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Q91YA2

- KPSH1_MOUSE

UniProt

Q91YA2 - KPSH1_MOUSE

Protein

Serine/threonine-protein kinase H1

Gene

Pskh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activity depends on Ca2+ concentration.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei127 – 1271ATPPROSITE-ProRule annotation
    Active sitei218 – 2181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi104 – 1129ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: MGI
    3. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein phosphorylation Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase H1 (EC:2.7.11.1)
    Alternative name(s):
    Protein serine kinase H1
    Short name:
    PSK-H1
    Gene namesi
    Name:Pskh1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:3528383. Pskh1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi apparatus Source: UniProtKB-SubCell
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nuclear speck Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 424423Serine/threonine-protein kinase H1PRO_0000086168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Modified residuei380 – 3801Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei381 – 3811Phosphoserine; by autocatalysisSequence Analysis

    Post-translational modificationi

    Autophosphorylated on serine residues.By similarity
    Myristoylated. Required for membrane association. Prerequisite for palmitoylation to occur By similarity.By similarity
    Palmitoylated.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiQ91YA2.
    PRIDEiQ91YA2.

    PTM databases

    PhosphoSiteiQ91YA2.

    Expressioni

    Gene expression databases

    BgeeiQ91YA2.
    CleanExiMM_PSKH1.
    GenevestigatoriQ91YA2.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YA2.
    SMRiQ91YA2. Positions 98-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 355258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117487.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    InParanoidiQ91YA2.
    KOiK08808.
    OMAiAASQCAN.
    OrthoDBiEOG7WHH9K.
    PhylomeDBiQ91YA2.
    TreeFamiTF314166.

    Family and domain databases

    InterProiIPR020636. 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]
    PANTHERiPTHR24347. PTHR24347. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q91YA2-1 [UniParc]FASTAAdd to Basket

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    MGCGTSKVLP EPPKDVQLDL VKKVEPFSGT KNDVYKHFIT EVDSVGPLKA    50
    GFPATSQYAP PCPGVPNTGH TAPPSEPPRR ARVAKYRAKF DPRVTAKYDI 100
    KALIGRGSFS RVVRVEHRAT RQPYAIKMIE TKYREGREVC ESELRVLRRV 150
    RHANIIQLVE VFETQERVYM VMELATGGEL FDRIIAKGSF TERDATRVLQ 200
    MVLDGVRYLH ALGITHRDLK PENLLYYHPG TDSKIIITDF GLASARKKGD 250
    DCLMKTTCGT PEYIAPEVLV RKPYTNSVDM WALGVIAYIL LSGTMPFEDD 300
    NRTRLYRQIL RGKYSYLGEP WPSVSNLAKD FIDRLLTVDP GARMTALQAL 350
    RHPWVVSMAA SSSMKNLHRS ISQNLLKRAS SRCQSTKSSQ STRSSRSTRS 400
    NKSRRVRERE LRELNLRYQQ QYNG 424
    Length:424
    Mass (Da):48,095
    Last modified:January 23, 2007 - v3
    Checksum:i81B7A29543C39F47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131G → S in BAE32682. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS22619.1.
    RefSeqiNP_775608.1. NM_173432.2.
    UniGeneiMm.27627.

    Genome annotation databases

    EnsembliENSMUST00000049699; ENSMUSP00000061700; ENSMUSG00000048310.
    GeneIDi244631.
    KEGGimmu:244631.
    UCSCiuc009nen.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS22619.1.
    RefSeqi NP_775608.1. NM_173432.2.
    UniGenei Mm.27627.

    3D structure databases

    ProteinModelPortali Q91YA2.
    SMRi Q91YA2. Positions 98-382.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q91YA2.

    Proteomic databases

    PaxDbi Q91YA2.
    PRIDEi Q91YA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049699 ; ENSMUSP00000061700 ; ENSMUSG00000048310 .
    GeneIDi 244631.
    KEGGi mmu:244631.
    UCSCi uc009nen.1. mouse.

    Organism-specific databases

    CTDi 5681.
    MGIi MGI:3528383. Pskh1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117487.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    InParanoidi Q91YA2.
    KOi K08808.
    OMAi AASQCAN.
    OrthoDBi EOG7WHH9K.
    PhylomeDBi Q91YA2.
    TreeFami TF314166.

    Miscellaneous databases

    NextBioi 386339.
    PROi Q91YA2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91YA2.
    CleanExi MM_PSKH1.
    Genevestigatori Q91YA2.

    Family and domain databases

    InterProi IPR020636. 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 ]
    PANTHERi PTHR24347. PTHR24347. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 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.

    Entry informationi

    Entry nameiKPSH1_MOUSE
    AccessioniPrimary (citable) accession number: Q91YA2
    Secondary accession number(s): Q3U3V3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3