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P97364

- SPS2_MOUSE

UniProt

P97364 - SPS2_MOUSE

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Protein

Selenide, water dikinase 2

Gene

Sephs2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Synthesizes selenophosphate from selenide and ATP.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Sequence Analysis
Sitei66 – 661Important for catalytic activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi322 – 3287ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. selenide, water dikinase activity Source: MGI

GO - Biological processi

  1. selenium compound metabolic process Source: MGI
  2. selenocysteine biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, Selenium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14949.
BRENDAi2.7.9.3. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Selenide, water dikinase 2 (EC:2.7.9.3)
Alternative name(s):
Selenium donor protein 2
Selenophosphate synthase 2
Gene namesi
Name:Sephs2
Synonyms:Sps2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:108388. Sephs2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 452451Selenide, water dikinase 2PRO_0000127651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP97364.
PaxDbiP97364.
PRIDEiP97364.

2D gel databases

REPRODUCTION-2DPAGEIPI00124181.

PTM databases

PhosphoSiteiP97364.

Expressioni

Gene expression databases

BgeeiP97364.
CleanExiMM_SEPHS2.
GenevestigatoriP97364.

Interactioni

Protein-protein interaction databases

IntActiP97364. 2 interactions.
MINTiMINT-1865888.

Structurei

3D structure databases

ProteinModelPortaliP97364.
SMRiP97364. Positions 41-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 98Poly-Ala
Compositional biasi433 – 4408Poly-Ala

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0709.
GeneTreeiENSGT00390000000950.
HOGENOMiHOG000219301.
HOVERGENiHBG001207.
InParanoidiP97364.
KOiK01008.
OMAiSVSQKMN.
OrthoDBiEOG7SR4MT.
PhylomeDBiP97364.
TreeFamiTF313811.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR016188. PurM_N-like.
IPR004536. SelD.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMiSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00476. selD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97364-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAAAAGAS GETMAALVAA EGSLGPAGWS AGRSFSNYRP FEPQTLGFSP
60 70 80 90 100
SWRLTSFSGM KGUGCKVPQE TLLKLLEGLT RPALQPPLTS GLVGGQEETV
110 120 130 140 150
QEGGLSTRPG PGSAFPSLSI GMDSCVIPLR HGGLSLVQTT DFFYPLVEDP
160 170 180 190 200
YMMGRIACAN VLSDLYAMGI TECDNMLMLL SVSQSMSEKE REKVTPLMIK
210 220 230 240 250
GFRDAAEEGG TAVTGGQTVV NPWIIIGGVA TVVCQQNEFI MPDSAVVGDV
260 270 280 290 300
LVLTKPLGTQ VAANAHQWLD NPEKWNKIKM VVSREEVELA YQEAMFNMAT
310 320 330 340 350
LNRTAAGLMH TFNAHAATDI TGFGILGHSQ NLAKQQKNEV SFVIHNLPII
360 370 380 390 400
AKMAAISKAS GRFGLLQGTS AETSGGLLIC LPREQAARFC SEIKSSKYGE
410 420 430 440 450
GHQAWIVGIV EKGNRTARII DKPRVIEVLP RGASAAAAAA PDNSNAASEP

SS
Length:452
Mass (Da):47,834
Last modified:February 26, 2008 - v3
Checksum:iCF82585D01ABE3BF
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei63 – 631Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS21863.1.
RefSeqiNP_033292.2. NM_009266.3.
UniGeneiMm.20294.

Genome annotation databases

EnsembliENSMUST00000082428; ENSMUSP00000081009; ENSMUSG00000049091.
GeneIDi20768.
KEGGimmu:20768.
UCSCiuc009jux.2. mouse.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS21863.1.
RefSeqi NP_033292.2. NM_009266.3.
UniGenei Mm.20294.

3D structure databases

ProteinModelPortali P97364.
SMRi P97364. Positions 41-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97364. 2 interactions.
MINTi MINT-1865888.

PTM databases

PhosphoSitei P97364.

2D gel databases

REPRODUCTION-2DPAGE IPI00124181.

Proteomic databases

MaxQBi P97364.
PaxDbi P97364.
PRIDEi P97364.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000082428 ; ENSMUSP00000081009 ; ENSMUSG00000049091 .
GeneIDi 20768.
KEGGi mmu:20768.
UCSCi uc009jux.2. mouse.

Organism-specific databases

CTDi 22928.
MGIi MGI:108388. Sephs2.

Phylogenomic databases

eggNOGi COG0709.
GeneTreei ENSGT00390000000950.
HOGENOMi HOG000219301.
HOVERGENi HBG001207.
InParanoidi P97364.
KOi K01008.
OMAi SVSQKMN.
OrthoDBi EOG7SR4MT.
PhylomeDBi P97364.
TreeFami TF313811.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14949.
BRENDAi 2.7.9.3. 3474.

Miscellaneous databases

NextBioi 299475.
PROi P97364.
SOURCEi Search...

Gene expression databases

Bgeei P97364.
CleanExi MM_SEPHS2.
Genevestigatori P97364.

Family and domain databases

Gene3Di 3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProi IPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR016188. PurM_N-like.
IPR004536. SelD.
[Graphical view ]
Pfami PF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view ]
SUPFAMi SSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsi TIGR00476. selD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiSPS2_MOUSE
AccessioniPrimary (citable) accession number: P97364
Secondary accession number(s): Q3TGI4, Q80ZY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 26, 2008
Last modified: October 1, 2014
This is version 112 of the entry and version 3 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

External Data

Dasty 3