Human Gene PSKH1 (uc002euv.3) Description and Page Index
  Description: Homo sapiens protein serine kinase H1 (PSKH1), mRNA.
Transcript (Including UTRs)
   Position: hg19 chr16:67,927,175-67,963,581 Size: 36,407 Total Exon Count: 3 Strand: +
Coding Region
   Position: hg19 chr16:67,942,653-67,961,545 Size: 18,893 Coding Exon Count: 2 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsCTDGene Alleles
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsOther NamesModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
Genomic Sequence (chr16:67,927,175-67,963,581)mRNA (may differ from genome)Protein (424 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards
OMIMPubMedStanford SOURCETreefamUniProtKBWikipedia

-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=Serine/threonine-protein kinase H1; EC=; AltName: Full=Protein serine kinase H1; Short=PSK-H1;
FUNCTION: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Activity depends on Ca(2+) concentration.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton, centrosome. Nucleus speckle. Endoplasmic reticulum membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Cytoplasm. Note=Localized in the brefeldin A-sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat speckle-like presence, membrane-associated to the endoplasmic reticulum (ER) and the plasma membrane (PM), and more diffusely in the cytoplasm. Found to concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells. The acylation-negative form may be only cytoplasmic and nuclear. Acylation seems to allow the sequestering to the intracellular membranes. Myristoylation may mediate targeting to the intracellular non-Golgi membranes and palmitoylation may mediate the targeting to the Golgi membranes. Dual acylation is required to stabilize the interaction with Golgi membranes.
TISSUE SPECIFICITY: Expressed in all tissues and cell lines tested with the highest level of abundance in testis.
PTM: Autophosphorylated on serine residues.
PTM: Myristoylated. Required for membrane association. Prerequisite for palmitoylation to occur.
PTM: Palmitoylated.
SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
SIMILARITY: Contains 1 protein kinase domain.

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): PSKH1
CDC HuGE Published Literature: PSKH1
Positive Disease Associations: Cholesterol, HDL
Related Studies:
  1. Cholesterol, HDL
    Tanya M Teslovich et al. Nature 2010, Biological, clinical and population relevance of 95 loci for blood lipids., Nature. [PubMed 20686565]

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 13.09 RPKM in Testis
Total median expression: 335.24 RPKM

View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -98.40170-0.579 Picture PostScript Text
3' UTR -928.252036-0.456 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR020636 - Ca/CaM-dep_Ca-dep_prot_Kinase
IPR011009 - Kinase-like_dom
IPR000719 - Prot_kinase_cat_dom
IPR017441 - Protein_kinase_ATP_BS
IPR002290 - Ser/Thr_dual-sp_kinase_dom
IPR008271 - Ser/Thr_kinase_AS

Pfam Domains:
PF00069 - Protein kinase domain
PF07714 - Protein tyrosine kinase
PF14531 - Kinase-like

SCOP Domains:
47473 - EF-hand
56112 - Protein kinase-like (PK-like)

ModBase Predicted Comparative 3D Structure on P11801
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologGenome BrowserNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
  Protein Sequence   

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016740 transferase activity

Biological Process:
GO:0006468 protein phosphorylation
GO:0007368 determination of left/right symmetry
GO:0007507 heart development
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0018107 peptidyl-threonine phosphorylation
GO:0035556 intracellular signal transduction

Cellular Component:
GO:0005575 cellular_component
GO:0005622 intracellular
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005794 Golgi apparatus
GO:0005815 microtubule organizing center
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016607 nuclear speck

-  Descriptions from all associated GenBank mRNAs
  AK309272 - Homo sapiens cDNA, FLJ99313.
JC506661 - Sequence 29 from Patent EP2733220.
JC737773 - Sequence 29 from Patent WO2014075939.
JC506666 - Sequence 34 from Patent EP2733220.
JC737778 - Sequence 34 from Patent WO2014075939.
JC506674 - Sequence 42 from Patent EP2733220.
JC737786 - Sequence 42 from Patent WO2014075939.
JC506688 - Sequence 56 from Patent EP2733220.
JC737800 - Sequence 56 from Patent WO2014075939.
BC062616 - Homo sapiens protein serine kinase H1, mRNA (cDNA clone MGC:70352 IMAGE:5188431), complete cds.
AJ272212 - Homo sapiens mRNA for protein serine kinase (PSKH1 gene).
JD138044 - Sequence 119068 from Patent EP1572962.
JD537566 - Sequence 518590 from Patent EP1572962.
AB528932 - Synthetic construct DNA, clone: pF1KE0742, Homo sapiens PSKH1 gene for protein serine kinase H1, without stop codon, in Flexi system.
KJ897400 - Synthetic construct Homo sapiens clone ccsbBroadEn_06794 PSKH1 gene, encodes complete protein.
M14504 - Human protein-serine kinase mRNA, clone PSK-H1.
BC037560 - Homo sapiens, clone IMAGE:5207595, mRNA.
JD159373 - Sequence 140397 from Patent EP1572962.
JD406469 - Sequence 387493 from Patent EP1572962.
JD353779 - Sequence 334803 from Patent EP1572962.
JD452201 - Sequence 433225 from Patent EP1572962.
JD100213 - Sequence 81237 from Patent EP1572962.
JD320908 - Sequence 301932 from Patent EP1572962.
BC021584 - Homo sapiens, clone IMAGE:4872558, mRNA.
JD345826 - Sequence 326850 from Patent EP1572962.
JD548387 - Sequence 529411 from Patent EP1572962.
JD149218 - Sequence 130242 from Patent EP1572962.
JD457893 - Sequence 438917 from Patent EP1572962.
JD162458 - Sequence 143482 from Patent EP1572962.
JD521241 - Sequence 502265 from Patent EP1572962.
JD194430 - Sequence 175454 from Patent EP1572962.
JD338846 - Sequence 319870 from Patent EP1572962.
JD271982 - Sequence 253006 from Patent EP1572962.
JD308612 - Sequence 289636 from Patent EP1572962.
JD326753 - Sequence 307777 from Patent EP1572962.
JD193073 - Sequence 174097 from Patent EP1572962.
JD113421 - Sequence 94445 from Patent EP1572962.
JD271587 - Sequence 252611 from Patent EP1572962.
JD049083 - Sequence 30107 from Patent EP1572962.
JD078703 - Sequence 59727 from Patent EP1572962.
JD148936 - Sequence 129960 from Patent EP1572962.
JD415530 - Sequence 396554 from Patent EP1572962.
JD252361 - Sequence 233385 from Patent EP1572962.
JD089411 - Sequence 70435 from Patent EP1572962.
JD555910 - Sequence 536934 from Patent EP1572962.
JD209707 - Sequence 190731 from Patent EP1572962.
JD376472 - Sequence 357496 from Patent EP1572962.
JD099175 - Sequence 80199 from Patent EP1572962.
JD140285 - Sequence 121309 from Patent EP1572962.
JD390239 - Sequence 371263 from Patent EP1572962.
JD122176 - Sequence 103200 from Patent EP1572962.
JD190648 - Sequence 171672 from Patent EP1572962.
JD229547 - Sequence 210571 from Patent EP1572962.
JD104481 - Sequence 85505 from Patent EP1572962.
JD081015 - Sequence 62039 from Patent EP1572962.
JD386146 - Sequence 367170 from Patent EP1572962.
JD054217 - Sequence 35241 from Patent EP1572962.
JD177894 - Sequence 158918 from Patent EP1572962.
JD395826 - Sequence 376850 from Patent EP1572962.
JD246474 - Sequence 227498 from Patent EP1572962.
JD261264 - Sequence 242288 from Patent EP1572962.
JD293608 - Sequence 274632 from Patent EP1572962.
JD396481 - Sequence 377505 from Patent EP1572962.
JD098231 - Sequence 79255 from Patent EP1572962.
JD392891 - Sequence 373915 from Patent EP1572962.
JD124293 - Sequence 105317 from Patent EP1572962.
JD301164 - Sequence 282188 from Patent EP1572962.
JD352734 - Sequence 333758 from Patent EP1572962.
JD126385 - Sequence 107409 from Patent EP1572962.
JD480011 - Sequence 461035 from Patent EP1572962.
JD389114 - Sequence 370138 from Patent EP1572962.
JD565902 - Sequence 546926 from Patent EP1572962.
JD489493 - Sequence 470517 from Patent EP1572962.
JD209494 - Sequence 190518 from Patent EP1572962.
JD475971 - Sequence 456995 from Patent EP1572962.
JD433185 - Sequence 414209 from Patent EP1572962.
JD391069 - Sequence 372093 from Patent EP1572962.
JD527089 - Sequence 508113 from Patent EP1572962.
JD154989 - Sequence 136013 from Patent EP1572962.
JD217197 - Sequence 198221 from Patent EP1572962.
JD348879 - Sequence 329903 from Patent EP1572962.
JD329326 - Sequence 310350 from Patent EP1572962.
JD477663 - Sequence 458687 from Patent EP1572962.
JD491330 - Sequence 472354 from Patent EP1572962.

-  Other Names for This Gene
  Alternate Gene Symbols: KPSH1_HUMAN, NM_006742, NP_006733, P11801, Q9NY19
UCSC ID: uc002euv.3
RefSeq Accession: NM_006742
Protein: P11801 (aka KPSH1_HUMAN)
CCDS: CCDS10851.1

-  Gene Model Information
category: coding nonsense-mediated-decay: no RNA accession: NM_006742.2
exon count: 3CDS single in 3' UTR: no RNA size: 3505
ORF size: 1275CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 2584.00frame shift in genome: no % Coverage: 99.32
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.