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Q91YA2 (KPSH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase H1

EC=2.7.11.1
Alternative name(s):
Protein serine kinase H1
Short name=PSK-H1
Gene names
Name:Pskh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activity depends on Ca2+ concentration By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Golgi apparatus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus speckle By similarity. Endoplasmic reticulum membrane; Lipid-anchor By similarity. Cell membrane; Lipid-anchor By similarity. Cytoplasm By similarity. 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 By similarity.

Post-translational modification

Autophosphorylated on serine residues By similarity.

Myristoylated. Required for membrane association. Prerequisite for palmitoylation to occur By similarity.

Palmitoylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 424423Serine/threonine-protein kinase H1
PRO_0000086168

Regions

Domain98 – 355258Protein kinase
Nucleotide binding104 – 1129ATP By similarity

Sites

Active site2181Proton acceptor By similarity
Binding site1271ATP By similarity

Amino acid modifications

Modified residue3801Phosphoserine; by autocatalysis Potential
Modified residue3811Phosphoserine; by autocatalysis Potential
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict2131G → S in BAE32682. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91YA2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 81B7A29543C39F47

FASTA42448,095
        10         20         30         40         50         60 
MGCGTSKVLP EPPKDVQLDL VKKVEPFSGT KNDVYKHFIT EVDSVGPLKA GFPATSQYAP 

        70         80         90        100        110        120 
PCPGVPNTGH TAPPSEPPRR ARVAKYRAKF DPRVTAKYDI KALIGRGSFS RVVRVEHRAT 

       130        140        150        160        170        180 
RQPYAIKMIE TKYREGREVC ESELRVLRRV RHANIIQLVE VFETQERVYM VMELATGGEL 

       190        200        210        220        230        240 
FDRIIAKGSF TERDATRVLQ MVLDGVRYLH ALGITHRDLK PENLLYYHPG TDSKIIITDF 

       250        260        270        280        290        300 
GLASARKKGD DCLMKTTCGT PEYIAPEVLV RKPYTNSVDM WALGVIAYIL LSGTMPFEDD 

       310        320        330        340        350        360 
NRTRLYRQIL RGKYSYLGEP WPSVSNLAKD FIDRLLTVDP GARMTALQAL RHPWVVSMAA 

       370        380        390        400        410        420 
SSSMKNLHRS ISQNLLKRAS SRCQSTKSSQ STRSSRSTRS NKSRRVRERE LRELNLRYQQ 


QYNG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 and NOD.
Tissue: Eye and Thymus.
[2]Bjoernslett M.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129S6/SvEvTac.
Tissue: Spleen.
[3]"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: Trophoblast stem cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK053397 mRNA. Translation: BAC35374.1.
AK153861 mRNA. Translation: BAE32217.1.
AF236365, AF236364 Genomic DNA. Translation: AAL11033.1.
AK154570 mRNA. Translation: BAE32682.1.
BC050128 mRNA. Translation: AAH50128.1.
RefSeqNP_775608.1. NM_173432.2.
UniGeneMm.27627.

3D structure databases

ProteinModelPortalQ91YA2.
SMRQ91YA2. Positions 98-382.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ91YA2.

Proteomic databases

PaxDbQ91YA2.
PRIDEQ91YA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049699; ENSMUSP00000061700; ENSMUSG00000048310.
GeneID244631.
KEGGmmu:244631.
UCSCuc009nen.1. mouse.

Organism-specific databases

CTD5681.
MGIMGI:3528383. Pskh1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117487.
HOGENOMHOG000233016.
HOVERGENHBG108055.
InParanoidQ91YA2.
KOK08808.
OMAAASQCAN.
OrthoDBEOG7WHH9K.
PhylomeDBQ91YA2.
TreeFamTF314166.

Gene expression databases

BgeeQ91YA2.
CleanExMM_PSKH1.
GenevestigatorQ91YA2.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio386339.
PROQ91YA2.
SOURCESearch...

Entry information

Entry nameKPSH1_MOUSE
AccessionPrimary (citable) accession number: Q91YA2
Secondary accession number(s): Q3U3V3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot