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Q15493

- RGN_HUMAN

UniProt

Q15493 - RGN_HUMAN

Protein

Regucalcin

Gene

RGN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca2+ signaling, and Ca2+-dependent cellular processes and enzyme activities By similarity.By similarity

    Catalytic activityi

    D-glucono-1,5-lactone + H2O = D-gluconate.2 Publications

    Cofactori

    Binds 1 divalent metal cation per subunit. Most active with zinc and manganese ions. The physiological cofactor is most likely calcium or magnesium.2 Publications

    Kineticsi

    1. KM=2.7 mM for gluconolactone (with Zn2+ as cofactor)1 Publication
    2. KM=0.6 mM for gluconolactone (with Mn2+ as cofactor)1 Publication
    3. KM=1.3 mM for gluconolactone (with Mg2+ as cofactor)1 Publication
    4. KM=3.7 mM for gluconolactone (with Ca2+ as cofactor)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181Divalent metal cation1 Publication
    Binding sitei101 – 1011Substrate
    Binding sitei103 – 1031Substrate
    Binding sitei121 – 1211SubstrateBy similarity
    Metal bindingi154 – 1541Divalent metal cation1 Publication
    Active sitei204 – 2041Proton donor/acceptor1 Publication
    Metal bindingi204 – 2041Divalent metal cation1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. enzyme regulator activity Source: InterPro
    3. gluconolactonase activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular calcium ion homeostasis Source: UniProtKB
    2. L-ascorbic acid biosynthetic process Source: Ensembl
    3. positive regulation of ATPase activity Source: UniProtKB
    4. regulation of calcium-mediated signaling Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regucalcin
    Short name:
    RC
    Alternative name(s):
    Gluconolactonase (EC:3.1.1.17)
    Short name:
    GNL
    Senescence marker protein 30
    Short name:
    SMP-30
    Gene namesi
    Name:RGN
    Synonyms:SMP30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9989. RGN.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181E → A: Reduces enzyme activity by about 90%. 1 Publication
    Mutagenesisi103 – 1031N → A: Reduces enzyme activity by about 95%. 1 Publication
    Mutagenesisi154 – 1541N → A: Reduces enzyme activity by about 95%. 1 Publication
    Mutagenesisi204 – 2041D → A: Reduces enzyme activity by over 98%. 1 Publication

    Organism-specific databases

    PharmGKBiPA34359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299RegucalcinPRO_0000173046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei144 – 1441N6-succinyllysineBy similarity
    Modified residuei244 – 2441N6-succinyllysineBy similarity
    Modified residuei253 – 2531N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ15493.
    PaxDbiQ15493.
    PeptideAtlasiQ15493.
    PRIDEiQ15493.

    PTM databases

    PhosphoSiteiQ15493.

    Expressioni

    Gene expression databases

    BgeeiQ15493.
    CleanExiHS_RGN.
    GenevestigatoriQ15493.

    Organism-specific databases

    HPAiHPA029102.
    HPA029103.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi114557. 1 interaction.
    MINTiMINT-3031653.
    STRINGi9606.ENSP00000253303.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi15 – 239
    Turni24 – 274
    Beta strandi28 – 336
    Turni34 – 374
    Beta strandi38 – 436
    Turni44 – 463
    Beta strandi49 – 535
    Beta strandi58 – 647
    Beta strandi67 – 737
    Beta strandi76 – 816
    Turni82 – 854
    Beta strandi86 – 927
    Beta strandi98 – 10710
    Beta strandi113 – 1197
    Beta strandi132 – 1376
    Beta strandi143 – 15816
    Beta strandi164 – 1696
    Helixi170 – 1723
    Beta strandi174 – 1807
    Turni182 – 1843
    Beta strandi187 – 1959
    Helixi198 – 2003
    Beta strandi202 – 2098
    Beta strandi214 – 2196
    Turni220 – 2223
    Beta strandi223 – 2275
    Turni229 – 2313
    Beta strandi234 – 2396
    Beta strandi241 – 2433
    Beta strandi245 – 2528
    Helixi253 – 2553
    Beta strandi257 – 2637
    Helixi269 – 2746
    Turni276 – 2794
    Beta strandi281 – 2855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3G4EX-ray1.42A/B3-299[»]
    3G4HX-ray1.92A/B3-299[»]
    4GNBX-ray1.50A/B1-299[»]
    4GNCX-ray1.75A/B1-299[»]
    ProteinModelPortaliQ15493.
    SMRiQ15493. Positions 3-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15493.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SMP-30/CGR1 family.Curated

    Phylogenomic databases

    eggNOGiCOG3386.
    HOGENOMiHOG000220627.
    HOVERGENiHBG004347.
    InParanoidiQ15493.
    KOiK01053.
    OMAiCVLRENC.
    OrthoDBiEOG77127C.
    PhylomeDBiQ15493.
    TreeFamiTF323663.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR008367. Regucalcin.
    IPR013658. SGL.
    IPR005511. SMP-30.
    [Graphical view]
    PfamiPF08450. SGL. 1 hit.
    [Graphical view]
    PRINTSiPR01791. REGUCALCIN.
    PR01790. SMP30FAMILY.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15493-1) [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

    MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ    50
    RVTMDAPVSS VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN 100
    RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGALYSLFPD HHVKKYFDQV 150
    DISNGLDWSL DHKIFYYIDS LSYSVDAFDY DLQTGQISNR RSVYKLEKEE 200
    QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL PVDKTTSCCF 250
    GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG 299
    Length:299
    Mass (Da):33,253
    Last modified:November 1, 1996 - v1
    Checksum:i95BA1C73B7B77635
    GO
    Isoform 2 (identifier: Q15493-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-187: Missing.
         188-188: S → A

    Note: No experimental confirmation available.

    Show »
    Length:227
    Mass (Da):24,968
    Checksum:i19BC938A52DA72D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2932IA → TS in BAD97080. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei116 – 18772Missing in isoform 2. 1 PublicationVSP_025456Add
    BLAST
    Alternative sequencei188 – 1881S → A in isoform 2. 1 PublicationVSP_025457

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31815 mRNA. Translation: BAA06602.1.
    AB028125 mRNA. Translation: BAA78693.1.
    AB032064 mRNA. Translation: BAA84082.1.
    AK290136 mRNA. Translation: BAF82825.1.
    AK223360 mRNA. Translation: BAD97080.1.
    AL513366 Genomic DNA. Translation: CAI41697.1.
    BC050371 mRNA. Translation: AAH50371.1.
    BC073173 mRNA. Translation: AAH73173.1.
    CCDSiCCDS14272.1. [Q15493-1]
    PIRiS60035.
    RefSeqiNP_001269777.1. NM_001282848.1.
    NP_001269778.1. NM_001282849.1. [Q15493-2]
    NP_004674.1. NM_004683.5. [Q15493-1]
    NP_690608.1. NM_152869.3. [Q15493-1]
    XP_006724630.1. XM_006724567.1. [Q15493-2]
    UniGeneiHs.77854.

    Genome annotation databases

    EnsembliENST00000336169; ENSP00000338400; ENSG00000130988. [Q15493-1]
    ENST00000352078; ENSP00000253303; ENSG00000130988. [Q15493-1]
    ENST00000397180; ENSP00000380365; ENSG00000130988. [Q15493-1]
    ENST00000457380; ENSP00000406568; ENSG00000130988. [Q15493-2]
    GeneIDi9104.
    KEGGihsa:9104.
    UCSCiuc004dgz.1. human. [Q15493-1]
    uc010nhp.1. human. [Q15493-2]

    Polymorphism databases

    DMDMi3334328.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31815 mRNA. Translation: BAA06602.1 .
    AB028125 mRNA. Translation: BAA78693.1 .
    AB032064 mRNA. Translation: BAA84082.1 .
    AK290136 mRNA. Translation: BAF82825.1 .
    AK223360 mRNA. Translation: BAD97080.1 .
    AL513366 Genomic DNA. Translation: CAI41697.1 .
    BC050371 mRNA. Translation: AAH50371.1 .
    BC073173 mRNA. Translation: AAH73173.1 .
    CCDSi CCDS14272.1. [Q15493-1 ]
    PIRi S60035.
    RefSeqi NP_001269777.1. NM_001282848.1.
    NP_001269778.1. NM_001282849.1. [Q15493-2 ]
    NP_004674.1. NM_004683.5. [Q15493-1 ]
    NP_690608.1. NM_152869.3. [Q15493-1 ]
    XP_006724630.1. XM_006724567.1. [Q15493-2 ]
    UniGenei Hs.77854.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3G4E X-ray 1.42 A/B 3-299 [» ]
    3G4H X-ray 1.92 A/B 3-299 [» ]
    4GNB X-ray 1.50 A/B 1-299 [» ]
    4GNC X-ray 1.75 A/B 1-299 [» ]
    ProteinModelPortali Q15493.
    SMRi Q15493. Positions 3-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114557. 1 interaction.
    MINTi MINT-3031653.
    STRINGi 9606.ENSP00000253303.

    PTM databases

    PhosphoSitei Q15493.

    Polymorphism databases

    DMDMi 3334328.

    Proteomic databases

    MaxQBi Q15493.
    PaxDbi Q15493.
    PeptideAtlasi Q15493.
    PRIDEi Q15493.

    Protocols and materials databases

    DNASUi 9104.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336169 ; ENSP00000338400 ; ENSG00000130988 . [Q15493-1 ]
    ENST00000352078 ; ENSP00000253303 ; ENSG00000130988 . [Q15493-1 ]
    ENST00000397180 ; ENSP00000380365 ; ENSG00000130988 . [Q15493-1 ]
    ENST00000457380 ; ENSP00000406568 ; ENSG00000130988 . [Q15493-2 ]
    GeneIDi 9104.
    KEGGi hsa:9104.
    UCSCi uc004dgz.1. human. [Q15493-1 ]
    uc010nhp.1. human. [Q15493-2 ]

    Organism-specific databases

    CTDi 9104.
    GeneCardsi GC0XP046937.
    HGNCi HGNC:9989. RGN.
    HPAi HPA029102.
    HPA029103.
    MIMi 300212. gene.
    neXtProti NX_Q15493.
    PharmGKBi PA34359.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3386.
    HOGENOMi HOG000220627.
    HOVERGENi HBG004347.
    InParanoidi Q15493.
    KOi K01053.
    OMAi CVLRENC.
    OrthoDBi EOG77127C.
    PhylomeDBi Q15493.
    TreeFami TF323663.

    Miscellaneous databases

    EvolutionaryTracei Q15493.
    GeneWikii RGN_(gene).
    GenomeRNAii 9104.
    NextBioi 34129.
    PROi Q15493.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15493.
    CleanExi HS_RGN.
    Genevestigatori Q15493.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR008367. Regucalcin.
    IPR013658. SGL.
    IPR005511. SMP-30.
    [Graphical view ]
    Pfami PF08450. SGL. 1 hit.
    [Graphical view ]
    PRINTSi PR01791. REGUCALCIN.
    PR01790. SMP30FAMILY.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNA clone encoding human homologue of senescence marker protein-30 (SMP30) and its location on the X chromosome."
      Fujita T., Mandel J.-L., Shirasawa T., Hino O., Shirai T., Maruyama N.
      Biochim. Biophys. Acta 1263:249-252(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Transcript heterogeneity of the human gene for Ca2+-binding protein regucalcin."
      Misawa H., Yamaguchi M.
      Int. J. Mol. Med. 5:283-287(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "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 1).
      Tissue: Thalamus.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Colon and PNS.
    7. "Crystal structure of human senescence marker protein 30: insights linking structural, enzymatic, and physiological functions."
      Chakraborti S., Bahnson B.J.
      Biochemistry 49:3436-3444(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEXES WITH CALCIUM AND ZINC IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF GLU-18; ASN-103; ASN-154 AND ASP-204.
    8. "Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase."
      Aizawa S., Senda M., Harada A., Maruyama N., Ishida T., Aigaki T., Ishigami A., Senda T.
      PLoS ONE 8:E53706-E53706(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL CATION AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiRGN_HUMAN
    AccessioniPrimary (citable) accession number: Q15493
    Secondary accession number(s): A4FTW1
    , A8K271, Q53FC9, Q5JRR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 117 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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