JPH1_HUMAN
ID JPH1_HUMAN Reviewed; 661 AA.
AC Q9HDC5; B2RTZ0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Junctophilin-1;
DE Short=JP-1;
DE AltName: Full=Junctophilin type 1;
GN Name=JPH1; Synonyms=JP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 421-661, AND TISSUE SPECIFICITY.
RX PubMed=10891348; DOI=10.1006/bbrc.2000.3011;
RA Nishi M., Mizushima A., Nakagawara K., Takeshima H.;
RT "Characterization of human junctophilin subtype genes.";
RL Biochem. Biophys. Res. Commun. 273:920-927(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-448; SER-452;
RP THR-461; SER-465 AND SER-469, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-220 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; THR-448; THR-461;
RP SER-465 AND SER-469, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Junctophilins contribute to the formation of junctional
CC membrane complexes (JMCs) which link the plasma membrane with the
CC endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a
CC structural foundation for functional cross-talk between the cell
CC surface and intracellular calcium release channels. JPH1 contributes to
CC the construction of the skeletal muscle triad by linking the t-tubule
CC (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
CC -!- INTERACTION:
CC Q9HDC5; Q13520: AQP6; NbExp=3; IntAct=EBI-465137, EBI-13059134;
CC Q9HDC5; P56851: EDDM3B; NbExp=3; IntAct=EBI-465137, EBI-10215665;
CC Q9HDC5; P54849: EMP1; NbExp=3; IntAct=EBI-465137, EBI-4319440;
CC Q9HDC5; O15529: GPR42; NbExp=3; IntAct=EBI-465137, EBI-18076404;
CC Q9HDC5; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-465137, EBI-12937691;
CC Q9HDC5; O95214: LEPROTL1; NbExp=3; IntAct=EBI-465137, EBI-750776;
CC Q9HDC5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-465137, EBI-16439278;
CC Q9HDC5; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-465137, EBI-2863634;
CC Q9HDC5; P60201-2: PLP1; NbExp=3; IntAct=EBI-465137, EBI-12188331;
CC Q9HDC5; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-465137, EBI-12243266;
CC Q9HDC5; P0DN84: STRIT1; NbExp=3; IntAct=EBI-465137, EBI-12200293;
CC Q9HDC5; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-465137, EBI-10171534;
CC Q9HDC5; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-465137, EBI-6656213;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}. Sarcoplasmic
CC reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein
CC {ECO:0000250}. Note=Localized predominantly on the plasma membrane. The
CC transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum
CC membrane, while the N-terminal part associates with the plasma
CC membrane. In skeletal muscle cells, it is predominantly localized at
CC the junction of the A and I bands (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle. Very low
CC levels in heart. {ECO:0000269|PubMed:10891348}.
CC -!- DOMAIN: The MORN (membrane occupation and recognition nexus) repeats
CC contribute to the plasma membrane binding, possibly by interacting with
CC phospholipids. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
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DR EMBL; AF110324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87029.1; -; Genomic_DNA.
DR EMBL; BC140875; AAI40876.1; -; mRNA.
DR EMBL; BC140876; AAI40877.1; -; mRNA.
DR EMBL; AB042635; BAB11986.1; -; Genomic_DNA.
DR CCDS; CCDS6217.1; -.
DR RefSeq; NP_001304759.1; NM_001317830.1.
DR RefSeq; NP_065698.1; NM_020647.3.
DR RefSeq; XP_005251331.1; XM_005251274.3.
DR RefSeq; XP_005251332.1; XM_005251275.4.
DR PDB; 7RW4; X-ray; 1.31 A; A=1-442.
DR PDBsum; 7RW4; -.
DR AlphaFoldDB; Q9HDC5; -.
DR SMR; Q9HDC5; -.
DR BioGRID; 121191; 215.
DR IntAct; Q9HDC5; 68.
DR MINT; Q9HDC5; -.
DR STRING; 9606.ENSP00000344488; -.
DR TCDB; 8.A.110.1.1; the junctophilin (jp) family.
DR CarbonylDB; Q9HDC5; -.
DR iPTMnet; Q9HDC5; -.
DR PhosphoSitePlus; Q9HDC5; -.
DR BioMuta; JPH1; -.
DR DMDM; 27805492; -.
DR EPD; Q9HDC5; -.
DR jPOST; Q9HDC5; -.
DR MassIVE; Q9HDC5; -.
DR MaxQB; Q9HDC5; -.
DR PaxDb; Q9HDC5; -.
DR PeptideAtlas; Q9HDC5; -.
DR PRIDE; Q9HDC5; -.
DR ProteomicsDB; 81850; -.
DR Antibodypedia; 2291; 157 antibodies from 27 providers.
DR DNASU; 56704; -.
DR Ensembl; ENST00000342232.5; ENSP00000344488.4; ENSG00000104369.5.
DR GeneID; 56704; -.
DR KEGG; hsa:56704; -.
DR MANE-Select; ENST00000342232.5; ENSP00000344488.4; NM_020647.4; NP_065698.1.
DR UCSC; uc003yae.4; human.
DR CTD; 56704; -.
DR DisGeNET; 56704; -.
DR GeneCards; JPH1; -.
DR HGNC; HGNC:14201; JPH1.
DR HPA; ENSG00000104369; Group enriched (skeletal muscle, tongue).
DR MalaCards; JPH1; -.
DR MIM; 605266; gene.
DR neXtProt; NX_Q9HDC5; -.
DR OpenTargets; ENSG00000104369; -.
DR PharmGKB; PA29998; -.
DR VEuPathDB; HostDB:ENSG00000104369; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000156130; -.
DR HOGENOM; CLU_008078_1_0_1; -.
DR InParanoid; Q9HDC5; -.
DR OMA; ASQSACQ; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q9HDC5; -.
DR TreeFam; TF317210; -.
DR PathwayCommons; Q9HDC5; -.
DR SignaLink; Q9HDC5; -.
DR BioGRID-ORCS; 56704; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; JPH1; human.
DR GeneWiki; JPH1; -.
DR GenomeRNAi; 56704; -.
DR Pharos; Q9HDC5; Tbio.
DR PRO; PR:Q9HDC5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9HDC5; protein.
DR Bgee; ENSG00000104369; Expressed in quadriceps femoris and 144 other tissues.
DR ExpressionAtlas; Q9HDC5; baseline and differential.
DR Genevisible; Q9HDC5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030314; C:junctional membrane complex; IBA:GO_Central.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; TAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR GO; GO:0060402; P:calcium ion transport into cytosol; TAS:BHF-UCL.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
DR InterPro; IPR017191; Junctophilin.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR23085; PTHR23085; 1.
DR Pfam; PF02493; MORN; 8.
DR PIRSF; PIRSF037387; Junctophilin; 1.
DR SMART; SM00698; MORN; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..661
FT /note="Junctophilin-1"
FT /id="PRO_0000159844"
FT TOPO_DOM 1..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REPEAT 14..36
FT /note="MORN 1"
FT REPEAT 38..59
FT /note="MORN 2"
FT REPEAT 60..82
FT /note="MORN 3"
FT REPEAT 106..128
FT /note="MORN 4"
FT REPEAT 129..151
FT /note="MORN 5"
FT REPEAT 281..303
FT /note="MORN 6"
FT REPEAT 304..326
FT /note="MORN 7"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 507
FT /note="T -> M (in dbSNP:rs16938829)"
FT /id="VAR_053445"
FT VARIANT 624
FT /note="D -> H (in dbSNP:rs16938828)"
FT /id="VAR_053446"
SQ SEQUENCE 661 AA; 71686 MW; D54DC069174F25B2 CRC64;
MTGGRFDFDD GGTYCGGWEE GKAHGHGICT GPKGQGEYSG SWSHGFEVVG GYTWPSGNTY
QGYWAQGKRH GLGVETKGKW MYRGEWSHGF KGRYGVRQSL CTPARYEGTW SNGLQDGYGV
ETYGDGGTYQ GQWAGGMRHG YGVRQSVPYG MATVIRSPLR TSLASLRSEQ SNGSVLHDAA
AAADSPAGTR GGFVLNFHAD AELAGKKKGG LFRRGSLLGS MKLRKSESKS SISSKRSSVR
SDAAMSRISS SDANSTISFG DVDCDFCPVE DHVDATTTET YMGEWKNDKR NGFGVSERSN
GMKYEGEWAN NKRHGYGCTV FPDGSKEEGK YKNNILVRGI RKQLIPIRHT KTREKVDRAI
EGAQRAAAMA RTKVEIANSR TAHARAKADA ADQAALAARQ ECDIARAVAR ELSPDFYQPG
PDYVKQRFQE GVDAKENPEE KVPEKPPTPK ESPHFYRKGT TPPRSPEASP KHSHSPASSP
KPLKKQNPSS GARLNQDKRS VADEQVTAIV NKPLMSKAPT KEAGAVVPQS KYSGRHHIPN
PSNGELHSQY HGYYVKLNAP QHPPVDVEDG DGSSQSSSAL VHKPSANKWS PSKSVTKPVA
KESKAEPKAK KSELAIPKNP ASNDSCPALE KEANSGPNSI MIVLVMLLNI GLAILFVHFL
T
