wanglab/gogpt-training-data huggingface dataset:
Protein: Mediator of RNA polymerase II transcription subunit 15 (Autonomous replication regulatory protein 3) (Basal expression activator protein 1) (Defective silencing suppressor protein 4) (Mediator complex subunit 15) (Transcription regulatory protein GAL11) (Ty insertion suppressor protein 13) (P19659)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. It has an important role in the negative regulation of Ty transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16630888}.
Interaction partners:
- General control transcription factor GCN4
- Mediator of RNA polymerase II transcription subunit 2
- Mediator of RNA polymerase II transcription subunit 3
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 8
Sequence:
MSAAPVQDKDTLSNAERAKNVNGLLQVLMDINTLNGGSSDTADKIRIHAKNFEAALFAKSSSKKEYMDSMNEKVAVMRNTYNTRKNAVTAAAANNNIKPVEQHHINNLKNSGNSANNMNVNMNLNPQMFLNQQAQARQQVAQQLRNQQQQQQQQQQQQRRQLTPQQQQLVNQMKVAPIPKQLLQRIPNIPPNINTWQQVTALAQQKLLTPQDMEAAKEVYKIHQQLLFKARLQQQQAQAQAQANNNNNGLPQNGNINNNINIPQQQQMQPPNSSANNNPLQQQSSQNTVPNVLNQINQIFSPEEQRSLLQEAIETCKNFEKTQLGSTMTEPVKQSFIRKYINQKALRKIQALRDVKNNNNANNNGSNLQRAQNVPMNIIQQQQQQNTNNNDTIATSATPNAAAFSQQQNASSKLYQMQQQQQAQAQAQAQAQAQAQAQAQAQAAQAAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAHAQHQPSQQPQQAQQQPNPLHGLTPTAKDVEVIKQLSLDASKTNLRLTDVTNSLSNEEKEKIKMKLKQGQKLFVQVSNFAPQVYIITKNENFLKEVFQLRIFVKEILEKCAEGIFVVKLDTVDRLIIKYQKYWESMRIQILRRQAILRQQQQMANNNGNPGTTSTGNNNNIATQQNMQQSLQQMQHLQQLKMQQQQQQQQQQQQQQQQQQQQQQQHIYPSSTPGVANYSAMANAPGNNIPYMNHKNTSSMDFLNSMENTPKVPVSAAATPSLNKTINGKVNGRTKSNTIPVTSIPSTNKKLSISNAASQQPTPRSASNTAKSTPNTNPSPLKTQTKNGTPNPNNMKTVQSPMGAQPSYNSAIIENAFRKEELLLKDLEIRKLEISSRFKHRQEIFKDSPMDLFMSTLGDCLGIKDEEMLTSCTIPKAVVDHINGSGKRKPTKAAQRARDQDSIDISIKDNKLVMKSKFNKSNRSYSIALSNVAAIFKGIGGNFKDLSTLVHSSSPSTSSNMDVGNPRKRKASVLEISPQDSIASVLSPDSNIMSDSKKIKVDSPDDPFMTKSGATTSEKQEVTNEAPFLTSGTSSEQFNVWDWNNWTSAT
Protein: C-C motif chemokine (F6R5P4)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361150}.
Interaction partners:
- C-C motif chemokine 5
- C-C chemokine receptor type 8
- C-C chemokine receptor type 10
- C-C motif chemokine ligand 26
- Atypical chemokine receptor 2
- C-C motif chemokine 25
- C-C chemokine receptor type 4
- C-C motif chemokine 22
- C-C chemokine receptor type 5
- C-X-C motif chemokine 14
Sequence:
MKTFTSAFGTMRSLQMLLLAALLLGTFLQHARAARATNVGRECCLDYFKGAIPIRKLVSWYKTSVECSRDAIVFLTVQGKLICADPKDKHVKKAIRLVKNPRP
Protein: ASXL transcriptional regulator 2 (A0A5F9ZHN2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLNGSALNNEFFTSAAQGWKERLSEGEFTPEMQVRIRQEIEKEKKVEPWKEQFFESYYGQSSGLSLEDSKKLTASPSDPKVKKTPAEQPKSMPVSEASLIRIVPVVSQSECKEEALQMSSPGRKEECESQGEVQPNFSTSSEPLLSSALNTHELSSILPIKCPKDEDLLEQKPVTSAEQESEKNHLTTASNYNKSESQESLVTSPSKPKSPGVEKPIVKPTAGAGPQETNMKEPLATLVDQSPESLKRKSSLTQEEAPVSWEKRPRVTENRQHQQPFQVSPQPFLNRGDRIQVRKVPPLKIPVSRISPMPFHPSQVSPRARFPVSITSPNRTGARTLADIKAKAQLVKAQRAAAAAAAAAAAAASVGGTIPGPGPGGGQGPGEGGEGQTARGGSPGSDRVSETGKGPTLELAGTGSRGGTRELLPCGPETQPQSETKTTPSQAQPHSVSGAQLQQTPPVPPTPAVS
Protein: rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase) (Nucleolar protein 1) (U6 snRNA 2'-O-methyltransferase fibrillarin) (P22509)
Organism: Rattus norvegicus (Rat)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (By similarity). Site specificity is provided by a guide RNA that base pairs with the substrate (By similarity). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity). Probably catalyzes 2'-O-methylation of U6 snRNAs in box C/D RNP complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:2414294}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P35550}. Note=Fibrillar region of the nucleolus.
Interaction partners:
- Nucleolar protein 58
- Nucleolar protein 56
- NHP2-like protein 1
- H/ACA ribonucleoprotein complex subunit DKC1
- Nucleolar and coiled-body phosphoprotein 1
- U3 small nucleolar RNA-interacting protein 2
- H/ACA ribonucleoprotein complex subunit 1
- Nucleolar protein 6
- 18S rRNA
- Periodic tryptophan protein 2 homolog
Sequence:
MKPGFSPRGGGFGGRGGFGDRGGRGGGRGGRGGFGGGRGGFGGGGRGRGGGGGGFRGRGGGGGRGGGFQSGGGRGRGGGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKAKN
Protein: Monothiol glutaredoxin-3 (Q03835)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable).
Interaction partners:
- BolA-like protein 2
- Iron-regulated transcriptional activator AFT1
- Fe-S cluster assembly protein DRE2
- Iron-regulated transcriptional activator AFT2
- BolA-like protein 1
- BolA-like protein 3
- Putative Xaa-Pro aminopeptidase FRA1
- Glutaredoxin-2
- NADPH-dependent diflavin oxidoreductase 1
- Iron-sulfur clusters transporter ATM1, mitochondrial
Sequence:
MPVIEINDQEQFTYLTTTAAGDKLIVLYFHTSWAEPCKALKQVFEAISNEPSNSNVSFLSIDADENSEISELFEISAVPYFIIIHKGTILKELSGADPKEYVSLLEDCKNSVNSGSSQTHTMENANVNEGSHNDEDDDDEEEEEETEEQINARLTKLVNAAPVMLFMKGSPSEPKCGFSRQLVGILREHQVRFGFFDILRDESVRQNLKKFSEWPTFPQLYINGEFQGGLDIIKESLEEDPDFLQHALQS
Protein: Gamma-glutamyl cyclotransferase gliK (GGCT gliK) (EC 4.3.2.9) (Gliotoxin biosynthesis protein K) (E9R9Y3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Gamma-glutamyl cyclotransferase-like protein; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Thioredoxin reductase gliT
- Glutathione S-transferase gliG
Sequence:
MGKAALQDPHGGIWYFAYGSNLRLSVLENRGIKALDIKAVIVPSHYLTFDIFGIPYAEPSFASVAPFAREKKTTLRLGDSPASRDVPPVQGLAYLLNPRDYRQLVISEGGGVAYDEVEVHASILDKDGKPDPGATLIARTLQAKYPWRPNGAPSARYLGLISTGCKQNEPLTAYSDYIDSLPAYEPPTSLHAKVGGLLFLMFWRPPLRLLIRLIRVNTDQDGHCPQWLGWIILTLYGLMWSYHDNIHSKIWGRGDGRKLHFEETPAKEVPVRH
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (Q2LIP0)
Organism: Oryza australiensis
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
RVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRNASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPTDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFSCGNGNAKYEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: 14-3-3 protein beta/alpha (Prepronerve growth factor RNH-1) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] (P35213)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}.
Interaction partners:
- M-phase inducer phosphatase 2
- 14-3-3 protein zeta/delta
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase A-Raf
- 14-3-3 protein theta
- RAF proto-oncogene serine/threonine-protein kinase
- Bcl2-associated agonist of cell death
- 14-3-3 protein epsilon
- M-phase inducer phosphatase
- Transcriptional coactivator YAP1
Sequence:
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICSDVLELLDKYLILNATHAESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4JCV6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGGAGPPPALFQQQAPPQLTRYTPATATTAATFVPPQQQQVVYNPQQQQHSSLRRSSRGKTGSCVSSAAAAQQQQHHQQQQHSSAAAAVQQQLLPPPGTYQYQQVGGNTVVVAVRHQQQLQQQQQQQQQLALHHQHQQQQHQQQQQQHQQQQHQQQQRATLVQPGFLFSYRSNQPQQQQQPAQQIHQGPKVTHSSAASDALTYSLMAQQPPSGPPHAGGQQITPGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: Phospholipid-transporting ATPase DRS2 (EC 7.6.2.1) (P39524)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10601336, ECO:0000269|PubMed:12372257, ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15249668, ECO:0000269|PubMed:16956384, ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:19898464}; Multi-pass membrane protein {ECO:0000269|PubMed:12372257, ECO:0000269|PubMed:14562095}. Endosome membrane {ECO:0000269|PubMed:16452632}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit CDC50
- Phospholipid-transporting ATPase accessory subunit LEM3
- Phospholipid-transporting ATPase DNF1
- ARF guanine-nucleotide exchange factor 2
- Phospholipid-transporting ATPase NEO1
- Oxysterol-binding protein homolog 4
- Recyclin-1
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- Kexin
- ADP-ribosylation factor 1
Sequence:
MNDDRETPPKRKPGEDDTLFDIDFLDDTTSHSGSRSKVTNSHANANYIPPSHVLPEETIDLDADDDNIENDVHENLFMSNNHDDQTSWNANRFDSDAYQPQSLRAVKPPGLFARFGNGLKNAFTFKRKKGPESFEMNHYNAVTNNELDDNYLDSRNKFNIKILFNRYILRKNVGDAEGNGEPRVIHINDSLANSSFGYSDNHISTTKYNFATFLPKFLFQEFSKYANLFFLCTSAIQQVPHVSPTNRYTTIGTLLVVLIVSAMKECIEDIKRANSDKELNNSTAEIFSEAHDDFVEKRWIDIRVGDIIRVKSEEPIPADTIILSSSEPEGLCYIETANLDGETNLKIKQSRVETAKFIDVKTLKNMNGKVVSEQPNSSLYTYEGTMTLNDRQIPLSPDQMILRGATLRNTAWIFGLVIFTGHETKLLRNATATPIKRTAVEKIINRQIIALFTVLIVLILISSIGNVIMSTADAKHLSYLYLEGTNKAGLFFKDFLTFWILFSNLVPISLFVTVELIKYYQAFMIGSDLDLYYEKTDTPTVVRTSSLVEELGQIEYIFSDKTGTLTRNIMEFKSCSIAGHCYIDKIPEDKTATVEDGIEVGYRKFDDLKKKLNDPSDEDSPIINDFLTLLATCHTVIPEFQSDGSIKYQAASPDEGALVQGGADLGYKFIIRKPNSVTVLLEETGEEKEYQLLNICEFNSTRKRMSAIFRFPDGSIKLFCKGADTVILERLDDEANQYVEATMRHLEDYASEGLRTLCLAMRDISEGEYEEWNSIYNEAATTLDNRAEKLDEAANLIEKNLILIGATAIEDKLQDGVPETIHTLQEAGIKIWVLTGDRQETAINIGMSCRLLSEDMNLLIINEETRDDTERNLLEKINALNEHQLSTHDMNTLALVIDGKSLGFALEPELEDYLLTVAKLCKAVICCRVSPLQKALVVKMVKRKSSSLLLAIGDGANDVSMIQAAHVGVGISGMEGMQAARSADIAVGQFKFLKKLLLVHGSWSYQRISVAILYSFYKNTALYMTQFWYVFANAFSGQSIMESWTMSFYNLFFTVWPPFVIGVFDQFVSSRLLERYPQLYKLGQKGQFFSVYIFWGWIINGFFHSAIVFIGTILIYRYGFALNMHGELADHWSWGVTVYTTSVIIVLGKAALVTNQWTKFTLIAIPGSLLFWLIFFPIYASIFPHANISREYYGVVKHTYGSGVFWLTLIVLPIFALVRDFLWKYYKRMYEPETYHVIQEMQKYNISDSRPHVQQFQNAIRKVRQVQRMKKQRGFAFSQAEEGGQEKIVRMYDTTQKRGKYGELQDASANPFNDNNGLGSNDFESAEPFIENPFADGNQNSNRFSSSRDDISFDI
Protein: Lambda-crystallin homolog (EC 1.1.1.45) (L-gulonate 3-dehydrogenase) (Gul3DH) (Q99KP3)
Organism: Mus musculus (Mouse)
Function: Has high L-gulonate 3-dehydrogenase activity. It also exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA) and L-threonate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P14755}.
Interaction partners:
- Aldo-keto reductase family 1 member A1
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- 3-ketoacyl-CoA thiolase A, peroxisomal
- 3-ketoacyl-CoA thiolase B, peroxisomal
- Acetyl-CoA acetyltransferase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Cocaine- and amphetamine-regulated transcript protein
- Acetyl-Coenzyme A acetyltransferase 3
- Alpha/beta-tubulin-N-acetyltransferase 9
Sequence:
MASPAAGGVVIVGSGLIGRSWAMLFASGGFKVKLYDIEQQQITDALENIRKEMKSLEQSGSLKGSLSAERQLSLISGCGNLAEAVEGAVHIQECVPENLELKKKIFAQLDRIVDDRVILSSSSSCLLPSKLFSGLAHVKQCIVAHPVNPPYYVPLVELVPHPETAPATMDRTYALMKKIGQSPVRVLKEIDGFVLNRLQYAVISEAWRLVEEEIVSPSDLDLVMSDGLGMRYAFIGPLETMHLNAEGVISYCERYSEGMKHVLSTFGPVPEFSGATVERVSEDMCMKVPDDPEHLAARRQWRDDCLMKLSILKYQMQPK
Protein: p44-15b outer membrane protein (Q2GIN4)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MRSRSKLFLGSVMMSLAIVMAGNDVRAHDDVSALDTGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDFVQFAKAVGVSHPSIDGKVCKTKADSSKKFPLYSDETHTKGASEGRTSLCGDNGSSTITNSGANVSETGQVFRDFIRATLKEDGSKNWPTSSGTGTPKPVTNDNAKAVAKDLVQELTPEEKTIVAGLLAKTIEGGEVIEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGIHYTNHL
Protein: Aldos-2-ulose dehydratase (AUDH) (EC 4.2.1.110) (Aldos-2-ulose dehydratase/isomerase) (D-arabino-hex-2-ulose dehydratase) (Pyranosone dehydratase) (P84193)
Organism: Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Function: A bifunctional enzyme which catalyzes the dehydration of anhydrofructose into ascopyrone M, and the isomerization of ascopyrone M into microthecin.
Interaction partners:
Sequence:
MYSKVFLKPHCEPEQPAALPLFQPQLVQGGRPDGYWVEAFPFRSDSSKCPNIIGYGLGTYDMKSDIQMLVNPYATTNNQSSSWTPVPLAKLDFPVAMHYADITKNGFNDVIITDQYGSSMDDIWAYGGRVSWLENPGELRDNWTMRTIGHSPGMHRLKAGHFTRTDRVQVVAVPIVVASSDLTTPADVIIFTAPDDPRSEQLWQRDVVGTRHLVHEVAIVPAAETDGEMRFDQIILAGRDGVDCLWYDGARWQRHLVGTGLPEERGDPYWGAGSAAVGRVGDDYAGYICSAEAFHGNTVSVYTKPAGSPTGIVRAEWTRHVLDVFGPLNGKHTGSIHQVVCADIDGDGEDEFLVAMMGADPPDFQRTGVWCYKLVDRTNMKFSKTKVSSVSAGRIATANFHSQGSEVDIATISYSVPGYFESPNPSINVFLSTGILAERLDEEVMLRVVRAGSTRFKTEMEFLDVAGKKLTLVVLPPFARLDVERNVSGVKVMAGTVCWADENGKHERVPATRPFGCESMIVSADYLESGEEGAILVLYKPSSTSGRPPFRSMDELVAHNLFPAYVPDSVRAMKFPWVRCADRPWAHGRFKDLDFFNLIGFHVNFADDSAAVLAHVQLWTAGIGVSAGFHNHVEASFCEIHACIANGTGRGGMRWATVPDANFNPDSPNLEDTELIVVPDMHEHGPLWRTRPDGHPLLRMNDTIDYPWHAWLAGAGNPSPQAFDVWVAFEFPGFETFSTPPPPRVLEPGRYAIRFGDPHQTASLALQKNDATDGTPVLALLDLDGGPSPQAWNISHVPGTDMYEIAHAKTGSLVCARWPPVKNQRVAGTHSPAAMGLTSRWAVTKNTKGQITFRLPEAPDHGPLFLSVSAIRHQQEADAIPVIVQGDSIELSAWSLVPAN
Protein: Class II major histocompatibility complex transactivator (A0A087X2I7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFIEHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVGPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLR
Protein: MutL homolog 3 (Q3V1X3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MIRCLSDDVKTKLRSGLAISSLGQCVEELTLNSIDAEVTCVAIRVNMETFQVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPAFYGFRGEALASIADMAGAVEISSKKNTTLKTFVKMFQNGKALATHEADLTRPSVGTTVTVYNLFYQFPVRRKSMDPRLEFEKVRQRVEALSLMHPSISFSLRNDVSGSMVLQLPKTKDICSRFCQIYGLGKSQKLREIRFKYKEFEFSGYISSEAHYNKNMQFLFVNRRLVLRTKLHKLIDFLLRKESIICRPKNGSASRQMNSSPRHRSASEPHGIYVINVQCPFCEYDVCIEPAKTLIEFQSWDTVLICIQEGVKRFLKQEKLFVELSGEDIKEFNEDNGFSLFGTTLQTHVSTHEKCDQSSFREACNKILDSYEMFNLQSKAVKRIATLENKTRQNPGDSETIRKKTVGSLYTDASDGPCYSKSVESVLQDSNNSAYLEPRVSEEEVAKTSHSGENEKWKKSFLENKTSGRIHETSPKMFSSPIQMHHLLEEREADLEMQTISSTVNVMAANIPQNNDIPSQLEKWKDAPEVGCQPLPFETTLLRVRGTQRKKERRKKEPSSRGRVNVFSYGQVKLCSTGFITHVVQSEHAKSTETEHSFKNYARPGPVSAQETFGKRTHHAIETPDSSDLTSTLSKESSQPPNKRFCRTNTGYGTENKPVATDDNLALFQESCKESHTDRLLPDASSFPWCRYVSDGCRKIDKRGSFKQVVRRKLSLRSQVGSLEKFKRQYGKVSSSLDTEKDNNTEVRTHLDPQNEPDVLLKDKSHLDMSDGCEITTVEHSETCQPLSPILYPEKILFSKEDRLEQMPHLRESPITLEELSHCNRKADVEKSAASLASKLSKLKDSEKEMQTVGMTGHTSELPDSNPSWKDNSQCTRLDLDFCELLKNKLEKIESDMLPMADSATEDGPINKNSELHPNNTTDDTEEPETPLLFPCNDSKISRDSDVLIRTSEQPTGNPDSVGKVIMSQVEDGIGSQGGVCPQGDESKARSCSKNEPNAHCMDWQQHFDVTLGRMVYINRMTGLSTFVAPTDDLHTACTKDLTTVAVDVLLGNDAVDAAAAAVSEPLQSLFSEWSNPVFARYPEVAVGVSSGQAESLAVKIHNVLYPYRFTKEMIHSVKVLQQVDNKFIACLMSTRMDEDGRTGGNLLVLVDQHAAHERIRLEQLITDSYEKQDPQSAGRKKLLSSTIIPPLAITVSEEQRRLLRSYHKHLEDLGLELLFPDASDSLILVGKVPLCFVEREASELRRGRSTVTKSIVEELIREQVELLQTTGGIQGTLPLTVQKVLASQACHGAIKFNDRLSLEESCRLIEALSLSQLPFQCAHGRPSMLPLADLDHLEQEKQVKPNLAKLRKMVRAWHLFGKTEQNLQQPIRPCEPP
Protein: Olfactory receptor 2A7 (Olfactory receptor OR7-18) (Q96R45)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MGDNITSITEFLLLGFPVGPRIQMLLFGLFSLFYVFTLLGNGTILGLISLDSRLHAPMYFFLSHLAVVDIAYACNTVPRMLVNLLHPAKPISFAGRMMQTFLFSTFAVTECLLLVVMSYDLYVAICHPLRYLAIMTWRVCITLAVTSWTTGVLLSLIHLVLLLPLPFCRPQKIYHFFCEILAVLKLACADTHINENMVLAGAISGLVGPLSTIVVSYMCILCAILQIQSREVQRKAFCTCFSHLCVIGLFYGTAIIMYVGPRYGNPKEQKKYLLLFHSLFNPMLNPLICSLRNSEVKNTLKRVLGVERAL