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Q6P6M7

- SPCS_MOUSE

UniProt

Q6P6M7 - SPCS_MOUSE

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Protein
O-phosphoseryl-tRNA(Sec) selenium transferase
Gene
Sepsecs, D5Ertd135e
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis By similarity.

Catalytic activityi

O-phospho-L-seryl-tRNA(Sec) + selenophosphate + H2O = L-selenocysteinyl-tRNA(Sec) + 2 phosphate.

Cofactori

Pyridoxal phosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei74 – 741May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate
Binding sitei75 – 751PLP
Binding sitei97 – 971Substrate
Binding sitei98 – 981Substrate
Binding sitei105 – 1051Substrate
Binding sitei271 – 2711tRNA variable arm By similarity
Binding sitei313 – 3131Substrate
Binding sitei398 – 3981tRNA discriminator base By similarity

GO - Molecular functioni

  1. protein binding Source: HGNC
  2. pyridoxal phosphate binding Source: InterPro
  3. tRNA binding Source: HGNC
  4. transferase activity, transferring selenium-containing groups Source: InterPro

GO - Biological processi

  1. selenocysteine incorporation Source: HGNC
  2. selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, RNA-binding, Selenium, tRNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14964.
UniPathwayiUPA00906; UER00898.

Names & Taxonomyi

Protein namesi
Recommended name:
O-phosphoseryl-tRNA(Sec) selenium transferase (EC:2.9.1.2)
Alternative name(s):
Selenocysteine synthase
Short name:
Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Sep-tRNA:Sec-tRNA synthase
Short name:
SepSecS
UGA suppressor tRNA-associated protein
Gene namesi
Name:Sepsecs
Synonyms:D5Ertd135e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1098791. Sepsecs.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051Q → E: 50% of wild-type activity. 1 Publication
Mutagenesisi313 – 3131R → E: Virtually inactive. 1 Publication
Mutagenesisi313 – 3131R → S: 30% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504O-phosphoseryl-tRNA(Sec) selenium transferase
PRO_0000219876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841N6-(pyridoxal phosphate)lysine

Proteomic databases

MaxQBiQ6P6M7.
PaxDbiQ6P6M7.
PRIDEiQ6P6M7.

PTM databases

PhosphoSiteiQ6P6M7.

Expressioni

Gene expression databases

ArrayExpressiQ6P6M7.
BgeeiQ6P6M7.
GenevestigatoriQ6P6M7.

Interactioni

Subunit structurei

Homotetramer formed by a catalytic dimer and a non-catalytic dimer serving as a binding platform that orients tRNASec for catalysis.1 Publication

Protein-protein interaction databases

MINTiMINT-1857229.
STRINGi10090.ENSMUSP00000031069.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3815
Helixi48 – 6013
Helixi63 – 653
Helixi82 – 876
Turni88 – 903
Beta strandi95 – 973
Helixi109 – 12921
Beta strandi136 – 1427
Helixi144 – 15815
Beta strandi164 – 1685
Helixi173 – 1819
Beta strandi185 – 1895
Beta strandi192 – 1943
Beta strandi197 – 1993
Helixi202 – 21211
Helixi214 – 2163
Beta strandi217 – 2259
Helixi235 – 24511
Beta strandi249 – 2524
Turni254 – 2585
Helixi260 – 27213
Beta strandi277 – 2815
Helixi282 – 2865
Beta strandi293 – 2986
Helixi300 – 30910
Helixi317 – 35842
Beta strandi370 – 3767
Turni378 – 3803
Beta strandi381 – 3855
Helixi387 – 39711
Beta strandi404 – 4063
Beta strandi411 – 4144
Beta strandi417 – 4204
Turni421 – 4255
Beta strandi433 – 4375
Helixi444 – 46522

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC8X-ray1.65A19-468[»]
3BCAX-ray2.25A19-468[»]
3BCBX-ray1.85A19-468[»]
ProteinModelPortaliQ6P6M7.
SMRiQ6P6M7. Positions 23-467.

Miscellaneous databases

EvolutionaryTraceiQ6P6M7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4444Tetramerization
Add
BLAST
Regioni96 – 10611Phosphate loop (P-loop)
Add
BLAST

Sequence similaritiesi

Belongs to the SepSecS family.

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00390000007332.
HOGENOMiHOG000254245.
HOVERGENiHBG061363.
InParanoidiQ6P6M7.
KOiK03341.
OMAiNDYPCAY.
OrthoDBiEOG71G9TX.
PhylomeDBiQ6P6M7.
TreeFamiTF314381.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
PANTHERiPTHR12944. PTHR12944. 1 hit.
PfamiPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
PIRSFiPIRSF017689. SepSecS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03531. selenium_SpcS. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6P6M7-1 [UniParc]FASTAAdd to Basket

« Hide

MNPESFAAGE RRVSPAYVRQ GCEARRAHEH LIRLLLEQGK CPEDGWDEST    50
LELFLHELAV MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD 100
ISAVQPKAAG SSLLNKITNS LVLNVIKLAG VHSVASCFVV PMATGMSLTL 150
CFLTLRHKRP KAKYIIWPRI DQKSCFKSMV TAGFEPVVIE NVLEGDELRT 200
DLKAVEAKIQ ELGPEHILCL HSTTACFAPR VPDRLEELAV ICANYDIPHV 250
VNNAYGLQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFNE 300
PFIQDISKMY PGRASASPSL DVLITLLSLG CSGYRKLLKE RKEMFVYLST 350
QLKKLAEAHN ERLLQTPHNP ISLAMTLKTI DGHHDKAVTQ LGSMLFTRQV 400
SGARAVPLGN VQTVSGHTFR GFMSHADNYP CAYLNAAAAI GMKMQDVDLF 450
IKRLDKCLNI VRKEQTRASV VSGADRNKAE DADIEEMALK LDDVLGDVGQ 500
GPAL 504
Length:504
Mass (Da):55,326
Last modified:March 29, 2005 - v2
Checksum:iE106674A0C80D98B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001E → D in AAH62133. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK033654 mRNA. Translation: BAC28410.1.
BC062133 mRNA. Translation: AAH62133.1.
CCDSiCCDS19286.1.
RefSeqiNP_766078.1. NM_172490.3.
UniGeneiMm.244719.

Genome annotation databases

EnsembliENSMUST00000031069; ENSMUSP00000031069; ENSMUSG00000029173.
GeneIDi211006.
KEGGimmu:211006.
UCSCiuc008xko.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK033654 mRNA. Translation: BAC28410.1 .
BC062133 mRNA. Translation: AAH62133.1 .
CCDSi CCDS19286.1.
RefSeqi NP_766078.1. NM_172490.3.
UniGenei Mm.244719.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BC8 X-ray 1.65 A 19-468 [» ]
3BCA X-ray 2.25 A 19-468 [» ]
3BCB X-ray 1.85 A 19-468 [» ]
ProteinModelPortali Q6P6M7.
SMRi Q6P6M7. Positions 23-467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1857229.
STRINGi 10090.ENSMUSP00000031069.

PTM databases

PhosphoSitei Q6P6M7.

Proteomic databases

MaxQBi Q6P6M7.
PaxDbi Q6P6M7.
PRIDEi Q6P6M7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031069 ; ENSMUSP00000031069 ; ENSMUSG00000029173 .
GeneIDi 211006.
KEGGi mmu:211006.
UCSCi uc008xko.1. mouse.

Organism-specific databases

CTDi 51091.
MGIi MGI:1098791. Sepsecs.

Phylogenomic databases

eggNOGi COG0076.
GeneTreei ENSGT00390000007332.
HOGENOMi HOG000254245.
HOVERGENi HBG061363.
InParanoidi Q6P6M7.
KOi K03341.
OMAi NDYPCAY.
OrthoDBi EOG71G9TX.
PhylomeDBi Q6P6M7.
TreeFami TF314381.

Enzyme and pathway databases

UniPathwayi UPA00906 ; UER00898 .
BioCyci MetaCyc:MONOMER-14964.

Miscellaneous databases

EvolutionaryTracei Q6P6M7.
NextBioi 373121.
PROi Q6P6M7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6P6M7.
Bgeei Q6P6M7.
Genevestigatori Q6P6M7.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view ]
PANTHERi PTHR12944. PTHR12944. 1 hit.
Pfami PF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view ]
PIRSFi PIRSF017689. SepSecS. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR03531. selenium_SpcS. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: Cecum.
  2. "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: Limb.
  3. "Structure and catalytic mechanism of eukaryotic selenocysteine synthase."
    Ganichkin O.M., Xu X.M., Carlson B.A., Mix H., Hatfield D.L., Gladyshev V.N., Wahl M.C.
    J. Biol. Chem. 283:5849-5865(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 19-468 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, SUBSTRATE-BINDING SITES, COFACTOR, MUTAGENESIS OF GLN-105 AND ARG-313.

Entry informationi

Entry nameiSPCS_MOUSE
AccessioniPrimary (citable) accession number: Q6P6M7
Secondary accession number(s): Q8BZS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: September 3, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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

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