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Q15493

- RGN_HUMAN

UniProt

Q15493 - RGN_HUMAN

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Protein

Regucalcin

Gene

RGN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ15493. baseline and differential.
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.
GeneTreeiENSGT00390000014995.
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

        10         20         30         40         50
MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ
60 70 80 90 100
RVTMDAPVSS VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN
110 120 130 140 150
RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGALYSLFPD HHVKKYFDQV
160 170 180 190 200
DISNGLDWSL DHKIFYYIDS LSYSVDAFDY DLQTGQISNR RSVYKLEKEE
210 220 230 240 250
QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL PVDKTTSCCF
260 270 280 290
GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG
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]
CCDS75968.1. [Q15493-2]
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 ]
CCDS75968.1. [Q15493-2 ]
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.
GeneTreei ENSGT00390000014995.
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.
ExpressionAtlasi Q15493. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 118 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