RNF213
entrez
57674
canonical
uniprot
Q63HN8
canonical
ensembl
ENSG00000173821
resolver
ensp
ENSP00000324392
resolver
ensp
ENSP00000425956
resolver
ensp
ENSP00000464087
resolver
enst
ENST00000508628
resolver
enst
ENST00000582970
resolver
genesymbol
RNF213
resolver
genesymbol_syn
ALO17
resolver
genesymbol_syn
C17orf27
resolver
genesymbol_syn
KIAA1554
resolver
genesymbol_syn
KIAA1618
resolver
genesymbol_syn
MYSTR
resolver
hgnc
HGNC:14539
resolver
uniprot
A0A0A0MTC1
resolver
uniprot
A0A0A0MTR7
resolver
uniprot
C9JCP4
resolver
uniprot
D6RI12
resolver
uniprot
F8WKS1
resolver
uniprot
Q658P6
resolver
uniprot
Q69YK7
resolver
uniprot
Q6MZR1
resolver
uniprot
Q8IWF4
resolver
uniprot
Q8IZX1
resolver
uniprot
Q8IZX2
resolver
uniprot
Q8N406
resolver
uniprot
Q8TEU0
resolver
uniprot
Q9H6C9
resolver
uniprot
Q9H6H9
resolver
uniprot
Q9H6P3
resolver
uniprot
Q9H8A9
resolver
uniprot
Q9HCF4
resolver
uniprot
Q9HCL8
resolver
uniprot_entry
A0A0A0MTC1_HUMAN
resolver
uniprot_entry
A0A0A0MTR7_HUMAN
resolver
uniprot_entry
RN213_HUMAN
resolver
uniprot_sec
C9JCP4
resolver
uniprot_sec
D6RI12
resolver
uniprot_sec
F8WKS1
resolver
uniprot_sec
Q658P6
resolver
uniprot_sec
Q69YK7
resolver
uniprot_sec
Q6MZR1
resolver
uniprot_sec
Q8IWF4
resolver
uniprot_sec
Q8IZX1
resolver
uniprot_sec
Q8IZX2
resolver
uniprot_sec
Q8N406
resolver
uniprot_sec
Q8TEU0
resolver
uniprot_sec
Q9H6C9
resolver
uniprot_sec
Q9H6H9
resolver
uniprot_sec
Q9H6P3
resolver
uniprot_sec
Q9H8A9
resolver
uniprot_sec
Q9HCF4
resolver
uniprot_sec
Q9HCL8
resolver
amino_acid_sequence
MECPSCQHVSKEETPKFCSQCGERLPPAAPIADSENNNSTMASASEGEMECGQELKEEGGPCLFPGSDSWQENPEEPCSKASWTVQESKKKKRKKKKKGNKSASSELASLPLSPASPCHLTLLSNPWPQDTALPHSQAQQSGPTGQPSQPPGTATTPLEGDGLSAPTEVGDSPLQAQALGEAGVATGSEAQSSPQFQDHTEGEDQDASIPSGGRGLSQEGTGPPTSAGEGHSRTEDAAQELLLPESKGGSSEPGTELQTTEQQAGASASMAVDAVAEPANAVKGAGKEMKEKTQRMKQPPATTPPFKTHCQEAETKTKDEMAAAEEKVGKNEQGEPEDLKKPEGKNRSAAAVKNEKEQKNQEADVQEVKASTLSPGGGVTVFFHAIISLHFPFNPDLHKVFIRGGEEFGESKWDSNICELHYTRDLGHDRVLVEGIVCISKKHLDKYIPYKYVIYNGESFEYEFIYKHQQKKGEYVNRCLFIKSSLLGSGDWHQYYDIVYMKPHGRLQKVMNHITDGPRKDLVKGKQIAAALMLDSTFSILQTWDTINLNSFFTQFEQFCFVLQQPMIYEGQAQLWTDLQYREKEVKRYLWQHLKKHVVPLPDGKSTDFLPVDCPVRSKLKTGLIVLFVVEKIELLLEGSLDWLCHLLTSDASSPDEFHRDLSHILGIPQSWRLYLVNLCQRCMDTRTYTWLGALPVLHCCMELAPRHKDAWRQPEDTWAALEGLSFSPFREQMLDTSSLLQFMREKQHLLSIDEPLFRSWFSLLPLSHLVMYMENFIEHLGRFPAHILDCLSGIYYRLPGLEQVLNTQDVQDVQNVQNILEMLLRLLDTYRDKIPEEALSPSYLTVCLKLHEAICSSTKLLKFYELPALSAEIVCRMIRLLSLVDSAGQRDETGNNSVQTVFQGTLAATKRWLREVFTKNMLTSSGASFTYVKEIEVWRRLVEIQFPAEHGWKESLLGDMEWRLTKEEPLSQITAYCNSCWDTKGLEDSVAKTFEKCIIEAVSSACQSQTSILQGFSYSDLRKFGIVLSAVITKSWPRTADNFNDILKHLLTLADVKHVFRLCGTDEKILANVTEDAKRLIAVADSVLTKVVGDLLSGTILVGQLELIIKHKNQFLDIWQLREKSLSPQDEQCAVEEALDWRREELLLLKKEKRCVDSLLKMCGNVKHLIQVDFGVLAVRHSQDLSSKRLNDTVTVRLSTSSNSQRATHYHLSSQVQEMAGKIDLLRDSHIFQLFWREAAEPLSEPKEDQEAAELLSEPEEESERHILELEEVYDYLYQPSYRKFIKLHQDLKSGEVTLAEIDVIFKDFVNKYTDLDSELKIMCTVDHQDQRDWIKDRVEQIKEYHHLHQAVHAAKVILQVKESLGLNGDFSVLNTLLNFTDNFDDFRRETLDQINQELIQAKKLLQDISEARCKGLQALSLRKEFICWVREALGGINELKVFVDLASISAGENDIDVDRVACFHDAVQGYASLLFKLDPSVDFSAFMKHLKKLWKALDKDQYLPRKLCDSARNLEWLKTVNESHGSVERSSLTLATAINQRGIYVIQAPKGGQKISPDTVLHLILPESPGSHEESREYSLEEVKELLNKLMLMSGKKDRNNTEVERFSEVFCSVQRLSQAFIDLHSAGNMLFRTWIAMAYCSPKQGVSLQMDFGLDLVTELKEGGDVTELLAALCRQMEHFLDSWKRFVTQKRMEHFYLNFYTAEQLVYLSTELRKQPPSDAALTMLSFIKSNCTLRDVLRASVGCGSEAARYRMRRVMEELPLMLLSEFSLVDKLRIIMEQSMRCLPAFLPDCLDLETLGHCLAHLAGMGGSPVERCLPRGLQVGQPNLVVCGHSEVLPAALAVYMQTPSQPLPTYDEVLLCTPATTFEEVALLLRRCLTLGSLGHKVYSLLFADQLSYEVARQAEELFHNLCTQQHREDYQLVMVCDGDWEHCYLPSAFSQHKVFVTPQAPLEAIQAYLAGHYRVPKQTLSAAAVFNDRLCVGIVASERAGVGKSLYVKRLHDKMKMQLNVKNVPLKTIRLIDPQVDESRVLGALLPFLDAQYQKVPVLFHLDVTSSVQTGIWVFLFKLLILQYLMDINGKMWLRNPCHLYIVEILERRTSVPSRSSSALRTRVPQFSFLDIFPKVTCRPPKEVIDMELSALRSDTEPGMDLWEFCSETFQRPYQYLRRFNQNQDLDTFQYQEGSVEGTPEECLQHFLFHCGVINPSWSELRNFARFLNYQLRDCEASLFCNPSFIGDTLRGFKKFVVTFMIFMARDFATPSLHTSDQSPGKHMVTMDGVREEDLAPFSLRKRWESEPHPYVFFNDDHTTMTFIGFHLQPNINGSVDAISHLTGKVIKRDVMTRDLYQGLLLQRVPFNVDFDKLPRHKKLERLCLTLGIPQATDPDKTYELTTDNMLKILAIEMRFRCGIPVIIMGETGCGKTRLIKFLSDLRRGGTNADTIKLVKVHGGTTADMIYSRVREAENVAFANKDQHQLDTILFFDEANTTEAISCIKEVLCDHMVDGQPLAEDSGLHIIAACNPYRKHSEEMICRLESAGLGYRVSMEETADRLGSIPLRQLVYRVHALPPSLIPLVWDFGQLSDVAEKLYIQQIVQRLVESISLDENGTRVITEVLCASQGFMRKTEDECSFVSLRDVERCVKVFRWFHEHSAMLLAQLNAFLSKSSVSKNHTERDPVLWSLMLAIGVCYHASLEKKDSYRKAIARFFPKPYDDSRLLLDEITRAQDLFLDGVPLRKTIAKNLALKENVFMMVVCIELKIPLFLVGKPGSSKSLAKTIVADAMQGPAAYSDLFRSLKQVHLVSFQCSPHSTPQGIISTFRQCARFQQGKDLQQYVSVVVLDEVGLAEDSPKMPLKTLHPLLEDGCIEDDPAPHKKVGFVGISNWALDPAKMNRGIFVSRGSPNETELIESAKGICSSDILVQDRVQGYFASFAKAYETVCKRQDKEFFGLRDYYSLIKMVFAAAKASNRKPSPQDIAQAVLRNFSGKDDIQALDIFLANLPEAKCSEEVSPMQLIKQNIFGPSQKVPGGEQEDAESRYLLVLTKNYVALQILQQTFFEGDQQPEIIFGSGFPKDQEYTQLCRNINRVKICMETGKMVLLLNLQNLYESLYDALNQYYVHLGGQKYVDLGLGTHRVKCRVHPNFRLIVIEEKDVVYKHFPIPLINRLEKHYLDINTVLEKWQKSIVEELCAWVEKFINVKAHHFQKRHKYSPSDVFIGYHSDACASVVLQVIERQGPRALTEELHQKVSEEAKSILLNCATPDAVVRLSAYSLGGFAAEWLSQEYFHRQRHNSFADFLQAHLHTADLERHAIFTEITTFSRLLTSHDCEILESEVTGRAPKPTLLWLQQFDTEYSFLKEVRNCLTNTAKCKILIFQTDFEDGIRSAQLIASAKYSVINEINKIRENEDRIFVYFITKLSRVGRGTAYVGFHGGLWQSVHIDDLRRSTLMVSDVTRLQHVTISQLFAPGDLPELGLEHRAEDGHEEAMETEASTSGEVAEVAEEAMETESSEKVGKETSELGGSDVSILDTTRLLRSCVQSAVGMLRDQNESCTRNMRRVVLLLGLLNEDDACHASFLRVSKMRLSVFLKKQEESQFHPLEWLAREACNQDALQEAGTFRHTLWKRVQGAVTPLLASMISFIDRDGNLELLTRPDTPPWARDLWMFIFSDTMLLNIPLVMNNERHKGEMAYIVVQNHMNLSENASNNVPFSWKIKDYLEELWVQAQYITDAEGLPKKFVDIFQQTPLGRFLAQLHGEPQQELLQCYLKDFILLTMRVSTEEELKFLQMALWSCTRKLKAASEAPEEEVSLPWVHLAYQRFRSRLQNFSRILTIYPQVLHSLMEARWNHELAGCEMTLDAFAAMACTEMLTRNTLKPSPQAWLQLVKNLSMPLELICSDEHMQGSGSLAQAVIREVRAQWSRIFSTALFVEHVLLGTESRVPELQGLVTEHVFLLDKCLRENSDVKTHGPFEAVMRTLCECKETASKTLSRFGIQPCSICLGDAKDPVCLPCDHVHCLRCLRAWFASEQMICPYCLTALPDEFSPAVSQAHREAIEKHARFRQMCNSFFVDLVSTICFKDNAPPEKEVIESLLSLLFVQKGRLRDAAQRHCEHTKSLSPFNDVVDKTPVIRSVILKLLLKYSFHDVKDYIQEYLTLLKKKAFITEDKTELYMLFINCLEDSILEKTSAYSRNDELNHLEEEGRFLKAYSPASRGREPANEASVEYLQEVARIRLCLDRAADFLSEPEGGPEMAKEKQCYLQQVKQFCIRVENDWHRVYLVRKLSSQRGMEFVQGLSKPGRPHQWVFPKDVVKQQGLRQDHPGQMDRYLVYGDEYKALRDAVAKAVLECKPLGIKTALKACKTPQSQQSAYFLLTLFREVAILYRSHNASLHPTPEQCEAVSKFIGECKILSPPDISRFATSLVDNSVPLLRAGPSDSNLDGTVTEMAIHAAAVLLCGQNELLEPLKNLAFSPATMAHAFLPTMPEDLLAQARRWKGLERVHWYTCPNGHPCSVGECGRPMEQSICIDCHAPIGGIDHKPRDGFHLVKDKADRTQTGHVLGNPQRRDVVTCDRGLPPVVFLLIRLLTHLALLLGASQSSQALINIIKPPVRDPKGFLQQHILKDLEQLAKMLGHSADETIGVVHLVLRRLLQEQHQLSSRRLLNFDTELSTKEMRNNWEKEIAAVISPELEHLDKTLPTMNNLISQDKRISSNPVAKIIYGDPVTFLPHLPRKSVVHCSKIWSCRKRITVEYLQHIVEQKNGKERVPILWHFLQKEAELRLVKFLPEILALQRDLVKQFQNVQQVEYSSIRGFLSKHSSDGLRQLLHNRITVFLSTWNKLRRSLETNGEINLPKDYCSTDLDLDTEFEILLPRRRGLGLCATALVSYLIRLHNEIVYAVEKLSKENNSYSVDAAEVTELHVISYEVERDLTPLILSNCQYQVEEGRETVQEFDLEKIQRQIVSRFLQGKPRLSLKGIPTLVYRHDWNYEHLFMDIKNKMAQDSLPSSVISAISGQLQSYSDACEVLSVVEVTLGFLSTAGGDPNMQLNVYTQDILQMGDQTIHVLKALNRCQLKHTIALWQFLSAHKSEQLLRLHKEPFGEISSRYKADLSPENAKLLSTFLNQTGLDAFLLELHEMIILKLKNPQTQTEERFRPQWSLRDTLVSYMQTKESEILPEMASQFPEEILLASCVSVWKTAAVLKWNREMR
uniprot
proteins
disease_involvement
DISEASE: Moyamoya disease 2 (MYMY2) [MIM:607151]: A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. {ECO:0000269|PubMed:21048783, ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:22377813, ECO:0000269|PubMed:22688072, ECO:0000269|PubMed:22931863, ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:23994138, ECO:0000269|PubMed:25278557, ECO:0000269|PubMed:25956231, ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26198278, ECO:0000269|PubMed:27736983, ECO:0000269|PubMed:27787485, ECO:0000269|PubMed:28635953, ECO:0000269|PubMed:29387438, ECO:0000269|PubMed:31645973, ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33568546, ECO:0000269|PubMed:34012115}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving RNF213 is associated with anaplastic large-cell lymphoma (ALCL). Translocation t(2;17)(p23;q25) with ALK. {ECO:0000269|PubMed:12112524}.
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115, PubMed:39375464). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (PubMed:34012115). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (PubMed:34012115). Also functions as an intracellular sensor for ISGylated proteins: upon type I interferon stimulation, undergoes ISGylation and oligomerizes on lipid droplets to form a binding platform for ISG15-modified substrate proteins, thereby acting as a broad-spectrum antimicrobial effector. Restricts intracellular bacterial pathogens, such as Listeria monocytogenes, in an ISG15-dependent manner by decorating the bacterial surface with ubiquitin to promote autophagic clearance (PubMed:34599178). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (PubMed:26766444). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:34012115). {ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26278786, ECO:0000269|PubMed:26766444, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:30846318, ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:34599178, ECO:0000269|PubMed:39375464}.
uniprot
proteins
mass_dalton
591407
uniprot
proteins
mutagenesis
MUTAGEN 2426; /note="K->A: Impaired ATP-binding leading to decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant A1A2; abolished ATP-binding and localization to lipid droplets; when associated with A-2775. Loss of coat formation on pathogens."; /evidence="ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:39375464"; MUTAGEN 2488; /note="E->A: Decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant B1B2; abolished ATPase activity and localization to lipid droplets; when associated with A-2845. Loss of coat formation on pathogens."; /evidence="ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:39375464"; MUTAGEN 2488; /note="E->Q: Loss of ATPase hydrolysis."; /evidence="ECO:0000269|PubMed:26126547"; MUTAGEN 2775; /note="K->A: Impaired ATP-binding leading to decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant A1A2; abolished ATP-binding and localization to lipid droplets; when associated with A-2426. Loss of coat formation on pathogens."; /evidence="ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:39375464"; MUTAGEN 2845; /note="E->A: Decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant B1B2; abolished ATPase activity and localization to lipid droplets; when associated with A-2488. Loss of coat formation on pathogens."; /evidence="ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:39375464"; MUTAGEN 4013; /note="D->R: Loss of interaction with S.Flexneri Ipah.4."; /evidence="ECO:0000269|PubMed:40164614"; MUTAGEN 4029; /note="Q->R: Loss of interaction with S.Flexneri Ipah.4."; /evidence="ECO:0000269|PubMed:40164614"; MUTAGEN 4036; /note="L->E: Abolsihes interaction with bacterial IpaH1.4."; /evidence="ECO:0000269|PubMed:40205224"; MUTAGEN 4036; /note="L->R: Loss of interaction with S.Flexneri Ipah.4 and disrupts ubiquitination."; /evidence="ECO:0000269|PubMed:40164614"; MUTAGEN 4509; /note="H->A: Abolished ability to ubiquitinate lipopolysaccharide. Loss of coat formation on pathogens. No effect on ubiquitination by S.Flexneri Ipah1.4 and Ipah2.5."; /evidence="ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:39375464, ECO:0000269|PubMed:40205224"; MUTAGEN 4516; /note="C->A: No effect on ubiquitination by S.Flexneri Ipah1.4."; /evidence="ECO:0000269|PubMed:40164614"; MUTAGEN 4516; /note="C->S: Loss of coat formation on pathogens."; /evidence="ECO:0000269|PubMed:39375464
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849, ECO:0000305|PubMed:21799892}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated. {ECO:0000269|PubMed:21799892}.; PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates oligomerization on lipid droplets. {ECO:0000269|PubMed:34599178}.; PTM: (Microbial infection) Ubiquitinated by S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its degradation by the proteasome, thereby preventing formation of the bacterial ubiquitin coat and activation of innate immunity. {ECO:0000269|PubMed:40164614, ECO:0000269|PubMed:40205224}.
uniprot
proteins
protein_family
AAA ATPase family
uniprot
proteins
pubmed
10997877
uniprot
proteins
pubmed
12112524
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20454556
uniprot
proteins
pubmed
21048783
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21799892
uniprot
proteins
pubmed
22377813
uniprot
proteins
pubmed
22688072
uniprot
proteins
pubmed
22931863
uniprot
proteins
pubmed
23110205
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23994138
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24658080
uniprot
proteins
pubmed
25043520
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25278557
uniprot
proteins
pubmed
25956231
uniprot
proteins
pubmed
26070522
uniprot
proteins
pubmed
26126547
uniprot
proteins
pubmed
26198278
uniprot
proteins
pubmed
26278786
uniprot
proteins
pubmed
26766444
uniprot
proteins
pubmed
27736983
uniprot
proteins
pubmed
27787485
uniprot
proteins
pubmed
28635953
uniprot
proteins
pubmed
29387438
uniprot
proteins
pubmed
30705059
uniprot
proteins
pubmed
30846318
uniprot
proteins
pubmed
31645973
uniprot
proteins
pubmed
32139119
uniprot
proteins
pubmed
33568546
uniprot
proteins
pubmed
33842849
uniprot
proteins
pubmed
34012115
uniprot
proteins
pubmed
34599178
uniprot
proteins
pubmed
39375464
uniprot
proteins
pubmed
40164614
uniprot
proteins
pubmed
40205224
uniprot
proteins
sequence_length
5207
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115}. Lipid droplet {ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34599178}.
uniprot
proteins