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Protein

Selenide, water dikinase 2

Gene

SEPHS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 sitei60 – 601Sequence analysis
Sitei63 – 631Important for catalytic activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi319 – 3257ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • selenide, water dikinase activity Source: UniProtKB

GO - Biological processi

  • selenocysteine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, Selenium

Enzyme and pathway databases

BRENDAi2.7.9.3. 2681.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:19686. SEPHS2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868765.

Polymorphism and mutation databases

DMDMi172044671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 448447Selenide, water dikinase 2PRO_0000127650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99611.
MaxQBiQ99611.
PaxDbiQ99611.
PRIDEiQ99611.

PTM databases

iPTMnetiQ99611.
PhosphoSiteiQ99611.

Expressioni

Gene expression databases

BgeeiQ99611.
CleanExiHS_SEPHS2.

Organism-specific databases

HPAiHPA047931.

Interactioni

Protein-protein interaction databases

BioGridi116588. 13 interactions.
IntActiQ99611. 1 interaction.
STRINGi9606.ENSP00000426234.

Structurei

3D structure databases

ProteinModelPortaliQ99611.
SMRiQ99611. Positions 38-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3939. Eukaryota.
COG0709. LUCA.
GeneTreeiENSGT00390000000950.
HOGENOMiHOG000219301.
HOVERGENiHBG001207.
InParanoidiQ99611.
KOiK01008.
PhylomeDBiQ99611.
TreeFamiTF313811.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR004536. SPS/SelD.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00476. selD. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q99611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEASATGAC GEAMAAAEGS SGPAGLTLGR SFSNYRPFEP QALGLSPSWR
60 70 80 90 100
LTGFSGMKGU GCKVPQEALL KLLAGLTRPD VRPPLGRGLV GGQEEASQEA
110 120 130 140 150
GLPAGAGPSP TFPALGIGMD SCVIPLRHGG LSLVQTTDFF YPLVEDPYMM
160 170 180 190 200
GRIACANVLS DLYAMGITEC DNMLMLLSVS QSMSEEEREK VTPLMVKGFR
210 220 230 240 250
DAAEEGGTAV TGGQTVVNPW IIIGGVATVV CQPNEFIMPD SAVVGDVLVL
260 270 280 290 300
TKPLGTQVAV NAHQWLDNPE RWNKVKMVVS REEVELAYQE AMFNMATLNR
310 320 330 340 350
TAAGLMHTFN AHAATDITGF GILGHSQNLA KQQRNEVSFV IHNLPIIAKM
360 370 380 390 400
AAVSKASGRF GLLQGTSAET SGGLLICLPR EQAARFCSEI KSSKYGEGHQ
410 420 430 440
AWIVGIVEKG NRTARIIDKP RVIEVLPRGA TAAVLAPDSS NASSEPSS
Length:448
Mass (Da):47,305
Last modified:February 26, 2008 - v3
Checksum:i309520C0CAE770F7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti269 – 2691P → A.
Corresponds to variant rs1804600 [ dbSNP | Ensembl ].
VAR_052345

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei60 – 601Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43286 mRNA. Translation: AAC50958.2.
AC116348 Genomic DNA. No translation available.
BC002381 mRNA. Translation: AAH02381.3.
BC016643 mRNA. Translation: AAH16643.1.
RefSeqiNP_036380.2. NM_012248.3.
UniGeneiHs.118725.

Genome annotation databases

EnsembliENST00000478753; ENSP00000418669; ENSG00000179918.
GeneIDi22928.
KEGGihsa:22928.

Keywords - Coding sequence diversityi

Polymorphism, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43286 mRNA. Translation: AAC50958.2.
AC116348 Genomic DNA. No translation available.
BC002381 mRNA. Translation: AAH02381.3.
BC016643 mRNA. Translation: AAH16643.1.
RefSeqiNP_036380.2. NM_012248.3.
UniGeneiHs.118725.

3D structure databases

ProteinModelPortaliQ99611.
SMRiQ99611. Positions 38-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116588. 13 interactions.
IntActiQ99611. 1 interaction.
STRINGi9606.ENSP00000426234.

PTM databases

iPTMnetiQ99611.
PhosphoSiteiQ99611.

Polymorphism and mutation databases

DMDMi172044671.

Proteomic databases

EPDiQ99611.
MaxQBiQ99611.
PaxDbiQ99611.
PRIDEiQ99611.

Protocols and materials databases

DNASUi22928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000478753; ENSP00000418669; ENSG00000179918.
GeneIDi22928.
KEGGihsa:22928.

Organism-specific databases

CTDi22928.
GeneCardsiSEPHS2.
H-InvDBHIX0012959.
HGNCiHGNC:19686. SEPHS2.
HPAiHPA047931.
MIMi606218. gene.
neXtProtiNX_Q99611.
PharmGKBiPA134868765.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3939. Eukaryota.
COG0709. LUCA.
GeneTreeiENSGT00390000000950.
HOGENOMiHOG000219301.
HOVERGENiHBG001207.
InParanoidiQ99611.
KOiK01008.
PhylomeDBiQ99611.
TreeFamiTF313811.

Enzyme and pathway databases

BRENDAi2.7.9.3. 2681.

Miscellaneous databases

ChiTaRSiSEPHS2. human.
GenomeRNAii22928.
NextBioi43647.
PROiQ99611.
SOURCEiSearch...

Gene expression databases

BgeeiQ99611.
CleanExiHS_SEPHS2.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR004536. SPS/SelD.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00476. selD. 1 hit.
ProtoNetiSearch...

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 sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Muscle and Skin.
  5. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSPS2_HUMAN
AccessioniPrimary (citable) accession number: Q99611
Secondary accession number(s): Q9BUQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 26, 2008
Last modified: March 16, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.