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Q99700 (ATX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-2
Alternative name(s):
Spinocerebellar ataxia type 2 protein
Trinucleotide repeat-containing gene 13 protein
Gene names
Name:ATXN2
Synonyms:ATX2, SCA2, TNRC13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. Ref.10

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.15

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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. Ref.1 Ref.2 Ref.5 Ref.6

Polymorphism

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.

Involvement in disease

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.
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. Ref.1 Ref.2 Ref.5

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.
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. Ref.15

Sequence similarities

Belongs to the ataxin-2 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseAmyotrophic lateral sclerosis
Neurodegeneration
Parkinsonism
Spinocerebellar ataxia
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Non-traceable author statement PubMed 15663938. Source: UniProtKB

RNA transport

Non-traceable author statement Ref.7. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cerebellar Purkinje cell differentiation

Inferred from electronic annotation. Source: Ensembl

cytoplasmic mRNA processing body assembly

Inferred from mutant phenotype PubMed 17392519. Source: UniProtKB

homeostasis of number of cells

Inferred from electronic annotation. Source: Ensembl

negative regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor internalization

Inferred from mutant phenotype Ref.10. Source: UniProtKB

neuromuscular process

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of translation

Non-traceable author statement Ref.8. Source: UniProtKB

stress granule assembly

Inferred from mutant phenotype PubMed 17392519. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 12812977PubMed 17097639. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay PubMed 17392519. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17097639. Source: UniProtKB

polysome

Inferred from direct assay Ref.8. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionRNA binding

Non-traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99700-1)

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.
Isoform 2 (identifier: Q99700-2)

The sequence of this isoform differs from the canonical sequence as follows:
     980-995: PLYPIPMTPMPVNQAK → YQICPNSGKTSIIRVP
     996-1313: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q99700-3)

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.
Isoform 4 (identifier: Q99700-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13131313Ataxin-2
PRO_0000064756

Regions

Compositional bias47 – 158112Pro-rich
Compositional bias55 – 6410Poly-Pro
Compositional bias166 – 18722Poly-Gln
Compositional bias213 – 22311Poly-Ser
Compositional bias551 – 734184Pro-rich
Compositional bias929 – 1085157Pro-rich

Amino acid modifications

Modified residue3931Phosphoserine Ref.16
Modified residue4661Phosphoserine Ref.12
Modified residue5541Phosphoserine Ref.12
Modified residue6841Phosphoserine Ref.12 Ref.14 Ref.16
Modified residue7411Phosphothreonine Ref.12
Modified residue7841Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue8571Phosphoserine Ref.12
Modified residue8611Phosphoserine Ref.12 Ref.18
Modified residue8651Phosphoserine Ref.18
Modified residue8881Phosphoserine Ref.12
Modified residue8891Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 981981Missing in isoform 3.
VSP_011574
Alternative sequence980 – 99516PLYPI…VNQAK → YQICPNSGKTSIIRVP in isoform 2.
VSP_011575
Alternative sequence982 – 99817YPIPM…AKTYR → MYYAVEILFNRQSAFFS in isoform 3.
VSP_011576
Alternative sequence996 – 1313318Missing in isoform 2.
VSP_011577
Alternative sequence1106 – 112318Missing in isoform 3.
VSP_011578
Alternative sequence11241I → V in isoform 3.
VSP_011579
Alternative sequence1244 – 131370Missing in isoform 4.
VSP_011582
Alternative sequence1249 – 12579AHVQSGMVP → VIPALANFL in isoform 3.
VSP_011580
Alternative sequence1258 – 131356Missing in isoform 3.
VSP_011581
Natural variant1071L → V. Ref.1 Ref.5
Corresponds to variant rs695871 [ dbSNP | Ensembl ].
VAR_047629
Natural variant2481S → N.
Corresponds to variant rs7969300 [ dbSNP | Ensembl ].
VAR_047630

Experimental info

Sequence conflict1881Missing in AAB19200. Ref.1
Sequence conflict1881Missing in CAA69589. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 40A2883FF9D5D118

FASTA1,313140,283
        10         20         30         40         50         60 
MRSAAAAPRS PAVATESRRF AAARWPGWRS LQRPARRSGR GGGGAAPGPY PSAAPPPPGP 

        70         80         90        100        110        120 
GPPPSRQSSP PSASDCFGSN GNGGGAFRPG SRRLLGLGGP PRPFVVLLLP LASPGAPPAA 

       130        140        150        160        170        180 
PTRASPLGAR ASPPRSGVSL ARPAPGCPRP ACEPVYGPLT MSLKPQQQQQ QQQQQQQQQQ 

       190        200        210        220        230        240 
QQQQQQQQPP PAAANVRKPG GSGLLASPAA APSPSSSSVS SSSATAPSSV VAATSGGGRP 

       250        260        270        280        290        300 
GLGRGRNSNK GLPQSTISFD GIYANMRMVH ILTSVVGSKC EVQVKNGGIY EGVFKTYSPK 

       310        320        330        340        350        360 
CDLVLDAAHE KSTESSSGPK REEIMESILF KCSDFVVVQF KDMDSSYAKR DAFTDSAISA 

       370        380        390        400        410        420 
KVNGEHKEKD LEPWDAGELT ANEELEALEN DVSNGWDPND MFRYNEENYG VVSTYDSSLS 

       430        440        450        460        470        480 
SYTVPLERDN SEEFLKREAR ANQLAEEIES SAQYKARVAL ENDDRSEEEK YTAVQRNSSE 

       490        500        510        520        530        540 
REGHSINTRE NKYIPPGQRN REVISWGSGR QNSPRMGQPG SGSMPSRSTS HTSDFNPNSG 

       550        560        570        580        590        600 
SDQRVVNGGV PWPSPCPSPS SRPPSRYQSG PNSLPPRAAT PTRPPSRPPS RPSRPPSHPS 

       610        620        630        640        650        660 
AHGSPAPVST MPKRMSSEGP PRMSPKAQRH PRNHRVSAGR GSISSGLEFV SHNPPSEAAT 

       670        680        690        700        710        720 
PPVARTSPSG GTWSSVVSGV PRLSPKTHRP RSPRQNSIGN TPSGPVLASP QAGIIPTEAV 

       730        740        750        760        770        780 
AMPIPAASPT PASPASNRAV TPSSEAKDSR LQDQRQNSPA GNKENIKPNE TSPSFSKAEN 

       790        800        810        820        830        840 
KGISPVVSEH RKQIDDLKKF KNDFRLQPSS TSESMDQLLN KNREGEKSRD LIKDKIEPSA 

       850        860        870        880        890        900 
KDSFIENSSS NCTSGSSKPN SPSISPSILS NTEHKRGPEV TSQGVQTSSP ACKQEKDDKE 

       910        920        930        940        950        960 
EKKDAAEQVR KSTLNPNAKE FNPRSFSQPK PSTTPTSPRP QAQPSPSMVG HQQPTPVYTQ 

       970        980        990       1000       1010       1020 
PVCFAPNMMY PVPVSPGVQP LYPIPMTPMP VNQAKTYRAV PNMPQQRQDQ HHQSAMMHPA 

      1030       1040       1050       1060       1070       1080 
SAAGPPIAAT PPAYSTQYVA YSPQQFPNQP LVQHVPHYQS QHPHVYSPVI QGNARMMAPP 

      1090       1100       1110       1120       1130       1140 
THAQPGLVSS SATQYGAHEQ THAMYACPKL PYNKETSPSF YFAISTGSLA QQYAHPNATL 

      1150       1160       1170       1180       1190       1200 
HPHTPHPQPS ATPTGQQQSQ HGGSHPAPSP VQHHQHQAAQ ALHLASPQQQ SAIYHAGLAP 

      1210       1220       1230       1240       1250       1260 
TPPSMTPASN TQSPQNSFPA AQQTVFTIHP SHVQPAYTNP PHMAHVPQAH VQSGMVPSHP 

      1270       1280       1290       1300       1310 
TAHAPMMLMT TQPPGGPQAA LAQSALQPIP VSTTAHFPYM THPSVQAHHQ QQL 

« Hide

Isoform 2 [UniParc].

Checksum: 91213B54F413FF7B
Show »

FASTA995106,048
Isoform 3 [UniParc].

Checksum: E361B49F7A135F23
Show »

FASTA25827,894
Isoform 4 [UniParc].

Checksum: 7D9C99E5F3CEC8CB
Show »

FASTA1,243132,884

References

« Hide 'large scale' references
[1]"Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2."
Pulst S.-M., Nechiporuk A., Nechiporuk T., Gispert S., Chen X.-N., Lopes-Cendes I., Pearlman S., Starkman S., Orozco-Diaz G., Lunkes A., DeJong P., Rouleau G.A., Auburger G., Korenberg J.R., Figueroa C., Sahba S.
Nat. Genet. 14:269-276(1996) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS."
Elden A.C., Kim H.J., Hart M.P., Chen-Plotkin A.S., Johnson B.S., Fang X., Armakola M., Geser F., Greene R., Lu M.M., Padmanabhan A., Clay-Falcone D., McCluskey L., Elman L., Juhr D., Gruber P.J., Rub U., Auburger G. expand/collapse author list , Trojanowski J.Q., Lee V.M., Van Deerlin V.M., Bonini N.M., Gitler A.D.
Nature 466:1069-1075(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70323 mRNA. Translation: AAB19200.1.
AK128613 mRNA. Translation: BAC87528.1.
AC002395 Genomic DNA. No translation available.
Y08262 mRNA. Translation: CAA69589.1.
RefSeqNP_002964.3. NM_002973.3.
UniGeneHs.76253.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KTRX-ray1.70B912-928[»]
ProteinModelPortalQ99700.
SMRQ99700. Positions 273-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112218. 31 interactions.
DIPDIP-33372N.
IntActQ99700. 25 interactions.
MINTMINT-1414788.
STRING9606.ENSP00000366843.

Chemistry

ChEMBLCHEMBL1795085.

PTM databases

PhosphoSiteQ99700.

Polymorphism databases

DMDM215273941.

Proteomic databases

PaxDbQ99700.
PRIDEQ99700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377617; ENSP00000366843; ENSG00000204842. [Q99700-1]
ENST00000550104; ENSP00000446576; ENSG00000204842. [Q99700-2]
GeneID6311.
KEGGhsa:6311.
UCSCuc001tsj.3. human. [Q99700-1]
uc001tsl.1. human. [Q99700-3]

Organism-specific databases

CTD6311.
GeneCardsGC12M111890.
HGNCHGNC:10555. ATXN2.
HPAHPA018295.
HPA020339.
HPA021146.
MIM183090. phenotype.
601517. gene.
neXtProtNX_Q99700.
Orphanet803. Amyotrophic lateral sclerosis.
98756. Spinocerebellar ataxia type 2.
PharmGKBPA34968.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268173.
HOGENOMHOG000234354.
HOVERGENHBG050623.
InParanoidQ99700.
OMASNTEHKR.
TreeFamTF326591.

Gene expression databases

ArrayExpressQ99700.
BgeeQ99700.
CleanExHS_ATXN2.
GenevestigatorQ99700.

Family and domain databases

InterProIPR009818. Ataxin-2_C.
IPR010920. LSM_dom.
IPR009604. LsmAD_domain.
IPR025852. SM_dom_ATX.
[Graphical view]
PfamPF06741. LsmAD. 1 hit.
PF07145. PAM2. 1 hit.
PF14438. SM-ATX. 1 hit.
[Graphical view]
SUPFAMSSF50182. SSF50182. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATXN2. human.
EvolutionaryTraceQ99700.
GeneWikiATXN2.
GenomeRNAi6311.
NextBio24501.
PROQ99700.
SOURCESearch...

Entry information

Entry nameATX2_HUMAN
AccessionPrimary (citable) accession number: Q99700
Secondary accession number(s): A6NLD4, Q6ZQZ7, Q99493
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: November 25, 2008
Last modified: March 19, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM