wanglab/gogpt-training-data huggingface dataset:
Protein: Choline O-acetyltransferase (CHOACTase) (Choline acetylase) (EC 2.3.1.6) [Cleaved into: Choline O-acetyltransferase 67 kDa chain; Choline O-acetyltransferase 54 kDa chain; Choline O-acetyltransferase 13 kDa chain] (P07668)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Interaction partners:
- Vesicular acetylcholine transporter
- LD22655p
- RE24176p
- Vesicular glutamate transporter, isoform A
- Peroxisomal multifunctional enzyme type 2
- Glutamate decarboxylase
- Congested-like trachea protein
- GH10249p
Sequence:
MASNEASTSAAGSGPESAALFSKLRSFSIGSGPNSPQRVVSNLRGFLTHRLSNITPSDTGWKDSILSIPKKWLSTAESVDEFGFPDTLPKVPVPALDETMADYIRALEPITTPAQLERTKELIRQFSAPQGIGARLHQYLLDKREAEDNWAYYYWLNEMYMDIRIPLPINSNPGMVFPPRRFKTVHDVAHFAARLLDGILSHREMLDSGELPLERAASREKNQPLCMAQYYRLLGSCRRPGVKQDSQFLPSRERLNDEDRHVVVICRNQMYCVVLQASDRGKLSESEIASQILYVLSDAPCLPAKPVPVGLLTAEPRSTWARDREMLQEDERNQRNLELIETAQVVLCLDEPLAGNFNARGFTGATPTVHRAGDRDETNMAHEMIHGGGSEYNSGNRWFDKTMQLIICTDGTWGLCYEHSCSEGIAVVQLLEKIYKKIEEHPDEDNGLPQHHLPPPERLEWHVGPQLQLRFAQASKSVDKCIDDLDFYVYRYQSYGKTFIKSCQVSPDVYIQLALQLAHYKLYGRLVATYESASTRRFLHGRVDCIRAASTEALEWAKAMCQGEGANVPLESDREDEEESRKVKFSIYSKDHLRELFRCAVARQTEVMVKNILGNGIDIPLLGLREASIEVTGEMHELFKDESYIISQCFLLSTSQVACSTDSFMGYGPVTPRGYGCSYNPHPEQIVFCVSAFYSCEDTSASRYAKSLQDSLDIMRDLLQN
Protein: Lysine--tRNA ligase (EC 2.7.7.-) (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) (Q99MN1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15046}. Cytoplasm {ECO:0000250|UniProtKB:Q15046}. Nucleus {ECO:0000250|UniProtKB:Q15046}. Cell membrane {ECO:0000250|UniProtKB:Q15046}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15046}. Secreted {ECO:0000250|UniProtKB:Q15046}. Note=Secretion is induced by TNF-alpha. Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobulin E. {ECO:0000250|UniProtKB:Q15046}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Valine--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MATLQESEVKVDGEQKLSKNELKRRLKAEKKLAEKEAKQKELSEKQLNQTASAPNHTADNGVGAEEETLDPNQYYKIRSQAVQQLKVTGEDPYPHKFHVDISLTQFIQEYSHLQPGDHLTDVTLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIIPQEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIVRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVKSITGSYKITYHPDGPEGQAYEVDFTPPFRRISMVEELEKALGVKLPETSLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKPEDKKETAATTETPESTEASPSV
Protein: Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2) (P58775)
Organism: Rattus norvegicus (Rat)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}.
Interaction partners:
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
- Actin, alpha cardiac muscle 1
- Troponin T, fast skeletal muscle
- Troponin T, slow skeletal muscle
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin I, slow skeletal muscle
- Myosin regulatory light polypeptide 9
Sequence:
MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
Protein: Activating transcription factor 7 interacting protein (F5H502)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSLEEPQKKVFKARKTMRVSDRQQLEAVYKVKEELLKTDVKLLNGNHENGDLDPTSPLENMDYIKDKEEVNGIEEICFDPEGSKAEWKETPCILSVNVKNKQDDDLNCEPLSPHNITPEPVSKLPAEPVSGDPAPGDLDAGDPASGVLASGDSTSGDPTSSEPSSSDAASGDATS
Protein: Insulin-like growth factor-binding protein 1 (A4IGH0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
RSDTQRQITPDIQLSSSCSSAMRAVCVCVLLVCVLVCVLDASPVPAPEPIRCAPCSADQLSACPAVSPGCAEVVRDPGCGCCSSCALRSGDSCGVHTANCGAGLRCVPRAGDPRPLHSLTRGHAVCVEHHPTEEDTELTSEPGSLHHLLSLNRALDPRDTAEAQESIKSQLNAIRQKLIQQGPCHTELLASLDVITESQQALGEKFTSFYLPNCDKHGFYKAKQCVSSLVAQAPRCWCVSSWNGKRLAGTADVEADTPCPQELTH
Protein: RxLR effector protein Avr3a (Avirulence protein 3a) (Q572D3)
Organism: Phytophthora infestans (Potato late blight agent) (Botrytis infestans)
Function: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways. Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, further abolishes host cell death during the biotrophic phase of infection. Associates with and affects also the function of the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis. The Avr3a(EM) form evades recognition by R3a, thus does not trigger R3a-mediated hypersensitivity and does not suppress INF1-induced cell death.
Subcellular location: Secreted {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host cytoplasm {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}.
Interaction partners:
Sequence:
MRLAIMLSATAVAINFATSSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTERADAKKLAKQLMGNDKLADAAYMWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY
Protein: Small ribosomal subunit protein eS1 (40S ribosomal protein S1) (Q6FK63)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122}.
Interaction partners:
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL2
- Ribosomal protein L15
- Candida glabrata strain CBS138 chromosome M complete sequence
- Small ribosomal subunit protein uS12
- 60S ribosomal protein L20
- 40S ribosomal protein S27
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL43
Sequence:
MAVGKNKRLSKGKKGLKKKVVDPFTRKEWYDIKAPSTFENRNVGKTLVNKSTGLKSASDALKGRVVEVCLADLQGSEDHSFRKVKLRVDDVQGKNLLTNFHGMDFTADKLRSMVRKWQTLIEANVTVKTSDEYIIRVFAIAFTRKQSNQVKRTAYAQSSHIRAIRKVISDILTREVSNSTLAQFTSKLIPEVINKEIENATKDIFPLQNVHIRKVKLLKQPKFDLGSLMALHGEGSAEEKGKKVSGFKDEVLETV
Protein: Pectin acetylesterase 3 (EC 3.1.1.-) (O80731)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- GLABROUS1 enhancer-binding protein-like 1
- AT3g18860/MCB22_3
- Polyprenal reductase 2
- Casparian strip membrane protein 2
Sequence:
MKSVLRIAAAIFWLWLFIVLGVIGSGNVRDTDDEISLLESQLVVTSPSQLLMVPLTLIQAAASKGAVCLDGTLPGYHLHPGSGSGANRWLIQLEGGGWCNTRRSCIFRKTTRRGSSNHMEKVLAFTGILSNKSNENPDFFNWNRVKLRYCDGASFTGDSQDESSQLYYRGQRIWHSAMEELLSKGMQKAEQALLSGCSAGGLASILHCDQFKELFPGTTTVKCLSDAGMFMDAVDVSGGHSLRKMFQGVVTVQNLQKELSTACTKHLDPTSCFFPQNLVSGIKTPMFLLNAAYDAWQVQESLAPPSVDLSGSWKACKSDHSHCNSSQIQFFQDFRTHMVDAVKSFATSTHNGVFINSCFAHCQSERQDTWYAPDSPTLHGKTVAESVGDWYFDRTTVKAIDCPYPCDKTCHNLIFK
Protein: DNA ligase (EC 6.5.1.1) (Q587E4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proliferating cell nuclear antigen
- DNA ligase, putative
- DNA ligase, putative
- Flap endonuclease 1
- DNA polymerase
- Replication factor C, subunit 2, putative
- KU70 protein
- KU80 protein
- DNA polymerase epsilon catalytic subunit
- Replication factor C, subunit 5, putative
Sequence:
MVSGPTATAVVQHKRIREDEDDIFDGERDDEMSAGCVNMAKIFLRTPPDPYGGCHASVWPRPQENQKQGPDTVPYAAVADTLADISAESSRLECIRLLSNFLVAVIQRNPIDLVPVVYLVINKQGPAHEGIELGVGDALLLKVVAECCGITEARAKEEYRQTGDLAEVAQSKKRIQSTLVKPKRLTALAVFQALREIALMSGKDVARRRGDVIKRLLRDAVGPEVNLIVRALQQKMRVGLAETSVLAAVGYAFAMSNIGVAKIPSLTPEQLQRELNVGAANLTRTYNEVPCLDVVLAAVLQHGLEVIVPTSAEANMHARALSVRPGIPVKPQLAHPTSGVSVILDRFNGKAFTSEYKYDGERAQIHYTRSSGVQIFSRNSETNTSKYPDIISMLPEAFSVDTVDSFIIDAEVVAVDKVTGALQAFQVLQHRGRKNVSFDNVKVPVCVFAFDILYFNGEPQMSKTLSQRREVLHTHFKPVSTKFRFAEYLDSNDVDDIQAFLDRAIRDGTEGLMVKTLEEESTYVPAKRSHYWLKLKKDYMDGVTDTLDLVPIGAYYGKGKRTGVFGGFLLACYDGEGDEYQSICKIGTGFQDDQLEAITKSLQPSILDEQPRYYRTEDKPDVWFQASQVWEVKAADLSISPAHFAAYGLVDASKGIALRFPRFIRVREDKKVHEATSAAQVAEMYHNQSLAQRGVGDME
Protein: Actinohivin (Q9KWN0)
Organism: Actinomycete sp. (strain K97-0003)
Interaction partners:
Sequence:
MNTLTKLTIGAVALTGSFLAAAPASAAPAADTTASPALGSQVSAQFASVTIRNAQTGRLLDSNYNGNVYTLPANGGNYQRWTGPGDGTVRNAQTGRCLDSNYDGAVYTLPCNGGSYQKWLFYSNGYIQNVETGRVLDSNYNGNVYTLPANGGNYQKWYTG
Protein: Protein JLP2 (DnaJ-like protein 2) (P40206)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome quality control complex subunit 2
Sequence:
MVYFYESKPTEYSTPYQIVMGKDKFENDLLIKWSYRELNYVWFHADKYSSGHVYLKLRPNEKTIDDIPQEVICDCLQLCKSESIQGNKMPQCTILITPWHNLRKNRYMNPGEVSFKSLRQCRKMECGARDNKILNRLAKTRVELFNNVEATLNEAKKTKNGDFFVNYIESNRSNLIEEEKLRKVAKKNQKKKNKQSKDEVTDDMQLEV
Protein: Uncharacterized protein (A0Q7I0)
Organism: Francisella tularensis subsp. novicida (strain U112)
Interaction partners:
Sequence:
MNDKYELNIYFEKIELPKTADFNMISKHDIKELRVDANLKKKIHLLQFDEDYLAYMRSLRAIHPSKIAMQKIKSIRNKEDSFIIAIFSLDKIIHKTKFISFGHKTVIFDFKKLWGLVDFVIVHTSNKTWVNHKLTSFMPSITYCNQNIIHLAYHSDFLYIYHTPEFMDDINVDRENRRELVAKIPDPYWVRADTKENKININSEEENIEKDLKKITKLKNFEISANDIFFSKAIKAAPRLQHKNKSKLFNSLAIENNEKIKRDIIDYAISNAWYKNEGLLENLMTFLDALVVRHLYLIAVYSVYEIEIGIKSVKPEYSKLLKAGLLNKDIQNQLIYDQKKISNIIWLGETFHGLDIEEAEDLCELIDQGDINPKINPINPEKLYRAYKENYGNEALSFREYKEKYNFLDNDKLREEHANKLSSILEDPKFRVLSYINAFLCSTKNYLVPYGYLGSNPLTYYNCMLETGKRRTSKEAYFADIRNKLFMVCYLPGFLSSVIADDDFIDWYSNKKENQELLKNSYLNNLYKSKQKYIKDFIDLDIIKLLKQTSSQIKPSYIPVAFRYGAFASTTALIRSNANVSNRMEFELYDSPERLHNQYSEKEEMIMPKSVNNPKDHSIDNGISLFSLNLTNEKEDGLRKVMLKVAQLYNLDFKVGISGNLDQAMTQALILGMATTKKNGDILLDEDQMLYMTYLYCIFMAHSVDHTVDEILMSANTYLLNSEEVKYPIFNIADFFARPVFGLSKDKEFKSLVEKYENSLKPNSKILKENYISRVVTLSEVYEDIYNLNCLYSSLSEGSLYNLLSTHSERHCTLLEQYSRKKKAEIGLVQDGEKIKVVNNYSGYAAINQYQRFVSLGRMYDSGAKYSSSHKKQIEKDFNLYLPDKEQINYLKYNFKDNKFDAVYKNKKSKEKNQSHIVYAKKQNTRYCYGYFNDFFVKNRITTFYKIKDKSGNYLVNLHNEKYSFATPNSDSKIYRVSPELLNNRDDFKRVSKDIIKSYKYISFDKQKEDIVKNFGKNLYHTNYEIWVGLSHQAISCFSVLDNIDTQEAANTFIDALYYVRLMQLYYGKTIPFLWISSEIVRYSSSETHYYIPTEENFENILKIALNNASKPVIERFLIILNIYNSTIDNNALILIRCRLPIILFEYEEQKLKLKALQKCADSYKKNNYKNEINFSAWFESIFHVQNLSLSPNYIGNNILILSLVEELKPKCSEYKKNMINQQITAKANELNFYQLLIRLIEISTYHRILTKSIITNTTSLLYDILNKPEFQTINKLINKLFIYKNKDLNTDKYKAFHTKLITIESTYKKINSLYKSDFFKKISS
Protein: Elongin-C (Q7JWD6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Elongin-B
- Cullin-5
- Transcription elongation factor B polypeptide 3
- Cullin-2
- RING-box protein 1A
- Protein Vhl
- Ubiquitin-like protein NEDD8
- Suppressor of cytokine signaling at 36E, isoform D
- Protein gustavus
- Suppressor of cytokine signaling at 16D, isoform B
Sequence:
MIAMDEQRGDKIYGGCEGPDAMYVKLISSDGHEFVVKREHALTSGTIRAMLSGPGQFAENEANEVHFREIPSHVLQKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Protein: Vacuolar protein sorting-associated protein 41 (A0A1D8PEQ9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Vacuole {ECO:0000256|PIRNR:PIRNR028921}.
Interaction partners:
- Probable vacuolar protein sorting-associated protein 16 homolog
- E3 ubiquitin-protein ligase PEP5
- Tethering complex ATP-binding subunit
- CNH domain-containing protein
- CORVET complex subunit
- CCZ1/INTU/HSP4 first Longin domain-containing protein
- V-SNARE protein
- Vacuolar fusion protein MON1
- Synaptobrevin homolog YKT6
- Vam7p
Sequence:
MTDTNISKESNEITAENEHEESIVKDLDDASVNEAIPAAQPETDEKQHHEGDHTSIEEDGDEDEEEEEEEEPPTLKYTRLNKLPANFFVKDPVSTSTFHETVFIFATHSGIIHICKPNFETIRTFKAHRASVLSVFTDGTYFATASMDGTVVIGSILDEKDIVAYDFQRPVHAVILDSNYYKTRSFISGGMAGQVIYSSKGWLGKRSDFVLEQGHGPIVSIQLIDDLVIWMNDKGISVFHLATRQIISVLEKPEDSPRSDLYWPRIAFPDPDRLIIGWSNYIWSLRVSLKTAQDEKEGTPISSGMSKILPSTASISFRAVQEKKVEVEHIFKLDSLISGIASFKDDLWMVLAYTPPEADAETGKKTFFNPDLKLINSTTGEVELEEELGLKEIANLGLNDFMLGTHIETIPKYYIISAKDGVIAEEFQISDRLEWYLDRKNYLQAWEISQHLVTPTKRLSYGILYVDSLIEEDNWEEAATFLQRLLVIKRDPNEIKSITQISTESNEEDLDKEILDYWETWSTIFINSNHVQELTNIIPNVTGLLPTSIYDTILRFWLKKDASRFKTLIELWDPSLYNISDIASELELEAKENETLERSLVTLYDKSHNPSKAVPHLIHLRDPNIIGYLSTNHILVPFVSELPVMIDLMFDKGDLKTLPVSKIEKRLQGVISILVDHRLEIPAKQIVNLFYESGLSFVSFFYLEKLADIDNFLVQGFGNERVKLYADYKREKLLPYLTKNDDYDIDTAITICETNDYTKELVYLLGKIGENKQALTLVINKLEDPVMAIEFAKHQNDKETWDILLDQSMSKPKFIKALIESSDESSNAFYDPITILQRMPQDFKIEGLNESVIEFSKNNDLNMLLNQIILKIIYKQSQETSEEFKSQKLRGFEVEIDKKIKKMIQQFQTIVAFVRDDNVKGGPKVVDIKLESDLTSDYSMVPYRDLAHKLDHLREIEENYF
Protein: 2,4-dinitroanisole O-demethylase subunit beta (DNAN hydrolase subunit beta) (DNHB) (EC 3.3.2.14) (A0A096ZED0)
Organism: Nocardioides sp. (strain JS1661)
Function: Involved in the degradation of 2,4-dinitroanisole (DNAN), an insensitive munition ingredient used in explosive formulations as a replacement for 2,4,6-trinitrotoluene (TNT). Catalyzes the removal of the methyl group from 2,4-dinitroanisole (DNAN) to yield 2,4-dinitrophenol (2,4-DNP) and methanol.
Interaction partners:
Sequence:
MTGRQRTTVVAPDRPVQDATISQLTTRVWTVAIDGYRTIVVEGETGIVAINSFGTPSAQTKYRELITQTFGDKPVVAVVASIDHLDHTGRLGPFANGAEVIGHELGQAIAFGRGLPEQKLADTVVTGPVTEIERAGVRLVLRYPAPTVGTGNLAVDLPDDDVVFMVGLQSGARYGIFPDFHFKHFLRATSEIAALGRRYFVPGRSEVMDAGQVRQALEYVNDFQNACQRCLAGGEVPHWLLEPTTAYLHDELSSKWSHLEGYDPVAVGLGGLRVVCHYYMGGWWLDDTDHHELLYDHLTVRTYREYRERLATAGTGRA
Protein: Cation efflux system protein CusA (P38054)
Organism: Escherichia coli (strain K12)
Function: Part of a cation efflux system that mediates resistance to copper and silver.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cation efflux system protein CusC
- Cation efflux system protein CusB
- Cation efflux system protein CusF
- Transcriptional regulatory protein CusR
- Sensor histidine kinase CusS
- Multicopper oxidase CueO
- HTH-type transcriptional regulator CueR
- Multidrug efflux pump subunit AcrA
- Macrolide export protein MacA
- Copper-exporting P-type ATPase
Sequence:
MIEWIIRRSVANRFLVLMGALFLSIWGTWTIINTPVDALPDLSDVQVIIKTSYPGQAPQIVENQVTYPLTTTMLSVPGAKTVRGFSQFGDSYVYVIFEDGTDPYWARSRVLEYLNQVQGKLPAGVSAELGPDATGVGWIYEYALVDRSGKHDLADLRSLQDWFLKYELKTIPDVAEVASVGGVVKEYQVVIDPQRLAQYGISLAEVKSALDASNQEAGGSSIELAEAEYMVRASGYLQTLDDFNHIVLKASENGVPVYLRDVAKVQIGPEMRRGIAELNGEGEVAGGVVILRSGKNAREVIAAVKDKLETLKSSLPEGVEIVTTYDRSQLIDRAIDNLSGKLLEEFIVVAVVCALFLWHVRSALVAIISLPLGLCIAFIVMHFQGLNANIMSLGGIAIAVGAMVDAAIVMIENAHKRLEEWQHQHPDATLDNKTRWQVITDASVEVGPALFISLLIITLSFIPIFTLEGQEGRLFGPLAFTKTYAMAGAALLAIVVIPILMGYWIRGKIPPESSNPLNRFLIRVYHPLLLKVLHWPKTTLLVAALSVLTVLWPLNKVGGEFLPQINEGDLLYMPSTLPGISAAEAASMLQKTDKLIMSVPEVARVFGKTGKAETATDSAPLEMVETTIQLKPQEQWRPGMTMDKIIEELDNTVRLPGLANLWVPPIRNRIDMLSTGIKSPIGIKVSGTVLADIDAMAEQIEEVARTVPGVASALAERLEGGRYINVEINREKAARYGMTVADVQLFVTSAVGGAMVGETVEGIARYPINLRYPQSWRDSPQALRQLPILTPMKQQITLADVADIKVSTGPSMLKTENARPTSWIYIDARDRDMVSVVHDLQKAIAEKVQLKPGTSVAFSGQFELLERANHKLKLMVPMTLMIIFVLLYLAFRRVGEALLIISSVPFALVGGIWLLWWMGFHLSVATGTGFIALAGVAAEFGVVMLMYLRHAIEAVPSLNNPQTFSEQKLDEALYHGAVLRVRPKAMTVAVIIAGLLPILWGTGAGSEVMSRIAAPMIGGMITAPLLSLFIIPAAYKLMWLHRHRVRK
Protein: Protein kinase AMP-activated non-catalytic subunit gamma 2 (A0A8I5Y6F6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSAAMDTKKKKEVSSPGGSSGKKNPSLKRRSLRVHIPDLSSFAMPLLDGDVENSEKHSSRKVDSPFSSGSPSRGLFSRGPQPRPSSPVSAPVRPKMSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPSTSPGGIRFFSRSRKTSSVSSSPSTPTQVTKQHPFPLESYKQEPERLESRIYASSSPPDTGQRFCLAFQSPVRLPLASPTHHAPLRTAALAAAPGPAEAGMLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVSELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCSKLETLETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAETSSFFHRVTDPRQR
Protein: Casein kinase I (EC 2.7.11.1) (Casein kinase 1) (PfCK1) (Q8IHZ9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Serine/threonine-protein kinase likely to be involved in many cellular processes. Phosphorylates rhoptry protein RON3, nucleosome assembly protein NAPL and DNA/RNA-binding protein ALBA4 in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26629826}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:26629826}. Secreted {ECO:0000269|PubMed:26629826}. Host cell surface {ECO:0000269|PubMed:26629826}. Note=At the ring and early trophozoite stages, localizes to the host erythrocyte cell surface (PubMed:26629826). In mature trophozoites, localizes to the parasite cytoplasm (PubMed:26629826). At the segmented schizont stage, localizes to a single dot, probably micronemes, in each merozoite (PubMed:26629826). {ECO:0000269|PubMed:26629826}.
Interaction partners:
- Protein LTV1 homolog
- Essential nuclear protein 1, putative
- Serine/threonine-protein kinase RIO2
- Deoxyribodipyrimidine photo-lyase
Sequence:
MEIRVANKYALGKKLGSGSFGDIYVAKDIVTMEEFAVKLESTRSKHPQLLYESKLYKILGGGIGVPKVYWYGIEGDFTIMVLDLLGPSLEDLFTLCNRKFSLKTVLMTADQMLNRIEYVHSKNFIHRDIKPDNFLIGRGKKVTLIHIIDFGLAKKYRDSRSHTHIPYKEGKNLTGTARYASINTHLGIEQSRRDDIEALGYVLMYFLRGSLPWQGLKAISKKDKYDKIMEKKISTSVEVLCRNASFEFVTYLNYCRSLRFEDRPDYTYLRRLLKDLFIREGFTYDFLFDWTCVYASEKDKKKMLENKNRFDQTADQEGRDQRNN
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 1 (Protein acetyltransferase BLOC1S1) (A0A8I5ZQV1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RDSVRSKRAKARSGSRSFREGPAVPAPSQTRPCCPACSKNTRQSRTNGRSCRVSSSVRSAAPGRGLASSGSLDLGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS
Protein: Serine/threonine-protein kinase UCN (EC 2.7.11.1) (AGC serine/threonine-protein kinase subfamily 2 member 3) (Protein UNICORN) (Q9SYB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates planar ovule integument development by suppressing aberrantly oriented growth. Maintains planar growth of integuments by repressing the developmental regulator and transcription factor KAN4 which is involved in the control of early integument growth and polarity. Restricts growth in stamen filaments, petals, and cotyledons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22927420}. Nucleus {ECO:0000269|PubMed:22927420}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Probable serine/threonine-protein kinase At1g01540
- Probable transcription factor KAN4
- SUN domain-containing protein 1
- Suppressor of mec-8 and unc-52 protein homolog 2
- Homeobox protein BEL1 homolog
Sequence:
METRPSSSSSLSPATNLNLDRLKVLKLLGKGATGTVFLVHDSVSDSSVSSPFALKLVDKSSASSLRRARWEIQILRRLSDDTNPNPFLPKLLASSESSEFIAWALPYCSGGDLNVLRQRQNDGVFSSSVIKFYLAEIVCALDHLHTMGIAYRDLKPENILLQESGHVTLTDFDLSCSLNKPTRPEFYHLSDPEPDPNPESNLSHNKKSLRIFRQKKKKTKSARVNPITRRRLSFSGGERSNSFVGTDEYISPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGRNKKETFRNVLVKEPEFAGKPSDLTDLIRRLLVKDPTKRFGFWRGAAEIKEHAFFKGVRWELLTEVLRPPFIPLRDDGDLTGKVTEESGFGIKEYFEKLKTPPLPLPHECSENNPFVDF
Protein: AGAMOUS-like 85 (T22H22.17 protein) (Q9ZVL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AGAMOUS-like 95
- AGAMOUS-like 48
- Agamous-like MADS-box protein AGL86
- AGAMOUS-like 33
- Agamous-like MADS-box protein AGL82
- AGAMOUS-like-34
- Agamous-like MADS-box protein AGL92
Sequence:
MKTDWSHYLSVEMESTISNELSILCGAEVAFLGYSCSGKPYTFGSPSFQAVAERFLNREASSSLQRSVMNAHQQAKIQELCKVYNRMVEEAKTEEAKVKKAAALAETMPVDEDAWWKVDPKEVEDHEEAKKIMEKCEGLYEKLCNEAAARIQRGDAENNNK
Protein: BEN domain-containing protein 7 (Q8N7W2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEFSERKRSRKSQSFKLVSRDYHHEVYKIPEFSNDVNGEAKETQPIFLGDESMEIKKQITGMRRLLNDSTGRIYQRVGKEGEKLKEEPQDLDLVWPPRLNSSAEAPQSLHPSSRGVWNELPPQSGQFSGQYGTRSRTFQSQPHPTTSSNGELPVVNSSAGSNCCTCNCQSTLQAILQELKTMRKLMQIQAVGTQNRQQPPISLICSQRTAVSRKRNKKKKVPPKTVEPLTVKQKPSGSEMEKKSVVASELSALQAAEHTSPEESRVLGFGIVLESPSSDPEVQLAEGFDVFMPKSQLDSILSNYTRSGSLLFRKLVCAFFDDKTLANSLPNGKRKRGLNDNRKGLDQNIVGAIKVFTEKYCTANHVDKLPGPRDWVQILQDQIKLARRRLKRGSEIADSDERLDGIALPPTVV
Protein: Rifin (C6KTF0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLYYTKILLFCLPLNILAHSKNKLYMKPHTRTTTSRVLSECDIEKSIYDNNPDMKYVKENFDRQTSQRFEEYKERMIKNRQKCKEQCEKDIKQIILKDKIDKPVEEKIEKVCLRCGCGLGGVAASVGVLGTAVVNVWKTAAMDAAIGDAITKGLTEGAAMGATEGVAEVIAGLKALNIDKLFPETLGSFISATNYDKASYIFNIVNMKYKGTCKILVPGGLSNPSNSICDSIQTWSLVQGSNHVNVTTDVAIGKEVVKVVTGAKTIAEKTAKMATENVTKGAIKTNVAEVNATYASCQTAIIASVVAILVIVLVMVIIYLILRYRRKKKMNKKLQYTKLLN
Protein: SWI/SNF and RSC complexes subunit arp42 (Actin-related protein 42) (Chromatin structure-remodeling complex subunit arp42) (Q09849)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chromatin structure-remodeling complex subunit snf21
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF chromatin-remodeling complex subunit snf22
- Chromatin structure-remodeling complex subunit rsc1
- Chromatin structure-remodeling complex subunit rsc4
- SWI/SNF chromatin-remodeling complex subunit snf5
- SWI/SNF and RSC complexes subunit ssr2
- Chromatin structure-remodeling complex subunit sfh1
- Probable actin-related protein 8
- SWI/SNF and RSC complexes subunit ssr1
Sequence:
MEEIPSLVIDPGSCWTRFGYAGEESPMTILPSYYGVRSDVTGRNKYVVDELQIHAPIPGMEVKNGKSNGIIQDWESTLYTWERGLKEKLQVNPTEYAMMITEPSWNPQSVRQQIMEAAFEQLHVPAFYLTKQAVCVAFANSKSTALIVDIGSDNASVTPVVDGLIIRKGIFKQSLAGDFLNANIEQLFNTMNIEFPPHYRIARKSVAIQQSGNMANGSADAVKPAVLYPPIQDLTSSYEIFQKRRVIEEWKESVLDVLDTPFDEAKASSRNPKPFEFPDGVTHKFGQERFRISEILFNPSFSASRSAETTPPQGSVGLHELVYQSILACDSELRSPLLNNIVVTGGTSLIPGLSERLQAEVQRLATGSRINVHTAETASATSNAVWFGGSILASLDNFQHLWVSKQEYDEVGVDRALFVEKRCK