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P51606

- RENBP_HUMAN

UniProt

P51606 - RENBP_HUMAN

Protein

N-acylglucosamine 2-epimerase

Gene

RENBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded.1 Publication

    Catalytic activityi

    N-acyl-D-glucosamine = N-acyl-D-mannosamine.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: Ensembl
    2. endopeptidase inhibitor activity Source: ProtInc
    3. N-acylglucosamine 2-epimerase activity Source: UniProtKB

    GO - Biological processi

    1. N-acetylglucosamine metabolic process Source: Ensembl
    2. N-acetylmannosamine metabolic process Source: Ensembl
    3. N-acetylneuraminate catabolic process Source: UniProtKB
    4. regulation of blood pressure Source: ProtInc

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    SABIO-RKP51606.
    UniPathwayiUPA00629.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acylglucosamine 2-epimerase (EC:5.1.3.8)
    Short name:
    AGE
    Alternative name(s):
    GlcNAc 2-epimerase
    N-acetyl-D-glucosamine 2-epimerase
    Renin-binding protein
    Short name:
    RnBP
    Gene namesi
    Name:RENBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9959. RENBP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34325.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427N-acylglucosamine 2-epimerasePRO_0000208949Add
    BLAST

    Proteomic databases

    MaxQBiP51606.
    PaxDbiP51606.
    PRIDEiP51606.

    PTM databases

    PhosphoSiteiP51606.

    Expressioni

    Gene expression databases

    ArrayExpressiP51606.
    BgeeiP51606.
    CleanExiHS_RENBP.
    GenevestigatoriP51606.

    Organism-specific databases

    HPAiHPA000428.
    HPA000522.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111905. 2 interactions.
    IntActiP51606. 2 interactions.
    MINTiMINT-1464879.
    STRINGi9606.ENSP00000377303.

    Structurei

    3D structure databases

    ProteinModelPortaliP51606.
    SMRiP51606. Positions 11-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni195 – 21622Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2942.
    HOGENOMiHOG000252296.
    HOVERGENiHBG102994.
    InParanoidiP51606.
    KOiK01787.
    OMAiILQHVQR.
    PhylomeDBiP51606.
    TreeFamiTF329027.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51606-1) [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

    MSKGLPARQD MEKERETLQA WKERVGQELD RVVAFWMEHS HDQEHGGFFT    50
    CLGREGRVYD DLKYVWLQGR QVWMYCRLYR TFERFRHAQL LDAAKAGGEF 100
    LLRYARVAPP GKKCAFVLTR DGRPVKVQRT IFSECFYTMA MNELWRATGE 150
    VRYQTEAVEM MDQIVHWVQE DASGLGRPQL QGAPAAEPMA VPMMLLNLVE 200
    QLGEADEELA GKYAELGDWC ARRILQHVQR DGQAVLENVS EGGKELPGCL 250
    GRQQNPGHTL EAGWFLLRHC IRKGDPELRA HVIDKFLLLP FHSGWDPDHG 300
    GLFYFQDADN FCPTQLEWAM KLWWPHSEAM IAFLMGYSDS GDPVLLRLFY 350
    QVAEYTFRQF RDPEYGEWFG YLSREGKVAL SIKGGPFKGC FHVPRCLAMC 400
    EEMLGALLSR PAPAPSPAPT PACRGAE 427
    Length:427
    Mass (Da):48,831
    Last modified:April 20, 2010 - v2
    Checksum:i40D5C485C30BE009
    GO
    Isoform 2 (identifier: P51606-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         230-254: RDGQAVLENVSEGGKELPGCLGRQQ → ATRWKPAGFCSVIAFGKATPNFEPT
         255-427: Missing.

    Show »
    Length:254
    Mass (Da):29,270
    Checksum:i9CB7FE6EED3368F7
    GO

    Sequence cautioni

    The sequence BAA01082.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAH15558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA01082.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361L → P in AAH15558. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691Q → R.
    Corresponds to variant rs2229241 [ dbSNP | Ensembl ].
    VAR_029339
    Natural varianti284 – 2841D → G.
    Corresponds to variant rs2269371 [ dbSNP | Ensembl ].
    VAR_049182

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei230 – 25425RDGQA…LGRQQ → ATRWKPAGFCSVIAFGKATP NFEPT in isoform 2. 1 PublicationVSP_039022Add
    BLAST
    Alternative sequencei255 – 427173Missing in isoform 2. 1 PublicationVSP_039023Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298125 mRNA. Translation: BAG60405.1.
    U52112 Genomic DNA. No translation available.
    BC015558 mRNA. Translation: AAH15558.1. Different initiation.
    D10232 mRNA. Translation: BAA01082.1. Sequence problems.
    CCDSiCCDS14738.2. [P51606-1]
    PIRiJX0188.
    RefSeqiNP_002901.2. NM_002910.5. [P51606-1]
    UniGeneiHs.158331.

    Genome annotation databases

    EnsembliENST00000393700; ENSP00000377303; ENSG00000102032. [P51606-1]
    GeneIDi5973.
    KEGGihsa:5973.
    UCSCiuc004fjo.2. human. [P51606-1]
    uc011mzh.1. human. [P51606-2]

    Polymorphism databases

    DMDMi294862458.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298125 mRNA. Translation: BAG60405.1 .
    U52112 Genomic DNA. No translation available.
    BC015558 mRNA. Translation: AAH15558.1 . Different initiation.
    D10232 mRNA. Translation: BAA01082.1 . Sequence problems.
    CCDSi CCDS14738.2. [P51606-1 ]
    PIRi JX0188.
    RefSeqi NP_002901.2. NM_002910.5. [P51606-1 ]
    UniGenei Hs.158331.

    3D structure databases

    ProteinModelPortali P51606.
    SMRi P51606. Positions 11-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111905. 2 interactions.
    IntActi P51606. 2 interactions.
    MINTi MINT-1464879.
    STRINGi 9606.ENSP00000377303.

    Chemistry

    DrugBanki DB00141. N-Acetyl-D-glucosamine.

    PTM databases

    PhosphoSitei P51606.

    Polymorphism databases

    DMDMi 294862458.

    Proteomic databases

    MaxQBi P51606.
    PaxDbi P51606.
    PRIDEi P51606.

    Protocols and materials databases

    DNASUi 5973.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393700 ; ENSP00000377303 ; ENSG00000102032 . [P51606-1 ]
    GeneIDi 5973.
    KEGGi hsa:5973.
    UCSCi uc004fjo.2. human. [P51606-1 ]
    uc011mzh.1. human. [P51606-2 ]

    Organism-specific databases

    CTDi 5973.
    GeneCardsi GC0XM153200.
    H-InvDB HIX0203300.
    HGNCi HGNC:9959. RENBP.
    HPAi HPA000428.
    HPA000522.
    MIMi 312420. gene.
    neXtProti NX_P51606.
    PharmGKBi PA34325.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2942.
    HOGENOMi HOG000252296.
    HOVERGENi HBG102994.
    InParanoidi P51606.
    KOi K01787.
    OMAi ILQHVQR.
    PhylomeDBi P51606.
    TreeFami TF329027.

    Enzyme and pathway databases

    UniPathwayi UPA00629 .
    SABIO-RK P51606.

    Miscellaneous databases

    GeneWikii RENBP.
    GenomeRNAii 5973.
    NextBioi 23253.
    PROi P51606.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51606.
    Bgeei P51606.
    CleanExi HS_RENBP.
    Genevestigatori P51606.

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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 2).
      Tissue: Lung.
    2. "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].
    3. "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: Skin.
    4. "Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif."
      Inoue H., Takahashi S., Fukui K., Miyake Y.
      J. Biochem. 110:493-500(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-427 (ISOFORM 1).
    5. "Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase."
      Takahashi S., Takahashi K., Kaneko T., Ogasawara H., Shindo S., Kobayashi M.
      J. Biochem. 125:348-353(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    6. "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid."
      Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.
      J. Biol. Chem. 287:28865-28881(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PATHWAY.

    Entry informationi

    Entry nameiRENBP_HUMAN
    AccessioniPrimary (citable) accession number: P51606
    Secondary accession number(s): B4DNZ3, Q96BI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 124 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

    Caution

    It is uncertain whether Met-1 or Met-11 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3