wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein 114 (B3SHH9)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lens fiber membrane intrinsic protein
- Beta-crystallin B1
- Beta-crystallin B2
- Gamma-crystallin D
- Charged multivesicular body protein 4b
- Gap junction alpha-3 protein
Sequence:
MRVHLGGLAGAAALTGALSFVLLAAAIGTDFWYIIDTERLERTGPGAQDLLGSINRSQPEPLSSHSGLWRTCRVQSPCTPLMNPFRLENVTVSESSRQLLTMHGTFVILLPLSLILMVFGGMTGFLSFLLQAYLLLLLTGILFLFGAMVTLAGISVYIAYSAAAFREALCLLEEKALLDQVDISFGWSLALGWISFIAELLTGAAFLAAARELSLRRRQDQAI
Protein: Type 4 fimbrial biogenesis protein PilV (G3XD84)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type 4 fimbrial biogenesis protein PilX
- Type 4 fimbrial biogenesis protein PilW
- Type II secretion system protein H
- Type IV pilus biogenesis factor PilY1
- Type IV pilus non-core minor pilin PilE
- Type 4 fimbrial biogenesis protein PilY2
- Type II secretion system protein H
- Type IV pilus inner membrane component PilO
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilP
Sequence:
MLLKSRHRSLHQSGFSMIEVLVALLLISIGVLGMIAMQGKTIQYTADSVERNKAAMLGSNLLESMRASPKALYDVKDQMATQSDFFKAKGSAFPTAPSSCTPLPDAIKDRLGCWAEQVKNELPGAGDLLKSDYYICRSSKPGDCDGKGSMLEIRLAWRGKQGACVNAADSSADTSLCYYTLRVEP
Protein: Ubiquitin-ribosomal protein eS31 fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S31)] (Q5A109)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein uL16
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKVYTTPKKIKHKHRKHKLAVLTYYKVDNEGNVERLRRECPAPTCGAGIFMANMKDRQYCGKCHLTLKAN
Protein: Two component signal transduction system response regulator (Q8EE50)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- Two component signal transduction system response regulator
- histidine kinase
- histidine kinase
- histidine kinase
- Signaling protein with FIST domain
- Sensory/regulatory protein RpfC
- histidine kinase
- NO-binding heme-dependent sensor protein
- Sensory/regulatory protein RpfC
- histidine kinase
Sequence:
MKTLKPSDIAQYCDVHQRTVSRWIAKGQLKGHKLPGRGNYRVLVEDFISFLHQQNMPMPEAFLASNNNELTVDKKSILIIDDELSMRNALRRALQSTPFTILTAQDGFQAGVKVIAEKPDLILLDLSLPGLDGFEVIQFIRQRPDLAKLKILVLSGLSSIELAESIRLGADDAIAKPFDNHDLLDRVNMLLS
Protein: Nidogen-2 (NID-2) (Osteonidogen) (Q14112)
Organism: Homo sapiens (Human)
Function: Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV, to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell-extracellular matrix interactions.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Laminin subunit gamma-1
- Laminin subunit beta-1
- Nidogen-1
- Laminin subunit alpha-4
- Laminin subunit alpha-1
- Agrin
- Laminin subunit alpha-5
- Laminin subunit alpha-2
- Fibulin-2
Sequence:
MEGDRVAGRPVLSSLPVLLLLPLLMLRAAALHPDELFPHGESWGDQLLQEGDDESSAVVKLANPLHFYEARFSNLYVGTNGIISTQDFPRETQYVDYDFPTDFPAIAPFLADIDTSHGRGRVLYREDTSPAVLGLAARYVRAGFPRSARFTPTHAFLATWEQVGAYEEVKRGALPSGELNTFQAVLASDGSDSYALFLYPANGLQFLGTRPKESYNVQLQLPARVGFCRGEADDLKSEGPYFSLTSTEQSVKNLYQLSNLGIPGVWAFHIGSTSPLDNVRPAAVGDLSAAHSSVPLGRSFSHATALESDYNEDNLDYYDVNEEEAEYLPGEPEEALNGHSSIDVSFQSKVDTKPLEESSTLDPHTKEGTSLGEVGGPDLKGQVEPWDERETRSPAPPEVDRDSLAPSWETPPPYPENGSIQPYPDGGPVPSEMDVPPAHPEEEIVLRSYPASGHTTPLSRGTYEVGLEDNIGSNTEVFTYNAANKETCEHNHRQCSRHAFCTDYATGFCCHCQSKFYGNGKHCLPEGAPHRVNGKVSGHLHVGHTPVHFTDVDLHAYIVGNDGRAYTAISHIPQPAAQALLPLTPIGGLFGWLFALEKPGSENGFSLAGAAFTHDMEVTFYPGEETVRITQTAEGLDPENYLSIKTNIQGQVPYVSANFTAHISPYKELYHYSDSTVTSTSSRDYSLTFGAINQTWSYRIHQNITYQVCRHAPRHPSFPTTQQLNVDRVFALYNDEERVLRFAVTNQIGPVKEDSDPTPGNPCYDGSHMCDTTARCHPGTGVDYTCECASGYQGDGRNCVDENECATGFHRCGPNSVCINLPGSYRCECRSGYEFADDRHTCILITPPANPCEDGSHTCAPAGQARCVHHGGSTFSCACLPGYAGDGHQCTDVDECSENRCHPAATCYNTPGSFSCRCQPGYYGDGFQCIPDSTSSLTPCEQQQRHAQAQYAYPGARFHIPQCDEQGNFLPLQCHGSTGFCWCVDPDGHEVPGTQTPPGSTPPHCGPSPEPTQRPPTICERWRENLLEHYGGTPRDDQYVPQCDDLGHFIPLQCHGKSDFCWCVDKDGREVQGTRSQPGTTPACIPTVAPPMVRPTPRPDVTPPSVGTFLLYTQGQQIGYLPLNGTRLQKDAAKTLLSLHGSIIVGIDYDCRERMVYWTDVAGRTISRAGLELGAEPETIVNSGLISPEGLAIDHIRRTMYWTDSVLDKIESALLDGSERKVLFYTDLVNPRAIAVDPIRGNLYWTDWNREAPKIETSSLDGENRRILINTDIGLPNGLTFDPFSKLLCWADAGTKKLECTLPDGTGRRVIQNNLKYPFSIVSYADHFYHTDWRRDGVVSVNKHSGQFTDEYLPEQRSHLYGITAVYPYCPTGRK
Protein: Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (O57535)
Organism: Gallus gallus (Chicken)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity).
Subcellular location: Cytoplasm. Cell membrane {ECO:0000250}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Uncharacterized protein.
- Guanylate kinase 1.
- Guanosine-3',5'-bis
- Thymidylate kinase
- Nucleoside-triphosphatase
- Ribonucleoside-diphosphate reductase
- CTP synthase
- CTP synthase 2
- UMP-CMP kinase 2, mitochondrial
Sequence:
MAANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFVHASEDLLKQHYIDLKDRPFYPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAQKEISLWFKPAELIDYRSCAHDWVYE
Protein: ARP protein (REF) (F4I3C3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Aldo-keto reductase family 4 member C8
- Pseudouridine kinase
- Probable receptor-like protein kinase At3g17420
- Molecular chaperone Hsp40/DnaJ family protein
- Enoyl-CoA delta isomerase 1, peroxisomal
- Peroxidase 18
- 4-coumarate--CoA ligase-like 2
- Nuclease
- Serpin-Z1
- Interferon-related developmental regulator family protein / IFRD protein family
Sequence:
MEIKPGLSALVTGGASGIGRALCLALAEKGVFVTVADFSEEKGQETTSLVREANAKFHQGLSFPSAIFVKCDVTNRGDLLAAFDKHLATFGTLDICINNAGISTPLRFDKDDTDGSKSWKHTINVDLIAVVEGTQLAIKAMKAKQKPGVIINMGSAAGLYPMPVDPIYAASKAGVVLFTRSLAYYRRQGIRINVLCPEFIKTDLAEAIDASILESIGGYMSMDMLIKGAFELITDEKKAGACLWITKRRGLEYWPTPMEETKYLVGSSSRKRPSFKVSTKIEFPQSFEKMIVHTLSHKFRSATRIVRAPLQLPIGPHQVLLKIIYAGVNASDVNFSSGRYFTGGSPKLPFDAGFEGVGLIAAVGESVKNLEVGTPAAVMTFGAYSEYMIVSSKHVLPVPRPDPEVVAMLTSGLTALIALEKLYDILKLLVQLSLTFSLSYGNSQAGQMKSGETVLVTAAAGGTGQFAVQLAKLSGNKVIATCGGSEKAKLLKELGVDRVIDYKSENIKTVLKKEFPKGVNIIYESVGGQMFDMCLNALAVYGRLIVIGMISQYQGEKGWEPAKYPGLCEKILAKSQTVAGFFLVQYSQLWKQNLDKLFNLYALGKLKVGIDQKKFIGLNAVADAVEYLHSGKSTGKVVVCIDPAFEQKTSRL
Protein: ATXN7L1 protein (Q9BTQ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDGADESEKLDCQFSTHHPRPLAFCSFGSRLMGRGYYVFDRRWDRFRFALNSMVEKHLNSQMWKHRNPSHRASGPSPLFRTCLTNLLSLSNIGAAWVSTLESVAPRYPLNLAAQTPGPGGPEPGGMAADGGVEDIRKKRNGQDSFFFNKHLTLHQEPPTQYSLSARKIPPAADSPLPSPAAHITTPVPASVLQPFSNPSAVYLPSAPISSRLTSSYIMTSAMLSNAAFVTSPDPSALMSHTTAFPHVAATLSIMDSTFKAPSAVSPIPAVIPSPSHKPSKTKTSKSSKVKDLSTRSDESPSNKKRKPQSSTSSSSSSSSSSLQTSLSSPLSGPHKKNCVLNASSALNSYQAAPPYNSLSVHNSNNGVSPLSAKLEPSGRTSLPGGPADIVRQVGAVGGSSDSCPLSVPSLALHAGDLSLASHNAVSSLPLSFDKSEGKKRKNSSSSSKACKITKMPGMNSVHKKNPPSLLAPVPDPVNSTSSRQVRDLLAPPSPALGGRGSWAAPLLSRAAPTGNTSLIPVLVFPEGSFHPLL
Protein: Aspartokinase (EC 2.7.2.4) (Aspartate kinase) (Q59229)
Organism: Bacillus sp. (strain MGA3)
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Interaction partners:
Sequence:
MGLIVQKFGGTSVGSVERILNVANRVIEEKKNGNDVVVVVSAMGKTTDELVDLAKQISAHPPKREMDMLLTTGEQVTISLLAMALNEKGYEAISYTGWQAGITTEPVFGNARILNIETEKIQKQLNEGKIVVVAGFQGIDEHGEITTLGRGGSDTTAVALAAALKAEKCDIYTDVTGVFTTDPRYVKSARKLASISYDEMLELANLGAGVLHPRAVEFAKNYGITLEVRSSMEREEGTIIEEEVTMEQNLVVRGVAFEDEITRVTVFGLPNSLTSLSTIFTTLAQNRINVDIIIQSATDAETTNLSFSIKSDDLEETMAVLENNKNLLNYQGIESETGLAKVSIVGSGMISNPGVAAKMFEVLALNGIQVKMVSTSEIKVSTVVEESQMIKAVEALHQAFELSGSAVKSER
Protein: Citrate (Re)-synthase (EC 2.3.3.3) (Re-citrate synthase) (A5N6T4)
Organism: Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NBRC 12016 / NCIMB 10680 / K1)
Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with oxaloacetate to form citrate. This enzyme is highly Re-face stereospecific with respect to the C-2 of oxaloacetate.
Interaction partners:
- Aconitase-related protein
- Citrate synthase
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate carboxylase
- PorA
- PorB
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Phosphoenolpyruvate carboxykinase
- PorC
Sequence:
MKKCSYDYKLNNVNDPNFYKDIFPYEEVPKIVFNNIQLPMDLPDNIYITDTTFRDGQQSMPPYTSREIVRIFDYLHELDNNSGIIKQTEFFLYTKKDRKAAEVCMERGYEFPEVTSWIRADKEDLKLVKDMGIKETGMLMSCSDYHIFKKLKMTRKETMDMYLDLAREALNNGIRPRCHLEDITRADFYGFVVPFVNELMKMSKEANIPIKIRACDTLGLGVPYNGVEIPRSVQGIIHGLRNICEVPSESIEWHGHNDFYGVVTNSSTAWLYGASSINTSFLGIGERTGNCPLEAMIFEYAQIKGNTKNMKLHVITELAQYFEKEIKYSVPVRTPFVGTDFNVTRAGIHADGILKDEEIYNIFDTDKILGRPVVVAVSQYSGRAGIAAWVNTYYRLKDEDKVNKNDSRIDQIKMWVDEQYRAGRTSVIGNNELELLVSKVMPEVIEKTEERAS
Protein: Glutamine synthetase, chloroplastic/mitochondrial (EC 6.3.1.2) (GS2) (Glutamate--ammonia ligase) (Q43127)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-modulated chloroplast/mitochondrial enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15273293}. Mitochondrion {ECO:0000269|PubMed:15273293}.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
- Glutamate synthase 1, chloroplastic
- Glutamate dehydrogenase 1
- Glutamate dehydrogenase 2
- Glutamate--glyoxylate aminotransferase 1
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Probable glutamate dehydrogenase 3
Sequence:
MAQILAASPTCQMRVPKHSSVIASSSKLWSSVVLKQKKQSNNKVRGFRVLALQSDNSTVNRVETLLNLDTKPYSDRIIAEYIWIGGSGIDLRSKSRTIEKPVEDPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFRDPFRGGNNILVICDTWTPAGEPIPTNKRAKAAEIFSNKKVSGEVPWFGIEQEYTLLQQNVKWPLGWPVGAFPGPQGPYYCGVGADKIWGRDISDAHYKACLYAGINISGTNGEVMPGQWEFQVGPSVGIDAGDHVWCARYLLERITEQAGVVLTLDPKPIEGDWNGAGCHTNYSTKSMREEGGFEVIKKAILNLSLRHKEHISAYGEGNERRLTGKHETASIDQFSWGVANRGCSIRVGRDTEAKGKGYLEDRRPASNMDPYIVTSLLAETTLLWEPTLEAEALAAQKLSLNV
Protein: Cecropin (P83403)
Organism: Glossina morsitans morsitans (Savannah tsetse fly)
Function: Cecropins have lytic and antibacterial activity against several Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:11886771}.
Interaction partners:
- RHD domain-containing protein
Sequence:
MNFYKIFVFIALILALSVSQSEAGWLKKIGKKIERVGQNTRDATVKGLEVAQQAANVAATVRG
Protein: Ankyrin-1 (ANK-1) (Erythrocyte ankyrin) (Q02357)
Organism: Mus musculus (Mouse)
Function: Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils.
Subcellular location: [Isoform Er1]: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Mu7]: Membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Mu8]: Sarcoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Band 3 anion transport protein
- Protein 4.1
- Spectrin beta chain, erythrocytic
- Neural cell adhesion molecule L1
- CD44 antigen
- Neurofascin
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Alpha-adducin
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Gamma-adducin
Sequence:
MGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLIYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQHILCHLNITMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPERRHGDREYSLSPSQVNGYSSLQDELLSPASLQYALPSPLCADQYWNEVTVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKRQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTLDWDKQGSTAVHPQEATQSSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: Antifungal protein B (D0EXD3)
Organism: Penicillium chrysogenum (Penicillium notatum)
Function: Antifungal protein that acts as an inhibitor of growth of human pathogenic molds and yeasts. Is active against the model organism Neurospora crassa, the opportunistic human pathogens Aspergillus fumigatus, Trichophyton rubrum, and Aspergillus terreus. Provokes a reduction of the incidence of infections caused by Penicillium digitatum and Penicillium italicum in oranges and by Penicillium expansum in apples. Low doses of pafB have self-inhibition activity. Shows also activity against the model yeast Saccaromyces cerevisiae and the opportunistic human pathogen Candida albicans. No antibacterial activity is observed on the Gram-negative Escherichia coli and the Gram-positive Bacillus subtilis. Finally, shows also anti-viral activity in a model of HCoV 229E infected L132 cells.
Subcellular location: Secreted {ECO:0000269|PubMed:19914321, ECO:0000269|PubMed:29379111}. Host cytoplasm {ECO:0000269|PubMed:29379111}.
Interaction partners:
Sequence:
MQITSIAIVFFAAMGAVANPIARESDDLDARDVQLSKFGGECSLKHNTCTYLKGGKNHVVNCGSAANKKCKSDRHHCEYDEHHKRVDCQTPV
Protein: RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) (Q5I1X5)
Organism: Mus musculus (Mouse)
Function: Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8WUF5}. Nucleus {ECO:0000250|UniProtKB:Q8WUF5}. Note=Predominantly cytoplasmic but also nuclear. {ECO:0000250|UniProtKB:Q8WUF5}.
Interaction partners:
- Cellular tumor antigen p53
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Tumor protein p73
- Tumor protein 63
- Hypoxia-inducible factor 1-alpha inhibitor
- Transcription factor p65
Sequence:
MDSEAFQHARDLLDLNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGAQAGVPSRMARYSTSPVPEHFGSRGSPQKIATDGIEARFGRSESAPSLHPYSPLSPKGRPSSPRTPIYLQPDTYSSLDRAPSPRPRAFDGAGSPHGRAPSPRPGIGPVRQPGPSTPFDYLGRAGSPRGSPLAEGPQAFFPERGPSPRPPAAAYDTAGTFGSPLLGAGGSAFTPPLRAQDDSTLRRRPPKAWNESDLDVAYEKKSSQTASYERLDVFTRPASPGLQLLPWRESSLDGLGASGKDHLTSATLPRNYKVSPLASDRRSDVGSYRRSLGSAGPSGTLPRSWQPVSRIPMPPSSPQPRSTPRQRPIPLSMIFKLQNAFWEHGAGRAVLPGSPIFSRAPPPKLPPQPPPQPQMQPQPQPQPQMQPQSQAQPQTPAPQQTWSPMNEGLLKSPAELEPEPELEVLLAPVEEAGDADEGTVTRPLSPTRLQPALPPEAQTVPELEEVARVLAEIPRPLKRRGSMEQSPAVALPPTHKKQYQQIINRLFHRHGGPGPGGPEPELSTITEGSEARAGPPAPAPPAPIPPPAPPQSSPPEQPQSMEMRSVLRKVGSPRKARRARLNPLVLLLDAALTGELDVVQQAVKEMNDPSQPNEEGITALHNAICGANYPIVDFLIAAGANVNSPDSHGWTPLHCAASCNDTAICTALVQHGAAIFATTLSDGATAIEKCDPYREGYADCATYLADVEQSMGLMHNGVVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWASLHGQEGYVPRNYFGLFPRVKSQRSKI
Protein: Proline dehydrogenase (EC 1.5.5.2) (Q5BCJ9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Proline-specific permease
Sequence:
MKAATPRPSVRALSSGRSYRTARFVSRTSNARSSLAADTNSLLQQAPPSPKKQLASPLAKLPLSSVLRSLLILSVSSSSILLKPCIYTLSALAHPKTALLDVAKNPLLNLLVKHTIYKQFNAGENKLEVQRSINAIKELGYRGVLLGYAREVLVGESKTDPRDEQASRQEIQTWLDGTLQTVDMAQEGDFVALKFTGMGIQALEYLQNQAPPSPFMDEAIKQVCDLAISRNVRLLVDAEEQAVQPGIEEWATMYQKYCNSRTPGRAIFYNTYQAYLCSTPATLARHLEISRKEGYTLGVKLVRGAYLKTEPRHLIWAKKEQTDECYDGIVEALLTRRYNHMLKPASAEHTTELPPVSVIVATHNRDSVRKAHALRLEQASRGEKSDVELSYAQLQGMADEISCELLQGFQTAGPENTKVAESPNVYKLLTWGSVKECMGFLLRRAVENTEAVGRTKQSQEAMFSELRRRARRAFGLRY
Protein: SKP1-like protein 1 (SKP1-like 1) (Q6PL11)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, a RING-box and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Subcellular location: Nucleus {ECO:0000269|PubMed:27436711}.
Interaction partners:
- Cullin-1
- Coronatine-insensitive protein homolog 1a
- Os01g0185400 protein
- F-box protein
- COP9 signalosome complex subunit 5
- Os01g0106800 protein
- Os02g0708300 protein
- Cyclin-dependent kinases regulatory subunit 1
- E2 ubiquitin-conjugating enzyme
- Protein SGT1 homolog
Sequence:
MAAEGEKKMITLKSSDGEEFEVEEAVAMESQTIRHMIEDDCADNGIPLPNVNSKILSKVIEYCNKHVHAAAAAASKAADDAASAAAAVPPPSGEDLKNWDADFVKVDQATLFDLILAANYLNIKGLLDLTCQTVADMIKGKTPEEIRKTFNIKNDFTPEEEEEIRRENQWAFE
Protein: Exocyst complex component SEC10a (AtSec10a) (Exocyst complex component 5) (X5JA13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24307681}. Secreted, extracellular exosome {ECO:0000269|PubMed:24307681}. Note=Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2. {ECO:0000269|PubMed:24307681}.
Interaction partners:
- Exocyst complex component SEC6
- Exocyst complex component SEC8
- Exocyst complex component SEC3A
- Exocyst complex component SEC15B
- Exocyst complex component EXO84B
- Exocyst complex component SEC5B
- Exocyst complex component SEC5A
- Exocyst complex component EXO70A1
- Exocyst complex component SEC3B
- Exocyst complex component SEC15A
Sequence:
MTEGIRARGPRSSSVNSVPLILDIEDFKGDFSFDALFGNLVNDLLPSFLDEEADSGDGHGNIAGVDGLTNGHLRGQSAPLSSAPFFPEVDGLLSLFKDACKELVDLRKQVDGRLNTLKKEVSTQDSKHRKTLTEIEKGVDGLFESFARLDGRISSVGQTAAKIGDHLQSADAQRETASQTIDLIKYLMEFNGSPGDLMELSALFSDDSRVAEAASIAQKLRSFAEEDIGRQGASAAAGNATPGRGLEVAVANLQDYCNELENRLLSRFDAASQRRDLSTMSECAKILSQFNRGTSAMQHYVATRPMFIDVEVMNSDIRLVLGDHGSQPSPSNVARGLSALFKEITDTVRKEAATITAVFPTPNEVMAILVQRVLEQRVTGILDKILAKPSLMSPPPVQEGGLLLYLRMLAVAYERTQELAKDLRAVGCGDLDVEDLTESLFSSHKDEYPEHERASLKQLYQAKMEELRAESQQVSESSGTIGRSKGASISSSLQQISVTVVTDFVRWNEEAITRCTLFSSQPATLAANVKAIFTCLLDQVSVYITEGLERARDSLSEAAALRERFVLGRRVAAAAASAAEAAAAAGESSFKSFMVAVQRCGSSVAIVQQYFANSISRLLLPVDGAHAASCEEMSTALSKAEAAAYKGLQQCIETVMAEVDRLLSSEQKSTDYRSTDDGIASDHRPTNACIRVVAYLSRVLESAFTALEGLNKQAFLTELGNRLEKLLLTHWQKFTFNPSGGLRLKRDLNEYVGFVKSFGAPSVDEKFELLGIIANVFIVAPDSLPTLFEGSPSIRKDAQRFIQLREDYKSAKLATKLSSLWPSLS
Protein: Myosin regulatory light chain (RMLC) (P13833)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Myosin-2 heavy chain
- Myosin, essential light chain
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco11
Sequence:
MASTKRRLNREESSVVLGEEQVAELKEAFELFDKDRTGFIKKDALKTTCKQFGVFVMEDQLDAMFAEADTTKSGAIGFPEFMSMMSRRMKQTSNEQILMNAFKTFDPEGNGYILTKDLSKALTTLGDKLTEAELQELLSISENEQKQVKYDLFVNTLFSKK