wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 2A activator 2 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase PTPA-2) (PPIase PTPA-2) (Rotamase PTPA-2) (Phosphotyrosyl phosphatase activator 2) (Q9P7H4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein phosphatase PP2A regulatory subunit A
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator 1
- Uncharacterized protein C63.05
- Uncharacterized protein C216.01c
- Putative serine/threonine-protein phosphatase C26H8.05c
- Leucine carboxyl methyltransferase 1
- Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MLSREEQNRCFVPVRRILDNEDLKLFKEGDAYKLIDSFICDLDEAVKDKPISASIPQSSSIEHVLNILDRVGEIKQENPAIDNMGSRFGNPAFQSFYDQVYIETPKLHQVFGIEHNAAMEAGRYFYESFGNRKRIDYGSGHELYFMSWLLILKQLGIFTKNDYPALVVRVFVKYVELMRSLQIFYTLEPAGSHGVWGLDDFHFLPFLFGAAQLVNHKYLRPKHVRDPEILEMCRADYMYLGYVYFLNKLKPSVSLRFHSPMIDDISAVKTWSKVNEGMIKMYRAEVLGKLPIMQHYLFGHLIPASPGMSPAPQDGDDSEVTHVHSHYADCCGIKIPSAISAAKNNGSRIPFD
Protein: FERM domain-containing protein 6 (Q8C0V9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96NE9}. Cell membrane {ECO:0000250|UniProtKB:Q96NE9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96NE9}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96NE9}. Note=Can colocalize with actin. {ECO:0000250|UniProtKB:Q96NE9}.
Interaction partners:
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L2
- Merlin
- Protein KIBRA
- Ras association domain-containing protein 8
- Transcriptional coactivator YAP1
- Serine/threonine-protein kinase LATS2
- Serine/threonine-protein kinase LATS1
- Protein salvador homolog 1
Sequence:
MNKLTFHNNKAMQDRRRVCIFLPNDKSVSIIINVKILCHQLLVQVCDLLRLKDSHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKVRQYEVTWGIDQFGPPMIIHFRVQYYVENGKLISDRIARYYYYWHLRKQVLHSQCVLREEAYFLLAAFALQADLGNFKRKLHHGDYFEPEAYFPAWVVSKRGKDYILKHIPNMHKDQFALTASEAYLKYIKEAVRLDDVAIHYYRLYKDKREAEGSLTLGLTMRGIQIFQNLEEEKQLLYDFPWTNVGKLVFVGKKFEILPDGLPSARKLVYYTGCPTRSRHLLQLLSNSHRLYMNLQPVLRHLRKQEENEEKKQYRESYISDNLDLDMDPLEKRSRASGSSAGSVKHKRLSRHSTASHSSSHTSGIEADTKPRDPGPEDSCSGSAMHRKLKTCSSMTSHGSSHTSGVESGGKDRLEEDSQDEEIEMLVDDPRDLEPMPEESLEVSPEMCIYITEDMLLSRKLNGHSGLIVKEIGSSTSSSSETVVRLRGQSTDSLPQTICRKPKTSTDRHSLSLDDIRLYQKDFLRIAGLCQDTAQSYTFGCGHELDESGLYCNSCLAQQCVNIQDAFPVKRASKYFSLDLTHDEVPEFVV
Protein: Succinyl-CoA:3-ketoacid coenzyme A transferase subunit B (EC 2.8.3.5) (OXCT B) (Succinyl-CoA:3-oxoacid CoA-transferase) (P56007)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A
- Acetyl coenzyme A acetyltransferase
- Conserved hypothetical integral membrane protein
Sequence:
MREAIIKRAAKELKEGMYVNLGIGLPTLVANEVSGMNIVFQSENGLLGIGAYPLEGSVDADLINAGKETITVVPGASFFNSADSFAMIRGGHIDLAILGGMEVSQNGDLANWMIPKKLIKGMGGAMDLVHGAKKVIVIMEHCNKYGESKVKKECSLPLTGKGVVHQLITDLAVFEFSNNAMKLVELQEGVSLDQVKEKTEAEFEVRL
Protein: Outer spore wall protein RRT8 (Regulator of rDNA transcription protein 8) (Q08219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall assembly. May be involved in the modulation of rDNA transcription.
Subcellular location: Prospore membrane {ECO:0000269|PubMed:23966878}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:14562095}. Spore wall {ECO:0000269|PubMed:23966878}. Note=Localizes to the ascal side of growing prospore membranes in mid-meiosis II and to the spore wall in post-meiotic cells. Localizes to a specific subset of lipid droplets associated with the exterior surface of the spore throughout spore wall formation. {ECO:0000269|PubMed:23966878}.
Interaction partners:
- Outer spore wall protein 6
- Outer spore wall protein 2
- Outer spore wall assembly protein SHE10
Sequence:
MKAGIELISHSQASHATYANSMTLAEKGPQRLKRQFKEHSSSKESNVSRWLKIFIRQFDIWFPETIPTMKVRYELLRKNFIKEIFNSRAFIYPFLGFYEVLTNPVYWKHILLFAVCYALIFVTIAGLFYVTLVPLLVTWAILLLGPLGVILVHIQWILQTNVLTAFVCRTLVLTHITNQIFDISLVLQDQDEFLNEVKVLPKPQKPHRKIDEPDAVRNFNTIKGSRIFKIPRLLFRMFFKVSNFTSLTLLSLIPIVGPILANQLMAPKRTFTYLQRYFLLKGFSKKQAKDFQYEHYASFICFGMSAGLLELIPFFTIVTISSNTVGAAKWCTSLLKGERKKE
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 (EC 2.8.2.30) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1) (3-OST-3A) (Heparan sulfate 3-O-sulfotransferase 3A1) (h3-OST-3A) (Q9Y663)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
- Sulfotransferase 1C4
- Sulfotransferase 1B1
- Sulfotransferase 1C3
Sequence:
MAPPGPASALSTSAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCQTLSGPVVGLSGGGEEAGAPGGGVLAGGPRELAVWPAAAQRKRLLQLPQWRRRRPPAPRDDGEEAAWEEESPGLSGGPGGSGAGSTVAEAPPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKGLAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERLISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEIDREVVRRLREFYRPFNLKFYQMTGHDFGWDG
Protein: Style cell-cycle inhibitor 1-B (NtSCI1) (A0A1S3XQD6)
Organism: Nicotiana tabacum (Common tobacco)
Function: Component of the auxin signaling transduction pathway that regulates cell proliferation and differentiation during flowers stigmas and styles development. Involved in the regulation of auxin-related genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:21388377}. Note=Inside the nucleus, confined to the interchromatic region. {ECO:0000269|PubMed:21388377}.
Interaction partners:
- Floral homeotic protein AGAMOUS
- Floral homeotic protein AGAMOUS
Sequence:
MGSDKKTTEEKRKHKRNSPSSPRDEVKSKRQNIKGDEERRKEKDKSKKEKHKSHKSKCHSSEEKKSGEKHKTKSHKHKDKSKNKFEELSKDDYFSKNNEFASWLKDKKNLFFSDLSSETARNLFSDFVIQWNKGKLDSQYYEGIATGPRSSHAWNIKK
Protein: Uncharacterized protein (G8BID5)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Uncharacterized protein
Sequence:
MRFFIPVSLLTLSSGALAAVRPVQLFASSDNKEIDGQGLSSTHEGAGINYFFLGSDAQNLQYNDEARVVYIELNSQPPAKQYLAFTGDVLSLTVAEQPLPVDIAEDGSVTFPGSDALAAAKNINDPYRYSESVFAVVKAGGEGSIPLTVSAKFGDVEEEEKPSSTEEAPESTDVSYANKTVTVFTTYCPEPTTLTLTVCETVCEETKVTVSEAGEVTVENVKSKAPTETAESTSVAASAGTQEPEVSSYEASAAAIGGAGLAAIAFAAGGLVF
Protein: Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A2) (H-rev 107 protein homolog) (HRAS-like suppressor 3) (HRSL3) (Q8R3U1)
Organism: Mus musculus (Mouse)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity,catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:33854238}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18614531}. Peroxisome membrane {ECO:0000269|PubMed:22134920}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:33854238}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Cytochrome P450 2E1
- Cytosolic phospholipase A2
- 85/88 kDa calcium-independent phospholipase A2
- Group IIE secretory phospholipase A2
- Group 10 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Phospholipase A2 group V
- Choline/ethanolaminephosphotransferase 1
- Group IID secretory phospholipase A2
Sequence:
MLAPIPEPKPGDLIEIFRPMYRHWAIYVGDGYVIHLAPPSEIAGAGAASIMSALTDKAIVKKELLCHVAGKDKYQVNNKHDEEYTPLPLSKIIQRAERLVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ
Protein: 50S ribosomal protein L34 (Q8LDL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSLSLISGSIHICAELRLRQSPSCLTISSSRPKFLSSRSKQFSLDHFPQISRPIKVIARSAMETTAETITGGVPNNTMKLLFVEMGVGYDQHGQDVTSAAMKACKNAISSNSIPAFRRGSIPGVSFGEMKLQIKLGVPHSLHQQLDLDKVKSIFPYGKIVNVEVVDGGLICSSGVLVEEMGDTNEDCYIVNVAVYVGY
Protein: Type II secretion system protein J (E0SLF8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004377}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004377}.
Interaction partners:
- Type II secretion system protein K
- Type II secretion system core protein G
- Type II secretion system protein I
- Type II secretion system protein H
- Type II secretion system protein L
- Type II secretion system protein M
- Secretin OutD
- Type II secretion system protein C
- Type II secretion system protein J
- Type II secretion system protein F
Sequence:
MKRPNHGFTLLEVMLALAIFAALSLAASQVMNGVMRNDEASARKEARLAELQRAFSLMERDFSQIVPRRSQGYELGFYAERYQLSSADWAVSFIRNGWLNPLGIMPRSELQRVGYRLRGDTLERLFYDSSEPLSTQEPAIRPVLTGVTGFVLRFFGKDGWLDRWDDPAHLPQGIAIVVTLRDYGEITRVFLVTPRYVEAPRKGGPNGNNGDENKDENNQEQPPQENTDSSAQQNQASPDDNGGGDS
Protein: CHK kinase-like domain-containing protein (Q9VBT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNIENPNESLVVPKWLNKSKFESLIAKDEPDFTKIDQFTTVAAVPPGGNFASVMLRVYLDIVMKDGSQKRKSYVVKTMLESDKGGKAVNEMRYFHKEQQMYSTYLPQFEKIYRVAGHPVQLMPKCLEIGEIDGNIYFIFEDLSTRNFVAADRTKGVNMEHMRLSLRKLAELHAASVIYKERYGPYHADFDNGFARKDKIEHSVRRFEVKAPEYKAAMKTWGIDECYLKNFPTTEQYGKLCLESLNVDPQDFNVLTHGDFSPSNILFKYNENGAPSEALILDFQICKWASPTQDLLMLIILSARKDSSYKEFDNIVRIYWEYLIDFLRVLKYKKPLPQLRELQSAIYKKNNTFSAFFAVMNHLPGDLLPVCKENNLHTFNLEDEVGKSFRTKVYTNPIFVEVVKELYPICCNRGLFNFEDY
Protein: Anion exchange protein (Q8IPI3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
- Uncharacterized protein
- Troponin C-akin-1 protein
- FI18412p1
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEGHRAHTVYVGVHVPGGRRHSQRRRKHHHSGPGGGGGGGGGGGSIGGSGSVGGGAGKDNVSEKQQEVERPVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKKKKSNSKHSRPAQNLSSITEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEDNHHQHPPGSGAGANYNADKSGPTTIHIPLSGNKTGTKGPTVNIPQEAVNRTAVWQQINKDGNGISEQLIIPVTLKVRQINGNHAPSSATLSPRLSPMHEADEYSEAPTNSPAHPAGNQQQQQQQINNCKEAAKLDGSCSNNSQISPANITPV
Protein: Anthranilate synthase component 1 (EC 4.1.3.27) (Anthranilate synthase component I) (P00899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
- Anthranilate phosphoribosyltransferase
- Chorismate synthase ARO2
- Chorismate mutase
- N-
- Aromatic/aminoadipate aminotransferase 1
- Pentafunctional AROM polypeptide
- Probable prephenate dehydratase
- Aminodeoxychorismate synthase
Sequence:
MTASIKIQPDIDSLKQLQQQNDDSSINMYPVYAYLPSLDLTPHVAYLKLAQLNNPDRKESFLLESAKTNNELDRYSFIGISPRKTIKTGPTEGIETDPLEILEKEMSTFKVAENVPGLPKLSGGAIGYISYDCVRYFEPKTRRPLKDVLRLPEAYLMLCDTIIAFDNVFQRFQIIHNINTNETSLEEGYQAAAQIITDIVSKLTDDSSPIPYPEQPPIKLNQTFESNVGKEGYENHVSTLKKHIKKGDIIQGVPSQRVARPTSLHPFNIYRHLRTVNPSPYLFYIDCLDFQIIGASPELLCKSDSKNRVITHPIAGTVKRGATTEEDDALADQLRGSLKDRAEHVMLVDLARNDINRICDPLTTSVDKLLTIQKFSHVQHLVSQVSGVLRPEKTRFDAFRSIFPAGTVSGAPKVRAMELIAELEGERRGVYAGAVGHWSYDGKTMDNCIALRTMVYKDGIAYLQAGGGIVYDSDEYDEYVETMNKMMANHSTIVQAEELWADIVGSA
Protein: Septin-9 (SL3-3 integration site 1 protein) (Q80UG5)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546647}. Note=In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes with actin stress fibers.
Interaction partners:
- Septin-7
- Septin-6
- Septin-11
- Septin-2
- Septin-4
- Neuronal-specific septin-3
- Septin-8
- Septin-5
- Septin-10
- Septin-14
Sequence:
MKKSYSGVTRTSSGRLRRLADPTGPALKRSFEVEEIEPPNSTPPRRVQTPLLRATVASSSQKFQDLGVKNSEPAARLVDSLSQRSPKPSLRRVELAGAKAPEPMSRRTEISIDISSKQVESTASAAGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESVLRRVETPASKIPEGSAVPATDAAPKRVEIQVPKPAEAPNCPLPSQTLENSEAPMSQLQSRLEPRPSVAEVPYRNQEDSEVTPSCVGDMADNPRDAMLKQAPASRNEKAPMEFGYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPEAQEM
Protein: Peroxisomal sarcosine oxidase (PSO) (EC 1.5.3.1) (EC 1.5.3.7) (L-pipecolate oxidase) (L-pipecolic acid oxidase) (Q9P0Z9)
Organism: Homo sapiens (Human)
Function: Metabolizes sarcosine and L-pipecolic acid.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10642506}.
Interaction partners:
- Sarcosine dehydrogenase, mitochondrial
- Glycine dehydrogenase
- Dimethylglycine dehydrogenase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Glycine N-methyltransferase
- D-amino-acid oxidase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYLEDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCLSSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINPGLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVSQAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSSFVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKILYELSMKLTPSYDLAPFRISRFPSLGKAHL
Protein: Uncharacterized protein (Q57VA4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVIKKDVPFKYTLHQGLCERDPVLSTPLIITAGVDGNELQYRLDMQVPSHSAIEGMEVTNVEFLFTSSKCNAGKSNQHLSKCSMLVYLYMQLLDGVGRPTSPPFPISCCNTHTGKGIFSCVKLPLQVNQQCRFYLVRRSCTDSASQSAMELKGVRFTSKLYLLYRSPLNSAKVRSQMDVLTGGDLKFTADTEVMTSTGAKRSREELERFGSENSDRKGKKAKRERETATTMDRASDDEPPNLIYAFVSGGDNES
Protein: Dynein light chain, putative (Q389U5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Dynein light chain, putative
- Dynein light chain, putative
- Dynein light chain, putative
- Dynein light chain 2B, cytoplasmic, putative
- Dynein light chain roadblock
- Dynein light chain roadblock
- Dynein light chain roadblock
- Dynein light chain 2B, cytoplasmic, putative
Sequence:
MKEKLTLADDARGICEDVVERYFTPVTKYQHEKIPGIVASITENIVQRLTQEAALPRKYVAHCIIIQKTGAGFHALSACMWNPTSDACYVYKAENKVMHCVVTVYGVVA
Protein: GH18834p (Uncharacterized protein, isoform A) (Q9VYX0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MICRLCLDDAEHSVPIFDQDDSGDQPVPSNLAELIEKHLQLVLLPNDGVSKSLCTQCWQQLADFEQFCAMVMKKQLGLQQLKMEPFSEDEDADTKAQILCEPEIDVSPAAADNEECNEIDGDASSNSRSSSIRTTSLREMRLPSPIRRRMRLPRAVTAPKTQAVKAKARTKTHKAEADEDEDAEGEGDPESRSSNSREMDSYIALHGRLECCICGGDEQFPNFAEMKRHFRNHHQSLGYVVCCQRRYKKRALYVDHLHMHNDPNYFRCKICSKQLVSRISYDVHMLRFHPNKDDLSFACDQCSKRFSKQFLLTIHSRVHQQERNEQCKHCDRSFRTAVDLRLHMRRTHDPAFVPFICDSCGAKFKTKQNLLVHKRTVHREGSQLPEVQCQECQVWLSDENSLRKHMYMHLDAASLRQWKCEQCGLEKGSRAKLAAHIRYHHPKEYHKCTHCAKEFKSSRSLEEHTATHTGQDLYECAFCERTFKNSGNMHKHRRQMHAAQVAALQQQKKVPPSKRKDKGDLLLDVLAAGGKDMSHVMGAGDMND
Protein: 18S rRNA aminocarboxypropyltransferase (EC 2.5.1.157) (20S S rRNA accumulation protein 3 homolog) (HsTsr3) (Q9UJK0)
Organism: Homo sapiens (Human)
Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) in 18S rRNA (Probable). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (Probable).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-Rule:MF_03146}.
Interaction partners:
- Pre-rRNA-processing protein TSR2 homolog
- tRNA N
- Pre-rRNA-processing protein TSR1 homolog
- Ribosomal RNA small subunit methyltransferase NEP1
- tRNA-uridine aminocarboxypropyltransferase 2
- tRNA wybutosine-synthesizing protein 2 homolog
- tRNA-uridine aminocarboxypropyltransferase 1
Sequence:
MGRRRAARGPGAEGGRPRHLPTRSLEAFAEEVGAALQASVEPGAADGEGGPGPAALPCTLAMWELGHCDPRRCTGRKLARLGLVRCLRLGHRFGGLVLSPVGKQYASPADRQLVAQSGVAVIDCSWARLDETPFGKMRGSHLRLLPYLVAANPVNYGRPYRLSCVEAFAATFCIVGFPDLAVILLRKFKWGKGFLDLNRQLLDKYAACGSPEEVLQAEQEFLANAKESPQEEEIDPFDVDSGREFGNPNRPVASTRLPSDTDDSDASEDPGPGAERGGASSSCCEEEQTQGRGAEARAPAEVWKGIKKRQRD
Protein: Virulence factors putative positive transcription regulator BvgA (A0A0E8BMW2)
Organism: Bordetella pertussis
Interaction partners:
Sequence:
MYNKVLIIDDHPVLRFAVRVLMEKEGFEVIGETDNGIDGLKIAREKIPNLVVLDIGIPKLDGLEVIARLQSLGLPLRVLVLTGQPPSLFARRCLNSGAAGFVCKHENLHEVINAAKAVMAGYTYFPSTTLSEMRMGDNAKSDSTLISVLSNRELTVLQLLAQGMSNKDIADSMFLSNKTVSTYKTRLLQKLNATSLVELIDLAKRNNLA
Protein: Large ribosomal subunit protein uL14m (39S ribosomal protein L14, mitochondrial) (L14mt) (MRP-L14) (Q9D1I6)
Organism: Mus musculus (Mouse)
Function: May form part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1, intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q6P1L8}.
Interaction partners:
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein uS12m
- Large ribosomal subunit protein mL54
- Small ribosomal subunit protein mS37
- Large ribosomal subunit protein mL62
- Mitochondrial assembly of ribosomal large subunit protein 1
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL2m
Sequence:
MAALTGLWGSFAHVSRAFSQRCFSTSGSLSAVQKMTRVRVVDNSALGSTPYHRPPRCIHVYNKSGVGKVGDQILLAIRGQKKKALIVGHRMPGSRMTPKFDSNNVVLIEDNGNPVGTRIKIPIPTSLRRREGEYSKVLAIAQNFV
Protein: PA2403 (PepSY domain-containing protein) (Peptidase) (Q5DIV6)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MSKKSRSRLWFLVHSWLALPIWFFVLIVCVTGTLAVVSQEIVWLANPDVRASKPYEDAEPLSFSQVLKAINEAQPDLLVESIQRPDEEHFALTAEVSYPGGSEATLYINPYTGAIQGESPSFDFRQFTRALHGWWLVPFNNGYSWGWYMVSLLGLPMLASLITGLVVYKRFWKGFLKPRLRINQGARIFWGDFHRLSGIWSIWFIALISITGTWFLIQAILADNHVTLTNDGIPPVIARADVPRAAPGQKVPYIELDEAVRLVTGRIPSLEASAVFLPGNAYSPMFVAGRGWYPLMFQSAALNPYTGKIETTRLLSDRTPLQFVTESMRPLHTGDFGGIWVKLIWFVFGLLLSMMVLSGLLIWSKRTAQATAALVKRGKRPARQPKPAKPAPVMANQTAEGQP
Protein: GH08712p (SNR1) (Snf5-related 1) (Q24090)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038126}.
Interaction partners:
- Supporter of activation of yellow protein
- Brahma associated protein 170kD
- Brahma-associated protein of 60 kDa
- ATP-dependent helicase brm
- Brahma associated protein 55kD
- Brahma associated protein 111kD
- Polybromo
- Brahma associated protein 155 kDa
- Trithorax group protein osa
- Bromodomain containing 7/9
Sequence:
MALQTYGDKPVAFQLEEGGEYYYVGSEVGNYMRHFRGILYKKYPGMTRIVLSNEERKRLAESGLSSHILASSVSLLRAVEVDDIMAGNDEKYRAVSVNTSDTPVPRESKSKKQPQYVPTMPNSSHLDAVPQATPINRNRVHTKKVRTFPMCFDDTDPTASLENAAQKECLVPIRLDMELEGQKLRDTFTWNKNESMITPEQFAEVLCDDLDLNPLPFVPAIAQAIRQQIEAFPNDPPILEETCDQRVIVKLNIHVGNTSLVDQVEWDMSEKNNNPEEFAIKLCAELGLGGEFVTAIAYSIRGQLSWHCRTYAFSEAPLSTIDVPFRNPSDADAWAPFLETLTDAEMEKKIRDQDRNTRRMRRLANTTTGW
Protein: Thioredoxin, putative (Q580L8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSATVGLRRYVTSILNVSRLRQEAIRGYALRRSGACLSGQLRIFTDHVNADAAVLVYFHTNRCKPCISITRALEEMETEKEQGVVSSSIPQCSSSHACSQEDTLGLTQRLLRLLGITFADVAVSPEALGVLREGVTRGVRIISVDTDENPVISALHDIRSVPTFVAYRCGRIIGHLEGASEQKLQELVSKLLVEEGGATN
Protein: Nuclear RNA export factor 7 (A2AEI4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MCSNERKQGSFRYTGRKKDRVSSLSYAGKRTDHYEHTGHTILPFKAQSDGGNLEMRAVLWNPSVRHTPYVGQHRSREEEHMEDQIHVTAQRDDKPEQREAGQFTEDGELGSWFKVTVPCGRKYDKTQLMNSIHSLCSVPFTPVDFHCDKHRIQFF
Protein: LicD/FKTN/FKRP nucleotidyltransferase domain-containing protein (Q381Y0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYSWRGCRVLLGSMPSFRPHIHRHPCTICSSAVTQYQDATETTSADICDDKNIRNDIHSASHVSCFNYLSSDKAATATPASLHFRDRQPSGWSGRALGATVCESRRAALNEWLGMMQNAAKTTQSQPEDAYLQQCWQAFRDPSRALTDREMEGAIELLDRQCEFQKSCTTSDKCLVGESANSFLMRLRGGDVHSVDEERQLSFQRTLLEFRDLANTIKLPFFLCCGTALAAHREGYFIPHDVDIDVGVFYEDLQDLGDPQKAVVGLLSHAALGGRFVLFDVCGTVEKGLELRFLHSETQVPIDLNVYYQPLPQDDKIVAEFGPFVWTATYYESSAARRHGMYRYRHAPFRAAMKHMSFCDTMASSSDPTNTVGFLVPPESYVEECYGKDWRTPRRFTYAEGLQNGGFANIIDE