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Q3TUA9 (SG196_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:
Protein O-mannose kinase

Short name=POMK
EC=2.7.1.-
Alternative name(s):
Protein kinase-like protein SgK196
Sugen kinase 196
Gene names
Name:Pomk
Synonyms:Sgk196
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-mannosylprotein = ADP + N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-(6-phospho)mannosylprotein.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Disruption phenotype

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. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. STKL subfamily.

Contains 1 protein kinase domain.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Protein O-mannose kinase
PRO_0000262998

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 4223Helical; Signal-anchor for type II membrane protein; Potential
Topological domain43 – 349307Lumenal Potential
Domain80 – 349270Protein kinase

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict51H → Y in BAC29393. Ref.1
Sequence conflict1581N → D in BAE42167. Ref.1
Sequence conflict2391V → I in AAH27296. Ref.2
Sequence conflict2761N → T in BAE42167. Ref.1
Sequence conflict3191E → K in AAH27296. Ref.2
Sequence conflict3351H → Q in BAE36062. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TUA9 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 0E8683A6DBAAE9C3

FASTA34939,969
        10         20         30         40         50         60 
MGQQHGTRNG LTHRELPRGV GLLLAMALMN VALYLCLDQL FISPGRSTAD SRRCPPGYFR 

        70         80         90        100        110        120 
MGRMRNCSRW LSCEELRTEV RQLKRVGEGA VKRVFLSEWK EHKVALSRLT RLEMKEDFLH 

       130        140        150        160        170        180 
GLQMLKSLQS EHVVTLVGYC EEDGTILTEY HPLGSLSNLE ETLNLSKYQD VNTWQHRLQL 

       190        200        210        220        230        240 
AMEYVSIINY LHHSPLGTRV MCDSNDLPKT LSQYLLTSNF SIVANDLDAL PLVDHDSGVL 

       250        260        270        280        290        300 
IKCGHRELHG DFVAPEQLWP YGEDTPFQDD LMPSYNEKVD IWKIPDVSSF LLGHVEGSDM 

       310        320        330        340 
VRFHLFDIHK ACKSQIPAER PTAQNVLDAY QRVFHSLRDT VMSQTKEML 

« 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: Aorta, Brain, Brain cortex, Cerebellum, Testis and Vein.
[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].
Strain: Czech II.
Tissue: Mammary gland.
[3]"Congenital hydrocephalus in genetically engineered mice."
Vogel P., Read R.W., Hansen G.M., Payne B.J., Small D., Sands A.T., Zambrowicz B.P.
Vet. Pathol. 49:166-181(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_083313.1. NM_029037.4.
UniGeneMm.17631.

3D structure databases

ProteinModelPortalQ3TUA9.
SMRQ3TUA9. Positions 49-341.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3TUA9.

Proteomic databases

PRIDEQ3TUA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061850; ENSMUSP00000053802; ENSMUSG00000037251.
GeneID74653.
KEGGmmu:74653.
UCSCuc009lhh.1. mouse.

Organism-specific databases

CTD84197.
MGIMGI:1921903. Pomk.

Phylogenomic databases

eggNOGNOG43701.
GeneTreeENSGT00390000004945.
HOGENOMHOG000006624.
HOVERGENHBG093945.
InParanoidQ3TUA9.
KOK17547.
OMAKACKSQT.
OrthoDBEOG7D59NT.
PhylomeDBQ3TUA9.
TreeFamTF328472.

Gene expression databases

BgeeQ3TUA9.
CleanExMM_4930444A02RIK.
GenevestigatorQ3TUA9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio341310.
PROQ3TUA9.
SOURCESearch...

Entry information

Entry nameSG196_MOUSE
AccessionPrimary (citable) accession number: Q3TUA9
Secondary accession number(s): Q3TBZ0 expand/collapse secondary AC list , Q8BZ83, Q8R2S2, Q9D5G4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 69 of the entry and version 2 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