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Q5T013 (HYI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Putative hydroxypyruvate isomerase

EC=5.3.1.22
Alternative name(s):
Endothelial cell apoptosis protein E-CE1
Gene names
Name:HYI
ORF Names:HT036, SB156
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde) By similarity.

Catalytic activity

Hydroxypyruvate = 2-hydroxy-3-oxopropanoate.

Induction

Up-regulated by exposure to 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (BPDE) after which is found in the culture medium of amniotic epithelial cells. Ref.7

Sequence similarities

Belongs to the hyi family.

Sequence caution

The sequence AAH06140.1 differs from that shown. Reason: Frameshift at position 271.

The sequence AAH19041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAV84474.1 differs from that shown. Reason: Frameshift at positions 215, 228, 232 and 238.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionhydroxypyruvate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5T013-1)

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: Q5T013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     248-277: Missing.
Isoform 3 (identifier: Q5T013-3)

The sequence of this isoform differs from the canonical sequence as follows:
     248-277: Missing.
Isoform 4 (identifier: Q5T013-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Putative hydroxypyruvate isomerase
PRO_0000289241

Natural variations

Alternative sequence1 – 7373Missing in isoform 2 and isoform 4.
VSP_025986
Alternative sequence248 – 27730Missing in isoform 2 and isoform 3.
VSP_025987
Natural variant2391D → N. Ref.6
Corresponds to variant rs17850049 [ dbSNP | Ensembl ].
VAR_032611

Experimental info

Sequence conflict181S → P in AAV84474. Ref.1
Sequence conflict181S → P in AAK67642. Ref.3
Sequence conflict181S → P in AAH19041. Ref.5
Sequence conflict2241S → KP in AAV84474. Ref.1

Sequences

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

Last modified May 29, 2007. Version 2.
Checksum: 79D5072A8717B4F7

FASTA27730,406
        10         20         30         40         50         60 
MAPLRFSANL SWLFPELSGL PARVRAAGSS GFEAVEVAWP YAETPEALAR AAREAGLRLV 

        70         80         90        100        110        120 
LINTPPGDQE KGEMGLGAVP GRQAAFREGL EQAVRYAKAL GCPRIHLMAG RVPQGADRIA 

       130        140        150        160        170        180 
VKAEMEAVFL ENLRHAAGVL AQEDLVGLLE PINTRITDPQ YFLDTPQQAA AILQKVGRPN 

       190        200        210        220        230        240 
LQLQMDIFHW QIMDGNLTGN IREFLPIVGH VQVAQVPGRG EPSSPGELNF PYLFQLLEDE 

       250        260        270 
GYKGFVGCEY QPRGDTVEGL SWLRSYWDRR GHPEAGQ 

« Hide

Isoform 2 [UniParc].

Checksum: D04A820535AB1705
Show »

FASTA17419,084
Isoform 3 [UniParc].

Checksum: DA0485BAB2BB5724
Show »

FASTA24726,874
Isoform 4 [UniParc].

Checksum: 80BF040C3520EBD7
Show »

FASTA20422,616

References

« Hide 'large scale' references
[1]"Study of a new protein that interacts with endostatin."
Zhang B.L., Fan B.X., Liu Y.N.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Liver.
[2]Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Hypothalamus.
[3]Li N., Zhang M., Wan T., Zhang W., Cao X.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] OF 41-247 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-247 (ISOFORM 3), VARIANT ASN-239.
Tissue: Kidney and Ovary.
[7]"Low concentration of anti-7,8-dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene induces alterations of extracellular protein profile of exposed epithelial cells."
Liu H., Shen J., Feng L., Yu Y.
Proteomics 9:4259-4264(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY775560 mRNA. Translation: AAV84474.1. Frameshift.
AF284750 mRNA. Translation: AAG59852.1.
AF284751 mRNA. Translation: AAG59853.1.
AY037165 mRNA. Translation: AAK67642.1.
AL583862 Genomic DNA. Translation: CAI14890.1.
AL583862 Genomic DNA. Translation: CAI14893.1.
CH471059 Genomic DNA. Translation: EAX07090.1.
CH471059 Genomic DNA. Translation: EAX07091.1.
CH471059 Genomic DNA. Translation: EAX07093.1.
CH471059 Genomic DNA. Translation: EAX07094.1.
BC006140 mRNA. Translation: AAH06140.1. Sequence problems.
BC019041 mRNA. Translation: AAH19041.1. Different initiation.
CCDSCCDS488.2. [Q5T013-3]
CCDS53309.1. [Q5T013-1]
RefSeqNP_001177809.1. NM_001190880.2. [Q5T013-1]
NP_001230455.1. NM_001243526.1.
NP_112484.3. NM_031207.5. [Q5T013-3]
UniGeneHs.709864.

3D structure databases

ProteinModelPortalQ5T013.
SMRQ5T013. Positions 5-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123621. 3 interactions.
IntActQ5T013. 1 interaction.
STRING9606.ENSP00000361507.

PTM databases

PhosphoSiteQ5T013.

Polymorphism databases

DMDM152125829.

Proteomic databases

MaxQBQ5T013.
PaxDbQ5T013.
PRIDEQ5T013.

Protocols and materials databases

DNASU81888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372425; ENSP00000361502; ENSG00000178922. [Q5T013-1]
ENST00000372432; ENSP00000361509; ENSG00000178922. [Q5T013-3]
ENST00000583037; ENSP00000461969; ENSG00000178922. [Q5T013-4]
GeneID81888.
KEGGhsa:81888.
UCSCuc001cjm.3. human. [Q5T013-1]

Organism-specific databases

CTD81888.
GeneCardsGC01M043916.
HGNCHGNC:26948. HYI.
HPAHPA040092.
neXtProtNX_Q5T013.
PharmGKBPA142671668.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3622.
HOVERGENHBG056845.
InParanoidQ5T013.
KOK01816.
PhylomeDBQ5T013.
TreeFamTF312858.

Gene expression databases

ArrayExpressQ5T013.
BgeeQ5T013.
CleanExHS_HYI.
GenevestigatorQ5T013.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
InterProIPR026040. HyI-like.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PIRSFPIRSF006241. HyI. 1 hit.
SUPFAMSSF51658. SSF51658. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi81888.
NextBio72232.
PROQ5T013.

Entry information

Entry nameHYI_HUMAN
AccessionPrimary (citable) accession number: Q5T013
Secondary accession number(s): D3DPX4 expand/collapse secondary AC list , D3DPX5, Q5Q9A2, Q7Z778, Q96S83, Q9BZR3, Q9BZR4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 81 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM