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Q99700

- ATX2_HUMAN

UniProt

Q99700 - ATX2_HUMAN

Protein

Ataxin-2

Gene

ATXN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane.1 Publication

    GO - Molecular functioni

    1. epidermal growth factor receptor binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cerebellar Purkinje cell differentiation Source: Ensembl
    3. cytoplasmic mRNA processing body assembly Source: UniProtKB
    4. homeostasis of number of cells Source: Ensembl
    5. negative regulation of multicellular organism growth Source: Ensembl
    6. negative regulation of receptor internalization Source: UniProtKB
    7. neuromuscular process Source: Ensembl
    8. neuron projection morphogenesis Source: Ensembl
    9. regulation of translation Source: UniProtKB
    10. RNA metabolic process Source: UniProtKB
    11. RNA transport Source: UniProtKB
    12. stress granule assembly Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ataxin-2
    Alternative name(s):
    Spinocerebellar ataxia type 2 protein
    Trinucleotide repeat-containing gene 13 protein
    Gene namesi
    Name:ATXN2
    Synonyms:ATX2, SCA2, TNRC13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10555. ATXN2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic stress granule Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleus Source: HPA
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. polysome Source: UniProtKB
    8. ribonucleoprotein complex Source: UniProtKB
    9. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 2 (SCA2) [MIM:183090]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA2 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA2 is characterized by hyporeflexia, myoclonus and action tremor and dopamine-responsive parkinsonism. In some patients, SCA2 presents as pure familial parkinsonism without cerebellar signs.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. SCA2 is caused by expansion of a CAG repeat resulting in about 36 to 52 repeats in some patients. Longer expansions result in earlier the expansion, onset of the disease.
    Amyotrophic lateral sclerosis 13 (ALS13) [MIM:183090]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. An increased risk for developing amyotrophic lateral sclerosis seems to be conferred by CAG repeat intermediate expansions greater than 23 but below the threshold for developing spinocerebellar ataxia.

    Keywords - Diseasei

    Amyotrophic lateral sclerosis, Neurodegeneration, Parkinsonism, Spinocerebellar ataxia

    Organism-specific databases

    MIMi183090. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    98756. Spinocerebellar ataxia type 2.
    PharmGKBiPA34968.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13131313Ataxin-2PRO_0000064756Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei393 – 3931Phosphoserine1 Publication
    Modified residuei466 – 4661Phosphoserine1 Publication
    Modified residuei554 – 5541Phosphoserine1 Publication
    Modified residuei684 – 6841Phosphoserine3 Publications
    Modified residuei741 – 7411Phosphothreonine1 Publication
    Modified residuei784 – 7841Phosphoserine3 Publications
    Modified residuei857 – 8571Phosphoserine1 Publication
    Modified residuei861 – 8611Phosphoserine2 Publications
    Modified residuei865 – 8651Phosphoserine1 Publication
    Modified residuei888 – 8881Phosphoserine1 Publication
    Modified residuei889 – 8891Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99700.
    PaxDbiQ99700.
    PRIDEiQ99700.

    PTM databases

    PhosphoSiteiQ99700.

    Expressioni

    Tissue specificityi

    Expressed in the brain, heart, liver, skeletal muscle, pancreas and placenta. Isoform 1 is predominant in the brain and spinal cord. Isoform 4 is more abundant in the cerebellum. In the brain, broadly expressed in the amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus and thalamus.4 Publications

    Gene expression databases

    ArrayExpressiQ99700.
    BgeeiQ99700.
    CleanExiHS_ATXN2.
    GenevestigatoriQ99700.

    Organism-specific databases

    HPAiHPA018295.
    HPA020339.
    HPA021146.

    Interactioni

    Subunit structurei

    Monomer By similarity. Can also form homodimers By similarity. Interacts with TARDBP; the interaction is RNA-dependent. Interacts with RBFOX1. Interacts with polyribosomes. Interacts with SH3GL2 and SH3GL3. Interacts with SH3KBP1 and CBL By similarity. Interacts with EGFR.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542534EBI-697691,EBI-930964
    DDX6P261967EBI-697691,EBI-351257
    G3BP1Q132834EBI-697691,EBI-1047359
    PABPC1P119406EBI-697691,EBI-81531
    SH3GL2Q999629EBI-697691,EBI-77938
    SH3GL3Q9996311EBI-697691,EBI-473910

    Protein-protein interaction databases

    BioGridi112218. 37 interactions.
    DIPiDIP-33372N.
    IntActiQ99700. 25 interactions.
    MINTiMINT-1414788.
    STRINGi9606.ENSP00000366843.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KTRX-ray1.70B912-928[»]
    ProteinModelPortaliQ99700.
    SMRiQ99700. Positions 273-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99700.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi47 – 158112Pro-richAdd
    BLAST
    Compositional biasi55 – 6410Poly-Pro
    Compositional biasi166 – 18722Poly-GlnAdd
    BLAST
    Compositional biasi213 – 22311Poly-SerAdd
    BLAST
    Compositional biasi551 – 734184Pro-richAdd
    BLAST
    Compositional biasi929 – 1085157Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ataxin-2 family.Curated

    Phylogenomic databases

    eggNOGiNOG268173.
    HOGENOMiHOG000234354.
    HOVERGENiHBG050623.
    InParanoidiQ99700.
    OMAiSNTEHKR.
    PhylomeDBiQ99700.
    TreeFamiTF326591.

    Family and domain databases

    InterProiIPR009818. Ataxin-2_C.
    IPR010920. LSM_dom.
    IPR009604. LsmAD_domain.
    IPR025852. SM_dom_ATX.
    [Graphical view]
    PfamiPF06741. LsmAD. 1 hit.
    PF07145. PAM2. 1 hit.
    PF14438. SM-ATX. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99700-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRSAAAAPRS PAVATESRRF AAARWPGWRS LQRPARRSGR GGGGAAPGPY     50
    PSAAPPPPGP GPPPSRQSSP PSASDCFGSN GNGGGAFRPG SRRLLGLGGP 100
    PRPFVVLLLP LASPGAPPAA PTRASPLGAR ASPPRSGVSL ARPAPGCPRP 150
    ACEPVYGPLT MSLKPQQQQQ QQQQQQQQQQ QQQQQQQQPP PAAANVRKPG 200
    GSGLLASPAA APSPSSSSVS SSSATAPSSV VAATSGGGRP GLGRGRNSNK 250
    GLPQSTISFD GIYANMRMVH ILTSVVGSKC EVQVKNGGIY EGVFKTYSPK 300
    CDLVLDAAHE KSTESSSGPK REEIMESILF KCSDFVVVQF KDMDSSYAKR 350
    DAFTDSAISA KVNGEHKEKD LEPWDAGELT ANEELEALEN DVSNGWDPND 400
    MFRYNEENYG VVSTYDSSLS SYTVPLERDN SEEFLKREAR ANQLAEEIES 450
    SAQYKARVAL ENDDRSEEEK YTAVQRNSSE REGHSINTRE NKYIPPGQRN 500
    REVISWGSGR QNSPRMGQPG SGSMPSRSTS HTSDFNPNSG SDQRVVNGGV 550
    PWPSPCPSPS SRPPSRYQSG PNSLPPRAAT PTRPPSRPPS RPSRPPSHPS 600
    AHGSPAPVST MPKRMSSEGP PRMSPKAQRH PRNHRVSAGR GSISSGLEFV 650
    SHNPPSEAAT PPVARTSPSG GTWSSVVSGV PRLSPKTHRP RSPRQNSIGN 700
    TPSGPVLASP QAGIIPTEAV AMPIPAASPT PASPASNRAV TPSSEAKDSR 750
    LQDQRQNSPA GNKENIKPNE TSPSFSKAEN KGISPVVSEH RKQIDDLKKF 800
    KNDFRLQPSS TSESMDQLLN KNREGEKSRD LIKDKIEPSA KDSFIENSSS 850
    NCTSGSSKPN SPSISPSILS NTEHKRGPEV TSQGVQTSSP ACKQEKDDKE 900
    EKKDAAEQVR KSTLNPNAKE FNPRSFSQPK PSTTPTSPRP QAQPSPSMVG 950
    HQQPTPVYTQ PVCFAPNMMY PVPVSPGVQP LYPIPMTPMP VNQAKTYRAV 1000
    PNMPQQRQDQ HHQSAMMHPA SAAGPPIAAT PPAYSTQYVA YSPQQFPNQP 1050
    LVQHVPHYQS QHPHVYSPVI QGNARMMAPP THAQPGLVSS SATQYGAHEQ 1100
    THAMYACPKL PYNKETSPSF YFAISTGSLA QQYAHPNATL HPHTPHPQPS 1150
    ATPTGQQQSQ HGGSHPAPSP VQHHQHQAAQ ALHLASPQQQ SAIYHAGLAP 1200
    TPPSMTPASN TQSPQNSFPA AQQTVFTIHP SHVQPAYTNP PHMAHVPQAH 1250
    VQSGMVPSHP TAHAPMMLMT TQPPGGPQAA LAQSALQPIP VSTTAHFPYM 1300
    THPSVQAHHQ QQL 1313
    Length:1,313
    Mass (Da):140,283
    Last modified:November 25, 2008 - v2
    Checksum:i40A2883FF9D5D118
    GO
    Isoform 2 (identifier: Q99700-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         980-995: PLYPIPMTPMPVNQAK → YQICPNSGKTSIIRVP
         996-1313: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:995
    Mass (Da):106,048
    Checksum:i91213B54F413FF7B
    GO
    Isoform 3 (identifier: Q99700-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-981: Missing.
         982-998: YPIPMTPMPVNQAKTYR → MYYAVEILFNRQSAFFS
         1106-1123: Missing.
         1124-1124: I → V
         1249-1257: AHVQSGMVP → VIPALANFL
         1258-1313: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:258
    Mass (Da):27,894
    Checksum:iE361B49F7A135F23
    GO
    Isoform 4 (identifier: Q99700-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1244-1313: Missing.

    Show »
    Length:1,243
    Mass (Da):132,884
    Checksum:i7D9C99E5F3CEC8CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881Missing in AAB19200. (PubMed:8896555)Curated
    Sequence conflicti188 – 1881Missing in CAA69589. (PubMed:8896557)Curated

    Polymorphismi

    The poly-Gln region of ATXN2 is polymorphic: 17 to 29 repeats are found in the normal population. Higher numbers of repeats result in different disease phenotypes depending on the length of the expansion.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071L → V.2 Publications
    Corresponds to variant rs695871 [ dbSNP | Ensembl ].
    VAR_047629
    Natural varianti248 – 2481S → N.
    Corresponds to variant rs7969300 [ dbSNP | Ensembl ].
    VAR_047630

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 981981Missing in isoform 3. 1 PublicationVSP_011574Add
    BLAST
    Alternative sequencei980 – 99516PLYPI…VNQAK → YQICPNSGKTSIIRVP in isoform 2. 1 PublicationVSP_011575Add
    BLAST
    Alternative sequencei982 – 99817YPIPM…AKTYR → MYYAVEILFNRQSAFFS in isoform 3. 1 PublicationVSP_011576Add
    BLAST
    Alternative sequencei996 – 1313318Missing in isoform 2. 1 PublicationVSP_011577Add
    BLAST
    Alternative sequencei1106 – 112318Missing in isoform 3. 1 PublicationVSP_011578Add
    BLAST
    Alternative sequencei1124 – 11241I → V in isoform 3. 1 PublicationVSP_011579
    Alternative sequencei1244 – 131370Missing in isoform 4. CuratedVSP_011582Add
    BLAST
    Alternative sequencei1249 – 12579AHVQSGMVP → VIPALANFL in isoform 3. 1 PublicationVSP_011580
    Alternative sequencei1258 – 131356Missing in isoform 3. 1 PublicationVSP_011581Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70323 mRNA. Translation: AAB19200.1.
    AK128613 mRNA. Translation: BAC87528.1.
    AC002395 Genomic DNA. No translation available.
    Y08262 mRNA. Translation: CAA69589.1.
    CCDSiCCDS31902.1. [Q99700-1]
    RefSeqiNP_002964.3. NM_002973.3. [Q99700-1]
    UniGeneiHs.76253.

    Genome annotation databases

    EnsembliENST00000377617; ENSP00000366843; ENSG00000204842. [Q99700-1]
    ENST00000550104; ENSP00000446576; ENSG00000204842. [Q99700-2]
    GeneIDi6311.
    KEGGihsa:6311.
    UCSCiuc001tsj.3. human. [Q99700-1]
    uc001tsl.1. human. [Q99700-3]

    Polymorphism databases

    DMDMi215273941.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70323 mRNA. Translation: AAB19200.1 .
    AK128613 mRNA. Translation: BAC87528.1 .
    AC002395 Genomic DNA. No translation available.
    Y08262 mRNA. Translation: CAA69589.1 .
    CCDSi CCDS31902.1. [Q99700-1 ]
    RefSeqi NP_002964.3. NM_002973.3. [Q99700-1 ]
    UniGenei Hs.76253.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KTR X-ray 1.70 B 912-928 [» ]
    ProteinModelPortali Q99700.
    SMRi Q99700. Positions 273-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112218. 37 interactions.
    DIPi DIP-33372N.
    IntActi Q99700. 25 interactions.
    MINTi MINT-1414788.
    STRINGi 9606.ENSP00000366843.

    Chemistry

    ChEMBLi CHEMBL1795085.

    PTM databases

    PhosphoSitei Q99700.

    Polymorphism databases

    DMDMi 215273941.

    Proteomic databases

    MaxQBi Q99700.
    PaxDbi Q99700.
    PRIDEi Q99700.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377617 ; ENSP00000366843 ; ENSG00000204842 . [Q99700-1 ]
    ENST00000550104 ; ENSP00000446576 ; ENSG00000204842 . [Q99700-2 ]
    GeneIDi 6311.
    KEGGi hsa:6311.
    UCSCi uc001tsj.3. human. [Q99700-1 ]
    uc001tsl.1. human. [Q99700-3 ]

    Organism-specific databases

    CTDi 6311.
    GeneCardsi GC12M111890.
    GeneReviewsi ATXN2.
    HGNCi HGNC:10555. ATXN2.
    HPAi HPA018295.
    HPA020339.
    HPA021146.
    MIMi 183090. phenotype.
    601517. gene.
    neXtProti NX_Q99700.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    98756. Spinocerebellar ataxia type 2.
    PharmGKBi PA34968.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268173.
    HOGENOMi HOG000234354.
    HOVERGENi HBG050623.
    InParanoidi Q99700.
    OMAi SNTEHKR.
    PhylomeDBi Q99700.
    TreeFami TF326591.

    Miscellaneous databases

    ChiTaRSi ATXN2. human.
    EvolutionaryTracei Q99700.
    GeneWikii ATXN2.
    GenomeRNAii 6311.
    NextBioi 24501.
    PROi Q99700.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99700.
    Bgeei Q99700.
    CleanExi HS_ATXN2.
    Genevestigatori Q99700.

    Family and domain databases

    InterProi IPR009818. Ataxin-2_C.
    IPR010920. LSM_dom.
    IPR009604. LsmAD_domain.
    IPR025852. SM_dom_ATX.
    [Graphical view ]
    Pfami PF06741. LsmAD. 1 hit.
    PF07145. PAM2. 1 hit.
    PF14438. SM-ATX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, INVOLVEMENT IN SCA2, TISSUE SPECIFICITY, VARIANT VAL-107.
    2. "Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT."
      Sanpei K., Takano H., Igarashi S., Sato T., Oyake M., Sasaki H., Wakisaka A., Tashiro K., Ishida Y., Ikeuchi T., Koide R., Saito M., Sato A., Tanaka T., Hanyu S., Takiyama Y., Nishizawa M., Shimizu N.
      , Nomura Y., Segawa M., Iwabuchi K., Eguchi I., Tanaka H., Takahashi H., Tsuji S.
      Nat. Genet. 14:277-284(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, INVOLVEMENT IN SCA2, TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Trachea.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats."
      Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M., Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O., Stevanin G., Agid Y., Brice A.
      Nat. Genet. 14:285-291(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-1313 (ISOFORM 2), POLYMORPHISM, INVOLVEMENT IN SCA2, TISSUE SPECIFICITY, VARIANT VAL-107.
    6. "Genomic structure of the human gene for spinocerebellar ataxia type 2 (SCA2) on chromosome 12q24.1."
      Sahba S., Nechiporuk A., Figueroa K.P., Nechiporuk T., Pulst S.-M.
      Genomics 47:359-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    7. "A novel protein with RNA-binding motifs interacts with ataxin-2."
      Shibata H., Huynh D.P., Pulst S.-M.
      Hum. Mol. Genet. 9:1303-1313(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBFOX1.
    8. "Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes."
      Satterfield T.F., Pallanck L.J.
      Hum. Mol. Genet. 15:2523-2532(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLYRIBOSOMES.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
      Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
      Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGFR; SH3GL2 AND SH3GL3.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-554; SER-684; THR-741; SER-857; SER-861; SER-888 AND SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. Cited for: INTERACTION WITH TARDBP, INVOLVEMENT IN ALS13, POLY-GLN REPEAT EXPANSION.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-684 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784; SER-861 AND SER-865, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATX2_HUMAN
    AccessioniPrimary (citable) accession number: Q99700
    Secondary accession number(s): A6NLD4, Q6ZQZ7, Q99493
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3