wanglab/gogpt-training-data huggingface dataset:
Protein: RING-type domain-containing protein (Q57ZW8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Leucine-rich repeat protein
Sequence:
MSRSVPWRNTCPEAVTDILNQLPSCQLLLVKRVGPTSFLLSKRDGLVKYRTSIGDPHSCSCDASREQCIHVVFVLCKVFFLPRENPLVWQRSLVAAEIDEILRSENRLRNAWKNVDDTRRDVAVPRPIEEGDVCPICFEEFGNDTSLDYCGGGCGKYIHTRCFKQYKRHNLVGPLRCPYCRSLWTNTVGATSKRCSGCKKYANGSCYKCLFCQEYFLCSDCFHRRETHSHHPFSLVGTREVAERHEGNSALPMPVSSEPTVSIPEELHPLMYREIDPEDYETLLRLDDQNSKRKLTAEEFSVLHSECWSSGLLTDECNICLDTFDVTSGCVWLPCGHFFHTSCAQRWLTEHVAECPIDHIPVVVDRADVQSLTVNSSSSAAVAPHILRPSRPRARVLPRRRLNVPYSSATVGVEPPARRNAERQRGSDVSLPFLELQAVSLGVGRRRGRYNEQFFYGTV
Protein: Ribosome-binding ATPase YchF (O53459)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Elongation factor 4
- Peptidyl-tRNA hydrolase
- Phenylalanine--tRNA ligase beta subunit
- Peptide chain release factor 1
- GMP synthase
- DUF6542 domain-containing protein
- Translation initiation factor IF-2
- Serine--tRNA ligase
- Arginine--tRNA ligase
- Ribosomal RNA small subunit methyltransferase A
Sequence:
MSLSLGIVGLPNVGKSTLFNALTRNNVVAANYPFATIEPNEGVVSLPDPRLDKLAELFGSQRVVPAPVTFVDIAGLVKGASEGAGLGNKFLAHIRECDAICQVVRVFVDDDVTHVTGRVDPQSDIEVVETELILADLQTLERATGRLEKEARTNKARKPVYDAALRAQQVLDAGKTLFAAGVDAAALRELNLLTTKPFLYVFNADEAVLTDPARVGELRALVAPADAVFLDAAIESELTELDDESAAELLESIGQSERGLDALARAGFHTLKLQTFLTAGPKEARAWTIHQGDTAPKAAGVIHSDFEKGFIKAEIVSYDDLVAAGSMAAAKAAGKVRIEGKDYVMADGDVVEFRFNV
Protein: Guanyl-specific ribonuclease T1 (RNase T1) (EC 4.6.1.24) (P00651)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- ribonuclease T2
Sequence:
MMYSKLLTLTTLLLPTALALPSLVERACDYTCGSNCYSSSDVSTAQAAGYQLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWPILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT
Protein: Inactive ribonuclease-like protein 9 (P60154)
Organism: Mus musculus (Mouse)
Function: Does not exhibit any ribonuclease activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKPLVIKFAWPLPLLLLLLLPPKLQGNYWDFGEYELNPEVRDFIREYESTGPTKPPTVKRIIEMITIGDQPFNDYDYCNTELRTKQIHYKGRCYPEHYIAGVPYGELVKACDGEEVQCKNGVKSCRRSMNLIEGVRCVLETGQQMTNCTYKTILMIGYPVVSCQWDEETKIFIPDHIYNMSLPK
Protein: Catalase-related peroxidase (EC 1.11.1.-) (Q73WB6)
Organism: Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis)
Function: Has an organic peroxide-dependent peroxidase activity. Exhibits strong peroxidase activity using organic hydroperoxides as cosubstrates, weak peroxidase activity using hydrogen peroxide and negligible catalase activity. May have a role in elimination of reactive oxygen species, in particular by deactivating hydroperoxides.
Interaction partners:
- FAD-binding PCMH-type domain-containing protein
- Oxidoreductase
- FAS1-like dehydratase domain-containing protein
Sequence:
MSGGLTPDQAIDAIRGTGGAQPGCRALHAKGTLYRGTFTATRDAVMLSAAPHLDGSTVPALIRFSNGSGNPKQRDGAPGVRGMAVKFTLPDGSTTDVSAQTARLLVSSTPEGFIDLLKAMRPGLTTPLRLATHLLTHPRLLGALPLLREANRIPASYATTEYHGLHAFRWIAADGSARFVRYHLVPTAAEEYLSASDARGKDPDFLTDELAARLQDGPVRFDFRVQIAGPTDSTVDPSSAWQSTQIVTVGTVTITGPDTEREHGGDIVVFDPMRVTDGIEPSDDPVLRFRTLVYSASVKLRTGVDRGAQAPPV
Protein: KNL (Kinetochore null) Binding Protein (O44956)
Organism: Caenorhabditis elegans
Interaction partners:
- Centromere/kinetochore protein zw10 homolog
- MAD related
Sequence:
MNPNHNEGLLELYTQAISLEALKDAEQFLENSLLGKDAQVERLLAQVLIEEQQIETNRKKIAQLRIEKEELEFDCANSDLKSLEQMQAERDELQRKCQPGQHTKSNHKSSEQLLRMKKETDALRAYMKKISQFED
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g06840 (EC 2.7.11.1) (C0LGD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFSTHHVSRLLIPLLFFFLFCCFSSTFAQDDITNPVEVRALRVIKESLNDPVHRLRNWKHGDPCNSNWTGVVCFNSTLDDGYLHVSELQLFSMNLSGNLSPELGRLSRLTILSFMWNKITGSIPKEIGNIKSLELLLLNGNLLNGNLPEELGFLPNLDRIQIDENRISGPLPKSFANLNKTKHFHMNNNSISGQIPPELGSLPSIVHILLDNNNLSGYLPPELSNMPRLLILQLDNNHFDGTTIPQSYGNMSKLLKMSLRNCSLQGPVPDLSSIPNLGYLDLSQNQLNGSIPAGKLSDSITTIDLSNNSLTGTIPTNFSGLPRLQKLSLANNALSGSIPSRIWQERELNSTESIIVDLRNNGFSNISGRSDLRPNVTVWLQGNPLCSDGNLLRLCGPITEEDINQGSTNSNTTICSDCPPPYEFSPEPLRRCFCAAPLLVGYRLKSPGFSDFVPYRSEFEQYITSGLSLNLYQLRLDSFQWQKGPRLRMYLKFFPVFGSNANNSFIFNRSEVRRIRGMFTGWNIRDEDLFGPYELMNFTLLDVYRDVFPSASPSGLSNGAVAGIVLGSVAAAVTLTAIIALIIMRKRMRGYSAVARRKRSSKASLKIEGVKSFTYAELALATDNFNSSTQIGQGGYGKVYKGTLGSGTVVAIKRAQEGSLQGEKEFLTEIELLSRLHHRNLVSLLGFCDEEGEQMLVYEYMENGTLRDNISVKLKEPLDFAMRLRIALGSAKGILYLHTEANPPIFHRDIKASNILLDSRFTAKVADFGLSRLAPVPDMEGISPQHVSTVVKGTPGYLDPEYFLTHQLTDKSDVYSLGVVLLELFTGMQPITHGKNIVREINIAYESGSILSTVDKRMSSVPDECLEKFATLALRCCREETDARPSMAEVVRELEIIWELMPESHVAKTADLSETMTHPSSSSNSSIMKHHYTSMDVSGSDLVSGVAPSVAPR
Protein: Homeobox protein orthopedia (Q5XKR4)
Organism: Homo sapiens (Human)
Function: Probably involved in the differentiation of hypothalamic neuroendocrine cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:10458915}.
Interaction partners:
- Single-minded homolog 1
- POU domain, class 3, transcription factor 2
- Oxytocin-neurophysin 1
Sequence:
MLSHADLLDARLGMKDAAELLGHREAVKCRLGVGGSDPGGHPGDLAPNSDPVEGATLLPGEDITTVGSTPASLAVSAKDPDKQPGPQGGPNPSQAGQQQGQQKQKRHRTRFTPAQLNELERSFAKTHYPDIFMREELALRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRAPGTLLPTPGLPQFPSAAAAAAAAMGDSLCSFHANDTRWAAAAMPGVSQLPLPPALGRQQAMAQSLSQCSLAAGPPPNSMGLSNSLAGSNGAGLQSHLYQPAFPGMVPASLPGPSNVSGSPQLCSSPDSSDVWRGTSIASLRRKALEHTVSMSFT
Protein: Cysteinyl leukotriene receptor 1 (CysLTR1) (Cysteinyl leukotriene D4 receptor) (LTD4 receptor) (G-protein coupled receptor HG55) (HMTMF81) (Q9Y271)
Organism: Homo sapiens (Human)
Function: Receptor for cysteinyl leukotrienes mediating bronchoconstriction of individuals with and without asthma. Stimulation by LTD4 results in the contraction and proliferation of smooth muscle, edema, eosinophil migration and damage to the mucus layer in the lung. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Cysteinyl leukotriene receptor 2
- Leukotriene C4 synthase
- Guanine nucleotide-binding protein G
- Arachidonate 5-lipoxygenase-activating protein
- Glutathione hydrolase 1 proenzyme
- Polyunsaturated fatty acid 5-lipoxygenase
- Thromboxane A2 receptor
- Guanine nucleotide-binding protein subunit alpha-15
- Leukotriene B4 receptor 2
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MDETGNLTVSSATCHDTIDDFRNQVYSTLYSMISVVGFFGNGFVLYVLIKTYHKKSAFQVYMINLAVADLLCVCTLPLRVVYYVHKGIWLFGDFLCRLSTYALYVNLYCSIFFMTAMSFFRCIAIVFPVQNINLVTQKKARFVCVGIWIFVILTSSPFLMAKPQKDEKNNTKCFEPPQDNQTKNHVLVLHYVSLFVGFIIPFVIIIVCYTMIILTLLKKSMKKNLSSHKKAIGMIMVVTAAFLVSFMPYHIQRTIHLHFLHNETKPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRKRLSTFRKHSLSSVTYVPRKKASLPEKGEEICKV
Protein: Naphthalene 1,2-dioxygenase system ferredoxin--NAD(P)(+), reductase component (EC 1.18.1.7) (Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase ferredoxin-specific)) (Q52126)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. Ferredoxin reductase catalyzes the transfer of electrons from NADH to ferredoxin (NdoA). NADPH is also effective but yields only 39% of the activity obtained with NADH. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.
Interaction partners:
Sequence:
MELLIQPNNRIIPFSAGANLLEVLRENGVAISYSCLSGRCGTCRCRVIDGSVIDSGAENGQSNLTDKQYVLACQSVLTGNCAIEVPEADEIVTHPARIIKGTVVAVESPTHDIRRLRVRLSKPFEFSPGQYATLQFSPEHARPYSMAGLPDDQEMEFHIRKVPGGRVTEYVFEHVREGTSIKLSGPLGTAYLRQKHTGPMLCVGGGTGLAPVLSIVRGALKSGMTNPILLYFGVRSQQDLYDAERLHKLAADHPQLTVHTVIATGPINEGQRAGLITDVIEKDILSLAGWRAYLCGAPAMVEALCTVTKHLGISPEHIYADAFYPGGI
Protein: Uncharacterized protein (Q385T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIVRAKSLWLLAFFALNTALLADAENVTLKIVRELVLRDVGDVVLTPRFRENVDKYLRRHTDRNVKANAYKSQPDVIVVARAWFTGDSKEATASYNRVKDIFDSWEAQPNDTLISDLNNVSLRELGVQPRLIELSDQCKYGESYIDQSAENFGFNNLTLEIRMSTNPQSDLRSRLCRMLPFVDCSLIVLDVVKRVNNLYTTKVTITSPNRNYCLVVLMNNFHYAAALLPDIIESVVIADKEVFRRPSVNMVEDGRLQSPCARRFWYLIFLLLLIPLSLFVGHKMYYSGLESGRKAARALERDIRGGVRYQGQASSQPLEGWQYMESNYAGSSSNGSPRIGSSSRQTNQSQRKVHHMYYDPNENWQNNEVQMMRSSSTIPSASSRQQ
Protein: Cadherin-7a (Cdh7 protein) (B0S6D4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
- Sema domain, transmembrane domain
- Catenin beta-1
- Catenin alpha-2
- Catenin, beta 2.
- Catenin
- Cadherin-related family member 5 isoform X2
- Junction plakoglobin b.
- Junction plakoglobin a.
- Catenin alpha-1
Sequence:
MTILLLAQRDVGCGGMTLNSVPLRSVSLRPLRDSVGTSLQRHKRNWVWNQFFVLEEYTGDEPLYVGKLHSDVDKGEGKVKYVLNGEGATSIFTIDENTGDIHATKRLDREEQAYYTLRAQARDRATNLPVEPESEFVIKVQDINDNEPKFLDGPYNAQVPEMSPVGTSVVEVKATDADDPTYGNSARVVYSILEGQPYFSVEPKTGIVRTALPNMDREARDQYLLVIQAKDMVGQMGGLSGTTSVTVTLTDVNDNPPRFSRKSYQFAVPESLPVASVVAKIKALDSDIGPNAEMDYRIIEGDGLGVFRVTTDKDTQEGVITLQKNLDFETKSSYTLKIEASNRNIDPRFLSQGPFSDTAMVRLTVENVDEPPVFSSPLSKMVVSEAAKVGTMIGTVSAMDPDTTNSPIRYSIDRNTDLERFFNIESTTGVISTAKPLDREANAVHNITILAIESMDPSQVGKGVALITVMDINDNAPVFAIEYETFLCESVGPGQVIETISAVDKDEPPSGHRFFFSLTAETAGNMNFTLRDNKDNTASVLTKRSGFQRRDQSMYRLPVLIVDSGTPALSSTNTLSIRVCDCDPDGTPQSCGTEAFMLSAGLSTGALIAILACIITLLVLVLLIVTMRRRKKEPLILDEDRDVRENIVRYDDEGGGEEDTEAFDMVALRNLNVVRDSKARRDVTPEVPTLYCSRPPPYKITPDNGIFREFIWDRLKDADVDPSAPPYDSLQTYAFEGSGSVAESLSSLDSLSTDSEQNYDYLSDWGPRFRKLADLYGHGDSSNIFSS
Protein: Serine/threonine-protein kinase Nek5 (EC 2.7.11.1) (NimA-related protein kinase 5) (AtNEK6) (AtNek5) (Q0WPH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in epidermal-cell morphogenesis in hypocotyls and roots. May act on the microtubule function. May have a secondary role in trichome branching.
Interaction partners:
- Kinesin-like protein KIN-14C
- Serine carboxypeptidase-like 41
- Nematode resistance protein-like HSPRO1
- Tubulin alpha-4 chain
- Non-canonical heme oxygenase HOZ, chloroplastic
- Protein salt-induced and EIN3/EIL1-dependent 1
- Serine carboxypeptidase-like 14
- Putative cyclin-T1-1
- Kinesin-like protein KIN-UC
Sequence:
MESRMDQYELMEQIGRGAFGAAILVHHKAERKKYVLKKIRLARQTERCRRSAHQEMSLIARVQHPYIVEFKEAWVEKGCYVCIVTGYCEGGDMAELMKKSNGVYFPEEKLCKWFTQLLLAVEYLHSNYVLHRDLKCSNIFLTKDQDVRLGDFGLAKTLKADDLTSSVVGTPNYMCPELLADIPYGFKSDIWSLGCCIYEMAAYRPAFKAFDMAGLISKVNRSSIGPLPPCYSPSLKALIKGMLRKNPEYRPNASEILKHPYLQPYVEQYRPTLSAASITPEKPLNSREGRRSMAESQNSNSSSEKDNFYVSDKNIRYVVPSNGNKVTETDSGFVDDEDILDHVQQSAENGNLQSVSATKPDGHGILKPVHSDQRPDVIQPRHPKTIRNIMMVLKEEKARENGSPMRSNRSRPSSVPTQKNNVETPSKIPKLGDIAHSSKTNASTPIPPSKLASDSARTPGSFPPKHHMPVIDSSPKLKPRNDRISPSPAAKHEAEEAMSVKRRQRTPPTLPRRTSLIAHQSRQLGADISNMAAKETAKLHPSVPSESETNSHQSRVHASPVSTTPEPKRTSVGSAKGMQSESSNSISSSLSMQAFELCDDASTPYIDMTEHTTPDDHRRSCHSEYSYSFPDISSEMMIRRDEHSTSMRLTEIPDSVSGVQNTIAHHQPEREQGSCPTVLKDDSPATLQSYEPNTSQHQHGDDKFTVKEFVSSVPGPAPLPLHVEPSHQVNSHSDNKTSVMSQNSALEKNNSHSHPHPVVDDVIHVIRHSSFRVGSDQPVMESVEVGVQNVDMGKLINVVRDEMEVRKGATPSESPTTRSIISEPDSRTEPRPKEPDPITNYSETKSFNSCSDSSPAETRTNSFVPEEETTPTPPVKETLDIKSFRQRAEALEGLLELSADLLEQSRLEELAIVLQPFGKNKVSPRETAIWLAKSLKGMMIEDINNNNSSGSSRNCS
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q57XI6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MHTTTVLQVIALLLSQRKAAAVAAGDNEHHFLDLCALIALTQRPIPELPETQQATTDYQEIQKLNISLSGTDWRKQFDKTGTPPKRAAYKPSGATEDSLRKERRPYWINAEDEIETDKGPEKILRSAGADGATQADRQRLLALLQPIAEAAASTFTEIENLKQASKALTAAAIHKKIQTATYGEQATAAADLTAAVFKAANGNPTNRKELCGDTTSASAKARTLTAFLYCICAGEQSQNAGGFKACSNAQPANADAQAALTNVHTAIQGLINVCPEPGNDKVTPDDITKLIAAVAGKTTSKAQQAFYGTFAATDCGGLSGSGLCVYYKTTTKADSKAYHNIQWKKQLSDAANDLRDQQLATQRLQGLLLQLKSLKKQAYNLRPQLEIYKKLQVTAGKSGTTQEAQAKKGDDCKQHTKNATCTENNCKWKATTEEAGTCEAKAEEQKSQGTGEGASGTSATTGCTRHGTDKTACENDKTGDKQNCAWRKGKDDEPDKETEKCRNGCFLVNNKFALMTASFASLVAF
Protein: Serine/threonine-protein kinase KIN82 (EC 2.7.11.1) (Flippase kinase 2) (P25341)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids.
Interaction partners:
- Phospholipid-transporting ATPase DNF2
- Phospholipid-transporting ATPase DNF1
- Probable phospholipid-transporting ATPase DNF3
- Protein ORM2
Sequence:
MTQQEYRSPSQRLSKGRSMSLPKIFARNLRSLQNNAPPGKNINVNCLNVNSCSLSASPSSQINMACNGNKQDLPIPFPLHVECNDSWSSSKLNKFKSMFNHNRSKSSGTTDASTSEKGTHKREPRSTIHTELLQSSIIGEPNVHSTTSSTLIPNEAICSTPNEISGSSSPDAELFTFDMPTDPSSFHTPSSPSYIAKDSRNLSNGSLNDINENEELQNFHRKISENGSASPLANLSLSNSPIDSPRKNSETRKDQIPMNITPRLRRAASEPFNTAKDGLMREDYIALKQPPSLGDIVEPRRSRRLRTKSFGNKFQDITVEPQSFEKIRLLGQGDVGKVYLVRERDTNQIFALKVLNKHEMIKRKKIKRVLTEQEILATSDHPFIVTLYHSFQTKDYLYLCMEYCMGGEFFRALQTRKSKCIAEEDAKFYASEVVAALEYLHLLGFIYRDLKPENILLHQSGHVMLSDFDLSIQATGSKKPTMKDSTYLDTKICSDGFRTNSFVGTEEYLAPEVIRGNGHTAAVDWWTLGILIYEMLFGCTPFKGDNSNETFSNILTKDVKFPHDKEVSKNCKDLIKKLLNKNEAKRLGSKSGAADIKRHPFFKKVQWSFLRNQDPPLIPALNDNGCELPFILSCNKHPKRNSVSEQETKMFCEKVANDDEIDEADPFHDFNSMSLTKKDHNILTYSENYTYGKILYKATCTRPRHNSSHRSFFKDIIPEL
Protein: Targeted effector protein (Q9RI13)
Organism: Yersinia pestis
Interaction partners:
Sequence:
MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGKNPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV
Protein: Peroxiredoxin-4 (EC 1.11.1.24) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372) (Thioredoxin-dependent peroxiredoxin 4) (O08807)
Organism: Mus musculus (Mouse)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not secreted. {ECO:0000269|PubMed:11229364}.
Interaction partners:
- Thioredoxin domain-containing protein 5
- Endoplasmic reticulum resident protein 44
- Protein disulfide-isomerase A6
- Thioredoxin
- Sulfiredoxin-1
- Peroxiredoxin-5, mitochondrial
- Protein disulfide-isomerase
- Glutathione peroxidase 7
Sequence:
MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
Protein: Complement component C9 [Cleaved into: Complement component C9a; Complement component C9b] (P02748)
Organism: Homo sapiens (Human)
Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC.
Subcellular location: Secreted {ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:8603752, ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}. Target cell membrane {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:9212048}; Multi-pass membrane protein {ECO:0000269|PubMed:26841934}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore. {ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:30111885, ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9634479}.
Interaction partners:
- Complement C5
- Complement component C8 alpha chain
- Complement component C6
- Complement component C8 gamma chain
- Complement component C8 beta chain
- Complement component C7
- CD59 glycoprotein
- Vitronectin
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Sequence:
MSACRSFAVAICILEISILTAQYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASSISLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELKDIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVNITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDFVNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLERAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFEGIACEISKQKISEGLPALEFPNEK
Protein: Kinetochore and Eb1-associated basic protein (F0JAI6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21912673}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21912673}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21912673}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21912673}. Note=During metaphase expressed in the kinetochores. During anaphase expression in the kinetochores progressively increases, and at late anaphase it is also expressed in the microtubules, specifically in the central spindle and centrosomal region. During telophase expression increases in the microtubules, and it is associated with residual spindle microtubules between chromosomes that have separated. At interphase it is expressed in the cytoplasm particularly around the nucleus. {ECO:0000269|PubMed:21912673}.
Interaction partners:
Sequence:
MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERSLYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKENQELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKGIKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQLQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKIEKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCIEAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP
Protein: Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.-) (EC 3.5.1.23) (Acylsphingosine deacylase 2) (N-acylsphingosine amidohydrolase 2) [Cleaved into: Neutral ceramidase soluble form] (Q9JHE3)
Organism: Mus musculus (Mouse)
Function: Plasma membrane ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at neutral pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine. Together with sphingomyelinase, participates in the production of sphingosine and sphingosine-1-phosphate from the degradation of sphingomyelin, a sphingolipid enriched in the plasma membrane of cells. Also participates in the hydrolysis of ceramides from the extracellular milieu allowing the production of sphingosine-1-phosphate inside and outside cells. This is the case for instance with the digestion of dietary sphingolipids in the intestinal tract.
Subcellular location: [Neutral ceramidase]: Cell membrane {ECO:0000269|PubMed:11591392, ECO:0000269|PubMed:12921776, ECO:0000269|PubMed:16126722}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Membrane raft {ECO:0000269|PubMed:12921776}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Membrane, caveola {ECO:0000269|PubMed:12921776}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NR71}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Mitochondrion {ECO:0000269|PubMed:21613224}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9NR71}. Note=Enriched in exosomes upon stimulation by cytokine (By similarity). Enriched in caveolae and lipid rafts (PubMed:12921776). {ECO:0000250|UniProtKB:Q9NR71, ECO:0000269|PubMed:12921776}.; SUBCELLULAR LOCATION: [Neutral ceramidase soluble form]: Secreted {ECO:0000269|PubMed:16126722}.
Interaction partners:
- Alkaline ceramidase 2
- Alkaline ceramidase 1
- Acid ceramidase
- Alkaline ceramidase 3
- Ceramide kinase
- Sphingosine kinase 2
- Sphingosine kinase 1
- Ceramide synthase 4
- Ceramide glucosyltransferase
- Ceramide synthase 5
Sequence:
MAKRTFSTLEAFLIFLLVIMTVITVALLTLLFVTSGTIENHKDSGNHWFSTTLGSTTTQPPPITQTPNFPSFRNFSGYYIGVGRADCTGQVSDINLMGYGKNGQNARGLLTRLFSRAFILADPDGSNRMAFVSVELCMISQRLRLEVLKRLESKYGSLYRRDNVILSAIHTHSGPAGFFQYTLYILASEGFSNRTFQYIVSGIMKSIDIAHTNLKPGKIFINKGNVANVQINRSPSSYLLNPQSERARYSSNTDKEMLVLKLVDLNGEDLGLISWFAIHPVSMNNSNHFVNSDNMGYAAYLFEQEKNKGYLPGQGPFVAGFASSNLGDVSPNILGPHCVNTGESCDNDKSTCPNGGPSMCMASGPGQDMFESTHIIGRIIYQKAKELYASASQEVTGPVLAAHQWVNMTDVSVQLNATHTVKTCKPALGYSFAAGTIDGVSGLNITQGTTEGDPFWDTLRDQLLGKPSEEIVECQKPKPILLHSGELTIPHPWQPDIVDVQIVTVGSLAIAAIPGELTTMSGRRFREAIKKEFALYGMKDMTVVIAGLSNVYTHYITTYEEYQAQRYEAASTIYGPHTLSAYIQLFRDLAKAIATDTVANMSSGPEPPFFKNLIASLIPNIADRAPIGKHFGDVLQPAKPEYRVGEVVEVIFVGANPKNSAENQTHQTFLTVEKYEDSVADWQIMYNDASWETRFYWHKGILGLSNATIYWHIPDTAYPGIYRIRYFGHNRKQELLKPAVILAFEGISSPFEVVTT
Protein: Protein RETICULATA-RELATED 3, chloroplastic (Q9C9Z2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in leaf development. Required for leaf mesophyll cell division in the early stages of leaf organogenesis.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305|PubMed:23596191}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Monothiol glutaredoxin-S11
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1
- UDP-glycosyltransferase 71C3
- 3-isopropylmalate dehydratase small subunit 1
- Protein RESPONSE TO LOW SULFUR 2
Sequence:
MAAMAAKLQLSAKSDQSSVRLPRVINLSRDPTTRVSFPRNGSVCSLHTNFSSPHLAKPCAGGGGGGSTGNNGGGSGSGGGGGGFGGSGGEASEESSPWGPIGLFIQGWRSRVAADPQFPFKVLMEEIVGLSACVLGDMASRPNFGLNELDFVFSTLVVGSILNFVLMYMLAPTAATLGSSQTLPGIFRNCPSSHMFEQGSFTVMNRFGTLVYKGMVFASVGLAAGLVGTAISNGLIMLRKKMDPSFETPNKPPPTVLNSLTWATHMGVSANARYQTLNGIEFLLAKVLPPLVFKTSVIVLRCANNVAGGMSFVLLARMTGSQSVEEKTEISEKEKDD