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Entry version 131 (17 Jun 2020)
Sequence version 3 (01 Dec 1992)
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Protein

Progranulin

Gene

Grn

Organism
Rattus norvegicus (Rat)
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 protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (By similarity). Regulates protein trafficking to lysosomes and, also the activity of lysosomal enzymes (By similarity). Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB (By similarity). 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 structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (By similarity). Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity (By similarity).By similarity
Inhibits epithelial cell proliferation and induces epithelial cells to secrete IL-8.By similarity
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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-6798695 Neutrophil degranulation

<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%5Fand%5Ftaxonomy%5Fsection">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:
ProgranulinBy similarity
Short name:
PGRNBy similarity
Alternative name(s):
AcrograninBy similarity
Epithelin precursor1 Publication
Granulin precursor1 Publication
Proepithelin
Short name:
PEPIBy similarity
Cleaved into the following 8 chains:
Alternative name(s):
Granulin G
Alternative name(s):
Granulin F
Alternative name(s):
Epithelin-21 Publication
Granulin B
Alternative name(s):
Epithelin-11 Publication
Granulin A
Alternative name(s):
Granulin C
Alternative name(s):
Granulin D
Alternative name(s):
Granulin E
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

Rat genome database

More...
RGDi
61983 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 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 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001271018 – 588ProgranulinAdd BLAST571
<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_000044633218 – 47ParagranulinBy similarityAdd BLAST30
PeptideiPRO_000001271158 – 113Granulin-1Add BLAST56
PeptideiPRO_0000012712122 – 178Granulin-2Add BLAST57
PeptideiPRO_0000012713204 – 259Granulin-3Add BLAST56
PeptideiPRO_0000012714278 – 334Granulin-4Add BLAST57
PeptideiPRO_0000012715361 – 413Granulin-5Add BLAST53
PeptideiPRO_0000012716438 – 492Granulin-6Add BLAST55
PeptideiPRO_0000012717512 – 567Granulin-7Add BLAST56

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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
Disulfide bondi281 ↔ 293By similarity
Disulfide bondi287 ↔ 303By similarity
Disulfide bondi294 ↔ 311By similarity
Disulfide bondi304 ↔ 318By similarity
Disulfide bondi312 ↔ 325By similarity
Disulfide bondi319 ↔ 332By similarity
Disulfide bondi363 ↔ 375By similarity
Disulfide bondi369 ↔ 385By similarity
Glycosylationi372N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi394 ↔ 407By similarity
Disulfide bondi401 ↔ 413By similarity
Glycosylationi525N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

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. Cleaved by CTSL in lysosome thus regulating the maturation and turnover of progranulin within the lysosome.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...
PaxDbi
P23785

PRoteomics IDEntifications database

More...
PRIDEi
P23785

<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

Ubiquitous; most abundant in the spleen and several tissues of endocrine significance.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Progranulin is secreted as a homodimer.

Interacts with SLPI; interaction protects progranulin from proteolysis.

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 delivery of progranulin; interaction occurs at the neuronal cell surface in a stressed nervous system.

Interacts with PSAP; facilitates lysosomal delivery of progranulin from the extracellular space and the biosynthetic pathway.

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.

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.

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247826, 3 interactors

Protein interaction database and analysis system

More...
IntActi
P23785, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000028557

<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

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

More...
SMRi
P23785

Database of comparative protein structure models

More...
ModBasei
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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23785

KEGG Orthology (KO)

More...
KOi
K23879

Database of Orthologous Groups

More...
OrthoDBi
162721at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23785

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

P23785-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWILVSWLAL VARLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP
60 70 80 90 100
IITSRRLDGS CQIRDHCPDG YSCLLTVSGT SSCCPFSEGV SCDDGQHCCP
110 120 130 140 150
RGFHCSADGK SCSQISDSLL GAVQCPGSQF ECPDSATCCI MIDGSWGCCP
160 170 180 190 200
MPQASCCEDR VHCCPHGASC DLVHTRCISP TGTHPLLKKF PAQRTNRAVA
210 220 230 240 250
SFSVVCPDAK TQCPDDSTCC ELPTGKYGCC PMPNAICCSD HLHCCPQDTV
260 270 280 290 300
CDLIQSKCIS KDYTTDLMTK LPGYPVNEVK CDLEVSCPDG YTCCRLNTGA
310 320 330 340 350
WGCCPFTKAV CCEDHIHCCP AGFQCHTETG TCELGVLQVP WMKKVTASLS
360 370 380 390 400
LPDPQILKND VPCDDFSSCP SNNTCCRLSS GDWGCCPMPE AVCCLDHQHC
410 420 430 440 450
CPQGFKCMDE GYCQKGDRMV AGLEKMPVRQ TTLLQHGDIG CDQHTSCPVG
460 470 480 490 500
QTCCPSLKGS WACCQLPHAV CCEDRQHCCP AGYTCNVKAR TCEKDAGSVQ
510 520 530 540 550
PSMDLTFGSK VGNVECGAGH FCHDNQSCCK DSQGGWACCP YVKGVCCRDG
560 570 580
RHCCPIGFHC SAKGTKCLRK KTPRWDILLR DPAPRPLL
Length:588
Mass (Da):63,370
Last modified:December 1, 1992 - v3
<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:i113D434F7E099B31
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
G3V8V1G3V8V1_RAT
Granulin, isoform CRA_c
Grn rCG_33205
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>
F1LMP7F1LMP7_RAT
Progranulin
Grn
524Annotation 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 conflicti201S → FP in CAA44198 (PubMed:1618805).Curated1
Sequence conflicti307 – 308TK → SB AA sequence (PubMed:2268320).Curated2
Sequence conflicti324Q → T AA sequence (PubMed:2268320).Curated1
Sequence conflicti388M → I in CAA44198 (PubMed:1618805).Curated1

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
M97750 mRNA Translation: AAA16903.1
X62322 mRNA Translation: CAA44198.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B38128

NCBI Reference Sequences

More...
RefSeqi
NP_058809.2, NM_017113.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29143

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29143

UCSC genome browser

More...
UCSCi
RGD:61983 rat

<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
M97750 mRNA Translation: AAA16903.1
X62322 mRNA Translation: CAA44198.1
PIRiB38128
RefSeqiNP_058809.2, NM_017113.2

3D structure databases

SMRiP23785
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi247826, 3 interactors
IntActiP23785, 2 interactors
STRINGi10116.ENSRNOP00000028557

Proteomic databases

PaxDbiP23785
PRIDEiP23785

Genome annotation databases

GeneIDi29143
KEGGirno:29143
UCSCiRGD:61983 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2896
RGDi61983 Grn

Phylogenomic databases

eggNOGiKOG4296 Eukaryota
ENOG410XR6S LUCA
InParanoidiP23785
KOiK23879
OrthoDBi162721at2759
PhylomeDBiP23785

Enzyme and pathway databases

ReactomeiR-RNO-6798695 Neutrophil degranulation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P23785

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_RAT
<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: P23785
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 1, 1992
Last modified: June 17, 2020
This is version 131 of the entry and version 3 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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