Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8BH69 (SPS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 1
EC=2.7.9.3
Alternative name(s):
Selenium donor protein 1
Selenophosphate synthase 1
Gene names
Name:Sephs1
Synonyms:Sps1
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 length392 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Synthesizes selenophosphate from selenide and ATP.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Caution

The conserved active site Cys (or selenocysteine) residue in position 29 is replaced by a Thr. However, as function in selenoprotein synthesis is probable, it is possible Cys-31 is the active site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Selenide, water dikinase 1
PRO_0000127649

Regions

Nucleotide binding67 – 693ATP By similarity
Nucleotide binding162 – 1643ATP; shared with dimeric partner By similarity
Nucleotide binding267 – 2737ATP By similarity

Sites

Active site311 Potential
Binding site321ATP By similarity
Binding site871ATP By similarity
Binding site1101ATP By similarity
Site321Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BH69 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 46627E6ADB3D593C

FASTA39242,907
        10         20         30         40         50         60 
MSTRESFNPE TYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV 

        70         80         90        100        110        120 
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD 

       130        140        150        160        170        180 
NMLMLLGVSN KMTDRERDKV IPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC 

       190        200        210        220        230        240 
QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA 

       250        260        270        280        290        300 
MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA 

       310        320        330        340        350        360 
AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG 

       370        380        390 
NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS

« Hide

References

[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. 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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK044971 mRNA. Translation: BAC32163.1.
AK053638 mRNA. Translation: BAC35456.1.
IPIIPI00221759.
RefSeqNP_780609.4. NM_175400.6.
UniGeneMm.34329.

3D structure databases

ProteinModelPortalQ8BH69.
SMRQ8BH69. Positions 6-377.
ModBaseSearch...

PTM databases

PhosphoSiteQ8BH69.

Proteomic databases

PaxDbQ8BH69.
PRIDEQ8BH69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027973; ENSMUSP00000027973; ENSMUSG00000026662.
ENSMUST00000115019; ENSMUSP00000110671; ENSMUSG00000026662.
GeneID109079.
KEGGmmu:109079.

Organism-specific databases

CTD22929.
MGIMGI:1923580. Sephs1.

Phylogenomic databases

eggNOGCOG0709.
GeneTreeENSGT00390000000950.
HOGENOMHOG000219301.
HOVERGENHBG001207.
InParanoidQ8BH69.
KOK01008.
OMAYEMASAS.
OrthoDBEOG4ZW5B4.

Gene expression databases

ArrayExpressQ8BH69.
BgeeQ8BH69.
CleanExMM_SEPHS1.
GenevestigatorQ8BH69.
GermOnlineENSMUSG00000026662. 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]
PIRSFPIRSF036407. Selenphspht_syn. 1 hit.
SUPFAMSSF56042. AIR_synth_C. 1 hit.
SSF55326. PurM_N-like. 1 hit.
TIGRFAMsTIGR00476. selD. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEPHS1. mouse.
NextBio361628.
SOURCESearch...

Entry information

Entry nameSPS1_MOUSE
AccessionPrimary (citable) accession number: Q8BH69
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 86 of the entry and version 1 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