wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein C16G5.07c (O60121)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Prohibitin-1
- Prohibitin-2
Sequence:
MLKLFLSTPRTLPNSRFLLLRRLQPLGLRYRSDASSLHLFTPTWRDHATNTIIKFVPQQVAYVVERMGRFSRILTPGVAFLAPIIDKIAYIHSLKERALEIPTQSAITLDNVSLGLDGVLYIQVYDPYKASYGVEDADYAISQLAQTTMRSEIGRLTLDHVLRERQSLNIHITDAINKAAESWGIRCLRHEIRDIRPPESVVMAMHQQVSAERQKRAEILESEGKRQAAINVAEGDKQAEILDSEGQKIKTINSALAEAQAIREKASATASGIAVLADSIKKQEHGLEAVSLYIAQQYITNFGKLAKASNSMIVPASTSDVSGMVAQALSIFKQVSKTTAPDKSTPKELHTDEK
Protein: Probable D-lactate dehydrogenase, mitochondrial (DLD) (Lactate dehydrogenase D) (EC 1.1.2.4) (F1QXM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in D-lactate, but not L-lactate catabolic process.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q7TNG8}.
Interaction partners:
- L-lactate dehydrogenase B-B chain
- L-lactate dehydrogenase A chain
- Hydroxyacylglutathione hydrolase, mitochondrial
- Pyruvate kinase
- Pyruvate kinase
- Pyruvate kinase
- L-lactate dehydrogenase B-A chain
- Pyruvate dehydrogenase E1 component subunit beta
- Malic enzyme.
- Malic enzyme
Sequence:
MTLFRHLVRITSPRLPFICGSSRRFSAKTAAVERVVSSFRSVTGDEGVSVGSAVREQHGRDESVHRCRPPDVVVFPRSVEEVSALAKICHHYRLPIIPFGTGTGLEGGVGALQGGVCFSLRKMEQVVDLHQEDFDVTVEPGVTRKSLNSYLRDTGLWFPVDPGADASLCGMAATSASGTNAVRYGTMRENVLNLEVVLADGTILHTAGKGRRPRKTAAGYNLTNLFVGSEGTLGIITKATLRLYGVPESMVSAVCSFPSVQSAVDSTVQILQAGVPIARIEFLDDVMINACNRFNNLSYAVTPTLFLEFHGSSKSMEEQVSVTEEITRDNGGSDFAWAEDEETRSRLWKARHDAWYAAMALRPGCKAYSTDVCVPISRLPQIIVETKADLISNNITGPIAGHVGDGNFHCLIVLDPNDTDEVQRVHSFTERLARRALAMDGTCTGEHGIGLGKRALLREEVGPLAIEVMKGLKASLDPRNLMNPGKVLELTQTNTEQ
Protein: Myb domain protein 110 (F4J1R5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein N-terminal asparagine amidohydrolase
- Transcription factor MYBC1
Sequence:
MKMDFSCFQEYPFEFHCRGTTFNGFRENNAVSETVEEFCNKRRMQKKSDDLKTKKKKKQSVSRVCSRGHWRISEDTQLMELVSVYGPQNWNHIAESMQGRTGKSCRLRWFNQLDPRINKRAFSDEEEERLLAAHRAFGNKWAMIAKLFNGRTDNALKNHWHVLMARKMRQQSSSYVQRFNGSAHESNTDHKIFNLSPGNVDDDEDVNLKKCSWEMLKEGTTNLKAQYLQEEYSSSRMPMQGPHHHYSTFPADSLALTLHVSIQEPSSSSSLSLPSSSTTGEHTMVTRYFETIKPPAFIDFLGVGH
Protein: cytochrome-c oxidase (EC 7.1.1.9) (Q9I3G0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Cbb3-type cytochrome c oxidase subunit
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Cbb3-type cytochrome c oxidase subunit
- Probable ferredoxin
- Oxygen-independent coproporphyrinogen III oxidase
- Cytochrome c oxidase, cbb3-type, CcoQ subunit
- Outer membrane protein OprG
- alcohol dehydrogenase
- Probable iron-sulfur protein
Sequence:
MSTTNPESAYNYKVVRQFAIMTVVWGIVGMTVGVLIAAQLVWPDLNFGLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYAVQRTCQVRLFSDTLASFTFWGWQLVILLAAISLPLGYTSSKEYAELEWPIDILITVVWVAYAVVFFGTLVKRKVKHIYVGNWFFGGFILTVAMLHVVNNLELPVTFTKSYSLYAGATDAMVQWWYGHNAVGFFLTAGFLGMMYYFVPKQAERPVYSYRLSIVHFWALIAVYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRSDPILRFLVVSLAFYGMSTFEGPMMAIKTVNALSHYTDWTIGHVHAGALGWVAMVSIGSLYHLIPKVFGREKMYSLGLINAHFWLATIGTVLYIASMWVNGITQGLMWRAVNEDGTLTYSFVEALAAGHPGFIVRMLGGFIFLLGMFLMAYNTWRTVSAAKPAEYEAAAQIA
Protein: Methionine synthase (MS) (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Cobalamin-dependent methionine synthase) (Vitamin-B12 dependent methionine synthase) (Q9Z2Q4)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate (By similarity). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99707}.
Interaction partners:
- Methylenetetrahydrofolate reductase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methionine synthase reductase
- Serine hydroxymethyltransferase
- Cystathionine gamma-lyase
- Cystathionine beta-synthase
- Adenosylhomocysteinase
- Serine hydroxymethyltransferase
- S-adenosylmethionine synthase isoform type-1
- S-adenosylmethionine synthase isoform type-2
Sequence:
MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEENFQGQEFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGSLGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQKLFEENYASPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIAEAVKNCKPRVPPDSVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAFRGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTHGKGGKKVIQTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARLNREKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREEARVLNGSVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDDYFEEILEEYEDIRQDHYESLKERKYLPLSQARKHSFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKAVGEEARKVYEDAQNMLSILISRKKLRARGVVGFWPAQSVQDDIHLYAEGAVPQAAEPIATFYGLRQQAEKDSSSTDPYHCLSDFVAPLHSGVRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQATGIRLTESLAMAPASAVSGLYFSNVKSKYFAVGKISKDQIEDYALRKNMSVAEVEKWLGPILGYDTD
Protein: F-box/kelch-repeat protein At1g26930 (Q84M94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFEGRPRDSCLVSTLFTMPSHKETKWSFLVSGKRSFLNNDESDLHFKKMYKLTTDSSEGEDNGSSSDSGTLIPGMNRDDSLSCLIRCSRADYCSIASVNRSLRSLIRSGEIYRLRRLQGTLEHWVYFSCHLNEWEAFDPRSKRWMHLPSMPQNECFRYADKESLAVGTDLLVFGWEVSSYVIYRYSLLTNSWSTAKSMNMPRCLFGSASYGEIAVLAGGCDSSGRILDTAELYNYEDQTWLVLPGMNKRRKMCSGVFMDGKFYVIGGIGVGEENEPKVLTCGEEFDLKTRKWTEIPEMSPPRSNQGNGMSAAAMAPPLVAVVNDQLYAADHAGMAVRRYDKEKRVWNKVGNLPEQAGSMNGWGLAFRACGDRIIVIGGPKAPGEGFIELNSWVPSVTTPEWHLLGKKQSVNFVYNCAVMSC
Protein: 3-isopropylmalate dehydratase small subunit (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) (P30126)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Interaction partners:
- 3-isopropylmalate dehydrogenase
- 3-isopropylmalate dehydratase large subunit
- 2-isopropylmalate synthase
- Ketol-acid reductoisomerase
- Dihydroxy-acid dehydratase
- Acetolactate synthase isozyme 1 large subunit
- Acetolactate synthase isozyme 3 small subunit
- Threonine synthase
- Pyruvate dehydrogenase
- Acetolactate synthase isozyme 3 large subunit
Sequence:
MAEKFIKHTGLVVPLDAANVDTDAIIPKQFLQKVTRTGFGAHLFNDWRFLDEKGQQPNPDFVLNFPQYQGASILLARENFGCGSSREHAPWALTDYGFKVVIAPSFADIFYGNSFNNQLLPVKLSDAEVDELFALVKANPGIHFDVDLEAQEVKAGEKTYRFTIDAFRRHCMMNGLDSIGLTLQHDDAIAAYEAKQPAFMN
Protein: GID complex subunit 9 (EC 2.3.2.27) (Glucose-induced degradation protein 9) (Probable E3 ubiquitin-protein ligase Gid9) (Q9URU9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GID complex subunit 8
- GID complex subunit 1
- E3 ubiquitin-protein ligase gid2
- GID complex substrate-recognition subunit 4
- GID complex subunit 7
- GID complex substrate-recognition subunit 10
- SPRY domain-containing protein C285.10c
- Bax inhibitor 1
- Uncharacterized glutaminase C222.08c
- Probable NADH-ubiquinone oxidoreductase C947.15c, mitochondrial
Sequence:
MNFRPEQQYILEKPGILLSFEQLRINFKHILRHLEHESHVINSTLTTLISQENASMDEKIEKIDSLLSRVSTVKKKMKHLHDCEALFIKQTKSRLLFMNRLQGIRDMESADFLDWSRVRLNRLVADYMMANGYHGAAALLCKDSQLENLVDLGIYKRYQLIHDSILQQELKEVLSWCSEHRAILKKNNSTLELEVRLQRFIELIKSKKLCQAIAFAKAHFGTWANEHPARLQLAAALLAFPEFTNGSPYSLLLSDDRWEYLASLFTSNFTAVHNIPSVPLLHALLAAGLSSLKTPLCYLDANDDNPLALQSQTVKQCPVCTPCLNDLGKALPYAHITQSAIVDSLTGEGLDSDNCPVAFPNGRVYGIQSLISWNEANGTREGFLRDPYSGKEFPFQLLRKVYVV
Protein: L-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.2) (C9JVN9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVPALRYLVGACGRARGLFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRQVAVRGPSWLWQQPMKVSDNNIYCFLWRCFALLLTGSACSFK
Protein: Autophagy-related protein 41 (Interacting with cytoskeleton protein 2) (Q12048)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in both selective and non-selective autophagy. Does not appear to play a role in determining the size of autophagosomes, but rather influences their formation rate. With ATG9, plays a role in the delivery of donor membrane to expanding phagophore.
Subcellular location: Preautophagosomal structure membrane {ECO:0000305|PubMed:26565778}; Peripheral membrane protein {ECO:0000305|PubMed:26565778}. Note=Shows a peri-mitochondrial distribution similar to ATG9 (PubMed:26565778). {ECO:0000269|PubMed:26565778}.
Interaction partners:
- Sporulation protein 24
- Autophagy-related protein 9
Sequence:
MSSVESSPISRYEDEVFPLSFSNVAFEPPMLSHSPDRSTYADDFSQSYQQELLTFPLSYPIVDESECTHTKDKTDSNIITSTEDDCMFDMEFNGNAASAVAAASKESNSASGFAFASNDAFANVAQQNYRLWLSSV
Protein: Radial spoke head 1 homolog (Cancer/testis antigen 79) (CT79) (Male meiotic metaphase chromosome-associated acidic protein) (Meichroacidin) (Testis-specific gene A2 protein) (Q8WYR4)
Organism: Homo sapiens (Human)
Function: May play an important role in male meiosis (By similarity). It is necessary for proper building of the axonemal central pair and radial spokes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8VIG3}. Chromosome {ECO:0000250|UniProtKB:Q8VIG3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:23993197}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q8VIG3}. Note=Cytoplasmic in late spermatocytes, secondary spermatocytes and round spermatids. Gathered around metaphase chromosomes during meiotic divisions. {ECO:0000250|UniProtKB:Q8VIG3}.
Interaction partners:
- Radial spoke head protein 4 homolog A
- Radial spoke head protein 9 homolog
- Radial spoke head protein 6 homolog A
- Zinc finger MYND domain-containing protein 10
- Radial spoke head protein 3 homolog
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal assembly factor 19
- Coiled-coil domain-containing protein 40
- Coiled-coil domain-containing protein 39
- Dynein regulatory complex protein 1
Sequence:
MSDLGSEELEEEGENDIGEYEGGRNEAGERHGRGRARLPNGDTYEGSYEFGKRHGQGIYKFKNGARYIGEYVRNKKHGQGTFIYPDGSRYEGEWANDLRHGHGVYYYINNDTYTGEWFAHQRHGQGTYLYAETGSKYVGTWVNGQQEGTAELIHLNHRYQGKFLNKNPVGPGKYVFDVGCEQHGEYRLTDMERGEEEEEEELVTVVPKWKATQITELALWTPTLPKKPTSTDGPGQDAPGAESAGEPGEEAQALLEGFEGEMDMRPGDEDADVLREESREYDQEEFRYDMDEGNINSEEEETRQSDLQD
Protein: Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic (AtG6PD5) (G6PDH5) (EC 1.1.1.49) (Q9LK23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21309870}.
Interaction partners:
- Glucose-6-phosphate isomerase 1, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Probable 6-phosphogluconolactonase 4
- Probable 6-phosphogluconolactonase 1
- 6-phosphogluconolactonase 3, chloroplastic
- Probable 6-phosphogluconolactonase 2
- Probable 6-phosphogluconolactonase 5
Sequence:
MGSGQWHMEKRSTLKNDSFVKEYNPVTETGSLSIIVLGASGDLAKKKTFPALFNLFHQGFLNPDEVHIFGYARSKITDEELRDKIRGYLVDEKNASKKTEALSKFLKLIKYVSGPYDSEEGFKRLDKAILEHEISKKTAEGSSRRLFYLALPPSVYPPVSKMIKAWCTNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGALFEEPQIYRIDHYLGKELVQNMLVLRFANRLFLPLWNRDNIANVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVIPIKDEEVVLGQYEGYRDDPTVPNDSNTPTFATTILRINNERWEGVPFILKAGKAMSSKKADIRIQFKDVPGDIFKCQNQGRNEFVIRLQPSEAMYMKLTVKQPGLEMQTVQSELDLSYKQRYQDVSIPEAYERLILDTIRGDQQHFVRRDELKAAWEIFTPLLHRIDKGEVKSVPYKQGSRGPAEADQLLKKAGYMQTHGYIWIPPTL
Protein: Podocan (Q7Z5L7)
Organism: Homo sapiens (Human)
Function: Negatively regulates cell proliferation and cell migration.
Subcellular location: [Isoform 1]: Secreted, extracellular space, extracellular matrix.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MAQSRVLLLLLLLPPQLHLGPVLAVRAPGFGRSGGHSLSPEENEFAEEEPVLVLSPEEPGPGPAAVSCPRDCACSQEGVVDCGGIDLREFPGDLPEHTNHLSLQNNQLEKIYPEELSRLHRLETLNLQNNRLTSRGLPEKAFEHLTNLNYLYLANNKLTLAPRFLPNALISVDFAANYLTKIYGLTFGQKPNLRSVYLHNNKLADAGLPDNMFNGSSNVEVLILSSNFLRHVPKHLPPALYKLHLKNNKLEKIPPGAFSELSSLRELYLQNNYLTDEGLDNETFWKLSSLEYLDLSSNNLSRVPAGLPRSLVLLHLEKNAIRSVDANVLTPIRSLEYLLLHSNQLREQGIHPLAFQGLKRLHTVHLYNNALERVPSGLPRRVRTLMILHNQITGIGREDFATTYFLEELNLSYNRITSPQVHRDAFRKLRLLRSLDLSGNRLHTLPPGLPRNVHVLKVKRNELAALARGALVGMAQLRELYLTSNRLRSRALGPRAWVDLAHLQLLDIAGNQLTEIPEGLPESLEYLYLQNNKISAVPANAFDSTPNLKGIFLRFNKLAVGSVVDSAFRRLKHLQVLDIEGNLEFGDISKDRGRLGKEKEEEEEEEEEEEETR
Protein: Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28) (Q96RU2)
Organism: Homo sapiens (Human)
Function: Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}.
Interaction partners:
- TP53-binding protein 1
- Polyubiquitin-C
- Myc proto-oncogene protein
- F-box/WD repeat-containing protein 7
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Claspin
- Serine/threonine-protein kinase Chk2
- Ubiquitin carboxyl-terminal hydrolase 8
Sequence:
MTAELQQDDAAGAADGHGSSCQMLLNQLREITGIQDPSFLHEALKASNGDITQAVSLLTDERVKEPSQDTVATEPSEVEGSAANKEVLAKVIDLTHDNKDDLQAAIALSLLESPKIQADGRDLNRMHEATSAETKRSKRKRCEVWGENPNPNDWRRVDGWPVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNVLENCRSHTEKRNIMFMQELQYLFALMMGSNRKFVDPSAALDLLKGAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIYMDRYMYRSKELIRNKRECIRKLKEEIKILQQKLERYVKYGSGPARFPLPDMLKYVIEFASTKPASESCPPESDTHMTLPLSSVHCSVSDQTSKESTSTESSSQDVESTFSSPEDSLPKSKPLTSSRSSMEMPSQPAPRTVTDEEINFVKTCLQRWRSEIEQDIQDLKTCIASTTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYINDKLPYFNAEAAPTESDQMSEVEALSVELKHYIQEDNWRFEQEVEEWEEEQSCKIPQMESSTNSSSQDYSTSQEPSVASSHGVRCLSSEHAVIVKEQTAQAIANTARAYEKSGVEAALSEVMLSPAMQGVILAIAKARQTFDRDGSEAGLIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGPDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK
Protein: Conserved hypothetical integral membrane protein (O25606)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Probable nicotinate-nucleotide adenylyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]
- 5'-nucleotidase SurE
- DNA replication/recombination mediator RecO N-terminal domain-containing protein
Sequence:
MKFKFLNMDNESGFILIEKELKRLNILAQVKEDCIELKGENTEQARIYLKTLFNSNIVELDDHQKSANALIERLKSLDLKIAVAESCSGGLLSHAFTSISGASAVFMGGIVCYNEEVKRELLKVNATTLKVFGVYSEECVKEMLLGVFLNFKVDLALAMSGVAGPNGGNKANPVGTIYIGAQKLGSQALIDRCFFEGNRESIQNKSVEHALNMLARML
Protein: tRNA (carboxymethyluridine(34)-5-O)-methyltransferase (EC 2.1.1.229) (tRNA (uracil-5-)-methyltransferase TRM9) (tRNA [Um34] methyltransferase) (tRNA methylase 9) (P49957)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
- Cytoplasmic tRNA 2-thiolation protein 1
- tRNA
- Cytoplasmic tRNA 2-thiolation protein 2
- Elongator complex protein 1
- Elongator complex protein 6
- Elongator complex protein 3
- Adenylyltransferase and sulfurtransferase UBA4
- Ubiquitin-related modifier 1
- Protein KTI13
Sequence:
MEINQAAEKEQEYVHKVYNEIAPHFSQTRYKPWPIVTQFLKTRPMGSIGIDVGCGNGKYLGVNPDIYIIGSDRSDGLIECARGINPSYNLLVADGLNLPHKNETFDFAISIAVVHHWSTRERRVEVIRHVLSKLRQGGQALIYCWALEQGSSRRGYHEGMEQDVFVPWVLPKSKSKPKTKSTPPAKVKTRPKPNLMNIPPKERSEYLQRWKEEQQRSKSLDDNDEKQQQDQEQEREEVKYRYYHLYREGELAEDCRQAGAAVHSEGFERDNWWVVAQKR
Protein: TRUD domain-containing protein (Q381B8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLQACGVEKFHVPVERVAVARLKDCPEDFIVAEVDPAGEATDAQTYKLPIPRTPTNSCGEVGSVQTVLSTATELNRGQCGGSAGDSEKHINVALPMDDSLNESLLETLLEVFGSKREAVAQYSSCAAARNLLFPTKEHDIGVFNERAEREQLHRAMKVSVPHLRSETRRHREATAGPVNIALDGDSAHICRDGDGGAIDYHIIVSYDCEFLLLSHLLGESVADALVAWNASVPQGPPLHLTAKFPVTASKEVRRSFHEVMSKRYPRITCRVSNGQVVIRGSSSGFGKRQRVDGNRETVGFTHLLIRKRNLDIMELRMLLAEHFCVPIDAVCTAGMKDKCAVTYQRCSVPCTRQLRHPREEESGIDGDVPLRLTWTDDLSSYVEILQTSGPHSAPVGIGELKGNMFHIRLRDVRGITPSELMQRSCRLEKEGFLNYFGQQRFSEHAECFMDHIGVHILGGRWPEAVRCLLRGAPELYDLFPTHMEPRYVPARLRDARCIVQALNRLHRTRYTTLTRADVTECTQLWRDVCRDALQAVPYAFRVLWLCGAQSLIFNRLLSMLHGPQLPVTLPLLGYNVSVEGGVRSAVDKVLMELNLGTVDEFAQRKKVLGVGMPGALRATVVRPVGCSVSFTTVEGGSSDVFDATLSFFLPSSSYATIFLREVLGCDTWW
Protein: Quick-to-court, isoform E (Q59E00)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMTSLQLETSLPAVEEQVQREKDNDSAEDSHTASTTPTRIPHPAVARFRRSASLRLRGNPAELGLRAEHCPAGGGGFSSRAKLTAIPSSLETRSHPVHLRRNRSWCNLGHKTEQEPEVEASTEALCNAAQCLSLDKEALAPKVGNSSMANGKPRNLSLQLNGGSDISSSGTSSSSSNNKESSPRTTRTPRTPQTPQTPQTPASGVAASVAETPHSCIRQGNCVKANQVKLSTLHESKISPRTPPVTPDSPSTYLDDDIDSMYSFATTTSGRSTMSCEHPYVARNGTTFSGRKMKYVVHCSNYAGQVGPDYLTPTQRAQRQIRRLKELLCIARQDLEQKDTELLRLTREVVELRLFKASLSSPEERSASSDAVTVREAELKTSQDVSPIVDMVDEGNAKGSPRHLSRQQQQQANHSLQAMQMSAEMQSSYADSGHFEDLTMSSVHSKDSQTQSEACGTATPDGEADVGCGAGGDSASNLENYELQRQELISMYEHRIEELIRSQDSATSDLKRSHNDKVEALLQKLAECNTRYSDMVPDYEQAKQRIRELEKQLEDLQRKLIEHEEKQNKMYLHMYQQGQEAERISRADQALDLAQRQPESKVSINELLHQLQSTQDELENIRTIYRRLLEAQKNRTHVDPEVTLQFLKSAIFYFLTDKENSQGHLQAIESILEFTDAEKQKISAANRTPK
Protein: Casein kinase I isoform 2 (EC 2.7.11.1) (B9VVJ6)
Organism: Trypanosoma brucei brucei
Function: Serine/threonine protein kinase. May phosphorylate ZC3H11 during unstressed conditions, leading to proteasome-dependent degradation of ZC3H11.
Interaction partners:
Sequence:
MSVELRVGNRFRIGQKIGSGSFGEIFRGTNIQTGDPVAIKLEQVKTRHPQLAFEARFYRVLNAGGGVVGIPNVLYHGVEGEFNVMVIDLLGPSLEDLFSFCGRRLSLKTTLMLAEQMIARIEFVHSKSIIHRDIKPDNFLMGTGKKGHHVYIIDFGLAKKYRDARTHQHIPYKEGKSLTGTARYCSINTHIGIEQSRRDDLEGIGYILMYFLRGSLPWQGLKAHTKQEKYARISDRKQTTSVETLCRSFPAEFAAYLNYTRSLHFEDKPDYSYLKRLFRELFVREGYHVDYVFDWTLKRIHDTLQEGRADQQQQQQQQQQRRGSEKEDEHPV