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Protein

Fumarylacetoacetate hydrolase domain-containing protein 2A

Gene

Fahd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May have hydrolase activity.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi159 – 1591Divalent metal cationBy similarity
Metal bindingi161 – 1611Divalent metal cationBy similarity
Metal bindingi190 – 1901Divalent metal cationBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarylacetoacetate hydrolase domain-containing protein 2A (EC:3.-.-.-)
Gene namesi
Name:Fahd2
Synonyms:Fahd2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1915376. Fahd2a.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Fumarylacetoacetate hydrolase domain-containing protein 2APRO_0000289797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei202 – 2021N6-acetyllysine; alternateCombined sources
Modified residuei202 – 2021N6-succinyllysine; alternateCombined sources
Modified residuei233 – 2331N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3TC72.
MaxQBiQ3TC72.
PaxDbiQ3TC72.
PeptideAtlasiQ3TC72.
PRIDEiQ3TC72.

2D gel databases

REPRODUCTION-2DPAGEIPI00121218.
Q3TC72.

PTM databases

iPTMnetiQ3TC72.
PhosphoSiteiQ3TC72.

Expressioni

Gene expression databases

BgeeiQ3TC72.

Interactioni

Protein-protein interaction databases

IntActiQ3TC72. 2 interactions.
MINTiMINT-4116821.
STRINGi10090.ENSMUSP00000028848.

Structurei

3D structure databases

ProteinModelPortaliQ3TC72.
SMRiQ3TC72. Positions 92-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAH family.Curated

Phylogenomic databases

eggNOGiKOG1535. Eukaryota.
COG0179. LUCA.
HOGENOMiHOG000063754.
HOVERGENiHBG104460.
InParanoidiQ3TC72.
OrthoDBiEOG7DFXDC.
PhylomeDBiQ3TC72.
TreeFamiTF300911.

Family and domain databases

Gene3Di3.90.850.10. 1 hit.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3TC72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGFGRRRLF SALLQVQKRP CQPSRNMRLV QFQAPHLEEP HLGLESGVGG
60 70 80 90 100
GVVDLNAFDS TLPKTMVQFL EQGETTLSVA RRALATQLPV IPRSQVTFLA
110 120 130 140 150
PVTRPEKVIC VGLNYADHCQ EQNVRVPKSP IIFSKFSSSI VGPYDEIILP
160 170 180 190 200
PESKEVDWEV EMAVVIGKKG KHIKATDVMA HVAGFTVAHD VSARDWQMRN
210 220 230 240 250
GKQWLLGKTF DTFCPLGPAL VTKDTIADPH NLKICCRVNG EVVQSSNTNQ
260 270 280 290 300
MVFKTEYLIA WVSQFVTLYP GDLLLTGTPP GVGMFRKPPV FLKKGDEVQC
310
EIEELGVIIN KVV
Length:313
Mass (Da):34,690
Last modified:October 11, 2005 - v1
Checksum:iBEB04730B0371E67
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061E → D in BAC38052 (PubMed:16141072).Curated
Sequence conflicti106 – 1061E → D in AAH30182 (PubMed:15489334).Curated
Sequence conflicti106 – 1061E → D in CAM13449 (PubMed:19468303).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080868 mRNA. Translation: BAC38052.1.
AK170875 mRNA. Translation: BAE42085.1.
BC030182 mRNA. Translation: AAH30182.1.
AL731831 Genomic DNA. Translation: CAM13449.1.
CCDSiCCDS16702.1.
RefSeqiNP_083905.1. NM_029629.2.
UniGeneiMm.288676.

Genome annotation databases

GeneIDi68126.
KEGGimmu:68126.
UCSCiuc008mfk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080868 mRNA. Translation: BAC38052.1.
AK170875 mRNA. Translation: BAE42085.1.
BC030182 mRNA. Translation: AAH30182.1.
AL731831 Genomic DNA. Translation: CAM13449.1.
CCDSiCCDS16702.1.
RefSeqiNP_083905.1. NM_029629.2.
UniGeneiMm.288676.

3D structure databases

ProteinModelPortaliQ3TC72.
SMRiQ3TC72. Positions 92-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3TC72. 2 interactions.
MINTiMINT-4116821.
STRINGi10090.ENSMUSP00000028848.

PTM databases

iPTMnetiQ3TC72.
PhosphoSiteiQ3TC72.

2D gel databases

REPRODUCTION-2DPAGEIPI00121218.
Q3TC72.

Proteomic databases

EPDiQ3TC72.
MaxQBiQ3TC72.
PaxDbiQ3TC72.
PeptideAtlasiQ3TC72.
PRIDEiQ3TC72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi68126.
KEGGimmu:68126.
UCSCiuc008mfk.2. mouse.

Organism-specific databases

CTDi51011.
MGIiMGI:1915376. Fahd2a.

Phylogenomic databases

eggNOGiKOG1535. Eukaryota.
COG0179. LUCA.
HOGENOMiHOG000063754.
HOVERGENiHBG104460.
InParanoidiQ3TC72.
OrthoDBiEOG7DFXDC.
PhylomeDBiQ3TC72.
TreeFamiTF300911.

Miscellaneous databases

PROiQ3TC72.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TC72.

Family and domain databases

Gene3Di3.90.850.10. 1 hit.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 108-125, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFAHD2_MOUSE
AccessioniPrimary (citable) accession number: Q3TC72
Secondary accession number(s): Q8K0V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.