ATM
entrez
472
canonical
uniprot
Q13315
canonical
ensembl
ENSG00000149311
resolver
ensp
ENSP00000278616
resolver
ensp
ENSP00000388058
resolver
ensp
ENSP00000432318
resolver
ensp
ENSP00000434327
resolver
ensp
ENSP00000469471
resolver
ensp
ENSP00000480205
resolver
ensp
ENSP00000491585
resolver
ensp
ENSP00000491957
resolver
ensp
ENSP00000492354
resolver
ensp
ENSP00000492487
resolver
ensp
ENSP00000501606
resolver
ensp
ENSP00000507125
resolver
ensp
ENSP00000507649
resolver
ensp
ENSP00000508178
resolver
ensp
ENSP00000508284
resolver
ensp
ENSP00000519148
resolver
ensp
ENSP00000519149
resolver
ensp
ENSP00000519150
resolver
ensp
ENSP00000519151
resolver
ensp
ENSP00000519152
resolver
enst
ENST00000278616
resolver
enst
ENST00000452508
resolver
enst
ENST00000526567
resolver
enst
ENST00000532931
resolver
enst
ENST00000601453
resolver
enst
ENST00000638443
resolver
enst
ENST00000639240
resolver
enst
ENST00000639953
resolver
enst
ENST00000640388
resolver
enst
ENST00000675843
resolver
enst
ENST00000682465
resolver
enst
ENST00000683150
resolver
enst
ENST00000683468
resolver
enst
ENST00000683914
resolver
enst
ENST00000713843
resolver
enst
ENST00000713844
resolver
enst
ENST00000713845
resolver
enst
ENST00000713846
resolver
enst
ENST00000713847
resolver
genesymbol
ATM
resolver
hgnc
HGNC:795
resolver
uniprot
A0AAQ5BH18
resolver
uniprot
A0ACM8Q3F6
resolver
uniprot
B2RNX5
resolver
uniprot
E9PRG7
resolver
uniprot
O15429
resolver
uniprot
Q12758
resolver
uniprot
Q16551
resolver
uniprot
Q6P7P1
resolver
uniprot
Q93007
resolver
uniprot
Q9NP02
resolver
uniprot
Q9UCX7
resolver
uniprot_entry
A0AAQ5BH18_HUMAN
resolver
uniprot_entry
A0ACM8Q3F6_HUMAN
resolver
uniprot_entry
ATM_HUMAN
resolver
uniprot_entry
Q6P7P1_HUMAN
resolver
uniprot_sec
B2RNX5
resolver
uniprot_sec
E9PRG7
resolver
uniprot_sec
O15429
resolver
uniprot_sec
Q12758
resolver
uniprot_sec
Q16551
resolver
uniprot_sec
Q93007
resolver
uniprot_sec
Q9NP02
resolver
uniprot_sec
Q9UCX7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the MRN (MRE11-RAD50-NBS1) complex in response to DNA double strand breaks (DSBs), which recruits ATM to DSBs and promotes its activation (PubMed:15064416, PubMed:15790808, PubMed:35076389). Inhibited by wortmannin (PubMed:9766667). {ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:35076389, ECO:0000269|PubMed:9766667}.
uniprot
proteins
amino_acid_sequence
MSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRAPRLKCQELLNYIMDTVKDSSNGAIYGADCSNILLKDILSVRKYWCEISQQQWLELFSVYFRLYLKPSQDVHRVLVARIIHAVTKGCCSQTDGLNSKFLDFFSKAIQCARQEKSSSGLNHILAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQHRLNDSLKEVIIELFQLQIYIHHPKGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRNIAVKENLIELMADICHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDFDLVPWLQIATQLISKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNLESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSACRPSCPAVCCLTLALTTSIVPGTVKMGIEQNMCEVNRSFSLKESIMKWLLFYQLEGDLENSTEVPPILHSNFPHLVLEKILVSLTMKNCKAAMNFFQSVPECEHHQKDKEELSFSEVEELFLQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLKESLDRCLLGLSEQLLNNYSSEITNSETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEEFRIGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKKPFDRGEVESMEDDTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSKQDLLFLDMLKFLCLCVTTAQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLKELPGEEYPLPMEDVLELLKPLSNVCSLYRRDQDVCKTILNHVLHVVKNLGQSNMDSENTRDAQGQFLTVIGAFWHLTKERKYIFSVRMALVNCLKTLLEADPYSKWAILNVMGKDFPVNEVFTQFLADNHHQVRMLAAESINRLFQDTKGDSSRLLKALPLKLQQTAFENAYLKAQEGMREMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALCKSVKENGLEPHLVKKVLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDFYRSCYKVLIPHLVIRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQRETATKVYDMLKSENLLGKQIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRPSCIMDVSLRSFSLCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLVYEQVEVQKQVLDLLKYLVIDNKDNENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFLSVSVYDALPLTRLEGLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEKEVLEAVGSCLGEVGPIDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCLKNILATKTGHSFWEIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDINLWIPLSENHDIWIKTLTCAFLDSGGTKCEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHVQGFFTSCLRHFSQTSRSTTPANLDSESEHFFRCCLDKKSQRTMLAVVDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQSCAAHFTALLYAEIYADKKSMDDQEKRSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPITRLRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYENKDWCPELEELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMDNSQRECIKDILTKHLVELSILARTFKNTQLPERAIFQIKQYNSVSCGVSEWQLEEAQVFWAKKEQSLALSILKQMIKKLDASCAANNPSLKLTYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTVKVQRELELDELALRALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMKRDGMKIPTYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFLTKPEVARRSRITKNVPKQSSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILANLDATQWKTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHPTLNADDQECKRNLSDIDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAWV
uniprot
proteins
disease_involvement
DISEASE: Ataxia telangiectasia (AT) [MIM:208900]: A rare recessive disorder characterized by progressive cerebellar ataxia, dilation of the blood vessels in the conjunctiva and eyeballs, immunodeficiency, growth retardation and sexual immaturity. Patients have a strong predisposition to cancer; about 30% of patients develop tumors, particularly lymphomas and leukemias. Cells from affected individuals are highly sensitive to damage by ionizing radiation and resistant to inhibition of DNA synthesis following irradiation. {ECO:0000269|PubMed:10234507, ECO:0000269|PubMed:10425038, ECO:0000269|PubMed:10817650, ECO:0000269|PubMed:10873394, ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:27664052, ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8589678, ECO:0000269|PubMed:8665503, ECO:0000269|PubMed:8698354, ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:8789452, ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:8808599, ECO:0000269|PubMed:8845835, ECO:0000269|PubMed:9043869, ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9443866, ECO:0000269|PubMed:9450874, ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9497252, ECO:0000269|PubMed:9521587, ECO:0000269|PubMed:9711876, ECO:0000269|PubMed:9792409, ECO:0000269|PubMed:9792410, ECO:0000269|PubMed:9872980, ECO:0000269|PubMed:9887333}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in ATM may contribute to T-cell acute lymphoblastic leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is characterized by a high white blood cell count, with a predominance of prolymphocytes, marked splenomegaly, lymphadenopathy, skin lesions and serous effusion. The clinical course is highly aggressive, with poor response to chemotherapy and short survival time. TPLL occurs both in adults as a sporadic disease and in younger AT patients. {ECO:0000269|PubMed:9288106, ECO:0000269|PubMed:9334731, ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9488043, ECO:0000269|PubMed:9573030}.; DISEASE: Note=Defects in ATM may contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL). {ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:10706620, ECO:0000269|PubMed:9288106}.; DISEASE: Note=Defects in ATM may contribute to B-cell chronic lymphocytic leukemia (BCLL). BCLL is the commonest form of leukemia in the elderly. It is characterized by the accumulation of mature CD5+ B-lymphocytes, lymphadenopathy, immunodeficiency and bone marrow failure. {ECO:0000269|PubMed:10023947, ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:9892178}.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15064416, PubMed:15448695, PubMed:15456891, PubMed:15790808, PubMed:15916964, PubMed:17923702, PubMed:21757780, PubMed:24534091, PubMed:27941124, PubMed:35076389, PubMed:9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15448695, PubMed:15456891, PubMed:15916964, PubMed:17923702, PubMed:24534091, PubMed:27941124, PubMed:9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, FBXO46, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4, UCHL3 and DCLRE1C (PubMed:10550055, PubMed:10766245, PubMed:10802669, PubMed:10839545, PubMed:10910365, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:21757780, PubMed:24534091, PubMed:26240375, PubMed:26774286, PubMed:27941124, PubMed:30171069, PubMed:30612738, PubMed:30886146, PubMed:30952868, PubMed:38128537, PubMed:9733515, PubMed:9843217). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (PubMed:19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed:15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed:15448695). Also involved in pexophagy by mediating phosphorylation of PEX5: translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed:26344566). {ECO:0000250|UniProtKB:Q62388, ECO:0000269|PubMed:10550055, ECO:0000269|PubMed:10766245, ECO:0000269|PubMed:10802669, ECO:0000269|PubMed:10839545, ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:11375976, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:19965871, ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26240375, ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:26774286, ECO:0000269|PubMed:27941124, ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:30171069, ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:30952868, ECO:0000269|PubMed:35076389, ECO:0000269|PubMed:38128537, ECO:0000269|PubMed:9733514, ECO:0000269|PubMed:9733515, ECO:0000269|PubMed:9843217}.
uniprot
proteins
mass_dalton
350687
uniprot
proteins
mutagenesis
MUTAGEN 367; /note="S->A: Loss of IR-induced S-367 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-1893 nor S-1981 autophosphorylation."; /evidence="ECO:0000269|PubMed:16858402"; MUTAGEN 1807; /note="K->E: Decreased phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 1893; /note="S->A: Loss of IR-induced S-1893 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1981 autophosphorylation."; /evidence="ECO:0000269|PubMed:16858402"; MUTAGEN 1941; /note="V->L: Decreased phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 1981; /note="S->A: Loss of IR-induced S-1981 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1893 autophosphorylation. No dimer disruption."; /evidence="ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:16858402"; MUTAGEN 1981; /note="S->D,E: Disrupts the dimer."; /evidence="ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:16858402"; MUTAGEN 2019; /note="Y->C: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2039; /note="E->K: Decreased phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2338; /note="L->P: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2394; /note="S->L: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2452; /note="L->P: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2685; /note="S->T: No effect on phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2699; /note="P->L: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2708; /note="D->N: Decreased phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2730; /note="Q->P: Loss of phosphorylation of target proteins."; /evidence="ECO:0000269|PubMed:19431188"; MUTAGEN 2870; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:9733515"; MUTAGEN 2875; /note="N->K: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:9733515"; MUTAGEN 3016; /note="K->Q: Mimics acetylation, preventing dephosphorylation and subsequent ATM deactivation during the late stage of DNA damage response."; /evidence="ECO:0000269|PubMed:30944854"; MUTAGEN 3016; /note="K->R: Loss of DNA damage-inducible acetylation. Retains constitutive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes S-1981 autophosphorylation."; /evidence="ECO:0000269|PubMed:17923702"; MUTAGEN 3018; /note="K->R: Retains DNA damage-inducible acetylation and S-1981 autophosphorylation."; /evidence="ECO:0000269|PubMed:17923702"; MUTAGEN 3047; /note="R->Q: Abolished interaction with PEX5 and translocation to peroxisomes in response to reactive oxygen species (ROS)."; /evidence="ECO:0000269|PubMed:26344566
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by NUAK1/ARK5 (PubMed:12409306). Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase (PubMed:12556884, PubMed:15790808, PubMed:16141325, PubMed:16858402, PubMed:21144835, PubMed:27664052). During the late stages of DNA damage response, dephosphorylated following deacetylation by SIRT7, leading to ATM deactivation (PubMed:30944854). {ECO:0000269|PubMed:12409306, ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:27664052, ECO:0000269|PubMed:30944854}.; PTM: Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1981 (PubMed:12556884, PubMed:16141325, PubMed:16858402, PubMed:17923702, PubMed:21144835). Acetylated in vitro by KAT5/TIP60 (PubMed:16141325). Deacetylated by SIRT7 during the late stages of DNA damage response, promoting ATM dephosphorylation and subsequent deactivation (PubMed:30944854). {ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:30944854}.
uniprot
proteins
protein_family
ATM subfamily
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
10023947
uniprot
proteins
pubmed
10217116
uniprot
proteins
pubmed
10234507
uniprot
proteins
pubmed
10397742
uniprot
proteins
pubmed
10425038
uniprot
proteins
pubmed
10500142
uniprot
proteins
pubmed
10534763
uniprot
proteins
pubmed
10550055
uniprot
proteins
pubmed
10706620
uniprot
proteins
pubmed
10766245
uniprot
proteins
pubmed
10783165
uniprot
proteins
pubmed
10802669
uniprot
proteins
pubmed
10817650
uniprot
proteins
pubmed
10839545
uniprot
proteins
pubmed
10873394
uniprot
proteins
pubmed
10910365
uniprot
proteins
pubmed
10973490
uniprot
proteins
pubmed
11375976
uniprot
proteins
pubmed
11418864
uniprot
proteins
pubmed
11897822
uniprot
proteins
pubmed
12086603
uniprot
proteins
pubmed
12409306
uniprot
proteins
pubmed
12556884
uniprot
proteins
pubmed
14871926
uniprot
proteins
pubmed
15064416
uniprot
proteins
pubmed
15448695
uniprot
proteins
pubmed
15456891
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15680327
uniprot
proteins
pubmed
15790808
uniprot
proteins
pubmed
15916964
uniprot
proteins
pubmed
15923642
uniprot
proteins
pubmed
16086026
uniprot
proteins
pubmed
16141325
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16858402
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17525732
uniprot
proteins
pubmed
17923702
uniprot
proteins
pubmed
18283122
uniprot
proteins
pubmed
18384426
uniprot
proteins
pubmed
18449195
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18710941
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19431188
uniprot
proteins
pubmed
19965871
uniprot
proteins
pubmed
20427287
uniprot
proteins
pubmed
20801936
uniprot
proteins
pubmed
20810650
uniprot
proteins
pubmed
21144835
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21757780
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22977523
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24534091
uniprot
proteins
pubmed
26240375
uniprot
proteins
pubmed
26344566
uniprot
proteins
pubmed
26774286
uniprot
proteins
pubmed
27664052
uniprot
proteins
pubmed
27941124
uniprot
proteins
pubmed
28202063
uniprot
proteins
pubmed
28508083
uniprot
proteins
pubmed
28726808
uniprot
proteins
pubmed
29203878
uniprot
proteins
pubmed
30171069
uniprot
proteins
pubmed
30612738
uniprot
proteins
pubmed
30886146
uniprot
proteins
pubmed
30944854
uniprot
proteins
pubmed
30952868
uniprot
proteins
pubmed
35076389
uniprot
proteins
pubmed
38128537
uniprot
proteins
pubmed
7792600
uniprot
proteins
pubmed
8521392
uniprot
proteins
pubmed
8589678
uniprot
proteins
pubmed
8665503
uniprot
proteins
pubmed
8698354
uniprot
proteins
pubmed
8755918
uniprot
proteins
pubmed
8789452
uniprot
proteins
pubmed
8797579
uniprot
proteins
pubmed
8808599
uniprot
proteins
pubmed
8845835
uniprot
proteins
pubmed
8969240
uniprot
proteins
pubmed
8988033
uniprot
proteins
pubmed
9043869
uniprot
proteins
pubmed
9050866
uniprot
proteins
pubmed
9108147
uniprot
proteins
pubmed
9150358
uniprot
proteins
pubmed
9168117
uniprot
proteins
pubmed
9199932
uniprot
proteins
pubmed
9288106
uniprot
proteins
pubmed
9334731
uniprot
proteins
pubmed
9443866
uniprot
proteins
pubmed
9450874
uniprot
proteins
pubmed
9463314
uniprot
proteins
pubmed
9488043
uniprot
proteins
pubmed
9497252
uniprot
proteins
pubmed
9521587
uniprot
proteins
pubmed
9573030
uniprot
proteins
pubmed
9707615
uniprot
proteins
pubmed
9711876
uniprot
proteins
pubmed
9733514
uniprot
proteins
pubmed
9733515
uniprot
proteins
pubmed
9766667
uniprot
proteins
pubmed
9792409
uniprot
proteins
pubmed
9792410
uniprot
proteins
pubmed
9843217
uniprot
proteins
pubmed
9872980
uniprot
proteins
pubmed
9887333
uniprot
proteins
pubmed
9892178
uniprot
proteins
sequence_length
3056
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9050866, ECO:0000269|PubMed:9150358}. Cytoplasmic vesicle {ECO:0000269|PubMed:9050866, ECO:0000269|PubMed:9150358}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q62388}. Peroxisome matrix {ECO:0000269|PubMed:26344566}. Note=Primarily nuclear (PubMed:9050866, PubMed:9150358). Found also in endocytic vesicles in association with beta-adaptin (PubMed:9707615). Translocated to peroxisomes in response to reactive oxygen species (ROS) by PEX5 (PubMed:26344566). {ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:9050866, ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9707615}.
uniprot
proteins