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P49903

- SPS1_HUMAN

UniProt

P49903 - SPS1_HUMAN

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Protein

Selenide, water dikinase 1

Gene
SEPHS1, SELD, SPS, SPS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 311 Reviewed prediction
Binding sitei32 – 321ATP
Sitei32 – 321Important for catalytic activity By 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
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 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

Isoform 1 : Cell membrane. Nucleus membrane 1 Publication
Isoform 2 : Cytoplasm 1 Publication
Isoform 3 : Cytoplasm 1 Publication
Isoform 4 : Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear membrane Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767Missing in isoform 3. VSP_046701Add
BLAST
Alternative sequencei251 – 32171Missing in isoform 2. VSP_046702Add
BLAST
Alternative sequencei322 – 39271GGLLI…PGATS → DVQ in isoform 4. VSP_047451Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601A → T in AAA87567. 1 Publication

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]
ENST00000537130; ENSP00000442768; ENSG00000086475. [P49903-3]
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 ]
ENST00000537130 ; ENSP00000442768 ; ENSG00000086475 . [P49903-3 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 126 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.

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

Similar proteinsi