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Q3TUA9

- SG196_MOUSE

UniProt

Q3TUA9 - SG196_MOUSE

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Protein

Protein O-mannose kinase

Gene

Pomk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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

Catalytic activityi

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.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. carbohydrate kinase activity Source: MGI
  3. phosphotransferase activity, alcohol group as acceptor Source: UniProtKB
  4. protein kinase activity Source: InterPro

GO - Biological processi

  1. brain development Source: MGI
  2. carbohydrate phosphorylation Source: UniProtKB
  3. learning or memory Source: MGI
  4. neuromuscular process Source: MGI
  5. neuron migration Source: MGI
  6. protein O-linked glycosylation Source: UniProtKB
  7. sensory perception of pain Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein O-mannose kinase (EC:2.7.1.-)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1921903. Pomk.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Protein O-mannose kinasePRO_0000262998Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ3TUA9.
PRIDEiQ3TUA9.

PTM databases

PhosphoSiteiQ3TUA9.

Expressioni

Gene expression databases

BgeeiQ3TUA9.
CleanExiMM_4930444A02RIK.
GenevestigatoriQ3TUA9.

Structurei

3D structure databases

ProteinModelPortaliQ3TUA9.
SMRiQ3TUA9. Positions 49-341.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini43 – 349307LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4223Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 349270Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. STKL subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43701.
GeneTreeiENSGT00390000004945.
HOGENOMiHOG000006624.
HOVERGENiHBG093945.
InParanoidiQ3TUA9.
KOiK17547.
OMAiKACKSQT.
OrthoDBiEOG7D59NT.
PhylomeDBiQ3TUA9.
TreeFamiTF328472.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51H → Y in BAC29393. (PubMed:16141072)Curated
Sequence conflicti158 – 1581N → D in BAE42167. (PubMed:16141072)Curated
Sequence conflicti239 – 2391V → I in AAH27296. (PubMed:15489334)Curated
Sequence conflicti276 – 2761N → T in BAE42167. (PubMed:16141072)Curated
Sequence conflicti319 – 3191E → K in AAH27296. (PubMed:15489334)Curated
Sequence conflicti335 – 3351H → Q in BAE36062. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22204.1.
RefSeqi NP_083313.1. NM_029037.4.
UniGenei Mm.17631.

3D structure databases

ProteinModelPortali Q3TUA9.
SMRi Q3TUA9. Positions 49-341.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q3TUA9.

Proteomic databases

MaxQBi Q3TUA9.
PRIDEi Q3TUA9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000061850 ; ENSMUSP00000053802 ; ENSMUSG00000037251 .
GeneIDi 74653.
KEGGi mmu:74653.
UCSCi uc009lhh.1. mouse.

Organism-specific databases

CTDi 84197.
MGIi MGI:1921903. Pomk.

Phylogenomic databases

eggNOGi NOG43701.
GeneTreei ENSGT00390000004945.
HOGENOMi HOG000006624.
HOVERGENi HBG093945.
InParanoidi Q3TUA9.
KOi K17547.
OMAi KACKSQT.
OrthoDBi EOG7D59NT.
PhylomeDBi Q3TUA9.
TreeFami TF328472.

Miscellaneous databases

NextBioi 341310.
PROi Q3TUA9.
SOURCEi Search...

Gene expression databases

Bgeei Q3TUA9.
CleanExi MM_4930444A02RIK.
Genevestigatori Q3TUA9.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: 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. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSG196_MOUSE
AccessioniPrimary (citable) accession number: Q3TUA9
Secondary accession number(s): Q3TBZ0
, Q8BZ83, Q8R2S2, Q9D5G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

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