| IED ID | IndEnz0002013951 |
| Enzyme Type ID | protease013951 |
| Protein Name |
Ataxin-1 Spinocerebellar ataxia type 1 protein |
| Gene Name | ATXN1 ATX1 SCA1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKSNQERSNECLPPKKREIPATSRSSEEKAPTLPSDNHRVEGTAWLPGNPGGRGHGGGRHGPAGTSVELGLQQGIGLHKALSTGLDYSPPSAPRSVPVATTLPAAYATPQPGTPVSPVQYAHLPHTFQFIGSSQYSGTYASFIPSQLIPPTANPVTSAVASAAGATTPSQRSQLEAYSTLLANMGSLSQTPGHKAEQQQQQQQQQQQQHQHQQQQQQQQQQQQQQHLSRAPGLITPGSPPPAQQNQYVHISSSPQNTGRTASPPAIPVHLHPHQTMIPHTLTLGPPSQVVMQYADSGSHFVPREATKKAESSRLQQAIQAKEVLNGEMEKSRRYGAPSSADLGLGKAGGKSVPHPYESRHVVVHPSPSDYSSRDPSGVRASVMVLPNSNTPAADLEVQQATHREASPSTLNDKSGLHLGKPGHRSYALSPHTVIQTTHSASEPLPVGLPATAFYAGTQPPVIGYLSGQQQAITYAGSLPQHLVIPGTQPLLIPVGSTDMEASGAAPAIVTSSPQFAAVPHTFVTTALPKSENFNPEALVTQAAYPAMVQAQIHLPVVQSVASPAAAPPTLPPYFMKGSIIQLANGELKKVEDLKTEDFIQSAEISNDLKIDSSTVERIEDSHSPGVAVIQFAVGEHRAQVSVEVLVEYPFFVFGQGWSSCCPERTSQLFDLPCSKLSVGDVCISLTLKNLKNGSVKKGQPVDPASVLLKHSKADGLAGSRHRYAEQENGINQGSAQMLSENGELKFPEKMGLPAAPFLTKIEPSKPAATRKRRWSAPESRKLEKSEDEPPLTLPKPSLIPQEVKICIEGRSNVGK |
| Enzyme Length | 815 |
| Uniprot Accession Number | P54253 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism (PubMed:21475249). In concert with CIC and ATXN1L, involved in brain development (By similarity). {ECO:0000250|UniProtKB:P54254, ECO:0000269|PubMed:21475249}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (10); Chain (1); Compositional bias (4); Cross-link (5); Domain (1); Helix (4); Modified residue (5); Motif (1); Mutagenesis (12); Natural variant (2); Region (8); Sequence conflict (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;DNA-binding;Isopeptide bond;Neurodegeneration;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Repressor;Spinocerebellar ataxia;Transcription;Transcription regulation;Triplet repeat expansion;Ubl conjugation |
| Interact With | Q969K4; Q13444-2; Q5TGY3; P54819; P31749; Q9H553; Q8IWZ3-2; Q8IWZ3-3; P39687; P13928; O43747-2; P63010-2; P05067; Q8N6T3-3; Q03989; Q0P5N6; Q8WXK3; Q9Y575-3; Q96DX5-3; Q96FT7-4; P18847; Q9H0Y0; P06576; P30049; P24539; P61421; P15313; Itself; Q99700; Q99700-5; O95816; Q9UQB8-6; Q14457; O14503; Q6AI39; O43684; Q5SWW7; Q32Q52; Q6P1W5; Q9NUB4; Q9BVC5; Q5SZD1; Q14012; P22681; Q9ULV8; Q9NPC3; O75909; O75909-2; P48643; P40227; Q9UJX2; Q8NHZ8; Q7Z7K6; Q8NHQ1-3; P23528; Q96RK0; Q14011; Q9NSE2; P38432; Q86WV2; Q8N684; Q8N684-3; P46108; P46108-2; Q8IUI8; O43186; P53672; P56545-3; Q13619; Q9NTM9; Q5D0E6-2; Q13117-3; Q15038; Q8WV16-4; O75935-2; Q5TDH0-2; Q8NDP9; O60479; Q09013; Q96EY1; Q96EY1-3; Q9UDY4; Q86Y13; Q3B7T1; O95967; O14602; P20042; O00303; Q14240-2; Q9NRA8; Q15717; O00472; Q8TE02; Q32P44; Q8TC29; O95208-2; Q13216-2; Q6NXG1; Q6NXG1-3; O43909; P0C7A2-2; Q92567-2; Q9NSD9; P14324; Q9UHY8; P26885; Q8TBE3; Q96NZ1; P02792; P06241; P06241-3; Q06547-2; F2Z2M7; P28676; Q9UKD1; Q9H8Y8; Q9UKJ3; Q93079; P15822; Q8WVV9-3; P09017; P37235; Q9UBD0; Q96LI6; P0DMV8; P11142; P80217-2; Q8IY31-3; P29218-3; Q6DN90-2; P53990; P53990-2; P53990-3; O14713; Q92993; Q92993-2; Q9NVX7-2; Q96SI1-2; P57682; Q13887; Q53G59; Q6TDP4; Q9Y2M5; Q8N4N3-2; P60329; Q3SY46; Q8IUB9; Q8IUC2; Q9BYQ4; Q96JM7-2; Q14847-2; O95447; Q9BYZ2; Q6DKI2; Q9UPM6; Q8N0U6; Q8TBB1; Q8N448; Q6UWE0; Q86VM6; Q9NR56-5; Q96RN5-2; Q9H7H0; Q9H7H0-2; Q8N6F8; Q8TDB4; A4FUJ8; Q9BUB5; O95396; Q8N594; Q9Y605; Q96HT8; O43776; O76041; Q86SG6; Q12986; P23511-2; Q5HYW2; Q9UBE8; O00746; P56597; Q15738; O43809; Q8NFH3; O15381-5; Q02218; Q96FW1; Q6GQQ9-2; P32243-2; Q6VY07; Q495U3; Q9BR81; P22061-2; Q9NV79; Q96HC4; Q13113; P12955; O00541; Q9NRX4; O75925; Q13492-3; P42336; Q9P1W9; Q96J94; O15496; Q9HAU0; Q494U1-3; O43660-2; Q7Z3K3; Q9P1U0; Q96HA1-2; Q6ZMI0-5; O60828; Q13162; P17612; O60260-5; Q6P2Q9; P86479; P86480; P48634; Q5JSZ5; Q5JSZ5-5; P25786; P25789; P28070; P28062-2; P17980; P41222; Q15032-2; Q9NS91; P54725; Q9Y620; Q8WZA2-3; Q13702-2; Q09028; Q9BYM8; Q9NWB1; Q9NWB1-5; O43251; O43251-10; Q96I25; Q06330; Q93062; Q93062-3; Q15293; Q04864; Q04864-2; Q8TAI7; Q9BQY4; Q9H871; Q6ZNA4-2; Q9ULX5; Q8WU17; Q96D59; Q99496; Q96EP0; Q9H0F5-2; P27635; P61313; Q07020; P84098; P35268; P39019; P46782; Q8N488; Q8N6K7-2; Q9NR31; O00560; P50454; Q15637-4; Q12874; Q15393; Q2NKQ1-4; Q8IUQ4-2; Q8N196; P63208; Q86UW1; Q9NSD5-3; Q96GM5; O95721; Q96DI7; P14678; P62316; P62318; Q9UPU3; O95416; P41225; Q99932-2; Q8IUW3; P61009; Q13501; P36956; Q969X2; Q6ZMT1; O75886; O95630; P55854; Q8NEM7; Q9NX95; Q9NX95-5; Q92609; Q9BZK7; Q16650; Q96SF7; Q9Y458; O15273; Q8N8B7-2; P28347-2; Q96IP4; Q96A09; Q15554-4; P37173; O95411; Q08117; Q9NV96-2; Q71RG4-4; Q13829; Q9H0E2; O94842; P06753; P06753-2; Q8N7U7-2; Q12933; P36406; Q13049; O00635; L8E9Q5; Q86WT6-2; Q86UV6-2; Q9C026; Q15654; Q86WV8; Q6DKK2; Q8WVJ9; Q01081; P26368; Q9BSL1; Q969T4; P63279; Q7KZS0; Q13404; O94941; Q9NRR5; O75604-3; Q70CQ3; P62068; Q70EL1; Q70EL1-9; P55072; O75351; P62760; Q96N03; Q9GZS3; Q9BRX9; P31946; P62258; Q04917; P27348; P63104; Q9H869; Q9H869-2; A0A0C4DGF1; O43298; Q96K80; Q86WB0-2; Q9UKY1; Q9H4I2-2; Q96NC0; O95789-4; Q8N554; Q8N895; Q96MN9; Q96MN9-2; Q8N988-2; Q8NBB4-2; Q2QGD7; Q9H669; Q9Y649; P38432 |
| Induction | INDUCTION: ATXN1 protein levels are directly regulated by PUM1 protein: PUM1 acts by binding to the 3'-UTR of ATXN1 mRNA, affecting ATXN1 mRNA stability and leading to reduced ATXN1 protein levels. {ECO:0000269|PubMed:25768905}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7647801}. Nucleus {ECO:0000269|PubMed:12093161, ECO:0000269|PubMed:7647801}. Note=Colocalizes with USP7 in the nucleus. {ECO:0000269|PubMed:12093161}. |
| Modified Residue | MOD_RES 82; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54254; MOD_RES 88; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 238; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 253; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54254; MOD_RES 775; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:12741986 |
| Post Translational Modification | PTM: Ubiquitinated by UBE3A, leading to its degradation by the proteasome. The presence of expanded poly-Gln repeats in spinocerebellar ataxia 1 (SCA1) patients impairs ubiquitination and degradation, leading to accumulation of ATXN1 in neurons and subsequent toxicity. {ECO:0000250|UniProtKB:P54254}.; PTM: Phosphorylation at Ser-775 increases the pathogenicity of proteins with an expanded polyglutamine tract. {ECO:0000269|PubMed:12741986}.; PTM: Sumoylation is dependent on nuclear localization and phosphorylation at Ser-775. It is reduced in the presence of an expanded polyglutamine tract. {ECO:0000269|PubMed:12741986, ECO:0000269|PubMed:15824120}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (6) |
| Cross Reference PDB | 1OA8; 2M41; 4APT; 4AQP; 4J2J; 4J2L; 6QIU; |
| Mapped Pubmed ID | 11121205; 11781699; 11804332; 11807410; 11973625; 12360291; 12411613; 12757707; 12757932; 12965213; 14756671; 14985428; 15148151; 15167689; 15292212; 15300851; 15615787; 15750336; 15878393; 16277991; 16311891; 16380905; 16389595; 16497448; 16614004; 16713569; 16831871; 16967484; 17110330; 17442486; 17540008; 17557114; 17925862; 18160752; 18182848; 18216249; 18231590; 18337722; 18439907; 18519031; 19049837; 19235102; 19259763; 19451621; 19500214; 19597981; 20018885; 20037628; 20069235; 20097758; 20132795; 20220018; 20308783; 20379614; 20417604; 20477910; 20711500; 20936779; 21302343; 21315774; 22330095; 22491195; 22511762; 22666429; 22780124; 22916034; 23197749; 23275563; 23294540; 23414517; 23512657; 23528090; 23536093; 23634774; 23719381; 23760502; 24032423; 24155902; 24858692; 25344417; 25416956; 25641559; 26522012; 26879337; 27193757; 27466200; 27577232; 27686464; 28212558; 28551466; 29055568; 29274668; 29852174; 30314815; 30391819; 30507379; 31381977; 32339968; 32408088; 32763910; 33159825; 34302818; 34635619; 9184318; |
| Motif | MOTIF 794..797; /note=Nuclear localization signal; /evidence=ECO:0000250|UniProtKB:P54254 |
| Gene Encoded By | |
| Mass | 86,923 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |