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P49903

- SPS1_HUMAN

UniProt

P49903 - SPS1_HUMAN

Protein

Selenide, water dikinase 1

Gene

SEPHS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (13 Dec 2002)
      Previous versions | rss
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    Functioni

    Synthesizes selenophosphate from selenide and ATP.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Activated by phosphate ions and by potassium ions.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei31 – 311Sequence Analysis
    Binding sitei32 – 321ATP
    Sitei32 – 321Important for catalytic activityBy similarity
    Binding sitei87 – 871ATP
    Binding sitei110 – 1101ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi67 – 693ATP
    Nucleotide bindingi162 – 1643ATP; shared with dimeric partner
    Nucleotide bindingi267 – 2737ATP

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. GTP binding Source: ProtInc
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. selenide, water dikinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc

    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 1 (EC:2.7.9.3)
    Alternative name(s):
    Selenium donor protein 1
    Selenophosphate synthase 1
    Gene namesi
    Name:SEPHS1
    Synonyms:SELD, SPS, SPS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:19685. SEPHS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear membrane Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851T → A: Strongly reduced ADP hydrolysis. 1 Publication
    Mutagenesisi268 – 2681G → C: No change in ATP-binding. 1 Publication
    Mutagenesisi270 – 2701G → R: No change in ATP-binding. 1 Publication
    Mutagenesisi273 – 2731G → A, D or V: Loss of ATP-binding. 1 Publication
    Mutagenesisi274 – 2741H → N: Reduced ATP-binding. 1 Publication
    Mutagenesisi274 – 2741H → Y: Increased ATP-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134905215.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 392391Selenide, water dikinase 1PRO_0000127648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP49903.
    PaxDbiP49903.
    PeptideAtlasiP49903.
    PRIDEiP49903.

    PTM databases

    PhosphoSiteiP49903.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are gradually expressed during the cell cycle until G2/M phase and then decreased. Isoform 3 is gradually expressed during the cell cycle until S phase and then decreased.1 Publication

    Gene expression databases

    ArrayExpressiP49903.
    BgeeiP49903.
    CleanExiHS_SEPHS1.
    GenevestigatoriP49903.

    Organism-specific databases

    HPAiHPA037645.

    Interactioni

    Subunit structurei

    Homodimer (isoform 1, isoform 2, isoform 3 and isoform 4). Heterodimer of isoform 1 and isoform 3. Heterodimer of isoform 2 and isoform 4.2 Publications

    Protein-protein interaction databases

    BioGridi116589. 23 interactions.
    IntActiP49903. 10 interactions.
    STRINGi9606.ENSP00000367893.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Helixi20 – 234
    Helixi35 – 428
    Beta strandi68 – 747
    Beta strandi81 – 899
    Helixi96 – 11318
    Beta strandi120 – 12910
    Helixi134 – 15421
    Beta strandi159 – 16911
    Beta strandi171 – 18010
    Helixi182 – 1843
    Beta strandi196 – 2016
    Helixi205 – 2139
    Helixi230 – 24516
    Helixi249 – 2579
    Beta strandi262 – 2654
    Helixi270 – 27910
    Beta strandi283 – 29614
    Helixi299 – 3057
    Turni306 – 3083
    Helixi312 – 3143
    Beta strandi324 – 3285
    Helixi330 – 34112
    Beta strandi352 – 36211
    Beta strandi364 – 37512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FD5X-ray1.90A/B1-392[»]
    3FD6X-ray1.95A/B1-392[»]
    ProteinModelPortaliP49903.
    SMRiP49903. Positions 6-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49903.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0709.
    HOGENOMiHOG000219301.
    HOVERGENiHBG001207.
    InParanoidiP49903.
    KOiK01008.
    OMAiDQKHLLC.
    OrthoDBiEOG7SR4MT.
    PhylomeDBiP49903.
    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]
    PIRSFiPIRSF036407. Selenphspht_syn. 1 hit.
    SUPFAMiSSF55326. SSF55326. 1 hit.
    SSF56042. SSF56042. 1 hit.
    TIGRFAMsiTIGR00476. selD. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49903-1) [UniParc]FASTAAdd to Basket

    Also known as: Major type, MT

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF    50
    QEDEQFLGAV MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG 100
    RIACANVLSD LYAMGVTECD NMLMLLGVSN KMTDRERDKV MPLIIQGFKD 150
    AAEEAGTSVT GGQTVLNPWI VLGGVATTVC QPNEFIMPDN AVPGDVLVLT 200
    KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA MMNMARLNRT 250
    AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA 300
    AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ 350
    AWIIGIVEKG NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS 392
    Length:392
    Mass (Da):42,911
    Last modified:December 13, 2002 - v2
    Checksum:iE9636E38146D926D
    GO
    Isoform 2 (identifier: P49903-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta E8

    The sequence of this isoform differs from the canonical sequence as follows:
         251-321: Missing.

    Show »
    Length:321
    Mass (Da):35,479
    Checksum:i1894C5DBC991ABA8
    GO
    Isoform 3 (identifier: P49903-3) [UniParc]FASTAAdd to Basket

    Also known as: Delta E2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-67: Missing.

    Show »
    Length:325
    Mass (Da):35,208
    Checksum:i6938A3EB8339E631
    GO
    Isoform 4 (identifier: P49903-4) [UniParc]FASTAAdd to Basket

    Also known as: E9 and E9a

    The sequence of this isoform differs from the canonical sequence as follows:
         322-392: GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS → DVQ

    Show »
    Length:324
    Mass (Da):35,620
    Checksum:i538F17DE5C1D3644
    GO

    Sequence cautioni

    The sequence AAA87567.1 differs from that shown. Reason: Frameshift at position 377.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti260 – 2601A → T in AAA87567. (PubMed:7665581)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6767Missing in isoform 3. 2 PublicationsVSP_046701Add
    BLAST
    Alternative sequencei251 – 32171Missing in isoform 2. 1 PublicationVSP_046702Add
    BLAST
    Alternative sequencei322 – 39271GGLLI…PGATS → DVQ in isoform 4. 1 PublicationVSP_047451Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34044 mRNA. Translation: AAA87567.1. Frameshift.
    GU954545 mRNA. Translation: ADF78120.1.
    GU954546 mRNA. Translation: ADF78121.1.
    GU954547 mRNA. Translation: ADF78122.1.
    GU954548 mRNA. Translation: ADF78123.1.
    GU954549 mRNA. Translation: ADF78124.1.
    AK301568 mRNA. Translation: BAG63062.1.
    AL138764, AL355870 Genomic DNA. Translation: CAI12907.1.
    AL355870, AL138764 Genomic DNA. Translation: CAI14198.1.
    CH471072 Genomic DNA. Translation: EAW86289.1.
    CH471072 Genomic DNA. Translation: EAW86290.1.
    CH471072 Genomic DNA. Translation: EAW86291.1.
    CH471072 Genomic DNA. Translation: EAW86292.1.
    CH471072 Genomic DNA. Translation: EAW86293.1.
    BC000941 mRNA. Translation: AAH00941.1.
    BC063816 mRNA. Translation: AAH63816.1.
    CCDSiCCDS55702.1. [P49903-3]
    CCDS55703.1. [P49903-2]
    CCDS7098.1. [P49903-1]
    RefSeqiNP_001182531.1. NM_001195602.1. [P49903-3]
    NP_001182533.1. NM_001195604.1. [P49903-2]
    NP_036379.2. NM_012247.4. [P49903-1]
    UniGeneiHs.124027.

    Genome annotation databases

    EnsembliENST00000327347; ENSP00000367893; ENSG00000086475. [P49903-1]
    ENST00000378614; ENSP00000367877; ENSG00000086475. [P49903-2]
    ENST00000545675; ENSP00000441119; ENSG00000086475. [P49903-4]
    GeneIDi22929.
    KEGGihsa:22929.
    UCSCiuc001imh.3. human. [P49903-1]
    uc021pnc.1. human.

    Polymorphism databases

    DMDMi27151792.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34044 mRNA. Translation: AAA87567.1 . Frameshift.
    GU954545 mRNA. Translation: ADF78120.1 .
    GU954546 mRNA. Translation: ADF78121.1 .
    GU954547 mRNA. Translation: ADF78122.1 .
    GU954548 mRNA. Translation: ADF78123.1 .
    GU954549 mRNA. Translation: ADF78124.1 .
    AK301568 mRNA. Translation: BAG63062.1 .
    AL138764 , AL355870 Genomic DNA. Translation: CAI12907.1 .
    AL355870 , AL138764 Genomic DNA. Translation: CAI14198.1 .
    CH471072 Genomic DNA. Translation: EAW86289.1 .
    CH471072 Genomic DNA. Translation: EAW86290.1 .
    CH471072 Genomic DNA. Translation: EAW86291.1 .
    CH471072 Genomic DNA. Translation: EAW86292.1 .
    CH471072 Genomic DNA. Translation: EAW86293.1 .
    BC000941 mRNA. Translation: AAH00941.1 .
    BC063816 mRNA. Translation: AAH63816.1 .
    CCDSi CCDS55702.1. [P49903-3 ]
    CCDS55703.1. [P49903-2 ]
    CCDS7098.1. [P49903-1 ]
    RefSeqi NP_001182531.1. NM_001195602.1. [P49903-3 ]
    NP_001182533.1. NM_001195604.1. [P49903-2 ]
    NP_036379.2. NM_012247.4. [P49903-1 ]
    UniGenei Hs.124027.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FD5 X-ray 1.90 A/B 1-392 [» ]
    3FD6 X-ray 1.95 A/B 1-392 [» ]
    ProteinModelPortali P49903.
    SMRi P49903. Positions 6-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116589. 23 interactions.
    IntActi P49903. 10 interactions.
    STRINGi 9606.ENSP00000367893.

    PTM databases

    PhosphoSitei P49903.

    Polymorphism databases

    DMDMi 27151792.

    Proteomic databases

    MaxQBi P49903.
    PaxDbi P49903.
    PeptideAtlasi P49903.
    PRIDEi P49903.

    Protocols and materials databases

    DNASUi 22929.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327347 ; ENSP00000367893 ; ENSG00000086475 . [P49903-1 ]
    ENST00000378614 ; ENSP00000367877 ; ENSG00000086475 . [P49903-2 ]
    ENST00000545675 ; ENSP00000441119 ; ENSG00000086475 . [P49903-4 ]
    GeneIDi 22929.
    KEGGi hsa:22929.
    UCSCi uc001imh.3. human. [P49903-1 ]
    uc021pnc.1. human.

    Organism-specific databases

    CTDi 22929.
    GeneCardsi GC10M013360.
    HGNCi HGNC:19685. SEPHS1.
    HPAi HPA037645.
    MIMi 600902. gene.
    neXtProti NX_P49903.
    PharmGKBi PA134905215.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0709.
    HOGENOMi HOG000219301.
    HOVERGENi HBG001207.
    InParanoidi P49903.
    KOi K01008.
    OMAi DQKHLLC.
    OrthoDBi EOG7SR4MT.
    PhylomeDBi P49903.
    TreeFami TF313811.

    Enzyme and pathway databases

    BRENDAi 2.7.9.3. 2681.

    Miscellaneous databases

    EvolutionaryTracei P49903.
    GeneWikii Selenophosphate_synthetase_1.
    GenomeRNAii 22929.
    NextBioi 35492713.
    PROi P49903.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49903.
    Bgeei P49903.
    CleanExi HS_SEPHS1.
    Genevestigatori P49903.

    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 ]
    PIRSFi PIRSF036407. Selenphspht_syn. 1 hit.
    SUPFAMi SSF55326. SSF55326. 1 hit.
    SSF56042. SSF56042. 1 hit.
    TIGRFAMsi TIGR00476. selD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis."
      Low S.C., Harney J.W., Berry M.J.
      J. Biol. Chem. 270:21659-21664(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ATP-BINDING, MUTAGENESIS OF GLY-268; GLY-270; GLY-273 AND HIS-274.
      Tissue: Liver.
    2. "Human selenophosphate synthetase 1 has five splice variants with unique interactions, subcellular localizations and expression patterns."
      Kim J.Y., Lee K.H., Shim M.S., Shin H., Xu X.M., Carlson B.A., Hatfield D.L., Lee B.J.
      Biochem. Biophys. Res. Commun. 397:53-58(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Mammary gland.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Placenta and PNS.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 5-16 AND 64-76, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structures of catalytic intermediates of human selenophosphate synthetase 1."
      Wang K.T., Wang J., Li L.F., Su X.D.
      J. Mol. Biol. 390:747-759(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM IONS AND PHOSPHATE, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF THR-85.

    Entry informationi

    Entry nameiSPS1_HUMAN
    AccessioniPrimary (citable) accession number: P49903
    Secondary accession number(s): B4DWK0
    , D3DRS9, D6PSQ9, Q5T5U8, Q5T5U9, Q9BVT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 13, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Caution

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3