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Protein

Protein O-mannose kinase

Gene

Pomk

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

Functioni

Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif (By similarity).By similarity

Caution

Although related to the Ser/Thr protein kinase family, has no protein kinase activity and acts as a mannose kinase instead.Curated

Catalytic activityi

ATP + O3-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-threonyl/L-seryl-[protein] = ADP + O3-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-(6-phospho)mannosyl)-L-threonyl/L-seryl-[protein].

GO - Molecular functioni

GO - Biological processi

  • brain development Source: MGI
  • carbohydrate phosphorylation Source: UniProtKB
  • learning or memory Source: MGI
  • neuromuscular process Source: MGI
  • neuron migration Source: MGI
  • protein O-linked glycosylation Source: UniProtKB
  • sensory perception of pain Source: MGI

Keywordsi

Molecular functionKinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5173105 O-linked glycosylation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein O-mannose kinase (EC:2.7.1.183)
Short name:
POMK
Alternative name(s):
Protein kinase-like protein SgK196
Sugen kinase 196
Gene namesi
Name:Pomk
Synonyms:Sgk196
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1921903 Pomk

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 42Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini43 – 349LumenalSequence analysisAdd BLAST307

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Hydrocephaly: mutant mice exhibit dome-shaped heads of varying severity. Surviving mutant mice display numerous behavioral abnormalities: tremors, and inverted screen testing show 5 of 8 falling off, suggesting impaired motor strength. Impaired sensorimotor gating/attention is suggested by decreased prepulse inhibition, and impaired learning/memory is detected with trace aversive conditioning testing. In testing nociception, decreased paw flinching is observed during both formalin phases, suggesting decreased sensitivity to acute and tonic pain. Histologically, the most obvious changes are hydrocephalus in 4 of 5 and cerebellar dysplasia in all 5. Abnormalities in neuronal migration are evident in other parts of the brain; in the cerebral cortex, there is disorganization of cortical neuron layers, and the dentate gyrus of the hippocampus has a scalloped appearance. The cerebellar dysplasia is characterized by multifocal disorganization of cerebellar cortical neurons, with clusters of external granular neurons being scattered on the surface of the cerebellum and multifocally within the molecular layer of the cerebellum. In some regions, there is incomplete separation of cerebellar folia, and Purkinje cell. neurons were occasionally found in the molecular layer.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002629981 – 349Protein O-mannose kinaseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi66N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi219N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ3TUA9
PaxDbiQ3TUA9
PeptideAtlasiQ3TUA9
PRIDEiQ3TUA9

PTM databases

iPTMnetiQ3TUA9
PhosphoSitePlusiQ3TUA9

Expressioni

Gene expression databases

BgeeiENSMUSG00000037251
CleanExiMM_4930444A02RIK
GenevisibleiQ3TUA9 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000053802

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi73 – 79Combined sources7
Beta strandi81 – 88Combined sources8
Beta strandi90 – 99Combined sources10
Beta strandi102 – 110Combined sources9
Helixi112 – 114Combined sources3
Helixi115 – 127Combined sources13
Beta strandi136 – 140Combined sources5
Turni141 – 144Combined sources4
Beta strandi145 – 149Combined sources5
Helixi156 – 158Combined sources3
Helixi159 – 162Combined sources4
Helixi174 – 192Combined sources19
Beta strandi197 – 199Combined sources3
Helixi207 – 212Combined sources6
Beta strandi214 – 216Combined sources3
Beta strandi222 – 224Combined sources3
Beta strandi250 – 253Combined sources4
Helixi255 – 257Combined sources3
Helixi269 – 271Combined sources3
Helixi278 – 292Combined sources15
Helixi298 – 312Combined sources15
Helixi317 – 319Combined sources3
Helixi323 – 336Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GZ8X-ray2.50A45-349[»]
5GZ9X-ray2.40A45-349[»]
ProteinModelPortaliQ3TUA9
SMRiQ3TUA9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 349Protein kinasePROSITE-ProRule annotationAdd BLAST270

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. STKL subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFAD Eukaryota
ENOG4111I05 LUCA
GeneTreeiENSGT00390000004945
HOGENOMiHOG000006624
HOVERGENiHBG093945
InParanoidiQ3TUA9
KOiK17547
OMAiQLWPYGE
OrthoDBiEOG091G0N7R
PhylomeDBiQ3TUA9
TreeFamiTF328472

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit

Sequencei

Sequence statusi: Complete.

Q3TUA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQQHGTRNG LTHRELPRGV GLLLAMALMN VALYLCLDQL FISPGRSTAD
60 70 80 90 100
SRRCPPGYFR MGRMRNCSRW LSCEELRTEV RQLKRVGEGA VKRVFLSEWK
110 120 130 140 150
EHKVALSRLT RLEMKEDFLH GLQMLKSLQS EHVVTLVGYC EEDGTILTEY
160 170 180 190 200
HPLGSLSNLE ETLNLSKYQD VNTWQHRLQL AMEYVSIINY LHHSPLGTRV
210 220 230 240 250
MCDSNDLPKT LSQYLLTSNF SIVANDLDAL PLVDHDSGVL IKCGHRELHG
260 270 280 290 300
DFVAPEQLWP YGEDTPFQDD LMPSYNEKVD IWKIPDVSSF LLGHVEGSDM
310 320 330 340
VRFHLFDIHK ACKSQIPAER PTAQNVLDAY QRVFHSLRDT VMSQTKEML
Length:349
Mass (Da):39,969
Last modified:November 28, 2006 - v2
Checksum:i0E8683A6DBAAE9C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5H → Y in BAC29393 (PubMed:16141072).Curated1
Sequence conflicti158N → D in BAE42167 (PubMed:16141072).Curated1
Sequence conflicti239V → I in AAH27296 (PubMed:15489334).Curated1
Sequence conflicti276N → T in BAE42167 (PubMed:16141072).Curated1
Sequence conflicti319E → K in AAH27296 (PubMed:15489334).Curated1
Sequence conflicti335H → Q in BAE36062 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036348 mRNA Translation: BAC29393.1
AK015374 mRNA Translation: BAB29817.1
AK032677 mRNA Translation: BAC27984.1
AK043620 mRNA Translation: BAC31598.1
AK138952 mRNA Translation: BAE23832.1
AK160873 mRNA Translation: BAE36062.1
AK170994 mRNA Translation: BAE42167.1
BC027296 mRNA Translation: AAH27296.1
CCDSiCCDS22204.1
RefSeqiNP_083313.1, NM_029037.4
UniGeneiMm.17631

Genome annotation databases

EnsembliENSMUST00000061850; ENSMUSP00000053802; ENSMUSG00000037251
GeneIDi74653
KEGGimmu:74653
UCSCiuc009lhh.1 mouse

Similar proteinsi

Entry informationi

Entry nameiSG196_MOUSE
AccessioniPrimary (citable) accession number: Q3TUA9
Secondary accession number(s): Q3TBZ0
, Q8BZ83, Q8R2S2, Q9D5G4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 25, 2018
This is version 90 of the entry and version 2 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

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