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Protein

Junctophilin-2

Gene

Jph2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH2 is 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Junctophilin-2
Short name:
JP-2
Alternative name(s):
Junctophilin type 2
Gene namesi
Name:Jph2Imported
Synonyms:Jp2By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1305196. Jph2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 670670CytoplasmicSequence analysisAdd
BLAST
Transmembranei671 – 69121Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 692692Junctophilin-2PRO_0000259403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei442 – 4421PhosphoserineCombined sources
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei470 – 4701PhosphothreonineBy similarity
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei483 – 4831PhosphothreonineCombined sources
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei533 – 5331PhosphoserineCombined sources
Modified residuei589 – 5891PhosphoserineBy similarity
Modified residuei593 – 5931PhosphoserineCombined sources
Modified residuei604 – 6041PhosphoserineCombined sources
Modified residuei609 – 6091PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated calcium ion release, interaction with TRPC3, and skeletal muscle myotubule development.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2PS20.
PRIDEiQ2PS20.

PTM databases

iPTMnetiQ2PS20.
PhosphoSiteiQ2PS20.

Interactioni

Protein-protein interaction databases

IntActiQ2PS20. 2 interactions.
STRINGi10116.ENSRNOP00000010938.

Structurei

3D structure databases

ProteinModelPortaliQ2PS20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati14 – 3623MORN 1Sequence analysisAdd
BLAST
Repeati38 – 5922MORN 2Sequence analysisAdd
BLAST
Repeati60 – 7920MORN 3Sequence analysisAdd
BLAST
Repeati82 – 10423MORN 4Sequence analysisAdd
BLAST
Repeati106 – 12823MORN 5Sequence analysisAdd
BLAST
Repeati129 – 15123MORN 6Sequence analysisAdd
BLAST
Repeati285 – 30723MORN 7Sequence analysisAdd
BLAST
Repeati308 – 33023MORN 8Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 142140Gly-richSequence analysisAdd
BLAST
Compositional biasi367 – 40236Ala-richSequence analysisAdd
BLAST
Compositional biasi446 – 629184Pro-richSequence analysisAdd
BLAST

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).By similarity

Sequence similaritiesi

Belongs to the junctophilin family.Sequence analysis
Contains 8 MORN repeats.Sequence analysis

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ2PS20.
KOiK19530.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ2PS20.
TreeFamiTF317210.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 8 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:iB24055782462322F
GO

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_006235526.2.
UniGeneiRn.6206.

Genome annotation databases

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

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_006235526.2.
UniGeneiRn.6206.

3D structure databases

ProteinModelPortaliQ2PS20.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ2PS20. 2 interactions.
STRINGi10116.ENSRNOP00000010938.

PTM databases

iPTMnetiQ2PS20.
PhosphoSiteiQ2PS20.

Proteomic databases

PaxDbiQ2PS20.
PRIDEiQ2PS20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi57158.
RGDi1305196. Jph2.

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ2PS20.
KOiK19530.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ2PS20.
TreeFamiTF317210.

Miscellaneous databases

PROiQ2PS20.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 8 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cloning of rat junctophilin-2 coding sequence."
    Bai Z., Geng X., Bi Q., Wang S.
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-DawleyImported.
    Tissue: HeartImported.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-440; SER-442; SER-462; SER-479; THR-483; SER-527; SER-533; SER-593 AND SER-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJPH2_RAT
AccessioniPrimary (citable) accession number: Q2PS20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 24, 2006
Last modified: June 8, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.