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Reviewed, UniProtKB/Swiss-Prot Q99700 (ATX2_HUMAN)

Last modified January 19, 2010. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Subunit structure

Monomer By similarity. Can also form homodimers By similarity.

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 in the normal population, expanded to about 36 to 52 repeats in spinocerebellar ataxia 2 (SCA2) patients.

Involvement in disease

Defects in ATXN2 are the cause of spinocerebellar ataxia type 2 (SCA2) [MIM:183090]; also known as olivopontocerebellar atrophy II (OPCA II or OPCA2). 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. SCA2 is caused by expansion of a CAG repeat in the coding region of ATXN2. Longer expansions result in earlier onset of the disease. In some patients with smaller CAG repeat expansions, SCA2 presents as pure familial parkinsonism without cerebellar signs. Ref.1 Ref.2 Ref.5

Sequence similarities

Belongs to the ataxin-2 family.

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 residue4661Phosphoserine Ref.11
Modified residue5541Phosphoserine Ref.11
Modified residue5581Phosphoserine Ref.11
Modified residue6441Phosphoserine By similarity
Modified residue6671Phosphoserine Ref.10 Ref.13
Modified residue6841Phosphoserine Ref.11 Ref.14
Modified residue7411Phosphothreonine Ref.11
Modified residue7441Phosphoserine Ref.11
Modified residue7491Phosphoserine Ref.14
Modified residue7711Phosphothreonine Ref.7 Ref.8
Modified residue7721Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue7761Phosphoserine Ref.7
Modified residue7841Phosphoserine Ref.10
Modified residue8281Phosphoserine Ref.8
Modified residue8391Phosphoserine Ref.8
Modified residue8491Phosphoserine Ref.11
Modified residue8571Phosphoserine Ref.11 Ref.13
Modified residue8611Phosphoserine Ref.11 Ref.13
Modified residue8631Phosphoserine Ref.11 Ref.13
Modified residue8651Phosphoserine Ref.13
Modified residue8881Phosphoserine Ref.11
Modified residue8891Phosphoserine Ref.11

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: dbSNP rs695871. Ref.1 Ref.5
VAR_047629
Natural variant2481S → N: dbSNP rs7969300.
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.

Checksum: 91213B54F413FF7B
Show »

FASTA995106,048
Isoform 3.

Checksum: E361B49F7A135F23
Show »

FASTA25827,894
Isoform 4.

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: 8896555] [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: 8896556] [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: 14702039] [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: 16541075] [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: 8896557] [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: 9480749] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[7]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-771; SER-772 AND SER-776, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-771; SER-772; SER-828 AND SER-839, MASS SPECTROMETRY.
[9]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, MASS SPECTROMETRY.
[10]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-784, MASS SPECTROMETRY.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-554; SER-558; SER-684; THR-741; SER-744; SER-849; SER-857; SER-861; SER-863; SER-888 AND SER-889, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-857; SER-861; SER-863 AND SER-865, MASS SPECTROMETRY.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-749, MASS SPECTROMETRY.
Tissue: T-cell.
+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.
IPIIPI00180154.
IPI00443693.
IPI00455359.
IPI00455363.
RefSeqNP_002964.3.
UniGeneHs.76253

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ99700. 20 interactions.
STRINGQ99700.

PTM databases

PhosphoSiteQ99700.

Proteomic databases

PRIDEQ99700.

Genome annotation databases

EnsemblENST00000377617; ENSP00000366843; ENSG00000204842; Homo sapiens. [Genome view]
GeneID6311.
KEGGhsa:6311.
UCSCuc001tsg.1. human.

Organism-specific databases

CTD6311.
GeneCardsGC12M110352.
H-InvDBHIX0011000.
HGNCHGNC:10555. ATXN2.
HPAHPA018295.
HPA020339.
HPA021146.
MIM183090. phenotype.
601517. gene.
Orphanet98756. Ataxia, spinocerebellar, type 2.
PharmGKBPA34968.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04446.
HOGENOMHBG715226.
HOVERGENQ99700.
InParanoidQ99700.
OMAPRMGQPG.
OrthoDBEOG9WQ3NC.

Gene expression databases

ArrayExpressQ99700.
BgeeQ99700.
CleanExHS_ATXN2.
GenevestigatorQ99700.
GermOnlineENSG00000204842. Homo sapiens.

Family and domain databases

InterProIPR009818. Ataxin-2_C.
IPR010920. LSM_related_domain.
IPR009604. LsmAD_domain.
[Graphical view]
PfamPF06741. LsmAD. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio24501.
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: January 19, 2010
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents