Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 138 (13 Feb 2019)
Sequence version 2 (01 Oct 1994)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Progranulin

Gene

Grn

Organism
Mus musculus (Mouse)
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

Secreted proteins that act as key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (PubMed:28073925, PubMed:8496151, PubMed:28541286, PubMed:28453791, PubMed:20026663, PubMed:23041626, PubMed:27789271, PubMed:12524533). Functions as regulator of proteins trafficking to lysosome and activity of lysosomal enzymes (PubMed:28453791, PubMed:28541286, PubMed:27789271). Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB (PubMed:28073925). In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structure (PubMed:12524533). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (PubMed:8496151). Moreover, modulates inflammation in neuron by preserving neuron survival, axonal outgrowth and neuronal integrity (PubMed:23041626, PubMed:20026663).8 Publications
Granulin-3: Inhibits epithelial cell proliferation and induces epithelial cells to secrete IL-8.By similarity
Granulin-7: Stabilizes CTSD through interaction with CTSD leading to maintain its aspartic-type peptidase activity.By similarity

<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

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 functionCytokine

<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:
Progranulin1 Publication
Short name:
PGRNBy similarity
Alternative name(s):
Acrogranin1 Publication
Epithelin/granulin precursor1 Publication
Glycoprotein of 88 Kda1 Publication
Short name:
GP88
Short name:
Glycoprotein 88
PC cell-derived growth factor1 Publication
Short name:
PCDGF1 Publication
Proepithelin1 Publication
Short name:
PEPIBy similarity
Cleaved into the following 8 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:Grn
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95832 Grn

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome, Secreted

<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

Young-adult Grn knockout mice are healthy and fertile, grow normally and show no abnormalities in hematogram or serum chemistries. However mice show an exaggerated inflammation, impaired host defense, and neuropathology (PubMed:20026663). Grn knockout mice displays a neuronal outgrowth deficit. Conditional knockout Grn mice in neuron show a significant delay in axonal regrowth and functional recovery after crush (PubMed:28453791). Grn knockout mice show an increase neuron death and microglial activation upon central nervous system injury (CNS). Conditional knockout Grn mice exibit a reduction in dopaminergic neurons and increased microgliosis after CNS injury (PubMed:23041626).3 Publications

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 171 PublicationAdd BLAST17
<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_000001270218 – 589ParagranulinAdd BLAST572
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000044633118 – 47ParagranulinBy similarityAdd BLAST30
PeptideiPRO_0000012703?58 – ?113Granulin-1Add BLAST56
PeptideiPRO_0000012704?122 – ?178Granulin-2Add BLAST57
PeptideiPRO_0000012705205 – 260Granulin-3Add BLAST56
PeptideiPRO_0000012706280 – 334Granulin-4Add BLAST55
PeptideiPRO_0000012707362 – ?414Granulin-5Add BLAST53
PeptideiPRO_0000012708440 – ?493Granulin-6Add BLAST54
PeptideiPRO_0000012709?517 – ?568Granulin-7Add BLAST52

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>Glycosylationi38N-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 bondi125 ↔ 138By similarity
Disulfide bondi132 ↔ 148By similarity
Glycosylationi263N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi282 ↔ 294By similarity
Disulfide bondi288 ↔ 304By similarity
Disulfide bondi295 ↔ 312By similarity
Disulfide bondi305 ↔ 319By similarity
Disulfide bondi313 ↔ 326By similarity
Disulfide bondi320 ↔ 333By similarity
Disulfide bondi364 ↔ 376By similarity
Disulfide bondi370 ↔ 386By similarity
Glycosylationi373N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi395 ↔ 408By similarity
Disulfide bondi402 ↔ 414By similarity
Glycosylationi526N-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

N-glycosylated.1 Publication
Cleaved by ELANE; proteolysis is blocked by SLPI and is concentration- and time-dependent and induces CXCL8/IL-8 production; granulin-3 and granulin-4 are resistant to ELANE (By similarity). Cleaved by CTSL in lysosome thus regulating the maturation and turnover of progranulin within the lysosome (PubMed:28835281).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P28798

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P28798

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P28798

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

More...
PaxDbi
P28798

PeptideAtlas

More...
PeptideAtlasi
P28798

PRoteomics IDEntifications database

More...
PRIDEi
P28798

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28798

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P28798

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed at the wound site and diminishes away from the wound. Not expressed in fibroblasts and endothelial cells in intact skin (PubMed:12524533). In adult brain, expressed primarily in neurons and in resting and reactive microglia (PubMed:23041626). Expressed in both neurons and microglia. Highly expressed in activated microglia in response to injury (PubMed:28541286). Expressed in macrophage (PubMed:27789271).4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Injury-stimulated induction in the fibroblasts and endothelial cells and by inflammatory cells entering the wound (PubMed:12524533). Injury-stimulated induction in neurons (PubMed:28453791). Strongly induced in activated microglial cells that surround motor neurons after peripheral axonal injury, but not by astrocytes (PubMed:21092856). Up-regulated in response to a cortical injury. Up-regulated in activated glia during normal aging (PubMed:28541286). Induced in response to inflammation (PubMed:27789271).5 Publications

<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

Progranulin is secreted as a homodimer (By similarity). Interacts with SLPI; interaction protects progranulin from proteolysis (PubMed:12526812). Interacts (via region corresponding to granulin-7 peptide) with CTSD; stabilizes CTSD and increases its proteolytic activity. Interacts (via region corresponding to granulin-7 peptide) with SORT1; this interaction mediates endocytosis and lysosome delivrery of progranulin; interaction occurs at the neuronal cell surface in a stressed nervous system (By similarity). Interacts with PSAP; facilitates lysosomal delivery of progranulin from the extracellular space and the biosynthetic pathway (PubMed:26370502). Forms a complex with PSAP and M6PR; PSAP bridges the binding between progranulin and M6PR. Forms a complex with PSAP and SORT1; progranulin bridges the interaction between PSAP and SORT1; facilitates lysosomal targeting of PSAP via SORT1; interaction enhances PSAP uptake in primary cortical neurons (By similarity). Interacts (via regions corresponding to granulin-2 and granulin-7 peptides) with GBA; this interaction prevents aggregation of GBA-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271). Interacts (via region corresponding to granulin-7 peptide) with HSPA1A; mediates recruitment of HSPA1A to GBA and prevents GBA aggregation in response to stress (By similarity).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P28798, 7 interactors

Molecular INTeraction database

More...
MINTi
P28798

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000046340

<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
P28798

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

More...
SMRi
P28798

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

<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 granulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4296 Eukaryota
ENOG410XR6S LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000845

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28798

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.500, 7 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000118 Granulin
IPR039036 Granulin_fam
IPR037277 Granulin_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12274 PTHR12274, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00396 Granulin, 7 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00277 GRAN, 7 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00799 GRANULINS, 7 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 4 potential isoforms that are computationally mapped.Show allAlign All

P28798-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWVLMSWLAF AAGLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP
60 70 80 90 100
RITSHHLDGS CQTHGHCPAG YSCLLTVSGT SSCCPFSKGV SCGDGYHCCP
110 120 130 140 150
QGFHCSADGK SCFQMSDNPL GAVQCPGSQF ECPDSATCCI MVDGSWGCCP
160 170 180 190 200
MPQASCCEDR VHCCPHGASC DLVHTRCVSP TGTHTLLKKF PAQKTNRAVS
210 220 230 240 250
LPFSVVCPDA KTQCPDDSTC CELPTGKYGC CPMPNAICCS DHLHCCPQDT
260 270 280 290 300
VCDLIQSKCL SKNYTTDLLT KLPGYPVKEV KCDMEVSCPE GYTCCRLNTG
310 320 330 340 350
AWGCCPFAKA VCCEDHIHCC PAGFQCHTEK GTCEMGILQV PWMKKVIAPL
360 370 380 390 400
RLPDPQILKS DTPCDDFTRC PTNNTCCKLN SGDWGCCPIP EAVCCSDNQH
410 420 430 440 450
CCPQGFTCLA QGYCQKGDTM VAGLEKIPAR QTTPLQIGDI GCDQHTSCPV
460 470 480 490 500
GQTCCPSLKG SWACCQLPHA VCCEDRQHCC PAGYTCNVKA RTCEKDVDFI
510 520 530 540 550
QPPVLLTLGP KVGNVECGEG HFCHDNQTCC KDSAGVWACC PYLKGVCCRD
560 570 580
GRHCCPGGFH CSARGTKCLR KKIPRWDMFL RDPVPRPLL
Length:589
Mass (Da):63,458
Last modified:October 1, 1994 - v2
<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:i1DE8229C413CB787
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U9N4Q3U9N4_MOUSE
Progranulin
Grn
602Annotation score:

Annotation score:3 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>
H3BLC9H3BLC9_MOUSE
Progranulin
Grn
214Annotation 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>
H3BJ90H3BJ90_MOUSE
Progranulin
Grn
335Annotation 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>
H3BJE0H3BJE0_MOUSE
Progranulin
Grn
247Annotation 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>

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 conflicti251V → L in AAA37191 (PubMed:8471244).Curated1
Sequence conflicti254L → V in AAA37191 (PubMed:8471244).Curated1
Sequence conflicti261 – 263SKN → YD AA sequence (PubMed:8496151).Curated3
Sequence conflicti350L → R in CAA44197 (PubMed:1618805).Curated1
Sequence conflicti402 – 403CP → SA in AAA37191 (PubMed:8471244).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D16195 Genomic DNA Translation: BAA03736.1
M86736 mRNA Translation: AAA37191.1
X62321 mRNA Translation: CAA44197.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C38128

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.1568

<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
D16195 Genomic DNA Translation: BAA03736.1
M86736 mRNA Translation: AAA37191.1
X62321 mRNA Translation: CAA44197.1
PIRiC38128
UniGeneiMm.1568

3D structure databases

ProteinModelPortaliP28798
SMRiP28798
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28798, 7 interactors
MINTiP28798
STRINGi10090.ENSMUSP00000046340

PTM databases

iPTMnetiP28798
PhosphoSitePlusiP28798

Proteomic databases

EPDiP28798
jPOSTiP28798
MaxQBiP28798
PaxDbiP28798
PeptideAtlasiP28798
PRIDEiP28798

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:95832 Grn

Phylogenomic databases

eggNOGiKOG4296 Eukaryota
ENOG410XR6S LUCA
HOVERGENiHBG000845
InParanoidiP28798

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Grn mouse

Protein Ontology

More...
PROi
PR:P28798

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

Gene3Di3.10.20.500, 7 hits
InterProiView protein in InterPro
IPR000118 Granulin
IPR039036 Granulin_fam
IPR037277 Granulin_sf
PANTHERiPTHR12274 PTHR12274, 2 hits
PfamiView protein in Pfam
PF00396 Granulin, 7 hits
SMARTiView protein in SMART
SM00277 GRAN, 7 hits
PROSITEiView protein in PROSITE
PS00799 GRANULINS, 7 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiGRN_MOUSE
<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: P28798
<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: December 1, 1992
Last sequence update: October 1, 1994
Last modified: February 13, 2019
This is version 138 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again