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Entry version 92 (26 Feb 2020)
Sequence version 1 (24 Jan 2006)
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Protein

Junctophilin-2

Gene

Jph2

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

Membrane-binding protein that provides a structural bridge between the plasma membrane and the sarcoplasmic reticulum and is required for normal excitation-contraction coupling in cardiomyocytes. Provides a structural foundation for functional cross-talk between the cell surface and intracellular Ca2+ release channels by maintaining the 12-15 nm gap between the sarcolemma and the sarcoplasmic reticulum membranes in the cardiac dyads. Necessary for proper intracellular Ca2+ signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release. Contributes to the construction of skeletal muscle triad junctions.By similarity
Transcription repressor required to safeguard against the deleterious effects of cardiac stress. Generated following cleavage of the Junctophilin-2 chain by calpain in response to cardiac stress in cardiomyocytes. Following cleavage and release from the membrane, translocates to the nucleus, binds DNA and represses expression of genes implicated in cell growth and differentiation, hypertrophy, inflammation and fibrosis. Modifies the transcription profile and thereby attenuates pathological remodeling in response to cardiac stress. Probably acts by competing with MEF2 transcription factors and TATA-binding proteins.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 functionDevelopmental protein, DNA-binding, Repressor
Biological processTranscription, Transcription regulation

<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:
Junctophilin-2
Short name:
JP-2
Alternative name(s):
Junctophilin type 2
Cleaved into the following chain:
Junctophilin-2 N-terminal fragmentBy similarity
Short name:
JP2NTBy similarity
<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:Jph2Imported
Synonyms:Jp2By similarity
<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: Chromosome 3

Organism-specific databases

Rat genome database

More...
RGDi
1305196 Jph2

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 670CytoplasmicSequence analysisAdd BLAST670
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei671 – 691Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Nucleus, Sarcoplasmic reticulum

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002594031 – 692Junctophilin-2Add BLAST692
ChainiPRO_00004463781 – 565Junctophilin-2 N-terminal fragmentBy similarityAdd BLAST565

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei162PhosphoserineCombined sources1
Modified residuei165PhosphoserineBy similarity1
Modified residuei440PhosphoserineCombined sources1
Modified residuei442PhosphoserineCombined sources1
Modified residuei462PhosphoserineCombined sources1
Modified residuei470PhosphothreonineBy similarity1
Modified residuei479PhosphoserineCombined sources1
Modified residuei483PhosphothreonineCombined sources1
Modified residuei527PhosphoserineCombined sources1
Modified residuei533PhosphoserineCombined sources1
Modified residuei589PhosphoserineBy similarity1
Modified residuei593PhosphoserineCombined sources1
Modified residuei604PhosphoserineCombined sources1
Modified residuei609PhosphoserineBy similarity1

<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

Proteolytically cleaved by calpain in response to cardiac stress. The major cleavage site takes place at the C-terminus and leads to the release of the Junctophilin-2 N-terminal fragment chain (JP2NT).By similarity
Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated calcium ion release, interaction with TRPC3, and skeletal muscle myotubule development.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>Sitei155 – 156Cleavage; by calpainBy similarity2
Sitei201 – 202Cleavage; by calpainBy similarity2
Sitei565 – 566Cleavage; by calpainBy similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q2PS20

PRoteomics IDEntifications database

More...
PRIDEi
Q2PS20

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q2PS20

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

More...
PhosphoSitePlusi
Q2PS20

<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
ENSRNOG00000008170 Expressed in skeletal muscle tissue and 7 other tissues

<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

Interacts with TRPC3 (By similarity). Junctophilin-2 N-terminal fragment:

Interacts with MEF2C (By similarity).

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q2PS20, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000010938

<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
Q2PS20

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

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>Repeati14 – 36MORN 1Sequence analysisAdd BLAST23
Repeati38 – 59MORN 2Sequence analysisAdd BLAST22
Repeati60 – 79MORN 3Sequence analysisAdd BLAST20
Repeati82 – 104MORN 4Sequence analysisAdd BLAST23
Repeati106 – 128MORN 5Sequence analysisAdd BLAST23
Repeati129 – 151MORN 6Sequence analysisAdd BLAST23
Repeati285 – 307MORN 7Sequence analysisAdd BLAST23
Repeati308 – 330MORN 8Sequence analysisAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi345 – 359Bipartite nuclear localization signalBy similarityAdd BLAST15
Motifi488 – 492Nuclear localization signalBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi3 – 142Gly-richSequence analysisAdd BLAST140
Compositional biasi367 – 402Ala-richSequence analysisAdd BLAST36
Compositional biasi446 – 629Pro-richSequence analysisAdd BLAST184

<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 MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, by interacting with phospholipids. Has affinity for phosphatidylserine, and phosphorylated phosphatidylinositols including PtdIns3P, PtdIns4P, PtdIns5P, PtdIns(3,5)P2 and PtdIns(3,4,5)P3.By similarity
The bipartite nuclear localization signal (bNLS) and Ala-rich (alanine-rich; ARR) regions are involved in DNA-binding.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 junctophilin family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0231 Eukaryota
COG4642 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159411

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_008078_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q2PS20

KEGG Orthology (KO)

More...
KOi
K19530

Identification of Orthologs from Complete Genome Data

More...
OMAi
AWNGEPS

Database of Orthologous Groups

More...
OrthoDBi
904294at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q2PS20

TreeFam database of animal gene trees

More...
TreeFami
TF317210

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017191 Junctophilin
IPR003409 MORN

The PANTHER Classification System

More...
PANTHERi
PTHR23085 PTHR23085, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02493 MORN, 8 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037387 Junctophilin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00698 MORN, 6 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>Sequencei

<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.

Q2PS20-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGGRFDFDD GGAYCGGWEG GKAHGHGLCT GPKGQGEYSG SWNFGFEVAG
60 70 80 90 100
VYTWPSGNTF EGYWSQGKRH GLGIETKGRW LYKGEWTHGF KGRYGIRQST
110 120 130 140 150
NSGAKYEGTW NNGLQDGYGT ETYADGGTYQ GQFTNGMRHG YGVRQSVPYG
160 170 180 190 200
MAVVVRSPLR TSLSSLRSEH SNGTVAPDSP AADGPTLPLP PVPRGGFALS
210 220 230 240 250
LLATAEAARP PGLFTRGALL GRLRRSESRT SLGSQRSRLS FLKSELSSGA
260 270 280 290 300
SDAASTGSLA EGAEGPDDAA APFDADIDAT TTETYMGEWK NDKRSGFGVS
310 320 330 340 350
ERSSGLRYEG EWLDNLRHGY GRTTLPDGHR EEGKYRHNVL VKGTKRRVLP
360 370 380 390 400
LKSNKVRQKV EHGVEGAQRA AAIARQKAEI AASRTSHAKA KAEAAEQAAL
410 420 430 440 450
AANQESNIAR TLAKELAPDF YQPGPEYQKR RLLQEILENS ESLLEPRERG
460 470 480 490 500
PGTGLPERPR ESPQLHERET PQPEGGPPSP AGTPPQPKRP RPGSSKDGLL
510 520 530 540 550
SPGAWNGEPG GEGSRPATPS DGAGRRSPAR PASEHMAIEA LQPPPAPSRE
560 570 580 590 600
PEVALYRGYH SYAVRTGPPE PPPLEDEPEP EPEVPRSDSE PPSPVSATVQ
610 620 630 640 650
EEESPAPRSR VPAKPATLEP KPIVPKAEPK AKARKTEARG LSKAGAKKKG
660 670 680 690
RKEVAQEAEA EVEVEEVPNT VLICMVILLN IGLAILFVHL LT
Length:692
Mass (Da):74,259
Last modified:January 24, 2006 - 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:iB24055782462322F
GO

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
DQ304564 mRNA Translation: ABC02402.1

NCBI Reference Sequences

More...
RefSeqi
NP_001033063.1, NM_001037974.1
XP_006235588.1, XM_006235526.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000010939; ENSRNOP00000010938; ENSRNOG00000008170

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
296345

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:296345

UCSC genome browser

More...
UCSCi
RGD:1305196 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
DQ304564 mRNA Translation: ABC02402.1
RefSeqiNP_001033063.1, NM_001037974.1
XP_006235588.1, XM_006235526.3

3D structure databases

SMRiQ2PS20
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ2PS20, 2 interactors
STRINGi10116.ENSRNOP00000010938

PTM databases

iPTMnetiQ2PS20
PhosphoSitePlusiQ2PS20

Proteomic databases

PaxDbiQ2PS20
PRIDEiQ2PS20

Genome annotation databases

EnsembliENSRNOT00000010939; ENSRNOP00000010938; ENSRNOG00000008170
GeneIDi296345
KEGGirno:296345
UCSCiRGD:1305196 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
57158
RGDi1305196 Jph2

Phylogenomic databases

eggNOGiKOG0231 Eukaryota
COG4642 LUCA
GeneTreeiENSGT00940000159411
HOGENOMiCLU_008078_1_0_1
InParanoidiQ2PS20
KOiK19530
OMAiAWNGEPS
OrthoDBi904294at2759
PhylomeDBiQ2PS20
TreeFamiTF317210

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q2PS20

Gene expression databases

BgeeiENSRNOG00000008170 Expressed in skeletal muscle tissue and 7 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR017191 Junctophilin
IPR003409 MORN
PANTHERiPTHR23085 PTHR23085, 1 hit
PfamiView protein in Pfam
PF02493 MORN, 8 hits
PIRSFiPIRSF037387 Junctophilin, 1 hit
SMARTiView protein in SMART
SM00698 MORN, 6 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 nameiJPH2_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: Q2PS20
<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: October 31, 2006
Last sequence update: January 24, 2006
Last modified: February 26, 2020
This is version 92 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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