Q5T945 (Q5T945_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Glyoxylate reductase/hydroxypyruvate reductase EMBL CAI13848.1

Submitted name:
Glyoxylate reductase/hydroxypyruvate reductase, isoform CRA_b EMBL EAW58284.1
Submitted name:
cDNA, FLJ96788, Homo sapiens glyoxylate reductase/hydroxypyruvate reductase(GRHPR), mRNA EMBL BAG38053.1

Gene names

Name:	GRHPR EMBL CAI13848.1
ORF Names:	hCG_30089 EMBL EAW58284.1, RP11-397D12.2-002 EMBL CAI13848.1

Organism

Homo sapiens (Human) EMBL CAI13848.1

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. RuleBase RU003719

Ontologies

Keywords
Ligand	Pyruvate EMBL CAI13848.1
Gene Ontology (GO)
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5T945 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 68A0E311AA4E5650	FASTA	328	35,668
	10 20 30 40 50 60 MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS 70 80 90 100 110 120 DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL 130 140 150 160 170 180 TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF 190 200 210 220 230 240 LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF 250 260 270 280 290 300 INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR 310 320 TRNTMSLLAA NNLLAGLRGE PMPSELKL

References

[1]	"The sequence of the human genome." Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H. , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X. Science 291:1304-1351(2001) [PubMed: 11181995] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"NEDO functional analysis of protein and research application project." Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T. Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Testis EMBL BAG38053.1.
[3]	Bird C. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	Mural R.J., Istrail S., Sutton 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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK315690 mRNA. Translation: BAG38053.1. AL158155 Genomic DNA. Translation: CAI13848.1. CH471071 Genomic DNA. Translation: EAW58284.1.
IPI	IPI00037448.
RefSeq	NP_036335.1. NM_012203.1.
UniGene	Hs.155742.
3D structure databases
ProteinModelPortal	Q5T945.
SMR	Q5T945. Positions 5-328.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5T945.
Proteomic databases
PRIDE	Q5T945.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9380.
KEGG	hsa:9380.
Organism-specific databases
CTD	9380.
PharmGKB	PA28965.
Phylogenomic databases
HOVERGEN	HBG051838.
OMA	RGDVVNQ.
PhylomeDB	Q5T945.
Gene expression databases
ArrayExpress	Q5T945.
Bgee	Q5T945.
Family and domain databases
InterPro	IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KO	K00015. K00049.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view]
PROSITE	PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35148.

Entry information

Entry name

Q5T945_HUMAN

Accession

Primary (citable) accession number: Q5T945

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Disclaimer

Any 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.