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P97364 (SPS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenide, water dikinase 2
EC=2.7.9.3
Alternative name(s):
Selenium donor protein 2
Selenophosphate synthase 2
Gene names
Name:Sephs2
Synonyms:Sps2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Synthesizes selenophosphate from selenide and ATP.

Catalytic activity

ATP + selenide + H2O = AMP + selenophosphate + phosphate.

Sequence similarities

Belongs to the selenophosphate synthase 1 family. Class I subfamily.

Ontologies

Keywords
   Coding sequence diversitySelenocysteine
   LigandATP-binding
Nucleotide-binding
Selenium
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

selenide, water dikinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Selenide, water dikinase 2
PRO_0000127651

Regions

Nucleotide binding322 – 3287ATP Potential
Compositional bias2 – 98Poly-Ala
Compositional bias433 – 4408Poly-Ala

Sites

Active site631 Potential
Site661Important for catalytic activity By similarity

Amino acid modifications

Non-standard residue631Selenocysteine

Sequences

Sequence LengthMass (Da)Tools
P97364 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: CF82585D01ABE3BF

FASTA45247,834
        10         20         30         40         50         60 
MAEAAAAGAS GETMAALVAA EGSLGPAGWS AGRSFSNYRP FEPQTLGFSP SWRLTSFSGM 

        70         80         90        100        110        120 
KGUGCKVPQE TLLKLLEGLT RPALQPPLTS GLVGGQEETV QEGGLSTRPG PGSAFPSLSI 

       130        140        150        160        170        180 
GMDSCVIPLR HGGLSLVQTT DFFYPLVEDP YMMGRIACAN VLSDLYAMGI TECDNMLMLL 

       190        200        210        220        230        240 
SVSQSMSEKE REKVTPLMIK GFRDAAEEGG TAVTGGQTVV NPWIIIGGVA TVVCQQNEFI 

       250        260        270        280        290        300 
MPDSAVVGDV LVLTKPLGTQ VAANAHQWLD NPEKWNKIKM VVSREEVELA YQEAMFNMAT 

       310        320        330        340        350        360 
LNRTAAGLMH TFNAHAATDI TGFGILGHSQ NLAKQQKNEV SFVIHNLPII AKMAAISKAS 

       370        380        390        400        410        420 
GRFGLLQGTS AETSGGLLIC LPREQAARFC SEIKSSKYGE GHQAWIVGIV EKGNRTARII 

       430        440        450 
DKPRVIEVLP RGASAAAAAA PDNSNAASEP SS

« Hide

References

« Hide 'large scale' references
[1]"A new approach to the study of haematopoietic development in the yolk sac and embryoid bodies."
Guimaraes M.J., Bazan J.F., Zlotnik A., Wiles M.V., Grimaldi J.C., Lee F., McClanahan T.
Development 121:3335-3346(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?"
Guimaraes M.J., Peterson D., Vicari A., Cocks B.G., Copeland N.G., Gilbert D.J., Jenkins N.A., Ferrick D.A., Kastelein R., Bazan J.F., Zlotnik A.
Proc. Natl. Acad. Sci. U.S.A. 93:15086-15091(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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. expand/collapse author list , 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: C57BL/6J.
Tissue: Amnion, Kidney and Liver.
[4]"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: Liver and Salivary gland.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 353-362, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43285 mRNA. Translation: AAC53024.2.
AK149516 mRNA. Translation: BAE28931.1.
AK168722 mRNA. Translation: BAE40564.1.
AK168965 mRNA. Translation: BAE40770.1.
BC016508 mRNA. Translation: AAH16508.1.
BC028966 mRNA. Translation: AAH28966.1.
BC043334 mRNA. Translation: AAH43334.2.
IPIIPI00124181.
RefSeqNP_033292.2. NM_009266.3.
UniGeneMm.20294.

3D structure databases

ProteinModelPortalP97364.
SMRP97364. Positions 41-430.
ModBaseSearch...

PTM databases

PhosphoSiteP97364.

2D gel databases

REPRODUCTION-2DPAGEIPI00124181.

Proteomic databases

PaxDbP97364.
PRIDEP97364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000082428; ENSMUSP00000081009; ENSMUSG00000049091.
GeneID20768.
KEGGmmu:20768.
UCSCuc009jux.1. mouse.

Organism-specific databases

CTD22928.
MGIMGI:108388. Sephs2.

Phylogenomic databases

eggNOGCOG0709.
GeneTreeENSGT00390000000950.
HOGENOMHOG000219301.
HOVERGENHBG001207.
InParanoidP97364.
KOK01008.
OMAGMDSCVI.
OrthoDBEOG4ZW5B4.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14949.
BRENDA2.7.9.3. 3474.

Gene expression databases

BgeeP97364.
CleanExMM_SEPHS2.
GenevestigatorP97364.
GermOnlineENSMUSG00000049091. Mus musculus.

Family and domain databases

InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR016188. PurM_N-like.
IPR004536. SelD.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMSSF56042. AIR_synth_C. 1 hit.
SSF55326. PurM_N-like. 1 hit.
TIGRFAMsTIGR00476. selD. 1 hit.
ProtoNetSearch...

Other

NextBio299475.
SOURCESearch...

Entry information

Entry nameSPS2_MOUSE
AccessionPrimary (citable) accession number: P97364
Secondary accession number(s): Q3TGI4, Q80ZY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 26, 2008
Last modified: April 3, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents