wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (p42A) (Q99JI4)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 6A
Sequence:
MPLENLEEEGLPKNPDLRIAQLRFLLSLPEHRGDAAVREELMAAVRENNMAPYYEALCKSLDWQMDVDLLSKMKKANEEELKRLDEELEDAEKNLGESEIRDAMMAKAEYLCQIGDKEGALTAFRKTYDKTVALGHRLDIVFYLLRIGLFYMDNDLITRNTEKAKSLIEEGGDWDRRNRLKVYQGLYCVAIRDFKQAAELFLDTVSTFTSYELMDYKTFVTYTVYVSMIALERPDLREKVIKGAEILEVLHSLPAVRQYLFSLYECRYSVFFQSLAIVEQEMKKDWLFAPHYRYYVREMRIHAYSQLLESYRSLTLGYMAEAFGVGVDFIDQELSRFIAAGRLHCKIDKVNEIVETNRPDSKNWQYQETIKKGDLLLNRVQKLSRVINM
Protein: Cytochrome c oxidase subunit 7, mitochondrial (Cytochrome c oxidase polypeptide VII) (P10174)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 8, mitochondrial
Sequence:
MANKVIQLQKIFQSSTKPLWWRHPRSALYLYPFYAIFAVAVVTPLLYIPNAIRGIKAKKA
Protein: Importin subunit alpha (Karyopherin alpha) (G5EB89)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Import of proteins with classical NLS composed of one or two clusters of basic residues is initiated by binding to the importin alpha/beta heterodimer, where importin alpha acts as an adapter subunit to bridge NLS cargos to importin beta, which transports the whole complex through the nuclear envelope. Involved in the nuclear accumulation of the light-dependent developmental regulator veA. Participates at different regulatory stages of asexual and sexual development, being required for the completion of both reproductive cycles with the formation of conidiospores and ascospores, respectively. Mediates secondary metabolite gene expression with positive regulation of penicillin production and negative regulation of mycotoxin biosynthesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B6HJ92}.
Interaction partners:
- Importin-95
- Nucleoporin NSP1
- Nuclear cap-binding protein subunit 2
- Importin N-terminal domain-containing protein
- Ribosomal RNA-processing protein 8
- Nuclear pore complex subunit Nup133, putative
- snRNA cap binding complex subunit
- GTP-binding nuclear protein
- Uncharacterized protein
- RCC1 Chromatin-associated guanine nucleotide exchange factor for Ran
Sequence:
MAERYIPEHRRTQYKARNQFRPDELRRRREEQQVEIRKQKREENLAKRRGIQTRDGGIGVGGGMAAAESDDEASAIESELNVELPEMVKGVFSDQIEAQIQATTKFRKLLSKERNPPIERVIETGVVSRFVEFLRSPHTLVQFEAAWALTNIASGSAQQTQVVIEAGAVPIFVELLSSPEPDVREQAVWALGNIAGDSPQCRDFVLNAGALRPLLTLINDGRKISMLRNATWTLSNFCRGKTPQPDWNTIAPALPVLAKLIYMLDDEVLIDACWAISYLSDGPNEKIQAVIEAGIPRRLVELLMHASTSVQTPALRSVGNIVTGDDVQTQVIINCGALPALLSLLSSTKDGIRKEACWTISNITAGNSSQIQSVIDAGIIPPLVHLLANGDFKTRKEACWAISNATSGGLQKPDQIRYLVTQGCIKPLCDLLACPDNKIIQVALDGLENILKVGEMDKEAGQGDAHVNRYALFIEEAGGMEKIHDCQNNANEEIYMKAYNIIEKYFSDEDEAAGDIDELAPQQTQTGFTLGATQQQPGGFSFGGANGGDSMDM
Protein: Adiponectin (30 kDa adipocyte complement-related protein) (Adipocyte complement-related 30 kDa protein) (ACRP30) (Adipocyte, C1q and collagen domain-containing protein) (Adipose most abundant gene transcript 1 protein) (apM-1) (Q3Y5Z3)
Organism: Bos taurus (Bovine)
Function: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW (By similarity).
Subcellular location: Secreted {ECO:0000305|PubMed:15378692}.
Interaction partners:
- Adiponectin receptor 1
- Adiponectin receptor 2
- Fatty acid-binding protein, adipocyte
- Leptin
- Perilipin
- Resistin
- Peroxisome proliferator-activated receptor gamma
- Insulin
- Solute carrier family 2, facilitated glucose transporter member 4
- Albumin
Sequence:
MLLQGALLLLLALPSHGEDNMEDPPLPKGACAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDPGLVGPKGDTGETGITGIEGPRGFPGTPGRKGEPGESAYVYRSAFSVGLERQVTVPNVPIRFTKIFYNQQNHYDGTTGKFLCNIPGLYYFSYHITVYLKDVKVSLYKNDKALLFTHDQFQDKNVDQASGSVLLYLEKGDQVWLQVYEGENHNGVYADNVNDSTFTGFLLYHNIVE
Protein: Jim, isoform G (M9PG92)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAINFSASFAACIAAGLKVPRQIMYCITQDTGQPYVLYKDSQDAERNPGAIGATPAQWGSEMYPNIQQQAQQHLTAQQQQQQQQQNAAQAAAQAAAVAAAAGQPQSPPGGGQEARDNGSGDGRQQQVSPSSSPYPSVQQQQRANGAGDEDPMNHQLANQQNPAPNQNQSSNDPQHSGSNAGESGNPHVQQNGGPQNDPGNSFRTPDYYDPRHAAPQGGMLAPPGFPPLHYLNKGVLPMEQSGGGGGAGGGEAYALPEMLPAQQNGQQNAGPANTNANEGGAGANGSGGVGGATGASVGVGSVGVTSGGRTGNGPGRPHKNKPHSDLRLFKCLTCGKDFKQKSTLLQHDRIHTDARPFPCSECGKRFRQQSHLTQHLRIHANEKPFTCPYCSRSFRQRAILNQHIRIHSDVSPHLIFKNGPHPTLWPSDVPFPGEDNDTKGDIAGTGGGYHDEDSQGTPDGSGGMHYPSYFKDGKGQKILPEVLQHIGVRPANMPLYVRCPICDKEFKQKTTLLQHGCIHIESRPYPCPECGKRFRQQSHLTQHLRIHTNEKPFGCMYCPRFFRQRTILNQHLRIHTGEKPYKCGQCGKDFRQKAILDQHTRTHQVQGDRPFCCPMPNCRRRFATENEVTKHIDNHMNPNTTKVRRQQQQQHQQQQQQQQQQQQQQQQQNNNAVAQVANHLMNDAKSLAAQQFLNNNNPSAVDNKANILPVRSIASNAAAAAVVQQSVVKNELYFPQCYGPPFQHPFQAQQQQAQQPSVAHANGGPTPPVTVTVANSVASGVVVQQNASASVVAQ
Protein: WD repeat-containing protein 46 (WD repeat-containing protein BING4) (O15213)
Organism: Homo sapiens (Human)
Function: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-interacting protein 2
- Something about silencing protein 10
- Ribosomal RNA-processing protein 7 homolog A
- Probable U3 small nucleolar RNA-associated protein 11
- Small subunit processome component 20 homolog
- WD repeat-containing protein 36
- Transducin beta-like protein 3
- Protein RRP5 homolog
- Ribosome biogenesis protein BMS1 homolog
- Nucleolar protein 10
Sequence:
METAPKPGKDVPPKKDKLQTKRKKPRRYWEEETVPTTAGASPGPPRNKKNRELRPQRPKNAYILKKSRISKKPQVPKKPREWKNPESQRGLSGTQDPFPGPAPVPVEVVQKFCRIDKSRKLPHSKAKTRSRLEVAEAEEEETSIKAARSELLLAEEPGFLEGEDGEDTAKICQADIVEAVDIASAAKHFDLNLRQFGPYRLNYSRTGRHLAFGGRRGHVAALDWVTKKLMCEINVMEAVRDIRFLHSEALLAVAQNRWLHIYDNQGIELHCIRRCDRVTRLEFLPFHFLLATASETGFLTYLDVSVGKIVAALNARAGRLDVMSQNPYNAVIHLGHSNGTVSLWSPAMKEPLAKILCHRGGVRAVAVDSTGTYMATSGLDHQLKIFDLRGTYQPLSTRTLPHGAGHLAFSQRGLLVAGMGDVVNIWAGQGKASPPSLEQPYLTHRLSGPVHGLQFCPFEDVLGVGHTGGITSMLVPGAGEPNFDGLESNPYRSRKQRQEWEVKALLEKVPAELICLDPRALAEVDVISLEQGKKEQIERLGYDPQAKAPFQPKPKQKGRSSTASLVKRKRKVMDEEHRDKVRQSLQQQHHKEAKAKPTGARPSALDRFVR
Protein: At5g61510 (GroES-like zinc-binding alcohol dehydrogenase family protein) (A1L4Y4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methionine aminopeptidase 1A
- non-specific serine/threonine protein kinase
- Isoflavone reductase homolog P3
- Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
- 26S proteasome regulatory subunit 4 homolog B
- Adenylate kinase 4
- Methylenetetrahydrofolate reductase 2
- ADP-ribosylation factor
Sequence:
MAALTLHHHHHHRHHSCLQASGHLSRRLYHRIFSSFPRNPVKDLNFRLSLADFSSFSLSTRGTVFAVRALSTVAVEESSEKKMVKGIRVYEHGGPEVLKWEDVEVGEPKEGEIRVKNKAIGLNFIDVYFRKGVYKPASMPFTPGMEAVGEVVAVGSGLTGRMIGDLVAYAGNPMGAYAEEQILPADKVVPVPSSIDPIVAASIMLKGMTAQFLLRRCFKVEPGHTILVHAAAGGVGSLLCQWANALGATVIGTVSTNEKAAQAKEDGCHHVIMYKNEDFVSRVNDITSGKGVNVVYDSVGKDTFKGSLACLKSRGYMVSFGQSSGSPDPIPLSDLAPKSLFLTRPSMMHYNETRDELLECAGEVFANVTSGILKARVNHKYPLSRVADAHADLENRITSGSVVLLP
Protein: ABC transporter G family member STR2 (EC 7.6.2.-) (Protein STUNTED ARBUSCULE 2) (A0A0M4FLW6)
Organism: Petunia hybrida (Petunia)
Function: Together with STR, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:D3GE74}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000250|UniProtKB:D3GE74}.
Interaction partners:
Sequence:
MRHANGRRGDTTIDIGKPVNFTGGLEFSNLTYTVIKKIKDSDGKWLNQEVDLLHQITGYAPKGCVTAVMGPSGAGKSTFLDGLAGRISSLRGRVSVDGMDMTPSFIKRTSAYIMQDDRLFPMLTVYETLLFAADLRLGPISMTDKRQRVEKLIEQLGLSSARNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSAHSVIDKVHAIARAGSTVILTIHQPSSRIQLLLDHLIILARGQLMYQGSPKDVSLHLGRMGRKVPKGESSIENLIDVIQEYDQSELGVEALAAFALTGMKPPPLGAHEMSIVPPSPAPSHREGRGHDRSNKRLHLKDQDFDHSLRSNWNTSKSWSASHSGVLQTLGFSPARHHRDHRNQNSVSSSLGDYAYTSENFRSIPTPHTQSSECTLNENDFMTPYAAANTNAYQYLGPKFANSFLSETWILMRRNFINIRRTPELFLSRLVVLTVMGIMMATMFMHPKKNLQGITNRLSFFIFTVCLFFFSSNDAVPAFIQERFIFVRETSHNKYRASSYTIAGLITYLPFLAVQAAVYAVIVWFALSLRGPFIYFLIVLYMSLLSTNSFVVFVSSVVPNYILGYAAVIAFTALFFLFCGYFLNSHDMPQYWKWMNYISTMTYPYEGLLMNQFQTSQTFGIDPLGRSITGNGILKSLNISQVESKKWEKVYIMLAWAIVYRILFYIVLRFFSKNQRT
Protein: Microtubule-actin cross-linking factor 1 (G5EFD1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDLLLDYFYFCAREVLCHTFGITCATGAGSEIALVARDPTTYYRPSSSNSDPTYRETGTPISWSEGGGGLSSTSSSSCPSASSQFPLILRSSPSPPQPPQQQHAQHREYSSFSFSSSSFTTPSSSSSYSSSSSSSSSNSHACDHCDSYVWHATSCLATTALLLFGLATTLTMLKVVRSYSKKAERKSESSRASAQGGSQQAISGGGGAGAGGGGNSSYYEEYSSRNGAAGGNGHVGNGGGQIIHHAHNQHLSNAQQAHGGFSESSSYETREHFERKVQRVKKTRGERERSRSGKRDDVSLHGSDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVERLLDAEDVDTNNPDEKSIITYVSSLYNALPHEPEMSRLQKVQEEYIEEAYEWREWVVRAIQLVDDRHLQGTASELIYELQRFREDDLPPREEQKRRLTLVYEHLEKVMRSTELFAIPHELSAPELQRVWNELQNSIDRRFDVLERHRIQEGNSNDLLSRLARGIGITNEKLDLILKRIEDVEARVDTSPPAAVERTVSEIVDDLNALESPIARFFEDVEELKSMQHPEANDFYKQVYGLHQRRTTYLDRLTNQILVRLGVRTDSLHKENQQRLENMRKTSFSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCELLRVLESEYQQLRDLSAGRMLDLDSLIAFVRAAQLELIWVSERESIEVTRNWSDIKQLDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVYLRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDFSLEEGERFLRELDEIKEILNKYHQVLMALTERCASISPLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIPPTDARLTALLNRLLQQFEKLKKLWDKKHRMVRFNMVLNTMRTIQGWDLDTFNSIDPDQRDAIMKALNDDANKLLSELDPNDPLALRLREELRRTNEHFWNLLNASQKPPEPDWASQYDQKMAELLKKLEEAWRELNDAVGKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQLPNPTPTQRVNHDRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADIVRQHEITLNSFDDLPAALDKLRGHHSQLLEINMVLKQQQTVIDQLNRNVALLRQHVSRTRINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESALQIQMVYRSEYETEMSWLDTVEETINRLRKPEELRPEQYQQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFIHEAKIFDAKLGQYSDGIVGIHGPGIKSEFRRTKPQPKNGSQIVTEELELLNRRFAQLSSLILERRNTMQVLIQNWKRQKQVSYRVFDISHISHHLLPS
Protein: ABI-1-like 1 (B3H5V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
METEISGMDNPAMTLDEVSMERNKSFVKALQELKNLRPQLYSAADYCEKSYLHSEQKQMVLDNLKDYTVKALVNAVDHLGTVASKLTDLFDHQNSDISTMEMRASCVSQQLLTCRTYIDKEGLRQQQLLAVIPLHHKHYILPNSVNKRVHFSPLRRTDTRQNHYQAISRLQPSGAMSSSLSLLVNNTSSQISNSLSNMLGLTHLDAPASKSLSWHLGSETKSTLKGTSTVAPSSKDSKAFSKTSGVFHLLGDDENIANKKPLAGSQVSGVPAASTAHKDLEVPKLLTAHRSLDNNPRREIIQAPVRTKSVLSAFFVKQKTPKLKAGYVS
Protein: Notch homolog 2 N-terminal-like protein B (P0DPK3)
Organism: Homo sapiens (Human)
Function: Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway. Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentiation genes, thereby delaying the differentiation of neuronal progenitors and leading to an overall final increase in neuronal production. Acts by enhancing the Notch signaling pathway via two different mechanisms that probably work in parallel to reach the same effect. Enhances Notch signaling pathway in a non-cell-autonomous manner via direct interaction with NOTCH2. Also promotes Notch signaling pathway in a cell-autonomous manner through inhibition of cis DLL1-NOTCH2 interactions, which promotes neuronal differentiation.
Subcellular location: Secreted {ECO:0000269|PubMed:29856954, ECO:0000269|PubMed:29856955}.
Interaction partners:
Sequence:
MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN
Protein: Lysophosphatidic acid:oleoyl-CoA acyltransferase 1 (LPAAT) (Lysophosphatidic acid acyltransferase) (EC 2.3.1.51) (Vacuolar protein sorting-associated protein 66) (Q06508)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and lipid droplet formation. Involved in vacuolar protein sorting.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:22090344}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:22090344}; Single-pass membrane protein {ECO:0000255}. Note=Lipid droplets consist of a surface phospholipid monolayer and a hydrophobic interior. The latter makes embedding of proteins containing transmembrane segments difficult, and these may instead adopt a hairpin or monotonic conformation when associated with lipid droplet membranes. Always localizes to lipid droplets, irrespective of whether cells are grown on glucose or oleate. {ECO:0000269|PubMed:21820081}.
Interaction partners:
- Nucleosome assembly protein
- Lysophospholipid acyltransferase
- Glycerol-3-phosphate O-acyltransferase 2
- Glycerol-3-phosphate O-acyltransferase 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Phosphatidic acid phosphohydrolase 1
- Triacylglycerol lipase 5
- Phosphatidate cytidylyltransferase
- Triacylglycerol lipase 4
- Lipid phosphate phosphatase 1
Sequence:
MEKYTNWRDNGTGIAPFLPNTIRKPSKVMTACLLGILGVKTIIMLPLIMLYLLTGQNNLLGLILKFTFSWKEEITVQGIKKRDVRKSKHYPQKGKLYICNCTSPLDAFSVVLLAQGPVTLLVPSNDIVYKVSIREFINFILAGGLDIKLYGHEVAELSQLGNTVNFMFAEGTSCNGKSVLPFSITGKKLKEFIDPSITTMNPAMAKTKKFELQTIQIKTNKTAITTLPISNMEYLSRFLNKGINVKCKINEPQVLSDNLEELRVALNGGDKYKLVSRKLDVESKRNFVKEYISDQRKKRK
Protein: Phosphorylase b kinase regulatory subunit (A0A8J8YFM3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}.
Interaction partners:
Sequence:
MAGEEGLMSEVSWKLLERRARAKRSGSVYEPLKSINLPRPDNETLWDKLDHYYRIVKSTMLTYQSPTTGLFPTKTCGGDQKSKVHESLYCAAGAWALALAYRRIDDDKGRTHELEHSAIKCMRGVLYCYMRQADKVQQFKQDPRPTTCLHSVFNVHTGDEVLSYEEYGHLQINAVSLFLLYLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCITYPAFALDDEALFSQTLDKVIRKLKGKYGFKRFLRDGYRTPLEDPNRRYYKPAEIKLFDGIECEFPIFFLYLMIDGVFRGNLEQVKEYQDLLTPLLHQTTEGYPVVPKYYYVPADFVEYEKRNPGSQKRFPSNCGRDGKLFLWGQALYIIAKLLADELISPKDIDPVHRFVPLQNQRNVSMRFSNQGPLENDLVVHVALVAESQRLQVFLNTYGIQTQTPQQVEPIQIWPQQELVKAYFHLGINEKLGLSGRPDRPIGCLGTSKIYRILGRTVVCYPIIFDLSDFYMSQDVLLLIDDIKNALQFIKQYWKMHGRPLFLVLIREDNIRGSRFNPILDMLAAFKKGIIGGVKVHVDRLQTLISGAVVEQLDFLRISDTEKLPEFKSFEELEFPKHSKVKRQSSTADAPELRQEPDITITEWKNKSTHEILQKLNDCGCLAGQTILLGILLKREGPNFITMEGTVSDHIERVYRRAGSKKLWLAVRYGAAFTQKFSSSIAPHITTFLVHGKQVTLGAFGHEEEVISNPLSPRVIKNIIYYKCNTHDEREAVIQQELVIHIGWIISNNPELFSGMLKIRIGWIIHAMEYELQIRGGDKPAVDLYQLSPSEVKQLLLDILQPQQSGRCWLNRRQIDGSLNRTPPGFYDRVWQILERTPNGIVVAGKHLPQQPTLSDMTMYEMNFSLLVEDMLGNIDQPKYRQIIVELLMVVSIVLERNPELEFQDKVDLDKLVKEAFHEFQKDESRLKEIEKQDGMTSFYNTPPLGQRGTCSYLTKVVMNSLLEGEVKPTNEDSCLVS
Protein: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC) (P21264)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Bifunctional purine biosynthetic protein ADE5,7
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate lyase
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- Orotidine 5'-phosphate decarboxylase
- 3-isopropylmalate dehydrogenase
- Imidazoleglycerol-phosphate dehydratase
- N-
Sequence:
MDSRTVGILGGGQLGRMIVEAANRLNIKTVILDAENSPAKQISNSNDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKNLQVKHPKLKIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASETSLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKNKEMIPEALEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENAIKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKNFTSFSTITTNAIMLNVLGDKHTKDKELETCERALATPGSSVYLYGKESRPNRKVGHINIIASSMAECEQRLNYITGRTDIPIKISVAQKLDLEAMVKPLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLPVIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEVLVKAQKLETVGYEAYLENK
Protein: Complement C4-A (Acidic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; C4b-A; C4d-A; Complement C4 gamma chain] (P0C0L4)
Organism: Homo sapiens (Human)
Function: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.
Subcellular location: Secreted. Synapse {ECO:0000269|PubMed:26814963}. Cell projection, axon {ECO:0000269|PubMed:26814963}. Cell projection, dendrite {ECO:0000269|PubMed:26814963}.
Interaction partners:
- Complement receptor type 1
- Complement C4-B
- C4b-binding protein alpha chain
- Membrane cofactor protein
- Complement C3
- Mannan-binding lectin serine protease 2
- C4b-binding protein beta chain
- Complement decay-accelerating factor
- Complement C1s subcomponent
- Complement C1r subcomponent
Sequence:
MRLLWGLIWASSFFTLSLQKPRLLLFSPSVVHLGVPLSVGVQLQDVPRGQVVKGSVFLRNPSRNNVPCSPKVDFTLSSERDFALLSLQVPLKDAKSCGLHQLLRGPEVQLVAHSPWLKDSLSRTTNIQGINLLFSSRRGHLFLQTDQPIYNPGQRVRYRVFALDQKMRPSTDTITVMVENSHGLRVRKKEVYMPSSIFQDDFVIPDISEPGTWKISARFSDGLESNSSTQFEVKKYVLPNFEVKITPGKPYILTVPGHLDEMQLDIQARYIYGKPVQGVAYVRFGLLDEDGKKTFFRGLESQTKLVNGQSHISLSKAEFQDALEKLNMGITDLQGLRLYVAAAIIESPGGEMEEAELTSWYFVSSPFSLDLSKTKRHLVPGAPFLLQALVREMSGSPASGIPVKVSATVSSPGSVPEVQDIQQNTDGSGQVSIPIIIPQTISELQLSVSAGSPHPAIARLTVAAPPSGGPGFLSIERPDSRPPRVGDTLNLNLRAVGSGATFSHYYYMILSRGQIVFMNREPKRTLTSVSVFVDHHLAPSFYFVAFYYHGDHPVANSLRVDVQAGACEGKLELSVDGAKQYRNGESVKLHLETDSLALVALGALDTALYAAGSKSHKPLNMGKVFEAMNSYDLGCGPGGGDSALQVFQAAGLAFSDGDQWTLSRKRLSCPKEKTTRKKRNVNFQKAINEKLGQYASPTAKRCCQDGVTRLPMMRSCEQRAARVQQPDCREPFLSCCQFAESLRKKSRDKGQAGLQRALEILQEEDLIDEDDIPVRSFFPENWLWRVETVDRFQILTLWLPDSLTTWEIHGLSLSKTKGLCVATPVQLRVFREFHLHLRLPMSVRRFEQLELRPVLYNYLDKNLTVSVHVSPVEGLCLAGGGGLAQQVLVPAGSARPVAFSVVPTAAAAVSLKVVARGSFEFPVGDAVSKVLQIEKEGAIHREELVYELNPLDHRGRTLEIPGNSDPNMIPDGDFNSYVRVTASDPLDTLGSEGALSPGGVASLLRLPRGCGEQTMIYLAPTLAASRYLDKTEQWSTLPPETKDHAVDLIQKGYMRIQQFRKADGSYAAWLSRDSSTWLTAFVLKVLSLAQEQVGGSPEKLQETSNWLLSQQQADGSFQDPCPVLDRSMQGGLVGNDETVALTAFVTIALHHGLAVFQDEGAEPLKQRVEASISKANSFLGEKASAGLLGAHAAAITAYALTLTKAPVDLLGVAHNNLMAMAQETGDNLYWGSVTGSQSNAVSPTPAPRNPSDPMPQAPALWIETTAYALLHLLLHEGKAEMADQASAWLTRQGSFQGGFRSTQDTVIALDALSAYWIASHTTEERGLNVTLSSTGRNGFKSHALQLNNRQIRGLEEELQFSLGSKINVKVGGNSKGTLKVLRTYNVLDMKNTTCQDLQIEVTVKGHVEYTMEANEDYEDYEYDELPAKDDPDAPLQPVTPLQLFEGRRNRRRREAPKVVEEQESRVHYTVCIWRNGKVGLSGMAIADVTLLSGFHALRADLEKLTSLSDRYVSHFETEGPHVLLYFDSVPTSRECVGFEAVQEVPVGLVQPASATLYDYYNPERRCSVFYGAPSKSRLLATLCSAEVCQCAEGKCPRQRRALERGLQDEDGYRMKFACYYPRVEYGFQVKVLREDSRAAFRLFETKITQVLHFTKDVKAAANQMRNFLVRASCRLRLEPGKEYLIMGLDGATYDLEGHPQYLLDSNSWIEEMPSERLCRSTRQRAACAQLNDFLQEYGTQGCQV
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (DNA topoisomerase II) (P12531)
Organism: Trypanosoma brucei brucei
Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MAEAHKYKKLTPIEHVLTRPEMYIGSLDTTATPMFIYDEQKGHMVWETVKLNHGLLKIVDEILLNASDNISNRSARMTYIRVTITDTGEITIENDGAGIPIVRSREHKLYIPEMVFGHLLTSSNYDDDNQNAVAGRHGYGAKLTNILSLSFSVCCRTNGREFHMSWQDHMRKATAPRVSNVGTKEKNVTRVKFLPDYERFGMKEKKISNDMKRVLYKRIMDLSAMFPNIQITLNGSSFGFKSFKDYATLYSAMTPKGEKPPPPYVYESKSGCVAFIPSVVPGVRRMFGVVNGVVTYNGGTHCNAAQDILTGCLDGVERELKKENKVMDTNRVLRHFTILVFLVQVQPKFDSQNKARLVSTPTMPRVPRQDVMKYLLRMPFLEAHVSTITGQLAQELNKEIGTGRRMSSKTLLTSITKLVDATSTRRDPKHTRTLIVTEGDSAKALAQNSLSSDQKRYTGVFPLRGKLLNVRNKNLKRLRNCKELQELFCALGLELDKDYTDADELRYQRILIMTDQDADGSHIKGLVINAFESLWPSLLVRNPGFISIFSTPIVKARLRDKSVVSFFSMKEFHKWQRSNANTPYTCKYYKGLGTSTTAEGKEYFKDMEKHTMRLLVDRSDHKLLDNVFDSQEVEWRKDWMTKANAFTGEVDIDRSKKMLTVTDFVHKEMVHFALVGNARALAHSVDGLKPSQRKIIWALMRRSGNEAAKVAQLSGYISEASAFHHGETSLQETMIKMAQSFTGGNNVNLLVPEGQFGSRQQLGNDHAAPRYIFTKLSKVARLLFPSEDDPLLDYIVEEGQQVEPNHYVPILPLLLCNGSVGIGFGFSSNIPPFHRLDVSAAVRAMISGERAKSVVRRLVPWAVGFQGEIRRGPEGEFIAVGTYTYCKGGRVHVTELPWTCSVEAFREHISYLATKDIVNRIADYSGANHVDIDVEVAQGAVNTYAECESELGLTQRIHINGTVFSPNGTLSPLESDLTPVLQWHYDRRLDLYKKRRQRNLTLLEQELAREKSTLKFVQHFGAGHIDFANATEATLEKVCSKLGLVRVDDSFDYILRKPITFYTKTSFENLLKKIAETERRIEALKKTTPVQLWLGELDQFDRFFQDHEKKMVEAILKERRQRSPPSDLLPGLQQPRLEVEEAKGGKKFEMRVQVRKYVPPPTKRGAGGRSDGDGGATAAGAAAAVGGRGEKKGPGRAGGVRRMVLDALAKRVTRLLPRLLF