871 (Ref. 2) Curated1
Sequence conflicti262K → Q in AAH92871 (Ref. 2) Curated1
Sequence conflicti304S → P in AAH92871 (Ref. 2) Curated1
Sequence conflicti474Q → QGTA in AAH92871 (Ref. 2) Curated1
Sequence conflicti689D → V in AAH92871 (Ref. 2) Curated1
Sequence conflicti712N → D in AAH92871 (Ref. 2) Curated1
Sequence conflicti740D → A in AAH92871 (Ref. 2) Curated1
Sequence conflicti746H → L in AAH92871 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
BX890572 Genomic DNA Translation: CAI11844.1
BC092871 mRNA Translation: AAH92871.1 Sequence problems.

NCBI Reference Sequences

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RefSeqi
NP_001038233.1, NM_001044768.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Dr.7927
Dr.87047

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSDART00000121714; ENSDARP00000106477; ENSDARG00000030153

Database of genes from NCBI RefSeq genomes

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GeneIDi
553365

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dre:553365

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX890572 Genomic DNA Translation: CAI11844.1
BC092871 mRNA Translation: AAH92871.1 Sequence problems.
RefSeqiNP_001038233.1, NM_001044768.3
UniGeneiDr.7927
Dr.87047

3D structure databases

ProteinModelPortaliQ5RGJ8
SMRiQ5RGJ8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000040444

Proteomic databases

PaxDbiQ5RGJ8
PRIDEiQ5RGJ8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000121714; ENSDARP00000106477; ENSDARG00000030153
GeneIDi553365
KEGGidre:553365

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
79158
ZFINiZDB-GENE-030131-4714 gnptab

Phylogenomic databases

eggNOGiENOG410IEF9 Eukaryota
ENOG410XYNB LUCA
GeneTreeiENSGT00390000006747
HOGENOMiHOG000007474
HOVERGENiHBG057712
InParanoidiQ5RGJ8
KOiK08239
OrthoDBi851009at2759
PhylomeDBiQ5RGJ8

Miscellaneous databases

Protein Ontology

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PROi
PR:Q5RGJ8

Gene expression databases

BgeeiENSDARG00000030153 Expressed in 28 organ(s), highest expression level in intestine
ExpressionAtlasiQ5RGJ8 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR010506 DMAP1-bd
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR035993 Notch-like_dom_sf
IPR000800 Notch_dom
IPR031358 Stealth_CR1
IPR021520 Stealth_CR2
IPR031357 Stealth_CR3
IPR031356 Stealth_CR4
PfamiView protein in Pfam
PF06464 DMAP_binding, 1 hit
PF00066 Notch, 2 hits
PF17101 Stealth_CR1, 1 hit
PF11380 Stealth_CR2, 1 hit
PF17102 Stealth_CR3, 1 hit
PF17103 Stealth_CR4, 1 hit
SMARTiView protein in SMART
SM01137 DMAP_binding, 1 hit
SM00004 NL, 2 hits
SUPFAMiSSF90193 SSF90193, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS50258 LNR, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGNPTA_DANRE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q5RGJ8
Secondary accession number(s): Q568G1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: December 21, 2004
Last modified: February 13, 2019
This is version 111 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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