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P51606

- RENBP_HUMAN

UniProt

P51606 - RENBP_HUMAN

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Protein
N-acylglucosamine 2-epimerase
Gene
RENBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. N-acylglucosamine 2-epimerase activity Source: UniProtKB
  3. endopeptidase inhibitor activity Source: ProtInc

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427N-acylglucosamine 2-epimerase
PRO_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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 21622Leucine-zipper
Add
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.

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.
VSP_039022Add
BLAST
Alternative sequencei255 – 427173Missing in isoform 2.
VSP_039023Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361L → P in AAH15558. 1 Publication

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]
ENST00000412763; ENSP00000387811; ENSG00000102032. [P51606-2]
ENST00000593344; ENSP00000473237; ENSG00000269198. [P51606-1]
ENST00000600627; ENSP00000472740; ENSG00000269198. [P51606-2]
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 ]
ENST00000412763 ; ENSP00000387811 ; ENSG00000102032 . [P51606-2 ]
ENST00000593344 ; ENSP00000473237 ; ENSG00000269198 . [P51606-1 ]
ENST00000600627 ; ENSP00000472740 ; ENSG00000269198 . [P51606-2 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 123 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.

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

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