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Protein

Junctophilin-2

Gene

Jph2

Organism
Mus musculus (Mouse)
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.3 Publications

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:Jph2
Synonyms:Jp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1891496. Jph2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 674674CytoplasmicSequence analysisAdd
BLAST
Transmembranei675 – 69521Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • junctional membrane complex Source: UniProtKB
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
  • sarcoplasmic reticulum Source: MGI
  • sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Null mice possess cardiomyocytes with deficiences in the junctional membrane complexes and have abnormal Ca2+ transients. Mice die from cardiac arrest at E10.5.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 696696Junctophilin-2PRO_0000159848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity
Modified residuei442 – 4421PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei470 – 4701PhosphothreonineCombined sources
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei483 – 4831PhosphothreonineCombined sources
Modified residuei527 – 5271PhosphoserineBy similarity
Modified residuei533 – 5331PhosphoserineBy similarity
Modified residuei593 – 5931PhosphoserineCombined sources
Modified residuei597 – 5971PhosphoserineCombined sources
Modified residuei613 – 6131PhosphoserineCombined sources

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

MaxQBiQ9ET78.
PaxDbiQ9ET78.
PRIDEiQ9ET78.

PTM databases

iPTMnetiQ9ET78.
PhosphoSiteiQ9ET78.

Expressioni

Tissue specificityi

Abundantly expressed in skeletal muscle and heart. Weak expression in stomach and lung.1 Publication

Developmental stagei

At E9.5, it is expressed in the periphery of cardiac myocytes in the looped cardiac tube of the developing heart. In skeletal muscle, expression increases during muscle maturation.

Gene expression databases

BgeeiQ9ET78.
CleanExiMM_JPH2.
GenevisibleiQ9ET78. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TRPC3G1U2U34EBI-8350389,EBI-10055313From a different organism.

Protein-protein interaction databases

BioGridi208526. 1 interaction.
IntActiQ9ET78. 4 interactions.
MINTiMINT-4099221.
STRINGi10090.ENSMUSP00000017961.

Structurei

3D structure databases

ProteinModelPortaliQ9ET78.
SMRiQ9ET78. Positions 24-146, 284-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 142140Gly-richAdd
BLAST
Compositional biasi367 – 40236Ala-richAdd
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.Curated
Contains 8 MORN repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9ET78.
KOiK19530.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ9ET78.
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.

Q9ET78-1 [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 AADGPMLPSP PVPRGGFALT
210 220 230 240 250
LLATAEAARP QGLFTRGTLL 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
LKSSKVRQKV EHGVEGAQRA AAIARQKAEI AASRTSHAKA KAEAAEQAAL
410 420 430 440 450
AANQESNIAR TLAKELAPDF YQPGPEYQKR RLLQEILENS ESLLEPPERG
460 470 480 490 500
LGTGLPERPR ESPQLHERET PQPEGGPPSP AGTPPQPKRP RPGASKDGLL
510 520 530 540 550
SPGSWNGEPG GEGSRPATPS DGAGRRSPAR PASEHMAIEA LQPPPAPSQE
560 570 580 590 600
PEVAMYRGYH SYAVRTGPPE PPPLEDEQEP EPEPEPEVRR SDSAPPSPVS
610 620 630 640 650
ATVPEEEPPA PRSPVPAKQA TLEPKPIVPK AEPKAKARKT EARGLSKAGA
660 670 680 690
KKKGRKEVAQ AKEAEVEVEE VPNTVLICMV ILLNIGLAIL FVHLLT
Length:696
Mass (Da):74,692
Last modified:January 17, 2003 - v2
Checksum:i346BA284E076A7FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024447 mRNA. Translation: BAB12044.1.
AB024448 Genomic DNA. Translation: BAB12045.1.
AK157145 mRNA. Translation: BAE33978.1.
AL589876 Genomic DNA. Translation: CAM13817.1.
CCDSiCCDS17008.1.
RefSeqiNP_001192005.1. NM_001205076.1.
NP_067541.1. NM_021566.2.
XP_006500035.1. XM_006499972.1.
UniGeneiMm.34459.

Genome annotation databases

EnsembliENSMUST00000017961; ENSMUSP00000017961; ENSMUSG00000017817.
ENSMUST00000109425; ENSMUSP00000105052; ENSMUSG00000017817.
GeneIDi59091.
KEGGimmu:59091.
UCSCiuc008nsp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024447 mRNA. Translation: BAB12044.1.
AB024448 Genomic DNA. Translation: BAB12045.1.
AK157145 mRNA. Translation: BAE33978.1.
AL589876 Genomic DNA. Translation: CAM13817.1.
CCDSiCCDS17008.1.
RefSeqiNP_001192005.1. NM_001205076.1.
NP_067541.1. NM_021566.2.
XP_006500035.1. XM_006499972.1.
UniGeneiMm.34459.

3D structure databases

ProteinModelPortaliQ9ET78.
SMRiQ9ET78. Positions 24-146, 284-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208526. 1 interaction.
IntActiQ9ET78. 4 interactions.
MINTiMINT-4099221.
STRINGi10090.ENSMUSP00000017961.

PTM databases

iPTMnetiQ9ET78.
PhosphoSiteiQ9ET78.

Proteomic databases

MaxQBiQ9ET78.
PaxDbiQ9ET78.
PRIDEiQ9ET78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017961; ENSMUSP00000017961; ENSMUSG00000017817.
ENSMUST00000109425; ENSMUSP00000105052; ENSMUSG00000017817.
GeneIDi59091.
KEGGimmu:59091.
UCSCiuc008nsp.2. mouse.

Organism-specific databases

CTDi57158.
MGIiMGI:1891496. Jph2.

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9ET78.
KOiK19530.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ9ET78.
TreeFamiTF317210.

Miscellaneous databases

NextBioi314738.
PROiQ9ET78.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ET78.
CleanExiMM_JPH2.
GenevisibleiQ9ET78. MM.

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. "Junctophilins: a novel family of junctional membrane complex proteins."
    Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.
    Mol. Cell 6:11-22(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
    Strain: 129 and C57BL/6J.
    Tissue: Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "New molecular components supporting ryanodine receptor-mediated Ca(2+) release: roles of junctophilin and TRIC channel in embryonic cardiomyocytes."
    Yamazaki D., Yamazaki T., Takeshima H.
    Pharmacol. Ther. 121:265-272(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; THR-470; SER-479; THR-483; SER-593; SER-597 AND SER-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.
  6. "Disrupted junctional membrane complexes and hyperactive ryanodine receptors after acute junctophilin knockdown in mice."
    van Oort R.J., Garbino A., Wang W., Dixit S.S., Landstrom A.P., Gaur N., De Almeida A.C., Skapura D.G., Rudy Y., Burns A.R., Ackerman M.J., Wehrens X.H.
    Circulation 123:979-988(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.

Entry informationi

Entry nameiJPH2_MOUSE
AccessioniPrimary (citable) accession number: Q9ET78
Secondary accession number(s): Q3U077, Q9ET79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 17, 2003
Last modified: May 11, 2016
This is version 122 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.