wanglab/gogpt-training-data huggingface dataset:
Protein: Dishevelled associated activator of morphogenesis, isoform A (Q7YZA4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPSVDELDTKFAELVEELDLTAPNKEAMLSLPAQKKWQIYCSRKLPLDAADGPDAAAVTQPPTAEHYIERLKELVVHISLSPEDSPSHELGNRLDGHAAFVDALKTALRTSTHSFVLRFVELDGLPALLDLLLQLDIRVANSPLHTSLIGCIKALMNNSMGRAHVLAHPTAIDTIARSLAADNIRTKIAALEILGAVCLVPGGHRKVLQAMLHFQVFATERTRFQSIVNDLDRSTYAYRDNVNLKTALMSFVNAVLNYGPGQENLEFRLHLRYEFLMLGIQPVIDKLRTHENETLDRHLDFFEMVRAEDEKEFARRFKEEHVDTKSAGSMFELLRRKLSHSPAYPHMLSLLQHMLLLPYTGHCTEHWLLIDRVVQQIVLQVEQRPNSDLIVDPDDPEKQLKLAAESPVHDPDVAPLQIDVAKLVRLLVKEEQLTQARKRADELERENFDVQSRLAKKEQELDLRMQEKEDLETGLARMRERLEKESAQHSQAVQRAQTAEMRAEDLQHRLISEQQERARLERLVTEGSIPDDQKVAGLTGCNGAVSPPPAPPMLKAIPPPPPPMAPSMMPPPPPPCPGAPPPPPSMAQTMAPAPPKVDLPKKNVPQPTNPLKSFNWSKLPDAKLQGTVWSELDESKLYNNMELESIDKLFSAYQKNGVSATDGSYEDLRVTGKAAKQKVLSVIDGRRAQNCTILLSKLKMSDMEISKAILSMDSNEQLQLDMVEQLLKFTPSAEERALLDEHSEDIESLARADRFLYEISKIPHYEQRLKSLHYKKRFMLTINDLVPRITSVMEASREVARSRRLRKLLELVLALGNYMNRGARGNASGFRLASLNRLADTKSSAAKGTTLLHYLVQVIERKFKDLLKLEDDIPHVREASKVSLGEMDKDIQMLRTGLADVAREIEFHRSSGPAQQGDRFLPVMREFHAQASVRFAELEDKFQDMKTRFDRAVRLFGEDGSVLQPDEFFGIFDSFLAAFAEARHDNESFRRRQEEEEKRAKQEAELKKRTIERKNKTGLMTSVARNLGLKSGSSNGDPDSPAKGGDNKGEFDDLISALRTGDVFGEDMAKFKRSRKARVLNGGGSSTGHTSPPRHGSLQREESGRERERTVRRQ
Protein: Transformer-2 sex-determining protein (P19018)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for female sex determination in somatic cells and for spermatogenesis in male germ cells. Positive regulator of female-specific splicing and/or polyadenylation of doublesex (dsx) pre-mRNA. Splicing requires an enhancer complex, dsxRE (dsx repeat element: which contains six copies of a 13-nucleotide repeat and a purine-rich enhancer (PRE)). DsxRE is formed through cooperative interactions between tra, tra2 and the sr proteins, and these interactions require both the repeat sequences and PRE. PRE is required for specific binding of tra2 to the dsxRE. Protein-RNA and protein-protein interactions are involved in tra-2 dependent activation and repression of alternative splicing. Together with tra-2, plays a role in switching fru splicing from the male-specific pattern to the female-specific pattern through activation of the female-specific fru 5'-splice site.
Interaction partners:
- Female-specific protein transformer
- RNA-binding protein 1
- LD40489p
- Protein doublesex
- RNA-binding protein Rsf1
- LD32469p
- Sex determination protein fruitless
- Serine/arginine-rich splicing factor x16
- Protein sex-lethal
- Serine-arginine protein 55
Sequence:
MDREPLSSGRLHCSARYKHKRSASSSSAGTTSSGHKDRRSDYDYCGSRRHQRSSSRRRSRSRSSSESPPPEPRHRSGRSSRDRERMHKSREHPQASRCIGVFGLNTNTSQHKVRELFNKYGPIERIQMVIDAQTQRSRGFCFIYFEKLSDARAAKDSCSGIEVDGRRIRVDFSITQRAHTPTPGVYLGRQPRGKAPRSFSPRRGRRVYHDRSASPYDNYRDRYDYRNDRYDRNLRRSPSRNRYTRNRSYSRSRSPQLRRTSSRY
Protein: Vacuolar protein-sorting-associated protein 11 homolog (AtVPS11) (Q9SJ40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulating membrane fusion at the tonoplast and the prevacuolar compartment.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12589039}; Peripheral membrane protein {ECO:0000269|PubMed:12589039}. Prevacuolar compartment membrane {ECO:0000269|PubMed:12589039}; Peripheral membrane protein {ECO:0000269|PubMed:12589039}.
Interaction partners:
- Protein VACUOLELESS1
- Vacuolar sorting protein 18
- Vacuolar sorting protein 3
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar sorting protein 39
- Vacuolar protein sorting-associated protein 41 homolog
- Transducin family protein / WD-40 repeat family protein
- Vacuolar fusion protein CCZ1 homolog A
- Syntaxin-22
- Vesicle transport v-SNARE 12
Sequence:
MYQLRKFDFFEEKYGGKIPEDVTGDIQCCSSGRGKVVIGSNDGSVSFLDRGVKFDSGFQAHSSSVLFLQHLKQRNFLVTVGEDEQISPQQSGMCLKVFDLDKVQEEGTSSSAPECIGILRIFTNQFPEAKITSFLVLEEVPPILLIAIGLDNGCIYCVKGDIARERITRFKLQVDGRSAITGLGFRMDGQALLLFAVTPESVNLFSMQAQPPKLQTLDHIGGSVNTVTMSDRSELIVGRPEAVYFYEVDGRGPCWAFEGEKKFMGWFRGYLLCVIDDSKTGNTVFNVYDLRNRLIAYSIVVDKVSNMLCEWGNIILIKADKSLLCITEKDMESKLDMLFKKNLYTVAINLVQSQHADAAATANVMRKYGDHLYGKQDFDEAMLQYINTIGYLEPSFVIQKFLDAQRIYNLTNYLEKLHEKGLASKDHTTLLLNCYTKLKDVEKLNTFIRKEDGIGELKFDVETAIRVCRAANYHEHAMYVAKKAGKHEWYLKILLEDLGNYDEALQYVSSLEPSQAGVTIEQYGKILIEHKPKETIDILMRLCTEQGIPNGVFLSMLPSPVDFITVFVQHPHSLMHFLERYAEIVQDSPAQAEINNTLLELYLSRDLNFPSISLSENGLDKDLIDHSVAAAVSKADPEKKTNADSKDAMEKDCTERQQKGLELLKMAWPSDLEQPLYDVDLAVILCEMNSFKDGLLYLYEKMKFYKEVIACYMQNHDHEGLIACCKRLGDSSKGGDPSLWADLLKYFGEIGEDCTKEVKEVLTYIERDDILPPIIVLQTLAKNPCLTLSVIKDYIARKLEQESKIIEEDRRAVEKYQETTKNMRKEIEDLRTNARIFQLSKCTACTFTLDIPAVHFMCMHSFHQRCLGDNEKECPECAPEYRSVMEMKRSLEQNSKDQDLFFQQVKGSKDGFSVIAEYFGKGIISKTRDATS
Protein: Homeobox protein Meis1 (Myeloid ecotropic viral integration site 1) (Q60954)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator of PAX6. Also acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:15882575}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-A9
- Homeobox protein Hox-A7
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-B13
- Pre-B-cell leukemia transcription factor 2
- Homeobox protein Hox-A10
- Homeobox protein Hox-A5
- Protein AF-9
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MAQRYDDLPHYGGMDGVGIPSTMYGDPHAARSMQPVHHLNHGPPLHSHQYPHTAHTNAMAPSMGSSVNDALKRDKDAIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEDVTRSANLTDQPSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKDKKRHKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVSQGTPYNPDGQPMGGFVMDGQQHMGIRAPGPMSGMGMNMGMEGQWHYM
Protein: Inorganic phosphate transporter 2-1, chloroplastic (H(+)/Pi cotransporter) (AtPht2;1) (Q38954)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low affinity H(+)/Pi chloroplastic cotransporter. Involved in inorganic phosphate (orthophosphate, Pi) uptake in green parts of plants in Pi-sufficient conditions. Required for Pi retranslocation during Pi deprivation.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:12172020, ECO:0000305|PubMed:15200639}; Multi-pass membrane protein {ECO:0000305|PubMed:12172020, ECO:0000305|PubMed:15200639}.
Interaction partners:
- Probable inorganic phosphate transporter 1-3
- Inorganic phosphate transporter 1-4
- Probable inorganic phosphate transporter 1-9
- Inorganic phosphate transporter 1-1
- Probable inorganic phosphate transporter 1-5
- Probable inorganic phosphate transporter 1-6
- Probable inorganic phosphate transporter 1-2
- Probable inorganic phosphate transporter 1-8
- Probable inorganic phosphate transporter 1-7
- Ascorbate transporter, chloroplastic
Sequence:
MTLPYRFSSVRNHSLLLKTSHLCTPRSALGCCFSPKESPFFRKNTAQFLSPQKHTSLPLKLVCPLASFSSYADSEGEEQHHADQPIQNPHESSTVSNESDGKGNAEATGDFSGMAQAFHISSTTARAISIVIAFSALTLPIFMKSLGQGLALKTKLLSYATLLFGFYMAWNIGANDVANAMGTSVGSGALTIRQAVMTAAVLEFSGALLMGTHVTSTMQKGILMANVFQGKDMLLFAGLLSSLAAAGTWLQVASYYGWPVSTTHCIVGSMVGFGLVYGGAGAVFWSSLAKVASSWVISPILGALVSFLVYKCIRRFVYSAPNPGQAAAAAAPVAVFVGVASISSAALPLSKIFPIALSQALACGVAGAIVFDRIIRKQLGHLLAKTKSPETSQNQPKTIGFLSDIAGPTGTQLEIVYGIFGYMQVLSACFMSFAHGGNDVSNAIGPLAAALSILQNGAAAGGAEIVIPMDVLAWGGFGIVAGLTMWGYRVIATIGKKITELTPTRGFAAEFAAASVVLFASKLGLPISATHTLVGAVMGVGFARGLNSVRAETVREIVASWLVTIPVGATLAVIYTWIFTKILSFVL
Protein: Cyclic beta 1-2 glucan synthetase (Q2YNV7)
Organism: Brucella abortus (strain 2308)
Interaction partners:
Sequence:
MPRIFALAWLYVAHTDSNFSLKMLTAMVKGFQTVEPLKIGELWALPSAVRYFLIENARRLAMRVDRAREMRNLANTAADRIVVAAEGAELDGILAQYASAACDSTFATHLLYRLRSSSTDTTAAASWLERILEQDGSNPEDAIIEEHARQSTGGVTMGNVIRSLKSIDDVDWETWFETVNEVDAILRDHSDFELLDFRSRNAYRVTIEKLARYSDMSEIDITWAALKLAEDGSRAEKAGHPEAEGKGAISYYLSGEGRRDLEKVCGYRAPFGVKALRLYRGLGLWGLFVPTAIFTVLTLLLVNYCMMRAGLSTDLRTLFTLLAIFPAMDASYSLFNVLVPWFVQPTRLIGFEYKDGLPPEARTLVAVPTFITSRDSIDEQIRNLEVHYLTNPRGEIYFALVSDWTDASQEIVPADMEIYEYARDEIAKLNEHYTGDDQPRFFLLHRRRLFNEKQGCWMGWERKRGKLHELNLLLRGDQDTSFFPADERLPKDIKYVMTLDADTRLTPEAVTHLAGKLNHPMNRPVIDEKTGKVVRGYGILQPRVTPSLTTGDEASFLQRVFSVNRGIDPYVFAVSDTYQDLLGEGTFTGKGLYDIDAFEAALKGRVPENTLLSHDLLEGGYARSALVSDVEVVEDYPTGYNVDVSRHHRWARGDWQLLPWLFSTGRGVSAITRWKMVDNLRRSLNPILWLIAAIVGWSVLPLGAAAVWQGFLILSMFVAPTFGIVTNLIPASMDYSLKGHAQSVLTDIALGTADVALRTTFIAHSAFLMADAIARTIYRLFISRRNLLEWRTAAQARTSPDTLLFYFQLMWPAMAIAGLAIFFPLAAESHAALIAAPFVVIWFASPLIAWLVSRSAKPQDTLEVLSSDKADLRRYARRTWRYFAEFANEENNHLPPDNFQEDPAPIVAQRTSPTNIGVYLLSVIAARDFGWIGFDETLDRVEATLGSLDKMEKYQGHLYNWYETNTLNPMRPLYVSAVDSGNLAGHLVTLSSALEEWAEAPSVYVQGDLDGIIDVNDILEETIARIPDDRRVLRPLRRRLEERIANFRRAVTSIKDEPETASFRTINLSLFASDIVRLMDELDSEVETVASAEAREWARILVDTCKAHTDDAIGEHDTDALRERLRDLATRARQLAFDMQFGFLERKERRLLSIGFRVQENELDESCYDLLASEARLASLFAIAKGDVPVEHWFKLGRLLVPVGWKGALLSWSGSMFEYLMPPLVMSEPLGSLLDQTNKLVVQRQIDYATSRDLPWGISEAAFNARDAHLNYQYSNFGVPNLGLQRGLSRNAVIAPYASLLAAQYQPAAAVANLKRLAKLGALGRYGFHDSVDFTPSRIREGETCAVVKNYYAHHHGMSIIAVNNVIFEGRMRERFHNDPVIEAAELLLQEKAPREIPMIYAKTENPMRVDSGGFDDAPMRIIDKPFRAPRTTHMMSNGQYALMVTANGSGYSRWHNWDITRFHADASEDMQGTFLFLRDMESGYWWSATGEPVRNPDEETKTVFTEDKAEFYKTAGDIKTVMEVIVASEADGEGRRLDIINTSPRDRMIEVTSYAELVLNDSDSDAAHPAFAKMFVETEIADSGSTIYAKRRKRAPSAPDIHAAHFVTDLSGALREIEVETDRRAFIGRGRSLRNAAAFDPGAKFTGSQGCVLDPIVSVRTRVRVPAHKKVSLVFWTFAGGSRDAVEHAVTMHRHPETFAREYSLSWTSSQVQLYHIGIKPAEAADYQKVAAYLLYPERTLRQPPETIASGLGKQSDLWPMSISGDYPIFALRIDNEADLDVLRGVLRAQEYWRSKGLIVDVVAVNERAFSYAQDTQRAIDWIVEGFRARGGGQPHIFAVRRDQMSEESYNTLLASARIVMHAQNGSLAEQLRRSEEITVDLAARSDARTATNGQASVQGLGAAGLAPVAIERGAEERRPVVKPPVDRPRPSGDDLRFWNGYGGFAEDGSYVVRINGRTSTPHPWINVIANPSFGFHVSAEGSAFTWAGNSRDYQLTPWANDPVTNRPGEAIYILDRETGRSFAPTANVLRDEAVTYEARHGHGYSAFSAQHGELALELTHIVDAEKPVRLSRLTITNKGRSKRKLRVYGYVEWVLGNARARNVPFIVPSQDEELGALFAGNPYHPDKSGQVAFFAASEKPQSVTADRGEFIGTAGSVDRPEIVLAGKVLSGTVEAGRDPCAALALDIEVGPGEAREIVFLLGNTADQKQAKALIADMRTASFEEKLVAARHQWESFFNRVQVKTPDPAFDLMVNGWLPYQAVACRIWARAAFYQVSGAFGFRDQLQDTLSLLLVDPSLAREQILNAASRQFREGDVQHWWLPATGAGVRTLISDDVVWLGYGASLYVETTGDRFILDEKLPFLEGRKLEEGEHDAFYEPEISKETASLYEHCALALDLAVARTGKHGLPLILGGDWNDGMNLVGVKGKGESVWLGWFLAYTLKAFIPLAEARKDQKRADLWKAHVESLTAALDRDGWDGEWYRRGFYDNGRPLGSKNSDECQIDAIAQSWSVLSGVADPKRAKKAMASLEKYLLDEDNALLRLFTPPFDVTPQEPGYIKGYPPGVRENGGQYTHGATWAILALARMGKAAEAWRLFSLISPVSHGRNPDVYRVEPYVIAADIYSVAPRCGQGGWTWYTGSAGWFYRVATEGILGVTKRGDRLHFQPALPPEWEGYEAELRFGEALYRVKVVAGAKAGTIRLNGRKLAKPDEGVALKPYGEHEIVVELPKQ
Protein: Putative transporter C83.11 (O94695)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pyruvyl transferase 1
- Uncharacterized transporter C22F8.04
- Uncharacterized protein C12G12.12
- UDP-galactose transporter homolog 1
- GDP-mannose transporter
- UDP-N-acetylglucosamine transporter yea4
- UDP-galactose transporter
- UDP-glucose:glycoprotein glucosyltransferase
Sequence:
MVLRERLSHILFHEKVGFLLLCLLWYISSAVTNTTSKSIFNELRCPVTLTFLQFGFVAFFSAVCLLFRKQFLGGTGIQKPSKYVLYTTLPLSIFQIGGHVFGSLATTKIPVSTVHTVKALSPLFTVLAYRFMFRHVYSAMTYFSLVPLTFGVTLACSFELSADIVGLLYALISTCIFVSQNIFGSKIFMEAKSHSTHTKKHYNKLNLLLYSSGVAFIVMIPVWLYQEGFAYLPEVGSPVFLNLIYNGLSHFFQNILAFTLLSIISPVAYSIASLIKRIFVIVVSIIWFQQATNFTQGSGIFLTAIGLWLYDRSKKGNLYESCKVKEFEKDALELEEQTMEDEKSYPSSGTQSPFYGKNFLPQITPRLDSVVPLISDSPMTPNSVYSNEGVTSSVSGNATPASVRQSTQNDFSNSNIHDRRSSYTFQLNNFKAPQPSRLWATETVPTLKI
Protein: Myb-like protein A (P34127)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May control cellular differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MQPKRMSHNLTVGEKAGSPFNVILNAANNTNSDNSSNNSDNENDDNQNNNNNNNNNNNNNNEEEEEEDDDDDDDSQQNRHNISIPFTINKNSINNNNNLINNINNNINNMNNNMNNNNNNNNMNNNINNNGNSNISNNNTPKVEKKKTKGKWTSEEDQILIKAVNLHNQKNWKKIAEHFPDRTDVQCHHRYQKVLHPNLVKGAWTKDEDDKVIELVKTYGPKKWSDIALHLKGRMGKQCRERWHNHLNPNIKKEAWSDEEDQIIRDQHAIHGNKWAEIAKFLPGRTDNAIKNHWNSSMKRVSNNNVHLKSHAIEHSLSSQDNQDSPKSIITSSSPIPTTTTTTTTTSTTLITPPPPPLLPPPPSINKKEKKIKQPKKRNASEIEQTLSQPHINQHESSPIVFENISNGNNKIDIPAAQYLMTNGISCINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNINNNNNNNNNINNNNNNNNNNNNNNNNNNHSNVSANTNNNNNTINNNVSLQPPSQLNSNIAQLPSTPKNLAHVNIANKLNSPGELMANIVTPIKFFQTATVSMNSSSKNYNNENTNNNNNNNNNHHHHHHNNNNNNNKRPRLDFSSATPTKNNESFSADLCSQFPDILFSPIQNKNNKESFLDNSGLSPLRSPLHTNFFETPMKNYEYLDFNSPKIPNTISPLKNFNSPFNKINNHSNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNHNPNHNSHNHNNHNNNHNHNHNEFAQPQPPQGNYQQSPYKNNSTTASSTLSTPSYSNNSSISSSSCSSSSSNSASKATKVIQLSSSGIDKNSLLTINAKLNNNHHKNYLDSSSSSSSSSSSSSSSSSSSSSSSSSSSSAASSSSTPNNQSDLATVPFTPDDNVFNNNNNNNPPTPGKTKFKSRFSPNSKPYSYPQEYDNYGQSSSTPQNINNTYNSICLGTNNNNNSNSSASNSFENNEENNNENDNNGSSSGGDKVPQMDSSFMALKLLKDNPNKSLFSKARKILGLGNISSSSLSPSSFVQQISNSASASSTPTSSSSTPLSSPTTTTSSVAAAIINKISSTPKYFSNQNQNQNNNNNNNNNNISNNSNLSAFSTPGGNDHVPNFESNSFLAQSPFQDILNSQKLDQLHQLTQTNQLSKSKVLLRNHKNSNQTESNSRSTIESINSNGSNNGNNSGSSNSGSNSDKNNGKPISFRLMESSKPIEGL
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (Beta-Ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase) (P0A2C9)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Acyl carrier protein
- Enoyl-[acyl-carrier-protein] reductase FabI
- Elongation factor Ts
- 30S ribosomal protein S1
Sequence:
MSFEGKIALVTGASRGIGRAIAETLVARGAKVIGTATSENGAKNISDYLGANGKGLMLNVTDPASIESVLENIRAEFGEVDILVNNAGITRDNLLMRMKDDEWNDIIETNLSSVFRLSKAVMRAMMKKRCGRIITIGSVVGTMGNAGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIASAVAFLASDEASYITGETLHVNGGMYMV
Protein: Repressor protein c (Repc) (CI) (Gene product 1) (gp1) (Mu repressor) (MuR) (P06019)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Promotes latency by binding operators O1 and O2 in the enhancer/operator region, thereby repressing the transcription from the Pe (early) promoter and blocking the expression of the genes required for replication (lytic growth). Competes with DDE-recombinase A for binding to the internal activation sequence (IAS), which overlaps O1 and O2. The outcome of this competition determines if the virus enters latency or starts replication. Makes the cell immune to superinfection by repressing genes expression of any subsequent incoming viral genome.
Subcellular location: Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MKSNFIEKNNTEKSIWCSPQEIMAADGMPGSVAGVHYRANVQGWTKQKKEGVKGGKAVEYDVMSMPTKEREQVIAHLGLSTPDTGAQANEKQDSSELINKLTTTLINMIEELEPDEARKALKLLSKGGLLALMPLVFNEQKLYSFIGFSQQSIQTLMMLDALPEEKRKEILSKYGIHEQESVVVPSQEPQEVKKAV
Protein: Pyroglutamylated RF-amide peptide receptor (AQ27) (G-protein coupled receptor 103) (Orexigenic neuropeptide QRFP receptor) (SP9155) (P83861)
Organism: Mus musculus (Mouse)
Function: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Orexigenic neuropeptide QRFP
Sequence:
MQALNITAEQFSRLLSAHNLTREQFIHRYGLRPLVYTPELPARAKLAFALAGALIFALALFGNSLVIYVVTRSKAMRTVTNIFICSLALSDLLIAFFCIPVTMLQNISDKWLGGAFICKMVPFVQSTAVVTEILTMTCIAVERHQGLIHPFKMKWQYTTRRAFTILGVVWLAAIIVGSPMWHVQRLEIKYDFLYEKEHVCCLEEWASPMHQRIYTTFILVILFLLPLVVMLVLYSKIGYELWIKKRVGDSSALQTIHGKEMSKIARKKKRAVVMMVTVVALFAACWAPFHVVHMMVEYSNFEKEYDDVTIKMVFAVAQTIGFFNSICNPFVYAFMNENFKKNFLSAVCYCIVRETFSPGQKPGNSGISMMQKRAKLSRSQRPVAEAKGDLFSDANVDVKLCEQPGEKRQLKRQLAFFSSELSENSTFGSGHEL
Protein: Succinate dehydrogenase assembly factor 1, mitochondrial (SDH assembly factor 1) (SDHAF1) (LYR motif-containing protein 8) (A6NFY7)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:19465911}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase assembly factor 2
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB
- Succinate dehydrogenase assembly factor 3, mitochondrial
- Succinate dehydrogenase assembly factor 4, mitochondrial
- Stress-70 protein, mitochondrial
Sequence:
MSRHSRLQRQVLSLYRDLLRAGRGKPGAEARVRAEFRQHAGLPRSDVLRIEYLYRRGRRQLQLLRSGHATAMGAFVRPRAPTGEPGGVGCQPDDGDSPRNPHDSTGAPETRPDGR
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4JNU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADSPQRRRDSRSPSPRKERARSRSRSRSRSRSRPRLRSRSRSLPRPVSPSRSRGRSRSRSRGRSEVENPGTTLYVTGLSTRVTDKDLEAHFAKEGKVASCFLVMEPRTRVSRGFAFVTMSSLKDAERCIKYLNQSVLEGRYITVERKILHQATIRDDKSTHPCSTSLSETQLDQSNRQLKHNHKQLYCLNSQLSTSQRTLSIQEKAPENSHPRPLSWLEKLQRQRSRRP
Protein: Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (O51244)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
Interaction partners:
- Acyl carrier protein
- Arginine--tRNA ligase
- Valine--tRNA ligase
- Tryptophan--tRNA ligase
- Putative membrane protein insertion efficiency factor
- Methionine--tRNA ligase
- Histidine--tRNA ligase
- Cysteine--tRNA ligase
- Elongation factor Tu
- Glycine--tRNA ligase
Sequence:
MLDLKFIRDNLDLVKRSIKARGLVLDIDKLIYLDDKRKKLITKIGELNAKRNENSSKMQENLDKVLKISLIETGKILKKQLIDLEEELERVSVDFDLENKKVPNILSPDVPIGSSEEDNFEIKRVGVVPQFDFKPKDHLELGRDLDLLDFDRAREISGSKFYYLKNEAVFLEIALINFSLNKLRDKGFDVFITPDVAREFIVDGIGFNPRGNESNIYKIEDTDKYLVGTSEITLGGYYYNKIIDLTLPIRMAGFSHCFRKEAGAYGQLSKGLYRVHQFSKVEMFCFCKAEESGVIHDEFLSIQEQIFTELEIPYRVLNICSFDLGSPAYKKYDIEAWMPGRDGKGGYGEVTSTSNCTDYQSRRLKIRYKDQDGQNKFAHMVNGTAIATTRVIISILENFQDQKGGVRIPKSLVKYTGFDYIPFKN
Protein: Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B) (Q5JSZ5)
Organism: Homo sapiens (Human)
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit I
- Ras GTPase-activating protein-binding protein 2
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit E
Sequence:
MSDRLGQITKGKDGKSKYSTLSLFDKYKGKSVDAIRSSVIPRHGLQSLGKVAAARRMPPPANLPSLKSENKGNDPNIVIVPKDGTGWANKQDQQDPKSSSATASQPPESLPQPGLQKSVSNLQKPTQSISQENTNSVPGGPKSWAQLNGKPVGHEGGLRGSSRLLSFSPEEFPTLKAAGGQDKAGKEKGVLDLSYGPGPSLRPQNVTSWREGGGRHIISATSLSTSPTELGSRNSSTGDGAPSSACTSDSKDPSLRPAQPVRKGASQFMGNVYHPPTYHDMLPAFMCSPKSSENQGTVERGSFPLPQLRLEPRVPFRQFQMNDQDGKENRLGLSRPLRPLRQLVERAPRPTIINAENLKGLDDLDADADDGWAGLHEEVDYSEKLKFSDDEEEEEVVKDGRPKWNSWDPRRQRQLSMSSADSADAKRTREEGKDWAEAVGASRVVRKAPDPQPPPRKLHGWAPGPDYQKSSMGSMFRQQSIEDKEDKPPPRQKFIQSEMSEAVERARKRREEEERRAREERLAACAAKLKQLDQKCKQARKAGEARKQAEKEVPWSPSAEKASPQENGPAVHKGSPEFPAQETPTTFPEEAPTVSPAVAQSNSSEEEAREAGSPAQEFKYQKSLPPRFQRQQQQQQQEQLYKMQHWQPVYPPPSHPQRTFYPHHPQMLGFDPRWMMMPSYMDPRITPTRTPVDFYPSALHPSGLMKPMMPQESLNGTGCRSEDQNCVPPLQERKVTPIDSPPVWSPEGYMALQSKGYPLPHPKSSDTLAMDMRVRNESSFSASLGRAGGVSAQRDLFEERGEEYLSAFDKKAQADFDSCISSQRIGQELLFPPQENVQDAGAPGGHTQNLRCSPLEPDFVPDEKKPECGSWDVSHQPETADTAHGVERETPREGTAFNISSWDKNGSPNKQPSSEPEWTPEPRSSSSQHPEQTGRTRRSGPIKKPVLKALKVEDKEKELEKIKQELGEESTRLAKEKEQSPTAEKDEDEENDASLANSSTTTLEDKGPGHATFGREATKFEEEEKPDKAWEARPPRESSDVPPMKRNNWIFIDEEQAFGVRGQARGRGRGFREFTFRGRPAGGNGSGLCGGGVLGARSIYCSSQRSGRGRGLREFARPEDCPRAKPRRRVASETHSEGSEYEELPKRRRQRGSENGNEGSLLEREESTLKKGDCRDSWRSNKGCSEDHSGLDAKSRGPRAFGRALPPRLSNCGYGRRTFVSKESPHWQSKSPGSSWQEYGPSDTCGSRRPTDRDYVPDSYRHPDAFGGRGFEDSRAEDKRSFFQDEHVADSENAENRPFRRRRPPRQDKPPRFRRLRQERESLGLWGPEEEPHLLAGQWPGRPKLCSGDKSGTVGRRSPELSYQNSSDHANEEWETASESSDFSERRERREGPGSEPDSQVDGGLSGASLGEKKELAKRSFSSQRPVVDRQSRKLEPGGFGEKPVRPGGGDTSPRYESQQNGTPLKVKRSPDEALPGGLSGCSSGSGHSPYALERAAHASADLPEASSKKAEKEAKLAAPRAGEQGEAMKQFDLNYGSAIIENCGSSPGEESEVGSMVGEGFIEVLTKKQRRLLEEERRKKEQAVQVPVKGRGLSSRIPPRFAKKQNNLCLEQGDVTVPGSSLGTEIWESSSQALPVQAPANDSWRKAVTAFSSTETGSAEQGFKSSQGDSGVDLSAESRESSATSSQRSSPYGTLKPEEMSGPGLAEPKADSHKEQAPKPSEQKDSEQGSGQSKEHRPGPIGNERSLKNRKGSEGAERLQGAVVPPVNGVEIHVDSVLPVPPIEFGVSPKDSDFSLPPGSASGPTGSPVVKLQDALASNAGLTQSIPILRRDHHIQRAIGLSPMSFPTADLTLKMESARKAWENSPSLPEQSSPGGAGSGIQPPSSVGASSGVNYSSFGGVSMPPMPVASVAPSASMPGSHLPPLYLDGHVFASQPRLVPQTIPQQQSYQQAAAAQQIPISLHTSLQAQAQLGLRGGLPVSQSQEIFSSLQPFRSQVYMHPSLSPPSTMILSGGTALKPPYSAFPGMQPLEMVKPQSGSPYQPMSGNQALVYEGQLSQAAGLGASQMLDSQLPQLTMPLPRYGSGQQPLILPQSIQLPPGQSLSVGAPRRIPPPGSQPPVLNTSREPSQMEMKGFHFADSKQNVPSGGPVPSPQTYRPSSASPSGKPSGSAVNMGSVQGHYVQQAKQRVDEKPSLGAVKLQEAPSAASQMKRTGAIKPRAVKVEESKA
Protein: Chromaffin granule amine transporter (Solute carrier family 18 member 1) (Vesicular amine transporter 1) (VAT1) (P54219)
Organism: Homo sapiens (Human)
Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports catecholamines and indolamines with higher affinity for serotonin. Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates presynaptic monoaminergic vesicle transport in the amygdala and prefrontal brain regions related with emotion processing in response to environmental stimuli.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:8643547}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8R090}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:16326835}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16326835}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 3
- Alpha-synuclein
- Vesicular acetylcholine transporter
- Synaptic vesicular amine transporter
- Sodium-dependent phosphate transport protein 1
- Monocarboxylate transporter 1
Sequence:
MLRTILDAPQRLLKEGRASRQLVLVVVFVALLLDNMLFTVVVPIVPTFLYDMEFKEVNSSLHLGHAGSSPHALASPAFSTIFSFFNNNTVAVEESVPSGIAWMNDTASTIPPPATEAISAHKNNCLQGTGFLEEEITRVGVLFASKAVMQLLVNPFVGPLTNRIGYHIPMFAGFVIMFLSTVMFAFSGTYTLLFVARTLQGIGSSFSSVAGLGMLASVYTDDHERGRAMGTALGGLALGLLVGAPFGSVMYEFVGKSAPFLILAFLALLDGALQLCILQPSKVSPESAKGTPLFMLLKDPYILVAAGSICFANMGVAILEPTLPIWMMQTMCSPKWQLGLAFLPASVSYLIGTNLFGVLANKMGRWLCSLIGMLVVGTSLLCVPLAHNIFGLIGPNAGLGLAIGMVDSSMMPIMGHLVDLRHTSVYGSVYAIADVAFCMGFAIGPSTGGAIVKAIGFPWLMVITGVINIVYAPLCYYLRSPPAKEEKLAILSQDCPMETRMYATQKPTKEFPLGEDSDEEPDHEE