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Protein

L-seryl-tRNA(Sec) kinase

Gene

Pstk

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

Functioni

Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis. No activity with other tRNAs has been detected.

Catalytic activityi

ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec).

Cofactori

Pathwayi: selenocysteinyl-tRNA(Sec) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. L-seryl-tRNA(Sec) kinase (Pstk)
  2. O-phosphoseryl-tRNA(Sec) selenium transferase (Sepsecs), O-phosphoseryl-tRNA(Sec) selenium transferase (Sepsecs)
This subpathway is part of the pathway selenocysteinyl-tRNA(Sec) biosynthesis, which is itself part of Aminoacyl-tRNA biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route), the pathway selenocysteinyl-tRNA(Sec) biosynthesis and in Aminoacyl-tRNA biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 328ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • seryl-selenocysteinyl-tRNA kinase activity Source: Reactome
  • tRNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14957.
BRENDAi2.7.1.164. 3474.
ReactomeiR-MMU-2408557. Selenocysteine synthesis.
UniPathwayiUPA00906; UER00897.

Names & Taxonomyi

Protein namesi
Recommended name:
L-seryl-tRNA(Sec) kinase (EC:2.7.1.164)
Alternative name(s):
O-phosphoseryl-tRNA(Sec) kinase
Gene namesi
Name:Pstk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2685945. Pstk.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359L-seryl-tRNA(Sec) kinasePRO_0000097081Add
BLAST

Proteomic databases

EPDiQ8BP74.
MaxQBiQ8BP74.
PaxDbiQ8BP74.
PeptideAtlasiQ8BP74.
PRIDEiQ8BP74.

PTM databases

PhosphoSiteiQ8BP74.

Expressioni

Gene expression databases

BgeeiQ8BP74.
CleanExiMM_PSTK.
GenevisibleiQ8BP74. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000075037.

Structurei

3D structure databases

ProteinModelPortaliQ8BP74.
SMRiQ8BP74. Positions 148-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-seryl-tRNA(Sec) kinase family.Curated

Phylogenomic databases

eggNOGiKOG4622. Eukaryota.
ENOG4111HI0. LUCA.
GeneTreeiENSGT00390000017554.
HOGENOMiHOG000115749.
HOVERGENiHBG064780.
InParanoidiQ8BP74.
KOiK10837.
OMAiISFFHYE.
OrthoDBiEOG7G1V7T.
PhylomeDBiQ8BP74.
TreeFamiTF321264.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013641. KTI12/PSTK.
IPR020028. L-seryl-tRNA_Sec_kinase_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF08433. KTI12. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
TIGRFAMsiTIGR03575. selen_PSTK_euk. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BP74-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MKTAAARGAT RRDGQPKLGL CVLCGLPAAG KSTFARALAL RLRRERGWAV
60 70 80 90 100
GVLSYDDVLP LALPDCDGTQ PRPSQWKMFR QELLKHLECF LVAVISGAQM
110 120 130 140 150
SAPPNRTEAV WEDFITCLKS QDLMIFPTAL EAQPCHLLAK PAVSRPLFLV
160 170 180 190 200
LDDNFYYQSM RYEVYQLARK YSLGFCQLFL DCPLETCLKR NGERSQPLPD
210 220 230 240 250
ETIQLMGRKI EKPNPEKNAW EHNSLIIQSS ACSLEASLEV TGLLLTALEN
260 270 280 290 300
PIKCVEDNTE QKETDRIICS TNILHKADET LRRTVSQTMR EAKDEQIPLN
310 320 330 340 350
NLKHLAEELN KLKADVLEDL RQGNRKYLCF QQTTDLSDII SSFCKERDTI

VQKYFSKQH
Note: No experimental confirmation available.
Length:359
Mass (Da):40,763
Last modified:May 1, 2007 - v2
Checksum:iE43BED6554DFFB2E
GO
Isoform 2 (identifier: Q8BP74-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     263-359: ETDRIICSTN...IVQKYFSKQH → NYLFY

Note: No experimental confirmation available.
Show »
Length:267
Mass (Da):30,072
Checksum:iF195D5CFBB13EBD9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei263 – 35997ETDRI…FSKQH → NYLFY in isoform 2. 1 PublicationVSP_024860Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077585 mRNA. Translation: BAC36878.1.
BC110381 mRNA. Translation: AAI10382.1.
BC115503 mRNA. Translation: AAI15504.2.
CCDSiCCDS21914.1. [Q8BP74-1]
RefSeqiNP_001034623.1. NM_001039534.1. [Q8BP74-1]
UniGeneiMm.272948.

Genome annotation databases

EnsembliENSMUST00000075610; ENSMUSP00000075037; ENSMUSG00000063179. [Q8BP74-1]
ENSMUST00000145114; ENSMUSP00000118636; ENSMUSG00000063179. [Q8BP74-2]
GeneIDi214580.
KEGGimmu:214580.
UCSCiuc009kbh.1. mouse. [Q8BP74-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077585 mRNA. Translation: BAC36878.1.
BC110381 mRNA. Translation: AAI10382.1.
BC115503 mRNA. Translation: AAI15504.2.
CCDSiCCDS21914.1. [Q8BP74-1]
RefSeqiNP_001034623.1. NM_001039534.1. [Q8BP74-1]
UniGeneiMm.272948.

3D structure databases

ProteinModelPortaliQ8BP74.
SMRiQ8BP74. Positions 148-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000075037.

PTM databases

PhosphoSiteiQ8BP74.

Proteomic databases

EPDiQ8BP74.
MaxQBiQ8BP74.
PaxDbiQ8BP74.
PeptideAtlasiQ8BP74.
PRIDEiQ8BP74.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075610; ENSMUSP00000075037; ENSMUSG00000063179. [Q8BP74-1]
ENSMUST00000145114; ENSMUSP00000118636; ENSMUSG00000063179. [Q8BP74-2]
GeneIDi214580.
KEGGimmu:214580.
UCSCiuc009kbh.1. mouse. [Q8BP74-1]

Organism-specific databases

CTDi118672.
MGIiMGI:2685945. Pstk.

Phylogenomic databases

eggNOGiKOG4622. Eukaryota.
ENOG4111HI0. LUCA.
GeneTreeiENSGT00390000017554.
HOGENOMiHOG000115749.
HOVERGENiHBG064780.
InParanoidiQ8BP74.
KOiK10837.
OMAiISFFHYE.
OrthoDBiEOG7G1V7T.
PhylomeDBiQ8BP74.
TreeFamiTF321264.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00897.
BioCyciMetaCyc:MONOMER-14957.
BRENDAi2.7.1.164. 3474.
ReactomeiR-MMU-2408557. Selenocysteine synthesis.

Miscellaneous databases

ChiTaRSiPstk. mouse.
PROiQ8BP74.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BP74.
CleanExiMM_PSTK.
GenevisibleiQ8BP74. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013641. KTI12/PSTK.
IPR020028. L-seryl-tRNA_Sec_kinase_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF08433. KTI12. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
TIGRFAMsiTIGR03575. selen_PSTK_euk. 1 hit.
ProtoNetiSearch...

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] (ISOFORM 2).
    Strain: C57BL/6J.
  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] (ISOFORM 1).
    Strain: Mix FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION, CHARACTERIZATION OF ENZYMATIC ACTIVITY.

Entry informationi

Entry nameiPSTK_MOUSE
AccessioniPrimary (citable) accession number: Q8BP74
Secondary accession number(s): Q0D2I7, Q14C09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 2007
Last modified: July 6, 2016
This is version 100 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

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. 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.