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Q9BR39

- JPH2_HUMAN

UniProt

Q9BR39 - JPH2_HUMAN

Protein

Junctophilin-2

Gene

JPH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (17 Jan 2003)
      Previous versions | rss
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    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.1 Publication

    GO - Molecular functioni

    1. calcium-release channel activity Source: UniProtKB
    2. phosphatidic acid binding Source: UniProtKB
    3. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    4. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
    5. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    6. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    7. phosphatidylinositol-4-phosphate binding Source: UniProtKB
    8. phosphatidylinositol-5-phosphate binding Source: UniProtKB
    9. phosphatidylserine binding Source: UniProtKB
    10. protein binding Source: UniProtKB

    GO - Biological processi

    1. calcium ion homeostasis Source: UniProtKB
    2. calcium ion transmembrane transport Source: GOC
    3. calcium ion transport into cytosol Source: BHF-UCL
    4. positive regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
    5. regulation of cardiac muscle tissue development Source: Ensembl
    6. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Junctophilin-2
    Short name:
    JP-2
    Alternative name(s):
    Junctophilin type 2
    Gene namesi
    Name:JPH2
    Synonyms:JP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:14202. JPH2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity. Sarcoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity
    Note: Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In heart cells, it predominantly associates along Z lines within myocytes. In skeletal muscle, it is specifically localized at the junction of A and I bands By similarity.By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. junctional membrane complex Source: Ensembl
    3. junctional sarcoplasmic reticulum membrane Source: BHF-UCL
    4. plasma membrane Source: UniProtKB-SubCell
    5. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, familial hypertrophic 17 (CMH17) [MIM:613873]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011S → R in CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis. 1 Publication
    VAR_065471
    Natural varianti141 – 1411Y → H in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. 1 Publication
    VAR_065472
    Natural varianti165 – 1651S → F in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3. 1 Publication
    VAR_065473

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi613873. phenotype.
    Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBiPA29999.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 696696Junctophilin-2PRO_0000159847Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei469 – 4691Phosphoserine1 Publication
    Modified residuei484 – 4841Phosphoserine1 Publication
    Modified residuei486 – 4861Phosphoserine1 Publication
    Modified residuei490 – 4901Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated calcium ion release, interaction with TRPC3, and skeletal muscle myotubule development.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BR39.
    PaxDbiQ9BR39.
    PRIDEiQ9BR39.

    PTM databases

    PhosphoSiteiQ9BR39.

    Expressioni

    Tissue specificityi

    Specifically expressed in skeletal muscle and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ9BR39.
    BgeeiQ9BR39.
    CleanExiHS_JPH2.
    GenevestigatoriQ9BR39.

    Organism-specific databases

    HPAiHPA052646.

    Interactioni

    Protein-protein interaction databases

    BioGridi121414. 2 interactions.
    STRINGi9606.ENSP00000362071.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BR39.
    SMRiQ9BR39. Positions 8-45, 53-144, 318-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 674674CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei675 – 69521Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    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
    Repeati291 – 31323MORN 7Add
    BLAST
    Repeati314 – 33623MORN 8Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 142140Gly-richAdd
    BLAST
    Compositional biasi373 – 40836Ala-richAdd
    BLAST
    Compositional biasi452 – 633182Pro-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.

    Sequence similaritiesi

    Belongs to the junctophilin family.Curated
    Contains 8 MORN repeats.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG324165.
    HOGENOMiHOG000264244.
    HOVERGENiHBG031648.
    InParanoidiQ9BR39.
    OMAiHERETPR.
    OrthoDBiEOG7J4463.
    PhylomeDBiQ9BR39.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BR39-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSGGRFDFDD GGAYCGGWEG GKAHGHGLCT GPKGQGEYSG SWNFGFEVAG    50
    VYTWPSGNTF EGYWSQGKRH GLGIETKGRW LYKGEWTHGF KGRYGIRQSS 100
    SSGAKYEGTW NNGLQDGYGT ETYADGGTYQ GQFTNGMRHG YGVRQSVPYG 150
    MAVVVRSPLR TSLSSLRSEH SNGTVAPDSP ASPASDGPAL PSPAIPRGGF 200
    ALSLLANAEA AARAPKGGGL FQRGALLGKL RRAESRTSVG SQRSRVSFLK 250
    SDLSSGASDA ASTASLGEAA EGADEAAPFE ADIDATTTET YMGEWKNDKR 300
    SGFGVSERSS GLRYEGEWLD NLRHGYGCTT LPDGHREEGK YRHNVLVKDT 350
    KRRMLQLKSN KVRQKVEHSV EGAQRAAAIA RQKAEIAASR TSHAKAKAEA 400
    AEQAALAANQ ESNIARTLAR ELAPDFYQPG PEYQKRRLLQ EILENSESLL 450
    EPPDRGAGAA GLPQPPRESP QLHERETPRP EGGSPSPAGT PPQPKRPRPG 500
    VSKDGLLSPG AWNGEPSGEG SRSVTPSEGA GRRSPARPAT ERMAIEALQA 550
    PPAPSREPEV ALYQGYHSYA VRTTPPEPPP FEDQPEPEVS GSESAPSSPA 600
    TAPLQAPTLR GPEPARETPA KLEPKPIIPK AEPRAKARKT EARGLTKAGA 650
    KKKARKEAAL AAEAEVEVEE VPNTILICMV ILLNIGLAIL FVHLLT 696
    Length:696
    Mass (Da):74,222
    Last modified:January 17, 2003 - v2
    Checksum:i80D62652CE48548B
    GO
    Isoform 2 (identifier: Q9BR39-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-129: TY → MC
         130-696: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:129
    Mass (Da):13,951
    Checksum:iF2008165B64B104B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011S → R in CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis. 1 Publication
    VAR_065471
    Natural varianti141 – 1411Y → H in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. 1 Publication
    VAR_065472
    Natural varianti165 – 1651S → F in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3. 1 Publication
    VAR_065473
    Natural varianti396 – 3961A → T.
    Corresponds to variant rs3810510 [ dbSNP | Ensembl ].
    VAR_053447
    Natural varianti436 – 4361R → C.1 Publication
    VAR_065474
    Natural varianti505 – 5051G → S in patients with cardiomyopathy; does not affect protein conformation as shown by circular dichroism; a patient with cardiomyopathy also carries V-26 and C-513 in MYH7. 1 Publication
    Corresponds to variant rs140740776 [ dbSNP | Ensembl ].
    VAR_065475

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 1292TY → MC in isoform 2. 1 PublicationVSP_002785
    Alternative sequencei130 – 696567Missing in isoform 2. 1 PublicationVSP_002786Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL132999 mRNA. Translation: CAB61347.1.
    AL035447, AL034419 Genomic DNA. Translation: CAI19380.1.
    AL034419, AL035447 Genomic DNA. Translation: CAI42199.1.
    AL035447 Genomic DNA. Translation: CAC18785.1.
    CH471077 Genomic DNA. Translation: EAW75940.1.
    CH471077 Genomic DNA. Translation: EAW75943.1.
    CCDSiCCDS13325.1. [Q9BR39-1]
    CCDS13326.1. [Q9BR39-2]
    RefSeqiNP_065166.2. NM_020433.4. [Q9BR39-1]
    NP_787109.2. NM_175913.3. [Q9BR39-2]
    XP_006723895.1. XM_006723832.1. [Q9BR39-1]
    UniGeneiHs.441737.

    Genome annotation databases

    EnsembliENST00000342272; ENSP00000344590; ENSG00000149596. [Q9BR39-2]
    ENST00000372980; ENSP00000362071; ENSG00000149596. [Q9BR39-1]
    GeneIDi57158.
    KEGGihsa:57158.
    UCSCiuc002xli.1. human. [Q9BR39-1]
    uc002xlj.3. human. [Q9BR39-2]

    Polymorphism databases

    DMDMi27805486.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL132999 mRNA. Translation: CAB61347.1 .
    AL035447 , AL034419 Genomic DNA. Translation: CAI19380.1 .
    AL034419 , AL035447 Genomic DNA. Translation: CAI42199.1 .
    AL035447 Genomic DNA. Translation: CAC18785.1 .
    CH471077 Genomic DNA. Translation: EAW75940.1 .
    CH471077 Genomic DNA. Translation: EAW75943.1 .
    CCDSi CCDS13325.1. [Q9BR39-1 ]
    CCDS13326.1. [Q9BR39-2 ]
    RefSeqi NP_065166.2. NM_020433.4. [Q9BR39-1 ]
    NP_787109.2. NM_175913.3. [Q9BR39-2 ]
    XP_006723895.1. XM_006723832.1. [Q9BR39-1 ]
    UniGenei Hs.441737.

    3D structure databases

    ProteinModelPortali Q9BR39.
    SMRi Q9BR39. Positions 8-45, 53-144, 318-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121414. 2 interactions.
    STRINGi 9606.ENSP00000362071.

    PTM databases

    PhosphoSitei Q9BR39.

    Polymorphism databases

    DMDMi 27805486.

    Proteomic databases

    MaxQBi Q9BR39.
    PaxDbi Q9BR39.
    PRIDEi Q9BR39.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342272 ; ENSP00000344590 ; ENSG00000149596 . [Q9BR39-2 ]
    ENST00000372980 ; ENSP00000362071 ; ENSG00000149596 . [Q9BR39-1 ]
    GeneIDi 57158.
    KEGGi hsa:57158.
    UCSCi uc002xli.1. human. [Q9BR39-1 ]
    uc002xlj.3. human. [Q9BR39-2 ]

    Organism-specific databases

    CTDi 57158.
    GeneCardsi GC20M042740.
    H-InvDB HIX0015833.
    HGNCi HGNC:14202. JPH2.
    HPAi HPA052646.
    MIMi 605267. gene.
    613873. phenotype.
    neXtProti NX_Q9BR39.
    Orphaneti 155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBi PA29999.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324165.
    HOGENOMi HOG000264244.
    HOVERGENi HBG031648.
    InParanoidi Q9BR39.
    OMAi HERETPR.
    OrthoDBi EOG7J4463.
    PhylomeDBi Q9BR39.
    TreeFami TF317210.

    Miscellaneous databases

    GeneWikii JPH2.
    GenomeRNAii 57158.
    NextBioi 63151.
    PROi Q9BR39.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BR39.
    Bgeei Q9BR39.
    CleanExi HS_JPH2.
    Genevestigatori Q9BR39.

    Family and domain databases

    InterProi IPR017191. Junctophilin.
    IPR003409. MORN.
    [Graphical view ]
    Pfami PF02493. MORN. 8 hits.
    [Graphical view ]
    PIRSFi PIRSF037387. Junctophilin. 1 hit.
    SMARTi SM00698. MORN. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Stavrides G.S., Huckle E.J., Deloukas P.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: IDENTIFICATION (ISOFORM 1), TISSUE SPECIFICITY.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-486 AND THR-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle."
      Woo J.S., Hwang J.H., Ko J.K., Weisleder N., Kim do H., Ma J., Lee E.H.
      Biochem. J. 427:125-134(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-165, INTERACTION WITH TRPC3, FUNCTION, CHARACTERIZATION OF VARIANT PHE-165.
    8. Cited for: VARIANTS CYS-436 AND SER-505, CHARACTERIZATION OF VARIANT SER-505.
    9. Cited for: VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165, CHARACTERIZATION OF VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165.
    10. "Human junctophilin-2 undergoes a structural rearrangement upon binding PtdIns(3,4,5)P3 and the S101R mutation identified in hypertrophic cardiomyopathy obviates this response."
      Bennett H.J., Davenport J.B., Collins R.F., Trafford A.W., Pinali C., Kitmitto A.
      Biochem. J. 456:205-217(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: MEMBRANE LIPID-BINDING, CHARACTERIZATION OF VARIANT CMH17 ARG-101.

    Entry informationi

    Entry nameiJPH2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BR39
    Secondary accession number(s): E1P5X1
    , O95913, Q5JY74, Q9UJN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: January 17, 2003
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3