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Q7Z5B4

- RIC3_HUMAN

UniProt

Q7Z5B4 - RIC3_HUMAN

Protein

Protein RIC-3

Gene

RIC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4.7 Publications

    GO - Biological processi

    1. cellular protein complex assembly Source: Ensembl
    2. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    3. protein folding Source: Ensembl
    4. synaptic transmission, cholinergic Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein RIC-3
    Alternative name(s):
    Resistant to inhibitor of cholinesterase 3
    Gene namesi
    Name:RIC3
    ORF Names:UNQ720/PRO1385
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:30338. RIC3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671066.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828By similarityAdd
    BLAST
    Chaini29 – 369341Protein RIC-3PRO_0000302731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
    Cross-linki202 – 202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ7Z5B4.
    PaxDbiQ7Z5B4.
    PRIDEiQ7Z5B4.

    PTM databases

    PhosphoSiteiQ7Z5B4.

    Expressioni

    Tissue specificityi

    Broadly expressed, with high levels in muscle, brain, heart, pancreas and testis. In the central nervous system, highest levels are detected in the cerebellum and pituitary gland. Over-expressed in brains from patients with bipolar disease or schizophrenia. Isoform 5 is predominantly expressed in the brain.3 Publications

    Gene expression databases

    ArrayExpressiQ7Z5B4.
    BgeeiQ7Z5B4.
    CleanExiHS_RIC3.
    GenevestigatoriQ7Z5B4.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CHRNB2, CHRNB4 and HTR3A.3 Publications

    Protein-protein interaction databases

    BioGridi122743. 2 interactions.
    IntActiQ7Z5B4. 1 interaction.
    MINTiMINT-8343009.
    STRINGi9606.ENSP00000344904.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z5B4.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 9567LumenalSequence AnalysisAdd
    BLAST
    Topological domaini117 – 369253CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei96 – 11621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili140 – 16930By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi81 – 9414Poly-GlyAdd
    BLAST
    Compositional biasi269 – 2724Poly-Glu

    Domaini

    The coiled-coil domain mediates transient homodimerization with other acetylcholine receptor-bound RIC3 molecules, promoting stepwise ACHR homomeric assembly at the membrane.By similarity

    Sequence similaritiesi

    Belongs to the ric-3 family.Curated

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46432.
    HOVERGENiHBG106009.
    InParanoidiQ7Z5B4.
    OMAiHRKITNF.
    OrthoDBiEOG7MKW7H.
    PhylomeDBiQ7Z5B4.
    TreeFamiTF333291.

    Family and domain databases

    InterProiIPR026160. Ric3.
    [Graphical view]
    PANTHERiPTHR21723. PTHR21723. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z5B4-1) [UniParc]FASTAAdd to Basket

    Also known as: a

    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

    MAYSTVQRVA LASGLVLALS LLLPKAFLSR GKRQEPPPTP EGKLGRFPPM    50
    MHHHQAPSDG QTPGARFQRS HLAEAFAKAK GSGGGAGGGG SGRGLMGQII 100
    PIYGFGIFLY ILYILFKLSK GKTTAEDGKC YTAMPGNTHR KITSFELAQL 150
    QEKLKETEAA MEKLINRVGP NGESRAQTVT SDQEKRLLHQ LREITRVMKE 200
    GKFIDRFSPE KEAEEAPYME DWEGYPEETY PIYDLSDCIK RRQETILVDY 250
    PDPKELSAEE IAERMGMIEE EESDHLGWES LPTDPRAQED NSVTSCDPKP 300
    ETCSCCFHED EDPAVLAENA GFSADSYPEQ EETTKEEWSQ DFKDEGLGIS 350
    TDKAYTGSML RKRNPQGLE 369
    Length:369
    Mass (Da):41,092
    Last modified:October 1, 2003 - v1
    Checksum:i15FD70384070345D
    GO
    Isoform 2 (identifier: Q7Z5B4-2) [UniParc]FASTAAdd to Basket

    Also known as: d

    The sequence of this isoform differs from the canonical sequence as follows:
         118-128: LSKGKTTAEDG → VSRIILIILHQ
         129-369: Missing.

    Show »
    Length:128
    Mass (Da):13,663
    Checksum:i01D76A36CC9F0C2F
    GO
    Isoform 3 (identifier: Q7Z5B4-3) [UniParc]FASTAAdd to Basket

    Also known as: c

    The sequence of this isoform differs from the canonical sequence as follows:
         41-222: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:187
    Mass (Da):20,954
    Checksum:iC51C0B8B8F21B4B2
    GO
    Isoform 4 (identifier: Q7Z5B4-5) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         174-174: Missing.

    Show »
    Length:368
    Mass (Da):41,005
    Checksum:iC66CFFD8641778DA
    GO
    Isoform 5 (identifier: Q7Z5B4-6) [UniParc]FASTAAdd to Basket

    Also known as: e

    The sequence of this isoform differs from the canonical sequence as follows:
         143-224: TSFELAQLQE...EAPYMEDWEG → S

    Show »
    Length:288
    Mass (Da):31,643
    Checksum:i2D0010517F3E6E20
    GO

    Sequence cautioni

    The sequence BAB13871.1 differs from that shown. Reason: Probable cloning artifact.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231Missing in AAP92163. (PubMed:12821669)Curated
    Sequence conflicti165 – 1651I → F in AAH22455. (PubMed:15489334)Curated
    Isoform 2 (identifier: Q7Z5B4-2)
    Sequence conflicti124 – 1241I → T in AAP92163. (PubMed:12821669)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571P → H.1 Publication
    Corresponds to variant rs17855498 [ dbSNP | Ensembl ].
    VAR_034943
    Natural varianti130 – 1301C → Y.
    Corresponds to variant rs55990541 [ dbSNP | Ensembl ].
    VAR_062208
    Natural varianti346 – 3461G → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036391

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei41 – 222182Missing in isoform 3. 1 PublicationVSP_027939Add
    BLAST
    Alternative sequencei118 – 12811LSKGKTTAEDG → VSRIILIILHQ in isoform 2. 2 PublicationsVSP_027940Add
    BLAST
    Alternative sequencei129 – 369241Missing in isoform 2. 2 PublicationsVSP_027941Add
    BLAST
    Alternative sequencei143 – 22482TSFEL…EDWEG → S in isoform 5. 1 PublicationVSP_043786Add
    BLAST
    Alternative sequencei174 – 1741Missing in isoform 4. 2 PublicationsVSP_027943

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY326435 mRNA. Translation: AAP92162.1.
    AY326436 mRNA. Translation: AAP92163.1.
    AM422214 mRNA. Translation: CAM12309.1.
    AY358475 mRNA. Translation: AAQ88839.1.
    AK021670 mRNA. Translation: BAB13871.1. Sequence problems.
    AK315379 mRNA. Translation: BAG37772.1.
    AL832601 mRNA. Translation: CAD89943.1.
    AC091013 Genomic DNA. No translation available.
    AC116456 Genomic DNA. No translation available.
    AC129895 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68628.1.
    CH471064 Genomic DNA. Translation: EAW68630.1.
    BC022455 mRNA. Translation: AAH22455.1.
    CCDSiCCDS44533.1. [Q7Z5B4-3]
    CCDS55741.1. [Q7Z5B4-6]
    CCDS55742.1. [Q7Z5B4-1]
    CCDS7788.1. [Q7Z5B4-5]
    RefSeqiNP_001128581.1. NM_001135109.2. [Q7Z5B4-3]
    NP_001193600.1. NM_001206671.2. [Q7Z5B4-1]
    NP_001193601.1. NM_001206672.2. [Q7Z5B4-6]
    NP_078833.3. NM_024557.4. [Q7Z5B4-5]
    XP_006718381.1. XM_006718318.1. [Q7Z5B4-5]
    XP_006718383.1. XM_006718320.1.
    UniGeneiHs.231850.
    Hs.568986.

    Genome annotation databases

    EnsembliENST00000309737; ENSP00000308820; ENSG00000166405. [Q7Z5B4-1]
    ENST00000335425; ENSP00000333988; ENSG00000166405. [Q7Z5B4-3]
    ENST00000343202; ENSP00000344904; ENSG00000166405. [Q7Z5B4-5]
    ENST00000419822; ENSP00000404415; ENSG00000166405. [Q7Z5B4-2]
    ENST00000425599; ENSP00000395320; ENSG00000166405. [Q7Z5B4-6]
    GeneIDi79608.
    KEGGihsa:79608.
    UCSCiuc001mgc.2. human. [Q7Z5B4-5]
    uc001mgd.2. human. [Q7Z5B4-1]
    uc001mge.2. human. [Q7Z5B4-3]
    uc001mgf.4. human. [Q7Z5B4-2]
    uc009yfm.2. human. [Q7Z5B4-6]

    Polymorphism databases

    DMDMi74713638.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY326435 mRNA. Translation: AAP92162.1 .
    AY326436 mRNA. Translation: AAP92163.1 .
    AM422214 mRNA. Translation: CAM12309.1 .
    AY358475 mRNA. Translation: AAQ88839.1 .
    AK021670 mRNA. Translation: BAB13871.1 . Sequence problems.
    AK315379 mRNA. Translation: BAG37772.1 .
    AL832601 mRNA. Translation: CAD89943.1 .
    AC091013 Genomic DNA. No translation available.
    AC116456 Genomic DNA. No translation available.
    AC129895 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68628.1 .
    CH471064 Genomic DNA. Translation: EAW68630.1 .
    BC022455 mRNA. Translation: AAH22455.1 .
    CCDSi CCDS44533.1. [Q7Z5B4-3 ]
    CCDS55741.1. [Q7Z5B4-6 ]
    CCDS55742.1. [Q7Z5B4-1 ]
    CCDS7788.1. [Q7Z5B4-5 ]
    RefSeqi NP_001128581.1. NM_001135109.2. [Q7Z5B4-3 ]
    NP_001193600.1. NM_001206671.2. [Q7Z5B4-1 ]
    NP_001193601.1. NM_001206672.2. [Q7Z5B4-6 ]
    NP_078833.3. NM_024557.4. [Q7Z5B4-5 ]
    XP_006718381.1. XM_006718318.1. [Q7Z5B4-5 ]
    XP_006718383.1. XM_006718320.1.
    UniGenei Hs.231850.
    Hs.568986.

    3D structure databases

    ProteinModelPortali Q7Z5B4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122743. 2 interactions.
    IntActi Q7Z5B4. 1 interaction.
    MINTi MINT-8343009.
    STRINGi 9606.ENSP00000344904.

    PTM databases

    PhosphoSitei Q7Z5B4.

    Polymorphism databases

    DMDMi 74713638.

    Proteomic databases

    MaxQBi Q7Z5B4.
    PaxDbi Q7Z5B4.
    PRIDEi Q7Z5B4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309737 ; ENSP00000308820 ; ENSG00000166405 . [Q7Z5B4-1 ]
    ENST00000335425 ; ENSP00000333988 ; ENSG00000166405 . [Q7Z5B4-3 ]
    ENST00000343202 ; ENSP00000344904 ; ENSG00000166405 . [Q7Z5B4-5 ]
    ENST00000419822 ; ENSP00000404415 ; ENSG00000166405 . [Q7Z5B4-2 ]
    ENST00000425599 ; ENSP00000395320 ; ENSG00000166405 . [Q7Z5B4-6 ]
    GeneIDi 79608.
    KEGGi hsa:79608.
    UCSCi uc001mgc.2. human. [Q7Z5B4-5 ]
    uc001mgd.2. human. [Q7Z5B4-1 ]
    uc001mge.2. human. [Q7Z5B4-3 ]
    uc001mgf.4. human. [Q7Z5B4-2 ]
    uc009yfm.2. human. [Q7Z5B4-6 ]

    Organism-specific databases

    CTDi 79608.
    GeneCardsi GC11M008127.
    H-InvDB HIX0009421.
    HGNCi HGNC:30338. RIC3.
    MIMi 610509. gene.
    neXtProti NX_Q7Z5B4.
    PharmGKBi PA142671066.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46432.
    HOVERGENi HBG106009.
    InParanoidi Q7Z5B4.
    OMAi HRKITNF.
    OrthoDBi EOG7MKW7H.
    PhylomeDBi Q7Z5B4.
    TreeFami TF333291.

    Miscellaneous databases

    GeneWikii RIC3.
    GenomeRNAii 79608.
    NextBioi 68650.
    PROi Q7Z5B4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z5B4.
    Bgeei Q7Z5B4.
    CleanExi HS_RIC3.
    Genevestigatori Q7Z5B4.

    Family and domain databases

    InterProi IPR026160. Ric3.
    [Graphical view ]
    PANTHERi PTHR21723. PTHR21723. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Conservation within the RIC-3 gene family. Effectors of mammalian nicotinic acetylcholine receptor expression."
      Halevi S., Yassin L., Eshel M., Sala F., Sala S., Criado M., Treinin M.
      J. Biol. Chem. 278:34411-34417(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, FUNCTION.
    2. "Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors."
      Seredenina T., Ferraro T., Terstappen G.C., Caricasole A., Roncarati R.
      Biosci. Rep. 28:299-306(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Hippocampus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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 4).
      Tissue: Brain and Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Spinal cord.
    6. 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 4), VARIANT HIS-57.
      Tissue: Brain.
    9. "Ric-3 promotes functional expression of the nicotinic acetylcholine receptor alpha7 subunit in mammalian cells."
      Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., Cohen C.J., Aiyar J.
      J. Biol. Chem. 280:1257-1263(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHRNA7.
    10. "Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3."
      Cheng A., McDonald N.A., Connolly C.N.
      J. Biol. Chem. 280:22502-22507(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HTR3A, SUBCELLULAR LOCATION.
    11. "Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic acetylcholine receptors."
      Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S., Sala S., Sala F., Criado M.
      J. Biol. Chem. 280:27062-27068(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
      Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
      Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHRNA7; CHRNA3; CHRNA4; CHRNB2 AND CHRNB4.
    13. "Differential subcellular localization of RIC-3 isoforms and their role in determining 5-HT3 receptor composition."
      Cheng A., Bollan K.A., Greenwood S.M., Irving A.J., Connolly C.N.
      J. Biol. Chem. 282:26158-26166(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION.
    14. "Lack of RIC-3 congruence with beta2 subunit-containing nicotinic acetylcholine receptors in bipolar disorder."
      Severance E.G., Yolken R.H.
      Neuroscience 148:454-460(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-202.
      Tissue: Mammary cancer.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-346.

    Entry informationi

    Entry nameiRIC3_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z5B4
    Secondary accession number(s): B0B1U0
    , B2RD25, D3DQU5, Q6UX78, Q7Z5B3, Q86T94, Q8TBJ9, Q9HAH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 81 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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