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P51606 (RENBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acylglucosamine 2-epimerase

Short name=AGE
EC=5.1.3.8
Alternative name(s):
GlcNAc 2-epimerase
N-acetyl-D-glucosamine 2-epimerase
Renin-binding protein
Short name=RnBP
Gene names
Name:RENBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

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

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation. Ref.6

Subunit structure

Homodimer. Ref.5

Sequence similarities

Belongs to the N-acylglucosamine 2-epimerase family.

Caution

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

Sequence caution

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.

The sequence BAA01082.1 differs from that shown. Reason: Contaminating sequence.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51606-1)

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.
Isoform 2 (identifier: P51606-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427N-acylglucosamine 2-epimerase
PRO_0000208949

Regions

Region195 – 21622Leucine-zipper

Natural variations

Alternative sequence230 – 25425RDGQA…LGRQQ → ATRWKPAGFCSVIAFGKATP NFEPT in isoform 2.
VSP_039022
Alternative sequence255 – 427173Missing in isoform 2.
VSP_039023
Natural variant1691Q → R.
Corresponds to variant rs2229241 [ dbSNP | Ensembl ].
VAR_029339
Natural variant2841D → G.
Corresponds to variant rs2269371 [ dbSNP | Ensembl ].
VAR_049182

Experimental info

Sequence conflict2361L → P in AAH15558. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 40D5C485C30BE009

FASTA42748,831
        10         20         30         40         50         60 
MSKGLPARQD MEKERETLQA WKERVGQELD RVVAFWMEHS HDQEHGGFFT CLGREGRVYD 

        70         80         90        100        110        120 
DLKYVWLQGR QVWMYCRLYR TFERFRHAQL LDAAKAGGEF LLRYARVAPP GKKCAFVLTR 

       130        140        150        160        170        180 
DGRPVKVQRT IFSECFYTMA MNELWRATGE VRYQTEAVEM MDQIVHWVQE DASGLGRPQL 

       190        200        210        220        230        240 
QGAPAAEPMA VPMMLLNLVE QLGEADEELA GKYAELGDWC ARRILQHVQR DGQAVLENVS 

       250        260        270        280        290        300 
EGGKELPGCL GRQQNPGHTL EAGWFLLRHC IRKGDPELRA HVIDKFLLLP FHSGWDPDHG 

       310        320        330        340        350        360 
GLFYFQDADN FCPTQLEWAM KLWWPHSEAM IAFLMGYSDS GDPVLLRLFY QVAEYTFRQF 

       370        380        390        400        410        420 
RDPEYGEWFG YLSREGKVAL SIKGGPFKGC FHVPRCLAMC EEMLGALLSR PAPAPSPAPT 


PACRGAE 

« Hide

Isoform 2 [UniParc].

Checksum: 9CB7FE6EED3368F7
Show »

FASTA25429,270

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14738.2. [P51606-1]
PIRJX0188.
RefSeqNP_002901.2. NM_002910.5. [P51606-1]
UniGeneHs.158331.

3D structure databases

ProteinModelPortalP51606.
SMRP51606. Positions 11-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111905. 2 interactions.
IntActP51606. 2 interactions.
MINTMINT-1464879.
STRING9606.ENSP00000377303.

Chemistry

DrugBankDB00141. N-Acetyl-D-glucosamine.

PTM databases

PhosphoSiteP51606.

Polymorphism databases

DMDM294862458.

Proteomic databases

MaxQBP51606.
PaxDbP51606.
PRIDEP51606.

Protocols and materials databases

DNASU5973.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393700; ENSP00000377303; ENSG00000102032. [P51606-1]
ENST00000412763; ENSP00000387811; ENSG00000102032. [P51606-2]
ENST00000593344; ENSP00000473237; ENSG00000269198. [P51606-1]
ENST00000600627; ENSP00000472740; ENSG00000269198. [P51606-2]
GeneID5973.
KEGGhsa:5973.
UCSCuc004fjo.2. human. [P51606-1]
uc011mzh.1. human. [P51606-2]

Organism-specific databases

CTD5973.
GeneCardsGC0XM153200.
H-InvDBHIX0203300.
HGNCHGNC:9959. RENBP.
HPAHPA000428.
HPA000522.
MIM312420. gene.
neXtProtNX_P51606.
PharmGKBPA34325.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2942.
HOGENOMHOG000252296.
HOVERGENHBG102994.
InParanoidP51606.
KOK01787.
OMAILQHVQR.
PhylomeDBP51606.
TreeFamTF329027.

Enzyme and pathway databases

SABIO-RKP51606.
UniPathwayUPA00629.

Gene expression databases

ArrayExpressP51606.
BgeeP51606.
CleanExHS_RENBP.
GenevestigatorP51606.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
ProtoNetSearch...

Other

GeneWikiRENBP.
GenomeRNAi5973.
NextBio23253.
PROP51606.
SOURCESearch...

Entry information

Entry nameRENBP_HUMAN
AccessionPrimary (citable) accession number: P51606
Secondary accession number(s): B4DNZ3, Q96BI6
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM