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P30626

- SORCN_HUMAN

UniProt

P30626 - SORCN_HUMAN

Protein

Sorcin

Gene

SRI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi83 – 94121CuratedAdd
    BLAST
    Calcium bindingi113 – 124122CuratedAdd
    BLAST

    GO - Molecular functioni

    1. calcium channel regulator activity Source: ProtInc
    2. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
    3. calcium ion binding Source: BHF-UCL
    4. ion channel binding Source: BHF-UCL
    5. protease binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. protein heterodimerization activity Source: BHF-UCL
    8. receptor binding Source: ProtInc

    GO - Biological processi

    1. action potential Source: ProtInc
    2. calcium ion transport Source: Ensembl
    3. cytoplasmic sequestering of transcription factor Source: Ensembl
    4. heart development Source: ProtInc
    5. intracellular sequestering of iron ion Source: ProtInc
    6. muscle organ development Source: ProtInc
    7. negative regulation of heart rate Source: BHF-UCL
    8. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    9. negative regulation of transcription regulatory region DNA binding Source: Ensembl
    10. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    11. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
    12. proteolysis Source: RefGenome
    13. regulation of calcium ion transport Source: BHF-UCL
    14. regulation of cardiac muscle cell contraction Source: BHF-UCL
    15. regulation of cell communication by electrical coupling Source: BHF-UCL
    16. regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
    17. regulation of heart contraction Source: ProtInc
    18. regulation of high voltage-gated calcium channel activity Source: BHF-UCL
    19. regulation of relaxation of muscle Source: BHF-UCL
    20. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    21. regulation of striated muscle contraction Source: ProtInc
    22. signal transduction Source: UniProtKB
    23. transport Source: ProtInc

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorcin
    Alternative name(s):
    22 kDa protein
    CP-22
    Short name:
    CP22
    V19
    Gene namesi
    Name:SRI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:11292. SRI.

    Subcellular locationi

    Cytoplasm. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: BHF-UCL
    3. endoplasmic reticulum membrane Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: BHF-UCL
    6. sarcoplasmic reticulum Source: BHF-UCL
    7. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
    8. T-tubule Source: BHF-UCL
    9. Z disc Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1121F → L: Reduces affinity for calcium 5-fold.

    Organism-specific databases

    PharmGKBiPA36117.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 198198SorcinPRO_0000073725Add
    BLAST

    Proteomic databases

    MaxQBiP30626.
    PaxDbiP30626.
    PRIDEiP30626.

    2D gel databases

    OGPiP30626.

    PTM databases

    PhosphoSiteiP30626.

    Expressioni

    Tissue specificityi

    Detected in cardiac myocytes.

    Gene expression databases

    ArrayExpressiP30626.
    BgeeiP30626.
    CleanExiHS_SRI.
    GenevestigatoriP30626.

    Organism-specific databases

    HPAiHPA019004.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with GCA, RYR2 and ANXA7.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAT3P407632EBI-750459,EBI-518675

    Protein-protein interaction databases

    BioGridi112595. 20 interactions.
    IntActiP30626. 10 interactions.
    MINTiMINT-4999795.
    STRINGi9606.ENSP00000265729.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 438
    Turni44 – 474
    Helixi51 – 6111
    Turni62 – 643
    Beta strandi65 – 684
    Helixi72 – 8211
    Beta strandi84 – 863
    Helixi92 – 11019
    Beta strandi118 – 1203
    Helixi122 – 13110
    Helixi138 – 14710
    Beta strandi150 – 1556
    Helixi156 – 17520
    Helixi178 – 1803
    Beta strandi182 – 1876
    Helixi188 – 1958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JUOX-ray2.20A/B1-198[»]
    2JC2X-ray2.50A/B/C/D1-198[»]
    ProteinModelPortaliP30626.
    SMRiP30626. Positions 27-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30626.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 6436EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 10334EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini100 – 13536EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 16936EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG298587.
    HOGENOMiHOG000231982.
    HOVERGENiHBG004492.
    OMAiIQCVMSI.
    OrthoDBiEOG7RV9FM.
    PhylomeDBiP30626.
    TreeFamiTF314682.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30626-1) [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

    MAYPGHPGAG GGYYPGGYGG APGGPAFPGQ TQDPLYGYFA AVAGQDGQID    50
    ADELQRCLTQ SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA 100
    VLNGWRQHFI SFDTDRSGTV DPQELQKALT TMGFRLSPQA VNSIAKRYST 150
    NGKITFDDYI ACCVKLRALT DSFRRRDTAQ QGVVNFPYDD FIQCVMSV 198
    Length:198
    Mass (Da):21,676
    Last modified:April 1, 1993 - v1
    Checksum:iA4829C7650A5E3FA
    GO
    Isoform 2 (identifier: P30626-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MAYPGHPGAGGGYYPGG → MQ

    Note: No experimental confirmation available.

    Show »
    Length:183
    Mass (Da):20,345
    Checksum:iA6B23B49FF8B9778
    GO
    Isoform 3 (identifier: P30626-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MAYPGHPGAGGGYYPGG → MQ
         191-198: FIQCVMSV → VSLRN

    Note: No experimental confirmation available.

    Show »
    Length:180
    Mass (Da):20,006
    Checksum:i2F652A7283896808
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717MAYPG…YYPGG → MQ in isoform 2 and isoform 3. 2 PublicationsVSP_046277Add
    BLAST
    Alternative sequencei191 – 1988FIQCVMSV → VSLRN in isoform 3. 1 PublicationVSP_054463

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12387 mRNA. Translation: AAA92155.1.
    M32886 mRNA. Translation: AAA60588.1.
    AK296601 mRNA. Translation: BAG59214.1.
    BM739144 mRNA. No translation available.
    AC003991 Genomic DNA. No translation available.
    AC005075 Genomic DNA. No translation available.
    CH471091 Genomic DNA. Translation: EAW76909.1.
    CH471091 Genomic DNA. Translation: EAW76910.1.
    BC011025 mRNA. Translation: AAH11025.1.
    CCDSiCCDS47638.1. [P30626-2]
    CCDS5612.1. [P30626-1]
    CCDS59063.1. [P30626-3]
    PIRiS52094.
    RefSeqiNP_001243820.1. NM_001256891.1.
    NP_001243821.1. NM_001256892.1. [P30626-3]
    NP_003121.1. NM_003130.3. [P30626-1]
    NP_944490.1. NM_198901.1. [P30626-2]
    UniGeneiHs.489040.

    Genome annotation databases

    EnsembliENST00000265729; ENSP00000265729; ENSG00000075142. [P30626-1]
    ENST00000394641; ENSP00000378137; ENSG00000075142. [P30626-2]
    ENST00000431660; ENSP00000391148; ENSG00000075142. [P30626-3]
    GeneIDi6717.
    KEGGihsa:6717.
    UCSCiuc003ujq.2. human. [P30626-1]

    Polymorphism databases

    DMDMi267021.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12387 mRNA. Translation: AAA92155.1 .
    M32886 mRNA. Translation: AAA60588.1 .
    AK296601 mRNA. Translation: BAG59214.1 .
    BM739144 mRNA. No translation available.
    AC003991 Genomic DNA. No translation available.
    AC005075 Genomic DNA. No translation available.
    CH471091 Genomic DNA. Translation: EAW76909.1 .
    CH471091 Genomic DNA. Translation: EAW76910.1 .
    BC011025 mRNA. Translation: AAH11025.1 .
    CCDSi CCDS47638.1. [P30626-2 ]
    CCDS5612.1. [P30626-1 ]
    CCDS59063.1. [P30626-3 ]
    PIRi S52094.
    RefSeqi NP_001243820.1. NM_001256891.1.
    NP_001243821.1. NM_001256892.1. [P30626-3 ]
    NP_003121.1. NM_003130.3. [P30626-1 ]
    NP_944490.1. NM_198901.1. [P30626-2 ]
    UniGenei Hs.489040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JUO X-ray 2.20 A/B 1-198 [» ]
    2JC2 X-ray 2.50 A/B/C/D 1-198 [» ]
    ProteinModelPortali P30626.
    SMRi P30626. Positions 27-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112595. 20 interactions.
    IntActi P30626. 10 interactions.
    MINTi MINT-4999795.
    STRINGi 9606.ENSP00000265729.

    PTM databases

    PhosphoSitei P30626.

    Polymorphism databases

    DMDMi 267021.

    2D gel databases

    OGPi P30626.

    Proteomic databases

    MaxQBi P30626.
    PaxDbi P30626.
    PRIDEi P30626.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265729 ; ENSP00000265729 ; ENSG00000075142 . [P30626-1 ]
    ENST00000394641 ; ENSP00000378137 ; ENSG00000075142 . [P30626-2 ]
    ENST00000431660 ; ENSP00000391148 ; ENSG00000075142 . [P30626-3 ]
    GeneIDi 6717.
    KEGGi hsa:6717.
    UCSCi uc003ujq.2. human. [P30626-1 ]

    Organism-specific databases

    CTDi 6717.
    GeneCardsi GC07M087834.
    HGNCi HGNC:11292. SRI.
    HPAi HPA019004.
    MIMi 182520. gene.
    neXtProti NX_P30626.
    PharmGKBi PA36117.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298587.
    HOGENOMi HOG000231982.
    HOVERGENi HBG004492.
    OMAi IQCVMSI.
    OrthoDBi EOG7RV9FM.
    PhylomeDBi P30626.
    TreeFami TF314682.

    Miscellaneous databases

    ChiTaRSi SRI. human.
    EvolutionaryTracei P30626.
    GeneWikii SRI_(gene).
    GenomeRNAii 6717.
    NextBioi 26200.
    PROi P30626.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30626.
    Bgeei P30626.
    CleanExi HS_SRI.
    Genevestigatori P30626.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and molecular cloning of human sorcin a calcium-binding protein in vincristine-resistant HOB1 lymphoma cells."
      Wang S.L., Tam M.F., Ho Y.S., Pai S.H., Kao M.C.
      Biochim. Biophys. Acta 1260:285-293(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Purification, cDNA cloning, and expression of human sorcin in vincristine-resistant HOB1 lymphoma cell lines."
      Lee W.P.
      Arch. Biochem. Biophys. 325:217-226(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Isolation of the cDNA clone for human CP22 overexpressed in multidrug-resistant cell lines."
      Sugimoto Y., Asami N., Okochi E., Ogura M., Tsuruo T.
      Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Colon.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Ascites.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    9. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 57-116; 128-135 AND 154-165, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    10. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 128-135 AND 154-165.
      Tissue: Keratinocyte.
    11. "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro."
      Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.
      FEBS Lett. 545:151-154(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCA.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family."
      Xie X., Dwyer M.D., Swenson L., Parker M.H., Botfield M.C.
      Protein Sci. 10:2419-2425(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    14. "Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor."
      Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia H.H., Chiancone E., Colotti G.
      FASEB J. 22:295-306(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT LEU-112, SUBUNIT, FUNCTION, CALCIUM-BINDING, INTERACTION WITH RYR2 AND ANXA7.

    Entry informationi

    Entry nameiSORCN_HUMAN
    AccessioniPrimary (citable) accession number: P30626
    Secondary accession number(s): A8MTH6, B4DKK2, D6W5Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 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

    Miscellaneous

    This protein is encoded by an amplified gene in multidrug-resistant cells.
    This protein has been shown to bind calcium with high affinity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3