wanglab/gogpt-training-data huggingface dataset:
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) (PDKII) (Q15119)
Organism: Homo sapiens (Human)
Function: Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- [Pyruvate dehydrogenase
- Signal transducer and activator of transcription 5A
- [Pyruvate dehydrogenase
- RAC-alpha serine/threonine-protein kinase
Sequence:
MRWVWALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS
Protein: ATF/CREB activator 2 (Chromosome stability protein CST6) (P40535)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources.
Subcellular location: Nucleus.
Interaction partners:
- Protein NAM8
- General control transcription factor GCN4
- CRE-binding bZIP protein SKO1
Sequence:
MFTGQEYHSVDSNSNKQKDNNKRGIDDTSKILNNKIPHSVSDTSAAATTTSTMNNSALSRSLDPTDINYSTNMAGVVDQIHDYTTSNRNSLTPQYSIAAGNVNSHDRVVKPSANSNYQQAAYLRQQQQQDQRQQSPSMKTEEESQLYGDILMNSGVVQDMHQNLATHTNLSQLSSTRKSAPNDSTTAPTNASNIANTASVNKQMYFMNMNMNNNPHALNDPSILETLSPFFQPFGVDVAHLPMTNPPIFQSSLPGCDEPIRRRRISISNGQISQLGEDIETLENLHNTQPPPMPNFHNYNGLSQTRNVSNKPVFNQAVPVSSIPQYNAKKVINPTKDSALGDQSVIYSKSQQRNFVNAPSKNTPAESISDLEGMTTFAPTTGGENRGKSALRESHSNPSFTPKSQGSHLNLAANTQGNPIPGTTAWKRARLLERNRIAASKCRQRKKVAQLQLQKEFNEIKDENRILLKKLNYYEKLISKFKKFSKIHLREHEKLNKDSDNNVNGTNSSNKNESMTVDSLKIIEELLMIDSDVTEVDKDTGKIIAIKHEPYSQRFGSDTDDDDIDLKPVEGGKDPDNQSLPNSEKIK
Protein: Small toxic protein TisB (LexA-regulated protein TisB) (A5A627)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system (Probable). Overexpression causes cessation of growth, induces stress-response, a number of membrane protein genes, and leads to cell death. Inhibits ATP synthesis, ATP levels drop drastically quickly after induction. Part of the programmed response to DNA damage; damage leads to increased accumulation of the protein which slows or stops bacterial growth, probably allowing DNA repair before cells continue to grow.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18761622, ECO:0000269|PubMed:24513967}; Single-pass membrane protein {ECO:0000269|PubMed:18761622, ECO:0000269|PubMed:24513967}.
Interaction partners:
- Small toxic protein ShoB
- Uncharacterized protein DinQ
- Toxic protein SymE
- Small toxic polypeptide LdrD
- Toxin GhoT
- Toxic protein HokB
- Serine/threonine-protein kinase toxin HipA
- LexA repressor
- Endodeoxyribonuclease toxin RalR
- Ribosome association toxin RatA
Sequence:
MNLVDIAILILKLIVAALQLLDAVLKYLK
Protein: Antifreeze protein type IV (Type IV antifreeze protein) (Zgc:161979) (Q4L216)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Antifreeze protein type IV
- 40S ribosomal protein S8
- Zinc finger, FYVE domain-containing 9b.
- SPRY domain-containing SOCS box protein 3
- SplA/ryanodine receptor domain and SOCS box-containing 3b.
- SPRY domain-containing SOCS box protein 3
Sequence:
MKFSLIAVIVVALAIGSESASLVKRDAPAELDKIAKYFQDLVDNLKNVEGAELANKANAYLEQSRAQFQPMVEKLQEQLKPFSGNIEEQIKPLAASVQSQVAPLAGMVQTHVEDMIKFVADQAKAMLPPQ
Protein: Glutathione S-transferase A4 (EC 2.5.1.18) (GST class-alpha member 4) (Glutathione S-transferase A4-4) (O15217)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4-hydroxynonenal (4-HNE).
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase A2
- Epoxide hydrolase 1
- Cytochrome P450 2E1
- Glutathione reductase, mitochondrial
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Cytochrome P450 3A4)
- Glutathione synthetase
Sequence:
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
Protein: Outer membrane protein assembly factor BamB (P77774)
Organism: Escherichia coli (strain K12)
Function: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00923, ECO:0000269|PubMed:15851030, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00923, ECO:0000269|PubMed:15851030, ECO:0000269|PubMed:27686148}.
Interaction partners:
- Outer membrane protein assembly factor BamA
- Outer membrane protein assembly factor BamD
- Outer membrane protein assembly factor BamE
- Outer membrane protein assembly factor BamC
- Chaperone SurA
- Ancillary SecYEG translocon subunit
- Chaperone protein Skp
- LPS-assembly protein LptD
- Translocation and assembly module subunit TamB
- Histidine--tRNA ligase
Sequence:
MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLRGESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVTLWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQKVDSSGFQTEPVAADGKLLIQAKDGTVYSITR
Protein: Dehydrodolichyl diphosphate synthase complex subunit Nus1 (EC 2.5.1.87) (Nogo-B receptor) (NgBR) (Nuclear undecaprenyl pyrophosphate synthase 1 homolog) (Q99LJ8)
Organism: Mus musculus (Mouse)
Function: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length. Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96E22}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96E22}. Note=Colocalizes with Nogo-B during VEGF and wound healing angiogenesis. {ECO:0000250|UniProtKB:Q96E22}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit Dhdds
- Reticulon-4
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Geranylgeranyl pyrophosphate synthase
- Protein farnesyltransferase subunit beta
- All trans-polyprenyl-diphosphate synthase PDSS1
- Farnesyl pyrophosphate synthase
- All trans-polyprenyl-diphosphate synthase PDSS2
- Squalene synthase
- Ribosome-recycling factor, mitochondrial
Sequence:
MTGLYELVWRVLHALLCLHLTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPRAVGRNRRHHRHPHGGPGPGPGPAATHPRLRWRADVRSLQKLPVHMGLLVTEEVQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGQDCSKYSAEFANSNDKDDQDLNCPSAVKVLSPEDGKADIVRAAQDFCQLVAQQQRKPTDLDVDLLGSLLSSHGFPDPDLVLKFGPVDSTLGFLPWQIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK
Protein: Exocyst complex component 3 (Exocyst complex component Sec6) (Q9V8K2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 6
- Exocyst complex component 4
- Exocyst complex component 1
- Rab11
- Protein ROP
- LD44762p
Sequence:
MDLQQLEEQARQAALKDIQNMLQRPGQLEKVEQYRHRIARKKASVEALLKTGMQGQLDGVRVGLKQLETCMQDVREVRRRMDEVERLLRGVPEVYDALEVVREENTKHSQYATAMENLKHIFNVDASVQKTMALIEDDKLLNAHQCLADLENSRDDLLYELHKQPKQHASDKITLKRHFEKVDTVSQELEKKLRLILSRTLNTLRKKPTIIVTALRIIEREEKNDQFALQQQKVTGFLPPGRPKAWRRMIMDVLQQSVITRIEGSKLEERADNKMWLVRDLEILRQIILEDLRVVKSLCVPCFPPHYDIFGEYVKFYHEGLSSYLDNIVRSGLEGNEYVSMMAWVTHTYPGVELMSHPDLNVDVHRQIGTLLRPEHLKALEDEYLQNMQRNFQEWMTKAAETEKQEWFTETVPDQDEEYYHTSAPVIIFQMIDQHLQVTNTIHQELTFKALVMSIQQVEIFGQTYLKNVIELKEHHFRNRDQIKYFTHYIITIVNNSQQMVELAQQMKQLYWPKSRTEHYEDFERLLATFQRIRAHAASYLLEEAFLDMECHFNDLFTAKWLASNIAVDTICVTLDDYFQDYNHLRPNNFEMVINEAQKLLAKRYIRALLSKRLSKPRAECDAITRKIKTEAKRFKLFFEKIAPKISLSDSPLDLISTLSALLSSDIELLVLDLHTLLGSYPSLNEDHLVRLFYIRNDVKAAEVREKVQDAMKSKKAMVSIAKQDCIFKEIVFSDKLW
Protein: 60S ribosomal protein L7a (Q57VM1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S26
- 40S ribosomal protein S16, putative
- 40S ribosomal protein S8
- 60S ribosomal protein L29
- Uncharacterized protein
- 60S ribosomal protein L19, putative
- Polyubiquitin, putative
- 40S ribosomal protein S18, putative
- Large ribosomal subunit protein eL18
Sequence:
MAGKEVKKAVKPTKKAGVPYKKPEVTQKKAKASAAAPSPFVARPKDFGIGRDVPYARDLSRFMRWPTFVTMQRKKRVLQRRLKVPPALNQFTKVLDRSSRNELLKLVKKYAPETRKARRDRLTKVAEEKKKNPKGTVSTKAPLCVVSGLQEVTRTIEKKTARLVLIANNVDPIELVLWMPTLCRANKIPYAIVKDKARLGDAIGRKTATCVAFTDVNAEDQAALKNLTRSVNARFLARSDVIRRQWGGLQLSLRSRAELRKKRARTAGNDAAAKAA
Protein: Pyruvate carboxylase (EC 6.4.1.1) (A0A0H3JRU9)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Interaction partners:
Sequence:
MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKATD
Protein: ComC supersandwich domain-containing protein (Q54FJ6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNIILILIIFLFFGNSISKLIPSETDCLYNLIVLSKNANTFKLRNDSNWGYYCEDYPNNFKCSDDKGLLTSLTMNGASVIKIDSNNLNCFQKENLIFNLSLFSLDNNFFFQGNNFKNYSFELNNCIIQSISNPIKNIDSLTISTNNLLQIALNASIPVSSLIELTSFTLLNNLPSGELYYFYTNDLSSTSSKSRIKSIDSVTRNIPSLTYVDSVESVNLYFTSGVKNDLSNLTSYLNVKTLQLNGGSSGLSYTFPSDSIKSLTNLNTLILNNIQFTKPTDGSIDLSTMTSLKSITIVNPGLFSTDAIKALPMKSLKSFSITQCSIKSGYPIPGIFNKANSVIESISITSCGMPDNLDIVLPLPKSLRYLELTNNPLKGTISNQFCTLQTLKLPNSILINGILPSCFSCHFKNNVILKSNLNLAIGVINIQNCTNLIANLKIDSILNRTIIYGSDLGFDTSYFTTTPSTNDWIVDIPSNQFYRNSVDINTFTFNFIYPSISMTLSTSGPVVTSVYVSNVGLLTIKGTGFSYSISGTIYTILNDQYCQIRSTTFDTIICQLFAYTNITKTKIDATSVLKITGQPDYIFNVTYLPDFTNYYLTCNQNCTGKGFCDRNSGECICNCHNKGSCDIRNKVCKCFTFWLGDQCIIPDHYVSSVVASNILGGNVTLKGWYGDDHVNPSVFIGGLECTPIYEIGYSSIKCLIGPGSGVKSVTVIQNGHSWAGQNIYLYNNTLLNCPNDCTNSTMGICDQRIGQCNCLKSNFIGPDCSIEVVQQPPKSNTTVDTGTGSTDLNNDKTKYTIKIKKLLELDFNNNPVNTIDLFENNWNFKKINSTSNNNNNNNNSNNLYIFNKIVPLKCNITYIIEEVENDKEFTFADITFKVTSGSIKLTVEINNYTYISGLNTLQLQMESSVGLTKNEDGTINGQQCDIANIENIDTENSALNYVTITKDGTVLYGRFINRALSDHRPTFITSQIVEKNISSITVGLNLPHCIDCIIDPDFSILVQNKEFKSDCKSGNSDDNERVWFLPVVIVVPVVSATIIVILSLVVYTKYRRALRLKLQSLMDPKTIKMNDLN
Protein: Alpha-(1,3)-fucosyltransferase FucT (EC 2.4.1.152) (4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase) (O30511)
Organism: Helicobacter pylori (Campylobacter pylori)
Function: Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor.
Subcellular location: Membrane {ECO:0000269|PubMed:9261149}; Peripheral membrane protein {ECO:0000269|PubMed:9261149}. Cytoplasm {ECO:0000269|PubMed:9261149}. Note=Predominantly localizes at the membrane. {ECO:0000269|PubMed:9261149}.
Interaction partners:
Sequence:
MFQPLLDAYVESASIEKMASKSPPPLKIAVANWWGDEEIKEFKNSVLYFILSQRYTITLHQNPNEFSDLVFGNPLGSARKILSYQNAKRVFYTGENESPNFNLFDYAIGFDELDFNDRYLRMPLYYDRLHHKAESVNDTTAPYKLKDNSLYALKKPSHCFKEKHPNLCAVVNDESDPLKRGFASFVASNPNAPIRNAFYDALNSIEPVTGGGSVRNTLGYNVKNKNEFLSQYKFNLCFENTQGYGYVTEKIIDAYFSHTIPIYWGSPSVAKDFNPKSFVNVHDFKNFDEAIDYIKYLHTHKNAYLDMLYENPLNTLDGKAYFYQNLSFKKILAFFKTILENDTIYHDNPFIFCRDLNEPLVTIDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRINYDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRVNYERLLSKATPLLELSQNTTSKIYRKAYQKSLPLLRAIRRWVKKLGL
Protein: Chromatin target of PRMT1 (X6R700)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLKNKQPTPVNIRASMQQQQQLASARNRRLAQQMENRPSVQAALKLKQSLKQRLGKSNIQARLGRPIGALARGAIGGRGLPIIQRGLPRGGLRGGRATRTLLRGGMSLRGQNLLRGGRAVAPRMGLRRGGVRGRGGPGRGGLGRGAMGRGGIGGRGRGMIGRGRGGFGGRGRGRGRGRGALARPVLTKEQLDNQLDAYMSKTKGHLDAELDAYMAQTDPETND
Protein: TAP binding protein (A0A8J8Y6W0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLLPLLVVVALGLATVVVSAGPQTIECWFVEDAGGGGLSKKPATLLLRHGPRGPPPRPDLDPKLYFKVDVCAFRPVYNPAGMLLAMSSYIPFPASAKWARGLSPQQNCSRALDGDWLMVSVSGTVFSLSSLLRPLPEPQREPVFITMATVVLTVLTRHPAPRIHLGKDAVLDLRFAYAPPALEDAPSVASGPPPFGLEWRRQHRGKGHLLLAAIPGLLEKMPPAREKAVAFAAWDDDNDPWGPWTGNGTLWLPAVSPSQEGVYLATVHLPYLQGQVSLELTVHKPPRVSLTPAPIVWAAPGEAPPELLCLVSHFYPEEGLEVEWELRGGPEGSSRKAEGKTWVSTVRHHSDGSVSQSGHLQLPPVTDKQHGVRYACRVRHPSLPSSGRSAEVTLEVAGFSGPSIEDGIGLFLSAFLLLGLFKALGWMAAYLTIPKILKEKASATSLTVPKDEKVRVQVLWPVFPGIAPQRPM
Protein: Small ribosomal subunit protein uS3y (40S ribosomal protein S3-2) (Q9M339)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS26z
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS26x
- Small ribosomal subunit protein eS26y
- Small ribosomal subunit protein uS17z
- Small ribosomal subunit protein uS5z
- Small ribosomal subunit protein eS28z/eS28y
Sequence:
MTTQISKKRKFVADGVFYAELNEVLTRELAEDGYSGVEVRVTPMRTEIIIRATRTQNVLGEKGRRIRELTSLVQKRFKFPVDSVELYAEKVNNRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFVMESGAKGCEVIVSGKLRAARAKSMKFKDGYMVSSGQPTKEYIDSAVRHVLLRQGVLGIKVKVMLDWDPKGISGPKTPLPDVVIIHSPKEEEAIYAPAQVAAPAALVADAPLTAVDYPAMIPVA
Protein: Secreted protein BARF1 (33 kDa early protein) (p33) (P0CW72)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Plays diverse functions in immunomodulation and oncogenicity, maybe by acting as a functional receptor for human CSF1. May inhibit interferon secretion from mononuclear cells. Exhibits oncogenic activity in vitro (By similarity).
Subcellular location: Secreted. Note=Massively secreted in the serum of EBV-induced nasophyryngeal carcinoma patients. {ECO:0000250}.
Interaction partners:
Sequence:
MARFIAQLLLLASCVAAGQAVTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFIEWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEAHGVYVSGYLSQ
Protein: Dolichol-phosphate mannose synthase subunit 2 (DPM synthase subunit 2) (Dol-P-Man synthase1) (Dolichol phosphate-mannose biosynthesis regulatory protein) (Q9CA79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPMS1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21558543}; Multi-pass membrane protein {ECO:0000255}. Note=May serve as regulatory subunit and membrane anchor for DPMS1. {ECO:0000269|PubMed:21558543}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 1
- dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannose synthase subunit 3
- Phosphatidylinositolglycan-like protein
- N-acetylglucosaminyl transferase component family protein / Gpi1 family protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase, GPI19/PIG-P subunit
- Dol-P-Man:Man
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Sequence:
MELADRAVGLLLSSISLSIFTYYTFWVIILPFVDSDHFIHKYFLPQDYAILVPVFAGIALLSLISVFIGMVMLKSKKKKA
Protein: Angiotensin-converting enzyme (EC 3.4.-.-) (A0NFU8)
Organism: Anopheles gambiae (African malaria mosquito)
Interaction partners:
- AGAP009750-PA
Sequence:
NRFGITCKGLFIPSVQQYVSDGDSANSSSRPVFPVQVLINGLAETIQWDWNVRRDSEKHIMASNIQWRSVWLMLLFASTIAAGPVKRRSTESEKAPSETEISQIVEWIEQRYQQTKAHQTLAAWEYGSNLTEFNLSKKTKAAADFAEVAKAVAEELQQFKTDQLTNATLKRRIKKLAKLGYAALPADQFKELLGAIASMESNYAKAKFCAYGDATKCDLSLDPELTEIFANHREPEELKYYWVQWYNATGAPVRESFQKYVELNRQAALRNNFSSGAAVWLNEYDDSTFEQQVDDVIEQIRPLYEQLHAYVRYKLRQKYGDKLVSPTGPIPMHLLGNLWAQTWDNIADFTTPFPEKKLLDVTDEMIRQGYTPIKMFQMGDDFFTSLNMTKLPQTFWDKSILEKPTDGRDLVCHASAWDFFAIDDVRIKQCTRVNMREFFVVHHELGHIQYYLQYQHQPVEFRGGANPGFHEAVGDVLSLSVSTPKHLKKVGLLKDYEEDEQVKINQFYRAGVTKLVFLPFAYTLDKYRWGVFRGDIKPREYNCKFWEMRSRYSGVEPPVVRTEQDFDPPAKYHVSADVEYLRYFVSYVIQFQFHRAACALAGEYVKGDPEKTLNNCDIYQSTAAGNQLKEMLALGSSKPWPDAMEVLTGERKMSADAILEYFDPLYQWLLEENKRLGAHVGWTDSQKCVSHPIDFMAA
Protein: Uncharacterized protein (Q382S7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSAVATDPSVPTGKSESEALVAQRECTWKVVKAGEGLERQQTWEKSSTHESTGCPTLPTVRSASQGGKEVEDTMSSSRRLRWGHLSNASVPALESAAPKAGLEEQAHASEVKKPAVPCRISPSGIPVERYRQKLEECASLHHQLQEMVSAHCVTQEQLCGVRAECDCLKNEIVRLRDLLATTTSELGIQQQHVVELERENLKLREELREKQVEGMTSQRKMNYILSNSTVSPQGGGVATYTRYSPRPSPATLVLPVTPTLMVQPGLTGAKNVLDAVELYVRECFRTNVLPHVELIHSLYDGGRLAAVDPPLTHAQLKALQRVLADVKWEVEVSGIPVETYVSRKPRLQGRSQRLKDPDGSYPLWFNKLETLTFRSESWRTCLGFDCRRSYVP
Protein: Uncharacterized protein C1604.12 (O94378)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adhesion defective protein 1
- Phospholipid-transporting ATPase C887.12
- Translation initiation factor eIF2B subunit gamma
- Uncharacterized protein C1805.14
- E3 ubiquitin-protein ligase gid2
- Uncharacterized N-acetyltransferase C9.02c
Sequence:
MERIQENDPIIKSADESKESPAETLSSIFKRPKIKSSSLNKAYLGKAGSVNGASNTSTNQISSLKVDVSSPPSTAPGSAGSTPKTTPVSLNAGVPPSNTGANITTNSNNNAQTISSSSQSVGHIDNPSGLGTHGKVRLSIKLSTGGSGGSSVTGKRTAPGNPWAIRSAERLASNPTSIGTSSPESIDNNSNNKKSAPSLYAAAAASAARHSMSAAYASFTGTVYDSNGNVIKGLDTSSSLSSSSHPSHEALSTIDTKNLQALAASAAPSSCRQQPVDEERQDRVSKISKHFQDSGTPVSEEVSPTRLPSPTSARRASHLSEGKWDEIDDEDDDDWGSTIEFEDGTTVVIDAKTRRYEPVKRQDTLASNHVPSAPSNESVSSAAPSKIPVPEEASINEHSNITDEAVSLPEPVYPNAPTSAVSVHNPTISDEAEPTERAFLKKEKPQISKEKKNPNVTHEEFVEKSTALPRHINKVEIVSDSSESFAHKNNEKRFDKEASGRINDLRAEQQQIMLEARQKAIERRRNEEEELARSRERARKKAEEIKISSSKMNSSPTITNERSSNVESSKKVEAIYTKEPQSITNSPEGLHSNQETTEIDPSSPRDDSTPLSWRSHSHPIPPVQVSPLFTSDKNDPLQLNPQSDDSTSSPKHGKSRSIDEVILSIKDVIFDNNLYKQRSYQSGVAANAHLPHRVPNEHGGVSRIGNSNALGQPVSSSSSYSHSKGRDTRSSSYVVSSETSSLKSSRLILSHANSVRIQRSKGDVILNLHLPKVNPERFLPTKSLKLEEMKPLEEKVPIYRSSSKQPLRIHPTHPLRVTVCLPGSKTIQVARRSFRNSMNANRYDPQRRERIDSGLWRAKN
Protein: Sodium stibogluconate resistance protein (Q57ZF5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- EF-hand domain-containing family member C2
Sequence:
MGGGSSVEDKRYSRLFQEGLKALHEGRFTYAEIYFDQAIEKHEGYPFWQRLDEMVEWERKGNTGKRKGEEQNEKDQWAKETKPETGGGEGAGEDGAEMDDLGGESDDTGVLVIPLDQRVFHVLEYLQLRTDISVAYLLAERYEEAHEHLQYVTSHTHVLLKCLRIARQSNMSEESGGEGGDTNPLEHVGVVERRFRAGLMGMEVEVEGILDAFEQYLRLHWFSGIANTVYIAFERFKGGQGDKKRKRELDAVVVTCETAKLELHKLVSRRAKSLTNSVLIEFLEKLINDMDSSASDSEDDGNANGGRSGGPAAKGRRKSDNREDGDKEELENFPFSARLQMLYERRLLYRGMPAPMQGAALRYLPWMDEDIRRVVPGTNYNLEIQCGMIDDRRKKQLQKKSLKHTVQKRFDFNDRVLFNKSMDEENALLLFPLLLVEADVQLELGAATKGIKALDMVEKLSTQLYGRQSLEQQSLMRRVLETRKRGGALFMMFDDQLN