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P28658 (ATX10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-10
Alternative name(s):
Brain protein E46
Spinocerebellar ataxia type 10 protein homolog
Gene names
Name:Atxn10
Synonyms:Sca10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for the survival of cerebellar neurons By similarity. Induces neuritogenesis by activating the Ras-MAP kinase pathway By similarity. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis By similarity.

Subunit structure

Homooligomer By similarity. Interacts with GNB2 By similarity. Interacts with OGT. Interacts with IQCB1 By similarity. Ref.6

Subcellular location

Cytoplasm › perinuclear region By similarity.

Tissue specificity

In high cell density areas; cerebellar cortex, dentate gyrus, hippocampus, anterior olfactory nucleus, primary olfactory cortex. Ref.5

Sequence similarities

Belongs to the ataxin-10 family.

Sequence caution

The sequence CAA43722.1 differs from that shown. Reason: Frameshift at position 409.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Iqcb1Q8BP002EBI-4284019,EBI-4282243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Ataxin-10
PRO_0000064749

Amino acid modifications

Modified residue121Phosphoserine By similarity

Experimental info

Sequence conflict311A → V in CAA43722. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28658 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 273FDB6EDFE519C7

FASTA47553,707
        10         20         30         40         50         60 
MAAPRMPPSR LSGIMVPAPI QDLEALRALT ALFKEQRNRE TAPRTIFQRV LDILKKSTHA 

        70         80         90        100        110        120 
VELACRDPSQ VEHLASSLQL ITECFRCLRN ACIECSVNQN SIRNLDTIGV AVDLVLLFRE 

       130        140        150        160        170        180 
LRVEQDSLLT AFRCGLQFLG NVASRNEESQ SIVWVHAFPE LFMSCLNHPD KKIVAYCSMI 

       190        200        210        220        230        240 
LFTSLNAERM KDLEENLNIA INVIEAHQKH PASEWPFLII SDHFLKSPEL VEAMYGKLSN 

       250        260        270        280        290        300 
QERITLLDIV IAKLVGEEQL TKDDISIFVR HAELIANSFM DQCRNVLKLT SEPHTEDKEA 

       310        320        330        340        350        360 
LVTIRLLDVL CEMTSNTELL GYLQVFPGLM ERVIDVLRVI HEVGKESTNI FSPSDSLKAE 

       370        380        390        400        410        420 
GDIEHMTEGF KSHLIRLIGN LCYKNKENQD KVNELDGIPL ILDSSNIDDN NPFMMQWVVY 

       430        440        450        460        470 
AVRNLTEDNS QNQDVIAKME EQGLADASLL KKMGFEIEKS GDKLILKSNN DIPPP

« Hide

References

« Hide 'large scale' references
[1]"A collection of cDNA clones with specific expression patterns in mouse brain."
Kato K.
Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"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: Bone marrow, Cerebellum, Embryo and Lung.
[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].
Strain: C57BL/6.
Tissue: Brain and Mammary gland.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 244-253, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Ataxin-10, the spinocerebellar ataxia type 10 neurodegenerative disorder protein, is essential for survival of cerebellar neurons."
Maerz P., Probst A., Lang S., Schwager M., Rose-John S., Otten U., Ozbek S.
J. Biol. Chem. 279:35542-35550(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta cells."
Andrali S.S., Maerz P., Ozcan S.
Biochem. Biophys. Res. Commun. 337:149-153(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OGT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X61506 mRNA. Translation: CAA43722.1. Frameshift.
AK003530 mRNA. Translation: BAB22840.1.
AK047170 mRNA. Translation: BAC32981.1.
AK078459 mRNA. Translation: BAC37285.1.
AK153271 mRNA. Translation: BAE31858.1.
AK165941 mRNA. Translation: BAE38473.1.
AK170507 mRNA. Translation: BAE41845.1.
BC002285 mRNA. Translation: AAH02285.1.
BC016410 mRNA. Translation: AAH16410.1.
BC046802 mRNA. Translation: AAH46802.1.
IPIIPI00123202.
PIRS16416.
RefSeqNP_058539.2. NM_016843.3.
UniGeneMm.248906.

3D structure databases

ProteinModelPortalP28658.
ModBaseSearch...

Protein-protein interaction databases

IntActP28658. 2 interactions.
MINTMINT-4088847.

PTM databases

PhosphoSiteP28658.

Proteomic databases

PaxDbP28658.
PRIDEP28658.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163242; ENSMUSP00000132450; ENSMUSG00000016541.
GeneID54138.
KEGGmmu:54138.
UCSCuc007xdd.1. mouse.

Organism-specific databases

CTD25814.
MGIMGI:1859293. Atxn10.

Phylogenomic databases

eggNOGNOG330117.
GeneTreeENSGT00390000010377.
HOGENOMHOG000034224.
HOVERGENHBG050622.
InParanoidP28658.
OMAPIQDLEA.
OrthoDBEOG40ZQXH.

Gene expression databases

BgeeP28658.
CleanExMM_ATXN10.
GenevestigatorP28658.
GermOnlineENSMUSG00000016541. Mus musculus.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR019156. Ataxin-10_domain.
[Graphical view]
PfamPF09759. Atx10homo_assoc. 1 hit.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
ProtoNetSearch...

Other

NextBio310953.
SOURCESearch...

Entry information

Entry nameATX10_MOUSE
AccessionPrimary (citable) accession number: P28658
Secondary accession number(s): Q543S3, Q99LP5, Q9D1I1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 18, 2001
Last modified: May 29, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents