wanglab/gogpt-training-data huggingface dataset:
Protein: Myricetin 7/4'-O-methyltransferase 2 (ShMOMT2) (3',4',5'-trimethyl myricetin 7-O-methyltransferase) (EC 2.1.1.-) (3',5'-dimethyl myricetin 7-O-methyltransferase) (7-O-methyl syringetin synthase) (Syringetin 7-O-methyltransferase) (EC 2.1.1.-) (3'-methyl quercetin 4'-O-methyltransferase) (4'-O-methyl isorhamnetin synthase) (Isorhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (3-methyl quercetin 7-O-methyltransferase) (EC 2.1.1.82) (4'-methyl kaempferol 7-O-methyltransferase) (7-O-methyl kaempferide synthase) (Kaempferide 7-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 4'-O-methyltransferase) (Rhamnacene synthase) (Rhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (Kaempferol 4'-O-methyltransferase) (Kaempferide synthase) (EC 2.1.1.155) (Myricetin 7-O-methyltransferase) (EC 2.1.1.-) (Quercetin 7-O-methyltransferase) (Rhamnetin synthase) (EC 2.1.1.-) (F2YTN5)
Organism: Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum)
Function: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including myricetin, quercetin and kaempferol. Mediates the formation of 4'-methyl derivatives from kaempferol, 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin) and 3'-methyl myricetin, producing 4'-methyl kaempferol (kaempferide), 3',4'-dimethyl quercetin (4'-O-methyl isorhamnetin), 7,4'-dimethyl quercetin (4'-O-methyl rhamnetin, rhamnacene) and 3',4'-dimethyl myricetin, respectively. Triggers the 7-O-methylation of quercetin, myricetin, 4'-methyl kaempferol (kaempferide), 3-methyl quercetin, 3',5'-dimethyl myricetin (syringetin) and 3',4',5'-trimethyl myricetin, thus leading to production of 7-methyl quercetin (rhamnetin), 7-methyl myricetin, 7,4'-dimethyl kaempferol (7-O-methyl kaempferide), 3,7-dimethyl quercetin, 7,3',5'-trimethyl myricetin (7-O-methyl syringetin) and 7,3',4',5'-tetramethyl myricetin, respectively.
Interaction partners:
Sequence:
MASNNNCAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP
Protein: Tissue alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucosidase I) (Alpha-L-fucoside fucohydrolase 1) (Alpha-L-fucosidase 1) (Q2KIM0)
Organism: Bos taurus (Bovine)
Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P04066}.
Interaction partners:
- Alpha-L-fucosidase
- Beta-galactosidase
- Alpha-N-acetylgalactosaminidase
- Alpha-galactosidase
Sequence:
MRSWVVGARLLLLLQLVLVLGAVRLPPCTDPRHCTDPPRYTPDWPSLDSRPLPAWFDEAKFGVFVHWGVFSVPAWGSEWFWWHWQGEKLPQYESFMKENYPPDFSYADFGPRFTARFFNPDSWADLFKAAGAKYVVLTTKHHEGYTNWPSPVSWNWNSKDVGPHRDLVGELGTAIRKRNIRYGLYHSLLEWFHPLYLRDKKNGFKTQYFVNAKTMPELYDLVNRYKPDLIWSDGEWECPDTYWNSTDFLAWLYNDSPVKDEVVVNDRWGQNCSCHHGGYYNCKDKFQPETLPDHKWEMCTSIDQRSWGYRRDMEMADITNESTIISELVQTVSLGGNYLLNVGPTKDGLIVPIFQERLLAVGKWLSINGEAIYASKPWRVQSEKNSVWYTSKGLAVYAILLHWPEYGILSLISPIATSTTKVTMLGIQKDLKWSLNPSGKGLLVFLPQLPPAALPTEFAWTIKLTGVK
Protein: Putative UDP-galactose transporter (Q4QAU5)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSCGRWQEYARGGTDVLVCCAGVRRGLLCLPLSRPSPPPRRGEPLTHHFACLPPHNTKHMHIRRQASEGSPKATRVKRHPRMRADATGASPLCPRKRRVSPAPTHTLFSSSTPLSPSTVPACSDESLKKHFVCRSSRSGTSHYHHCSVDMGSFSSPMWVRRYVLNFNAAALVLLAVQNAGYLVLISYSQQQGKEYQLPAGGAEAEEEEGRTVTFKASHFLAATELVKLFLSFLWCVVDEARAMQQERCSAGAVATPTAALPVEDSGRCSIAPFAETPKSVAGASCHLSHNLDDAADNMDAEYFDHAVPLRFLFSRKRFAAVFLSRMRHALGLDHKYKEALLMIVPAIVYAIQGLLLIYSLKLLDPTVFQVLYQVRILFLAVMMRVVLDFRLSPIRWGALVALMFGITLAQMGAQSTRADMTTSKADDAARSEMEIAAATEKTSSTWSMEGTLAALAGGFLSAFSGVFMEFVVKKRGNQFHLSARNIHLAFFSVVYFFIVFLCEVFQPEEGGGGLDEFASTFFDGFTRLVWFLVVLQAIGGILVALVVRYCDNIVKSFSTAFAIVLSGTASVFLLHTPLNGTFLLGSFLVMTSITMYTAKK
Protein: Uncharacterized protein (Q386F7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVPRLRVPDQNDEQSSAKHFPADDCPAKSSSVRTTAANGQSTAQSINVSARFLPYDDICGIGPTLHSSPTEENEMNWSHEHGANRFLSDRETHGTRRLCFTGGSSGGGTLSESQETTASEFVMELRDALKQTMAEGNSPTDLEVDGSAGPAIWMRLFERWPLELAASGYAEWWLRHPKCGEDASQLFQMFIDGIAREECRRNPLDGEKDGEELRDGVLQGALVMLQALYADPPQSLRAAFGTPLYHQQLFFRTCRLGALGDGRELALCLSLAAAIAQRIAGNKLAMRHDLSRFIGRVRRNWQALREKWSDEEKLVLEVGKVEALLAFALD
Protein: Protein phosphatase PTC7 homolog (EC 3.1.3.16) (T-cell activation protein phosphatase 2C) (TA-PP2C) (Q6NVE9)
Organism: Mus musculus (Mouse)
Function: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (By similarity). Dephosphorylates the ubiquinone biosynthesis protein COQ7 which is likely to lead to its activation (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8NI37}.
Interaction partners:
Sequence:
MFSVLSYGRLVARAVLGGLSQTDPRAGGGGGGGGGSSGDYGLVTAGCGFGKDFRKGLLKKGACYGDDACFVARHRSADVLGVADGVGGWRDYGVDPSQFSGTLMRTCERLVKEGRFVPSNPVGILTTSYCELLQNKVPLLGSSTACIVVLDRSSHRLHTANLGDSGFLVVRGGEVVHRSDEQQHYFNTPFQLSIAPPEAEGVVLSDSPDAADSTSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNSNYESIQRTARSIAEQAHELAYDPNYMSPFAQFACDNGLNVRGGKPDDITVLLSIVAEYTD
Protein: Ubiquitin-conjugating enzyme E2 A (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme A) (RAD6 homolog A) (HR6A) (hHR6A) (Ubiquitin carrier protein A) (Ubiquitin-protein ligase A) (P49459)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA.
Subcellular location: Late endosome {ECO:0000269|PubMed:25582440}. Lysosome {ECO:0000269|PubMed:25582440}.
Interaction partners:
- E3 ubiquitin-protein ligase RAD18
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 B
- Ubiquitin conjugating enzyme E2 V1
- E3 ubiquitin-protein ligase UBR1
- Ubiquitin-conjugating enzyme E2 variant 2
- E3 ubiquitin-protein ligase UBR2
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFTEEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWRDC
Protein: Acyl-CoA-binding domain-containing protein 4 (Acyl-CoA binding protein 4) (Q9MA55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with oleoyl-CoA, barely with palmitoyl-CoA, but not with arachidonyl-CoA. May function as an intracellular carrier of acyl-CoA esters. Plays a role in the biosynthesis of membrane lipids including galactolipids and phospholipids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18773301, ECO:0000269|PubMed:18836139}. Note=Also to the periphery of the nucleus.
Interaction partners:
- UPF0235 protein At5g63440
- Acyl-CoA-binding domain-containing protein 3
- Acyl-CoA-binding domain-containing protein 6
- Ethylene-responsive transcription factor RAP2-3
- AT3G13950 protein
- Ankyrin repeat-containing protein BDA1
- Ankyrin
- RING finger family protein
- Pentatricopeptide repeat-containing protein At5g25630
- Probable cysteine protease RD21B
Sequence:
MAMPRATSGPAYPERFYAAASYVGLDGSDSSAKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGWYSRASNDIPDPVVDVQINRAKDEPVVENGSTFSETKTISTENGRLAETQDKDVVSEDSNTVSVYNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVETKVATESQETSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWSMLKTYGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEIDAVGVSPSPRSDHAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASVQGRVPLASEGLSLVVSSYNGEDVLVAFGGYNGRYNNEINLLKPSHKSTLQTKTLEAPLPGSLSAVNNATTRDIESEVEVSQEGRVREIVMDNVNPGSKVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASEQAAMNAKRQGSGGVWGWLAGSPQEKDDDSP
Protein: Lysophospholipase 1 (EC 3.1.1.5) (CaPLB1) (Phospholipase B 1) (Q9UWF6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the release of fatty acids from lysophospholipids (By similarity). Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase GDE1
- Lysophospholipid acyltransferase
- PNPLA domain-containing protein
Sequence:
MILHHLLILLIINYCVATSPTNGYAPGPVSCPSSQLIRSGSQGINPNEQSYINARYPIAKQALSKFLHNANLQNFDVDSFLAHSNPTIGLAFSGGGYRAMLTGAGEISSLDSRTKTNTPVLAGILQASSYIAGLSGGSWLVGSLASNNLNSVDDMLSQGLWELTHSFLSYYGIEHPIKQVEEWVNVGNQVASKRNANFNVSLTDIYGRLLSYPLLTNTEDEGDAYLWSDVTSASNFQSHQMPFPILISDGRAPDTTIINLNSTVIELTPYEFGSWDPSLNEFVDTRYLGTKLDNGRPTGKCYNGFDNAGFFMGTSSALFNEAVLSITEANIPSFLKDIIDDILVDPILKSNIDVSAYNPNPFFKSSGSNTAISQSKNLYLVDGGEDGQNIPISPLLHRNVSAIFAFDNSNDVLNWPDGTSLVKTYERQFSSQGNGIAFPYVPDQYTFRNLNLTSKPTFFGCDAKNLTSLTKDIYDVPLVIYLANRPFTYWSNTSTFKLTYDDNERQGMISNGFEIATRSSGSLDDEWAACVGCAIIRREQERQGIEQTEQCKRCFENYCWDGTIYKGEPLGENFSDDGLTNSATEYNSNNVAGFNDGGTSILKKA
Protein: Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2) (O57429)
Organism: Gallus gallus (Chicken)
Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Possesses both ubiquitin-specific peptidase and isopeptidase activities. May play a role in the regulation of the circadian clock.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}.
Interaction partners:
- Rhodanese domain-containing protein.
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase.
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MAARMAPTPRSSKVVQGLTGLRNLGNTCFMNSILQCLSNTKELRDYCLQNQYLRDLNNNSRMRTALMSEFAKLIQLLWTSSPNDSVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHGEVNRVLVRPRANADTLDHLPDDEKSRQMWRRYQEREDSRVSDLFVGQLKSSLTCSECGYCSTAFDPFWDLSLPIPKKGYGEVTLMDCLRLFTKEDVLDGDEKPTCCRCKARTRCTKKFSIQKFPKILVLHLKRFSEARIRASKLTTFVNFPLKDLDLREFASQSCNHAVYNLYAVSNHSGTTMGGHYTAYCKSPISSEWHSFNDSRVTPMSSSHVRSSDAYLLFYELASPSSRM
Protein: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5) (Q9LVC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein
- Protein ABC transporter 1, mitochondrial
- FAD/NAD
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- AT5g10730/MAJ23_90
- NAD
- Polyketide cyclase / dehydrase and lipid transport protein
Sequence:
MALRSVSRRLGSRILNQRSFVASLHSHATSFGFQEVKEEEKSKLVGNVFTNVASSYDIMNDVMSGGLHRLWKERLVGKLSPFAGMKHLDVAGGTGDVAFRIYDAVYSVKRRALQKVDEASLEETQIYVCDINPNMLNVGKQRAAERGLRDNKSLVWVEGDAEALSFDDNSMDGYTIAFGIRNVTHIEKALAEAYRVLKRGGRFLCLELSHVEIPVFKNLYDLYSFQVIPNLGELIAGDRESYQYLVESVRRFPPQERFASMIADAGFEKVEYENLVGGVVAIHSAIKL
Protein: Probable proteasome maturation factor ump1 (O74416)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Short-lived chaperone present in the precursor form of the 20S proteasome and absent in the mature complex. Required for the correct assembly and enzymatic activation of the proteasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit alpha type-3
- Probable proteasome subunit alpha type-4
- Probable proteasome subunit beta type-7
- Probable proteasome subunit alpha type-1
- Probable proteasome subunit alpha type-7
- Probable proteasome subunit alpha type-6
- Probable proteasome subunit beta type-6
- Probable proteasome subunit beta type-4
- Probable proteasome subunit beta type-5
- Probable proteasome subunit beta type-3
Sequence:
MKIVPDVEPAAEVSGNFKVSVLEPSIPAVHRVENKHPLESRLKNWEAQQQQIRLDSMRRIYGLHEPVRREMEQKLASQSSRPLALGGSANFHLDILANREAVLDETDIYAAPIPLEMTYQNEMAIRYGL
Protein: Rab32, isoform B (A1Z7S3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cyclin-G-associated kinase
- Vacuolar protein sorting-associated protein 35
- non-specific serine/threonine protein kinase
- Rab proteins geranylgeranyltransferase component A
- Rab GDP dissociation inhibitor
- Hermansky-Pudlak syndrome 4, isoform A
- GH27401p
- Geranylgeranyl transferase type-2 subunit alpha
Sequence:
MPNVDEQRGKAATKRAESEQSEEKGDRQEGDGDPKDESEEATAKIKGRSRFTAALRSLSKTKTKRERELDKSTDRETRSAEEEAQETPGELEDVASSISTDSGALGKTKKKSLTRRLLLGGLRKSGKTPKGRPHSLATSDDISVEHLETTPLPSPPGSPTSAGSSTLQITISGKKVEPSPAKKSGKSRPKSDTDYLTPAAEERKPRKKTTTTTVTTRDTSSSTRTTKLLVSKKKPQSPERESPSASPSPLITTTESTRDTPPRERAPAKPSRVQSASGTGAVRKSQSSSASSRKLELMQQQQQRGHRLNARPLAELANTEPQPSGQQSLDPSTSPPAAEDGVSSAESAQTIANPPPVVRFEVGSAVRSPLSAYEAALAAAASQQPNSNEELSDSSIRRLSFAQQQLILGDHDSIEGRRETLHYQSVASEYSNQDSGSEDDSEEQADTTEPENAKPMPAFGDLTMDQEMEPAIMTSTSDKREHLYKILVIGELGTGKTSFIKRYVHQFFSQNYRATIGVDFALKVLQWDANTIVRLQLWDIAGQERFGNMTRVYYKEAVGAFIVFDVTRSGTFDCVSKWKEDLDSKVQLPDGSPIPCILLANKCDQEKQGIITQPEKMDEYVRENGFAGWFETSAKENINIDEAARALVNKILINDKLISADLADGDKFNLSAADATGSDAKNKCSC
Protein: Interferon alpha-6 (IFN-alpha-6) (Interferon alpha-8) (IFN-alpha-8) (P07350)
Organism: Mus musculus (Mouse)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon alpha-11
- Interferon alpha-5
- Interferon alpha-1
- Interferon 1ai2
- Interferon regulatory factor 7
- Interferon regulatory factor 3
- Interferon gamma receptor 1
- Tyrosine-protein kinase JAK2
- Epidermal growth factor receptor
Sequence:
MARLCAFLMVLAVLSYWPTCSLGCDLPQTHNLRNKRALTLLVKMRRLSPLSCLKDRKDFGFPQEKVGAQQIQEAQAIPVLTELTQQILTLFTSKDSSAAWNATLLDSFCNDLHQLLNDLQGCLMQQVEIQALPLTQEDSLLAVRTYFHRITVFLREKKHSPCAWEVVRAEVWRALSSSAKLLARLNEDE
Protein: Fe2OG dioxygenase domain-containing protein (B1V8J4)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein disulfide-isomerase 2
- Hypoxia-inducible factor prolyl hydroxylase
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase
Sequence:
MYPIYIFFIYSTYIFNFLTPFTDETLEFNDKIWDKCGKELRGDSSRDGRLVCYRLHKHLLIRKVEILSSEPFILQYHNQVHRRLAKRAVQEAEALRLEQLKISGFTTTPEKSQVRAANGTWLIHTGRPSFARIFEGLQANINSLDLSTAEPWQILSYNADGYYAPHYDYLNPATNVQLVEGRGNRIATVLVILQIAKKGGTTVFPRLNLNIRPKAGDVIVWLNTLSTGESNSQTLHAACPIHEGTKIGATLWVHEKIFSQNTKSTGLSRQNSLARTGGKTIT
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (C9J453)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNS
Protein: mitochondrial processing peptidase (EC 3.4.24.64) (Beta-MPP) (Q5BFD3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 6, mitochondrial
- quinol--cytochrome-c reductase
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Complex III subunit 9
- Mitochondrial-processing peptidase subunit alpha
- Uncharacterized protein
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase 39 kDa subunit, putative
Sequence:
MASRRLAYNFNQALRSRAALKSIQPVKRGFASPVALPSTTQSTTLSNGFTIATEYSPWAQTSTVGVWIDAGSRAETDKTNGTAHFLEHLAFKGTSKRSQHQLELEIENMGAHLNAYTSRENTVYYAKSFNNDVPKAVDILADILQNSKLESAAIERERDVILREQEEVDKQLEEVVFDHLHATAYQHQPLGRTILGPKENIQTITRDNLTDYIKTNYTADRMVLVGAGGIPHEQLVKLAEQHFGSLPSKPPTSALAALTAEQKRQPEFIGSEIRIRDDTLPTAHIALAVEGVSWKDDDYFTALVAQAIVGNWDRAMGNSPYLGSKLSSFVERNNLANSFMSFSTSYSDTGLWGIYLVSENMTGLDDLIHFALREWSRLSFNVTAAEVERAKAQLKASILLSLDGTTAIAEDIGRQIITTGRRLSPEDIERTIGQITEKDVMDFANRKLWDQDIAMSAVGSIEGILDYNRIRSDMSRNAY
Protein: Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64) (P01106)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:38225354}. Nucleus {ECO:0000269|PubMed:22719065, ECO:0000269|PubMed:38225354}. Cytoplasm {ECO:0000269|PubMed:22719065}. Note=Localization to the nucleolus is dependent on HEATR1. {ECO:0000269|PubMed:38225354}.
Interaction partners:
- Histone acetyltransferase p300
- F-box/WD repeat-containing protein 7
- Transformation/transcription domain-associated protein
- Breast cancer type 1 susceptibility protein
- Myc box-dependent-interacting protein 1
- Zinc finger and BTB domain-containing protein 17
- Protein max
- Cyclin-dependent kinase inhibitor 2A
- Cellular tumor antigen p53
- Glycogen synthase kinase-3 beta
Sequence:
MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
Protein: Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Lafora PTPase) (LAFPTPase) (Q9WUA5)
Organism: Mus musculus (Mouse)
Function: Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro). Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95278}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95278}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95278}; Cytoplasmic side {ECO:0000250|UniProtKB:O95278}. Cell membrane {ECO:0000250|UniProtKB:O95278}. Note=Colocalizes with glycogen synthase in punctate structures in the cytoplasm. Primarily associated with polyribosomes at the rough endoplasmic reticulum, and also detected at the plasma membrane. Under glycogenolytic conditions localizes to the nucleus. {ECO:0000250|UniProtKB:O95278}.
Interaction partners:
- E3 ubiquitin-protein ligase NHLRC1
- Glycogen [starch] synthase, muscle
- Protein phosphatase 1 regulatory subunit 3C
- Glycogen debranching enzyme
- EPM2A-interacting protein 1
Sequence:
MLFRFGVVVPPAVAGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAAALALQEPGLWLAEVELEAYEEAGGAEPGRVDTFWYKFLQREPGGELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQLEHVTIKLKHELGVTAVMNFQTEWDIIQNSSGCNRYPEPMTPDTMMKLYKEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQQDFSQKFGKVHSSICAL