Q9NQ88 (TIGAR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable fructose-2,6-bisphosphatase TIGAR
EC=3.1.3.46

Alternative name(s):
TP53-induced glycolysis and apoptosis regulator

Gene names

Name:	TIGAR
Synonyms:	C12orf5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable fructose-biphosphatase. Lowers cellular levels of fructose 2,6-bisphosphate. Protects cells against reactive oxygen species and against apoptosis induced by p53/TP53. Ref.6
Catalytic activity	Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Induction	Rapidly up-regulated by p53/TP53. Ref.6
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8
Sequence similarities	Belongs to the phosphoglycerate mutase family.
Caution	Not expected to have any kinase activity.

Ontologies

Keywords
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	intracellular Inferred from direct assay. Source: LIFEdb
Molecular function	fructose-2,6-bisphosphate 2-phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Probable fructose-2,6-bisphosphatase TIGAR

PRO_0000179957

Sites

Active site

11

1

Tele-phosphohistidine intermediate By similarity

Active site

198

1

Probable

Amino acid modifications

Modified residue

34

1

Phosphothreonine Ref.8

Modified residue

50

1

N6-acetyllysine Ref.9

Modified residue

154

1

Phosphoserine Ref.7

Experimental info

Mutagenesis

11

1

H → A: Abolishes ability to lower cellular fructose-2,6-bisphosphate levels; when associated with A-102 and A-198. Ref.6

Mutagenesis

102

1

E → A: Abolishes ability to lower cellular fructose-2,6-bisphosphate levels; when associated with A-11 and A-198. Ref.6

Mutagenesis

198

1

H → A: Abolishes ability to lower cellular fructose-2,6-bisphosphate levels; when associated with A-11 and A-102. Ref.6

Secondary structure

1

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270

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Helix

15 – 19

5

Helix

37 – 41

5

Turn

45 – 48

4

Beta strand

52 – 56

5

Helix

60 – 66

7

Helix

70 – 72

3

Beta strand

81 – 83

3

Helix

85 – 87

3

Helix

100 – 109

10

Turn

114 – 116

3

Helix

125 – 130

6

Helix

134 – 149

16

Helix

161 – 167

7

Beta strand

192 – 197

6

Helix

201 – 211

11

Helix

223 – 227

5

Beta strand

236 – 242

7

Beta strand

251 – 258

8

Sequences

	Sequence		Length	Mass (Da)
	Q9NQ88 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B85D59659AD96E39	FASTA	270	30,063
	10 20 30 40 50 60 MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM 70 80 90 100 110 120 RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP 130 140 150 160 170 180 GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV 190 200 210 220 230 240 NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII 250 260 270 NFEEGREVKP TVQCICMNLQ DHLNGLTETR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23." White K.E., Evans W.E., O'Riordan J.L.H., Speer M.C., Econs M.J., Lorenz-Depiereux B., Grabowski M., Meitinger T., Strom T.M. Nat. Genet. 26:345-348(2000) [PubMed: 11062477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Screening and cloning of the target genes transactivated by human gene 2 transactivated by nonstructural protein 3 of Hepatitis C virus using suppression subtractive hybridization technique." Cheng J., Dang X., Wang J., Ji D., Wang C., Yang Q., Liu Y. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	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. , 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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: B-cell.
[6]	"TIGAR, a p53-inducible regulator of glycolysis and apoptosis." Bensaad K., Tsuruta A., Selak M.A., Vidal M.N., Nakano K., Bartrons R., Gottlieb E., Vousden K.H. Cell 126:107-120(2006) [PubMed: 16839880] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-11; GLU-102 AND HIS-198, INDUCTION.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ272206 mRNA. Translation: CAC01127.1.
AY425618 mRNA. Translation: AAQ98969.1.
AK313226 mRNA. Translation: BAG36037.1.
CH471116 Genomic DNA. Translation: EAW88849.1.
BC012340 mRNA. Translation: AAH12340.1.

IPI

IPI00006907.

RefSeq

NP_065108.1. NM_020375.2.

UniGene

Hs.504545.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DCY	X-ray	1.75	A	2-270	[»]

ProteinModelPortal

Q9NQ88.

SMR

Q9NQ88. Positions 2-264.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQ88. 1 interaction.

STRING

Q9NQ88.

PTM databases

PhosphoSite

Q9NQ88.

Polymorphism databases

DMDM

74734311.

Proteomic databases

PRIDE

Q9NQ88.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000179259; ENSP00000179259; ENSG00000078237.

GeneID

57103.

KEGG

hsa:57103.

NMPDR

fig|9606.3.peg.6983.

UCSC

uc001qmp.1. human.

Organism-specific databases

CTD

57103.

GeneCards

GC12P004430.

HGNC

HGNC:1185. C12orf5.

HPA

CAB034010.

MIM

610775. gene.

neXtProt

NX_Q9NQ88.

PharmGKB

PA25506.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17541.

GeneTree

ENSGT00390000013224.

HOGENOM

HBG445749.

HOVERGEN

HBG108569.

InParanoid

Q9NQ88.

OMA

ETGFKQA.

OrthoDB

EOG40GCRZ.

PhylomeDB

Q9NQ88.

Gene expression databases

ArrayExpress

Q9NQ88.

Bgee

Q9NQ88.

CleanEx

HS_C12orf5.

Genevestigator

Q9NQ88.

GermOnline

ENSG00000078237. Homo sapiens.

Family and domain databases

InterPro

IPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]

KO

K14634.

Pfam

PF00300. His_Phos_1. 1 hit.
[Graphical view]

SMART

SM00855. PGAM. 1 hit.
[Graphical view]

PROSITE

PS00175. PG_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

62937.

SOURCE

Search...

Entry information

Entry name

TIGAR_HUMAN

Accession

Primary (citable) accession number: Q9NQ88
Secondary accession number(s): B2R840

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.