Q99700 (ATX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1313 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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.14
Sequence similarities	Belongs to the ataxin-2 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Amyotrophic lateral sclerosis Neurodegeneration Parkinsonism Spinocerebellar ataxia
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA 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: Compara cytoplasmic mRNA processing body assembly Inferred from mutant phenotype PubMed 17392519. Source: UniProtKB homeostasis of number of cells Inferred from electronic annotation. Source: Compara negative regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara negative regulation of receptor internalization Inferred from mutant phenotype Ref.10. Source: UniProtKB neuromuscular process Inferred from electronic annotation. Source: Compara neuron projection morphogenesis Inferred from electronic annotation. Source: Compara regulation of translation Non-traceable author statement Ref.8. Source: UniProtKB stress granule assembly Inferred from mutant phenotype PubMed 17392519. Source: UniProtKB
Cellular_component	Golgi 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_function	RNA binding Non-traceable author statement Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	4	EBI-697691,EBI-930964
PABPC1	P11940	3	EBI-697691,EBI-81531
SH3GL2	Q99962	4	EBI-697691,EBI-77938
SH3GL3	Q99963	7	EBI-697691,EBI-473910

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1313	1313	Ataxin-2		PRO_0000064756
Regions
	Compositional bias	47 – 158	112	Pro-rich
	Compositional bias	55 – 64	10	Poly-Pro
	Compositional bias	166 – 187	22	Poly-Gln
	Compositional bias	213 – 223	11	Poly-Ser
	Compositional bias	551 – 734	184	Pro-rich
	Compositional bias	929 – 1085	157	Pro-rich
Amino acid modifications
	Modified residue	393	1	Phosphoserine Ref.15
	Modified residue	466	1	Phosphoserine Ref.12
	Modified residue	554	1	Phosphoserine Ref.12
	Modified residue	644	1	Phosphoserine By similarity
	Modified residue	684	1	Phosphoserine Ref.12 Ref.13 Ref.15
	Modified residue	741	1	Phosphothreonine Ref.12
	Modified residue	772	1	Phosphoserine By similarity
	Modified residue	784	1	Phosphoserine Ref.11 Ref.15 Ref.17
	Modified residue	857	1	Phosphoserine Ref.12
	Modified residue	861	1	Phosphoserine Ref.12 Ref.17
	Modified residue	865	1	Phosphoserine Ref.17
	Modified residue	888	1	Phosphoserine Ref.12
	Modified residue	889	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	1 – 981	981	Missing in isoform 3.		VSP_011574
	Alternative sequence	980 – 995	16	PLYPI…VNQAK → YQICPNSGKTSIIRVP in isoform 2.		VSP_011575
	Alternative sequence	982 – 998	17	YPIPM…AKTYR → MYYAVEILFNRQSAFFS in isoform 3.		VSP_011576
	Alternative sequence	996 – 1313	318	Missing in isoform 2.		VSP_011577
	Alternative sequence	1106 – 1123	18	Missing in isoform 3.		VSP_011578
	Alternative sequence	1124	1	I → V in isoform 3.		VSP_011579
	Alternative sequence	1244 – 1313	70	Missing in isoform 4.		VSP_011582
	Alternative sequence	1249 – 1257	9	AHVQSGMVP → VIPALANFL in isoform 3.		VSP_011580
	Alternative sequence	1258 – 1313	56	Missing in isoform 3.		VSP_011581
	Natural variant	107	1	L → V. Ref.1 Ref.5 Corresponds to variant rs695871 [ dbSNP | Ensembl ].		VAR_047629
	Natural variant	248	1	S → N. Corresponds to variant rs7969300 [ dbSNP | Ensembl ].		VAR_047630
Experimental info
	Sequence conflict	188	1	Missing in AAB19200. Ref.1
	Sequence conflict	188	1	Missing in CAA69589. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 40A2883FF9D5D118	FASTA	1,313	140,283
	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
	Isoform 2 [UniParc]. Checksum: 91213B54F413FF7B	FASTA	995	106,048
	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 PVCFAPNMMY PVPVSPGVQY QICPNSGKTS IIRVP
	Isoform 3 [UniParc]. Checksum: E361B49F7A135F23	FASTA	258	27,894
	10 20 30 40 50 60 MYYAVEILFN RQSAFFSAVP NMPQQRQDQH HQSAMMHPAS AAGPPIAATP PAYSTQYVAY 70 80 90 100 110 120 SPQQFPNQPL VQHVPHYQSQ HPHVYSPVIQ GNARMMAPPT HAQPGLVSSS ATQYGAHEQT 130 140 150 160 170 180 HAMYVSTGSL AQQYAHPNAT LHPHTPHPQP SATPTGQQQS QHGGSHPAPS PVQHHQHQAA 190 200 210 220 230 240 QALHLASPQQ QSAIYHAGLA PTPPSMTPAS NTQSPQNSFP AAQQTVFTIH PSHVQPAYTN 250 PPHMAHVPQV IPALANFL
	Isoform 4 [UniParc]. Checksum: 7D9C99E5F3CEC8CB	FASTA	1,243	132,884
	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 TPPSMTPASN TQSPQNSFPA AQQTVFTIHP SHVQPAYTNP PHM

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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. , 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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00180154.
IPI00443693.
IPI00455359.
IPI00455363.

RefSeq

NP_002964.3. NM_002973.3.

UniGene

Hs.76253.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KTR	X-ray	1.70	B	912-928	[»]

ProteinModelPortal

Q99700.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33372N.

IntAct

Q99700. 20 interactions.

MINT

MINT-1414788.

STRING

9606.ENSP00000366843.

PTM databases

PhosphoSite

Q99700.

Polymorphism databases

DMDM

215273941.

Proteomic databases

PaxDb

Q99700.

PRIDE

Q99700.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377617; ENSP00000366843; ENSG00000204842.
ENST00000482777; ENSP00000448848; ENSG00000204842.
ENST00000550104; ENSP00000446576; ENSG00000204842.

GeneID

6311.

KEGG

hsa:6311.

UCSC

uc001tsj.3. human.
uc001tsl.1. human.

Organism-specific databases

CTD

6311.

GeneCards

GC12M111890.

HGNC

HGNC:10555. ATXN2.

HPA

HPA018295.
HPA020339.
HPA021146.

MIM

183090. phenotype.
601517. gene.

neXtProt

NX_Q99700.

Orphanet

803. Amyotrophic lateral sclerosis.
98756. Spinocerebellar ataxia type 2.

PharmGKB

PA34968.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG268173.

HOGENOM

HOG000234354.

HOVERGEN

HBG050623.

InParanoid

Q99700.

OMA

NGGVPWP.

OrthoDB

EOG4BP1B3.

Gene expression databases

ArrayExpress

Q99700.

Bgee

Q99700.

CleanEx

HS_ATXN2.

Genevestigator

Q99700.

GermOnline

ENSG00000204842. Homo sapiens.

Family and domain databases

InterPro

IPR009818. Ataxin-2_C.
IPR010920. LSM_dom.
IPR009604. LsmAD_domain.
IPR025852. SM_dom_ATX.
[Graphical view]

Pfam

PF06741. LsmAD. 1 hit.
PF07145. PAM2. 1 hit.
PF14438. SM-ATX. 1 hit.
[Graphical view]

SUPFAM

SSF50182. Sm_like_riboprot. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1795085.

ChiTaRS

ATXN2. human.

EvolutionaryTrace

Q99700.

GenomeRNAi

6311.

NextBio

24501.

SOURCE

Search...

Entry information

Entry name

ATX2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.