wanglab/gogpt-training-data huggingface dataset:
Protein: Multidrug resistance protein MdtB (Multidrug transporter MdtB) (P76398)
Organism: Escherichia coli (strain K12)
Function: The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01423}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01423}.
Interaction partners:
- Multidrug resistance protein MdtA
- Periplasmic chaperone Spy
- Multidrug resistance protein MdtC
- Signal transduction histidine-protein kinase BaeS
- Putative multidrug resistance protein MdtD
- Outer membrane protein TolC
- Transcriptional regulatory protein BaeR
- Multidrug efflux pump subunit AcrA
- Probable aminoglycoside efflux pump
- Multidrug export protein EmrA
Sequence:
MQVLPPSSTGGPSRLFIMRPVATTLLMVAILLAGIIGYRALPVSALPEVDYPTIQVVTLYPGASPDVMTSAVTAPLERQFGQMSGLKQMSSQSSGGASVITLQFQLTLPLDVAEQEVQAAINAATNLLPSDLPNPPVYSKVNPADPPIMTLAVTSTAMPMTQVEDMVETRVAQKISQISGVGLVTLSGGQRPAVRVKLNAQAIAALGLTSETVRTAITGANVNSAKGSLDGPSRAVTLSANDQMQSAEEYRQLIIAYQNGAPIRLGDVATVEQGAENSWLGAWANKEQAIVMNVQRQPGANIISTADSIRQMLPQLTESLPKSVKVTVLSDRTTNIRASVDDTQFELMMAIALVVMIIYLFLRNIPATIIPGVAVPLSLIGTFAVMVFLDFSINNLTLMALTIATGFVVDDAIVVIENISRYIEKGEKPLAAALKGAGEIGFTIISLTFSLIAVLIPLLFMGDIVGRLFREFAITLAVAILISAVVSLTLTPMMCARMLSQESLRKQNRFSRASEKMFDRIIAAYGRGLAKVLNHPWLTLSVALSTLLLSVLLWVFIPKGFFPVQDNGIIQGTLQAPQSSSFANMAQRQRQVADVILQDPAVQSLTSFVGVDGTNPSLNSARLQINLKPLDERDDRVQKVIARLQTAVDKVPGVDLFLQPTQDLTIDTQVSRTQYQFTLQATSLDALSTWVPQLMEKLQQLPQLSDVSSDWQDKGLVAYVNVDRDSASRLGISMADVDNALYNAFGQRLISTIYTQANQYRVVLEHNTENTPGLAALDTIRLTSSDGGVVPLSSIAKIEQRFAPLSINHLDQFPVTTISFNVPDNYSLGDAVQAIMDTEKTLNLPVDITTQFQGSTLAFQSALGSTVWLIVAAVVAMYIVLGILYESFIHPITILSTLPTAGVGALLALLIAGSELDVIAIIGIILLIGIVKKNAIMMIDFALAAEREQGMSPREAIYQACLLRFRPILMTTLAALLGALPLMLSTGVGAELRRPLGIGMVGGLIVSQVLTLFTTPVIYLLFDRLALWTKSRFARHEEEA
Protein: Triggering receptor expressed on myeloid cells 1 (D4ABU7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Triggering receptor expressed on myeloid cells 2
- High mobility group protein B1
- High mobility group protein B1
- Trem-like transcript 2 protein
- Peptidoglycan recognition protein 1
- Interleukin-1 alpha
- Transcription initiation factor IIA subunit 2
- Toll-like receptor 4
- Triggering receptor expressed on myeloid cells-like 4
Sequence:
MRKAGLWGLLLVFFVSEVKAAIVPEEERYDLVEGQTLTVNCPFNIMKYARSRKAWQRLSAGKEPLTLVVTERSSTTSSEVRVGKYTLKDDPTEAMLFVQMTDLQVTDSGLYRCVIYHPPNDPVLLFHPVRLVVTKGSSGVSVPDIIPTTKPTEVPVLITTKHSTPTRSLPKSTAVVSSPDPGVTINNGTDPTSVSTYNVVVPVVCGLLIKTLIFFVLFVVTKRSFG
Protein: Nerylneryl diphosphate synthase CPT2, chloroplastic (EC 2.5.1.142) (Cis-prenyltransferase 2) (SlCPT2) (K7WQ45)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23134568}.
Interaction partners:
Sequence:
MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY
Protein: Unique GC organizer UGO (S7UQV8)
Organism: Toxoplasma gondii (strain ATCC 50853 / GT1)
Function: In tachyzoites, required for the cellular trafficking of guanylate cyclase GC to the cell membrane and for GC guanylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000305|PubMed:30742070}; Multi-pass membrane protein {ECO:0000255}. Note=In intracellular tachyzoites, localizes to the apical cap, to the cytoplasm in disperse foci and to the residual body. {ECO:0000269|PubMed:30742070}.
Interaction partners:
Sequence:
MRMQWFLLRHAYFIKGEDFAVAVALLDLALYVLIGTNSLQFLDQSPEKALFGMITSALIFIIALCGFVIVRMFRTSKYKIETYIMPVLIICNIASVFYMQLINKLVGFMTLQLPVLTFLITGYPYVWLVAFVLIGMGGGLIAQSVVCSVSLGSSCPPSVWVDVGLYALQLISGSVAYFTVYELGILIVRYKRHPARYLDAFSDLTALDTIVFSPVFGLGGETARQVQVNQLMAPEKPNLDGLTFLRSASQVSQTTNRIVSRAFYHANTPPHSSSRDALPADKALGAERSDRAGSAVFSPNTLGPLGAPSAGLRDFGPGRPVPGASVVVPKSLKQHAAALHAGANSPHGSPPLQPHGALPGAPRSNTLRGCSGQVSLVPREEESDPACGSLRASVESKATHRSAATLSACESKSRSGRVAGLFRGLSKRPGGPDCEEAAPAEPATSLGSKELGRKKTAGSKAQSSVPILLPRPQSIEETTWRGLASGDLSKDTPVASLASRRNLRMDEQSGDADKASSDVSRDPAKKGAGPFVAEAPVHTAVLPSSSFHSEFPLSRRDSGKELLSDLRESRERTARAASHDTHAAADDSGLQGDPALAAEARVRTALHYHRRWFFSQLFHFRRARRRHRRGAGARDGELVFERGEPDEVESEESCDDSRSRPRETASLSHFSRLSRSRRHKTRTYRRGRSSDGTTAGTSDSDSHGESLEDEGSDSGQESESEESRRRRMRSSRNRRRETSSEDSSSGTSVRSEGRHCREGRANSSVFSSGIRRYFSFFSAATRCAHAASSEEERPVRPARHSWRRGSGDSRECSASTSGVSEACEHSSDASWASSSSLCGSCEKRSIRMSRRRRREGKSRPHASSVSRAERHRGHVSVDLAPLLPSRLFFDTFLNSVRRAERLSKEGRLPASVSRQSSETRGSRTAFLNGDKGCSPTSEAPERSFPASANEVSFRRNEGWERYYDMLLPSLPPFPSARPLYVKPRKNSQAFQNVAVSVSRNETEMTASSPATSFDGPRAVSLSPEGRGARESSDGGGATAPSDLHSRPARAKSLVAAMLHTYPTCPQPPSDLSLFTTPPASPSSLNEVQASRSSSARITSVELGALGKQQGEAAPAGTDAVEEDRDATEDARGSLSSPTGASRRGDRCRRSWSSCEARSSVEMKPNLSIRDARASESPLQSAAPLLSEEKKSRKAQSCAQCRRCGRSRTRLQPSGRLGSSSREDLVGEADSHVSPEKEVFVSSRREKREEQVPRSRREERRDRRGRRWRRGRRRRKARECSETEERRDSSSEWSGTQYSSQERRSHEAVGGVAQLTPICVDDECGKGDAGLSPLLRSEAEESEGEGDMRERQIYETHSDGDVEELSEEEREDRGRSWLRWLFPWGAGEGQGGEKNRRKRSRSEGRREREFISAERRYLEHHRRSRVSSVADSRWGSGSEASADAYPALRRRKGSRVYPVSKPQWFQPSGLTACSSKNSWLAVPPDISLVSAAPALPTPSPSSLSFSGLDQELDCDANSSTAVSSSLPDSTAWQGSGAAASASSPSLRASVDAHFAEAELHAAEHSDGVSVSPRNSPGALSARPMSAAGMPNPDSGIATQTPQTPQTPHTQRPLLLAQSLVAASGKPLPPTRADFEAQRSQGLGDLSQKTPRVFSPQGLGRSQGYGPGGSSYALDSSREAGPSGRLSATPSTRLQGSGGPAFPHSSFPQAIGAAGTPTAPSRDSRTFFGDTGAARASRAGLSGRLASRGTALAPKGTRRLKSGYSVGAADAKDKQKGKVLRYQLVQKFHDRLPWWVARIIVYTDAALENCRRRRRLMQRATWKTKVAMPVRNMLGLFSDEKIETWYVQWLNAFNAKYYPRVAWLLFLICFYATAFHGLLRLRGFIENYPLCIDAVRASPLGEAGFLILVAVRFASQPILSFLLLLPLLRHSGSRLIDFLFCSRAPATPLKSYKLYRWMLALSFLQFVYAVFDNTWHLIAEPGSRHVNPLTIIPASPSLEIAAVQTVYILAVRTPTINLIFLLYIITYIIIFFVALPPGVQQVQLFTISMAGWLFTCVGGQLFYTRAFEVNRRRLFCKYVLPYMLYLEEIAAILYSNPQGEYPLDEGSEDEVSMGSGHLVGDRSA
Protein: Conserved protein (O05316)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- HTH-type transcriptional regulatory protein RaaS
- Multidrug efflux system permease protein Rv1217c
- Probable conserved integral membrane protein
- Multidrug efflux system ATP-binding protein Rv1218c
- Uncharacterized protein
- Probable O-methyltransferase Rv1220c
Sequence:
MARNPSPALDRPWRRPGALRYALERVRGVAKPPITVTDPPADVVIERDVEVPTRDGTLLRINVFRSAEGGARPVIASIHPYGKDALPRRRGNRWTFSPQYRMLRQPKPLTFSALTGWEAPDPAWWTAQGFVVVNADSRGCGRSDGTGDLLSHQEAEDTYDLVGWLADQAWSDGRVVMLGVSYLAISQYAVAALQPPALRAICPWEGFTDAYRDLAFPGGIRESGFTRLWSRGVRRRTRQTYDMEQMQEAHPLRDDFWRSRVPDLSAIKVPMLVCGSFSDNNLHSRGSIRAFTRSGCGHARLYTHRGGKWETFYSATALSEQLKFLRDALAGSSGSRSVRLEVREDRDTITAVREETQWPLAGTRWRPMYLAGPGLLATEPPPTAGSIRFQTRSRAAAFNWTIPEDIELTGPMAARLWVQLDGCDDANLFVGVEKWRDGQFVAFEGSYGWGRDRVTTGWQRVSLRELDPELSQPWEPVPACARPRPVTAGEVVAVDVALGPSATLFRAGEQLRLVVGGRWLSPRNPLTGQFPAAYPRPPRGRVTLHWGPRYDAHLLIPEVPG
Protein: Col6a3 protein (Q99K31)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
LSPDPKASQHFARVAVVQQSTYESVDNASVPPVKVEFSLTDYGAKEKLLDFLSRRMTQLQGTMGLGNAIEYTIENIFESAPNPRDLKIMVLMLTGDMQRQQLEEAQRAILQAKCKGYFFVVLGIGRKVNIKEVYSFASEPNDVFFKFVDKSTELNEEPLMRFGRLLPSFVSSENAFYLPPDLRKQCDWFQGDQPVKNGVKFGHKQINPPHTANSSLTSKVVTTMKPVTTTKPTAIVNLTPAKPAPARPAPAQPVLAKPDPAKPAQARPAPAKPASAKLVPPQPVHVQPAPAQTASVRPAPAKPAPPQPAAAKPVPAKPAVPAQPAPPQPAAAKPVPAKPAVPAQPAAAQPMPAQPVLTKSAAVKPASANKPVAAKPVATNTATATARPALAAKPAAAKPAATRPLAAAVRPVATKPEAPRQQAKPAATKPATTKPLARVSREVQVSEVTENSARLHWERPEPSSSFFYDLTVTSAHDQSLVLRQNLTVTDRVIGGLLAGQLYHVVVVSYLQSQVRAIYQGSFNTKKTQPPPLQAAHRASSSTINLMVNTEPLFLTKTDICKLSRHAGTCVDFKLLWHYDLESKSCKRFWYGGCGGNENRFHSQEECEKMCSPELTV
Protein: AT01932p (Q8T4E8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESEEHAVDAMENRRLPLFPIEPEPSVTATQRLTLLATRLLRALQLNWRIIVSGITLTLLAVIWYYPTFFLFFAFVVYSLVLVFAAVAGTVYIHYIFTTNEPTPPSRVPSRLLYNATKSNIFDLPKPIKNPSNLPLIFGKTVDLQLQQIIEYVMRDFMLPWLGYVVTKPKLINDVVREDLWNAIQKIHERALRMDAAKIIAVDMVNRVTVHLEKIRIAEARAAETNTPPVFSTNSYLADEEKEMEFLRKLCEIMVILLLPRGYSLPPLKVLLSEILSYKIFFPMIKMLTAPDYINQKVVQNIETRLAAAAMSKRSYEYAASFEDFLKIINNSGNLEELSLIRKSIVNDLMHATTMQNLQRAKGLDPDHEDHSLSKSELTAAVRLKRYVRQLTMAKGECEKNLAKFGWNGNYSSDIDLTLVEILNTAVGRRYFTLFLEPLKASALIGFYLAVEEIKHAHKSASHQLGTEIFYTYIRVPKSEIQIDKHERKLIETFLLGDAEPDIFYDIQRNVLRTLEEKYYPPFVLSDQYRQLKEALDSNEIADPTLLMCHTIGDVQEPLADEQPVAADGLNGGAGGAIDVAAHTSYARRKLEQIQERIDKKNQALDALKYSVKPESKVLTILEKEMEWLKSEKRQTEAHLRRTDAWTEHLGKWKATIQSVEVSDEKESLQFMILVHVDEDINAPVQPTSSKNGDSGHANLRKRPSGISSGWVVMRSLNQVHELQRKLRHVSSNLKAIDLPTNFKFFFLKTDRHGQEKAKSQIQKFLNFILEDDHLNGSEAIYTFLSPSSDHLKQSLPSPKKSKFSLSTLFRSDAGKAHEASKATDPFWGLQRDDEDISTYLDGESGGEAKMLAADLDSKDSIAEPMYALMGEIFDMGGVFKWLRKSLISFVQITYGRTINRQIRESVAYLFEESMLHNYFSAILKSFWPGGVLASAYPTRSEDMREMTTTAAKALLTDHIPEVLCNLVGAQAAKRGVLKVFDALQNPAYNKQLFYELLEILMIEFFPEIRQLRVSNSNGTKLNTATAGAAAASAAAALVAATASASLPSLNHSGGGHSASTGGHQNHQGSSSASGSSAGASGATGGGAASHHQSHYHHGSHHHQQQQHHHSQAGSSK
Protein: Neuropeptide precursor capa-1 (CAPA (insect neuropeptide) related protein) [Cleaved into: AFFYTPRI-amide (PK-like) (pyrokinin-like); APHPSSALLVPYPRV-amide (PVK-1); LYMARV-amide (PVK-2)] (Q9N563)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptors family 1 profile domain-containing protein
- Neuromedin U receptor homolog nmur-2
- Neuropeptide-like protein 38
Sequence:
MLLWIVATLLIFSLPVSTALDYNDFSLQRIARAPHPSSALLVPYPRVGKRSNILNNNSESQNSVQKRLYMARVGKRAFFYTPRIGK
Protein: Auxin-responsive protein IAA30 (Indoleacetic acid-induced protein 30) (Q9M1R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 7
- Auxin response factor 5
- Auxin-responsive protein IAA33
- Auxin response factor 9
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 8
- Auxin transporter protein 1
- Auxin response factor 12
- NAC domain-containing protein 69
- Auxin response factor 6
Sequence:
MGRGRSSSSSSIESSCKSNPFGVSSSNTRNLSTDLRLGLSFGSSSGQYYNGGDNHEYDGVGAAEEMMIMEEEEQNECNSVGSFYVKVNMEGVPIGRKIDLLSLNGYHDLITTLDYMFNASILWAEEEDMCSEKSHVLTYADKEGDWMMVGDVPWEMFLSSVRRLKISRAYHY
Protein: 2-amino-4-ketopentanoate thiolase alpha subunit (EC 2.3.1.263) (AKP thiolase) (AKPT) (C1FW06)
Organism: Unknown prokaryotic organism
Function: Involved in the ornithine fermentation pathway. Catalyzes the thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP.
Interaction partners:
Sequence:
MSEKCKKDDWVEIHYVVLEARERTGDIPEDTRKVPLECWIKGWAEKEGTVGEEVTIRTPANRYVKGTLTRINPEYTHTFGPCASELSAIGQELRATLKEGK
Protein: FI16602p1 (Q9W1P0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}.
Interaction partners:
- LD04844p
Sequence:
MSSFARVPSTPPPSYEEAMGWETRRSHSTTWLLAENTSSLMICPMCHDEIETTTKIRRRWIAYVASGIVLFTTCGIGCWLIPCILDCFNEIHHSCPVCKATLGIVPQQDQRWPT
Protein: Prepilin leader peptidase/N-methyltransferase (Protein PilD) (Protein secretion protein XCPA) [Includes: Leader peptidase (EC 3.4.23.43) (Prepilin peptidase); N-methyltransferase (EC 2.1.1.-)] (P22610)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for pilus biogenesis PilE, PilV, PilW, and PilX as well as some components of the type II general secretory apparatus GspG, GspH, GspI and GspJ.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:8331069}; Multi-pass membrane protein.
Interaction partners:
- Type IV pilus assembly ATPase PilB
- Type IV pilus retractation ATPase PilT
- Type IV pilus ATPase PilU
- Type IV pilus inner membrane component PilM
- Fimbrial assembly protein PilQ
- Type IV pilus non-core minor pilin PilE
- Type II secretion system protein E
- Type IV pilus inner membrane component PilO
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilP
Sequence:
MPLLDYLASHPLAFVLCTILLGLLVGSFLNVVVHRLPKMMERNWKAEAREALGLEPEPKQATYNLVLPNSACPRCGHEIRPWENIPLVSYLALGGKCSSCKAAIGKRYPLVELATALLSGYVAWHFGFTWQAGAMLLLTWGLLAMSLIDADHQLLPDVLVLPLLWLGLIANHFGLFASLDDALFGAVFGYLSLWSVFWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQILPLTILLSSLVGAILGVIMLRLRNAESGTPIPFGPYLAIAGWIALLWGDQITRTYLQFAGFK
Protein: 40-kDa huntingtin-associated protein (CpG island protein) (Factor VIII intron 22 protein) (Q00558)
Organism: Mus musculus (Mouse)
Function: RAB5A effector molecule that is involved in vesicular trafficking of early endosomes. Mediates the recruitment of HTT by RAB5A onto early endosomes (By similarity). The HTT-F8A1/F8A2/F8A3-RAB5A complex stimulates early endosomal interaction with actin filaments and inhibits interaction with microtubules, leading to the reduction of endosome motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11035034, ECO:0000269|PubMed:23749422}. Nucleus {ECO:0000269|PubMed:11035034, ECO:0000269|PubMed:23749422}. Early endosome {ECO:0000250|UniProtKB:P23610}. Nucleus, nuclear body {ECO:0000269|PubMed:23749422}. Note=Diffuse presence in the cytoplasm and accumulation in the nucleus (By similarity). In absence of HTT, F8A1/F8A2/F8A3 is concentred in cytoplasm (PubMed:11035034). Colocalized with HTT in endosomes (By similarity). In neuron found in intranuclear structures, the intranuclear rodlets (INRs), also known as rodlets of Roncoroni, in association with ubiquitin (PubMed:23749422). {ECO:0000250|UniProtKB:P23610, ECO:0000269|PubMed:11035034, ECO:0000269|PubMed:23749422}.
Interaction partners:
- Huntingtin
Sequence:
MAAGSASSLGGGAWPGSEAGDFLARYRQVSNKLKKRFLRKPNVAEAGEQFAQLARELRAQECLPYAAWCQLAVARCQQALFHGPGEALALTEAARLFLRQECDARQRLGCPAAYGEPLQAAASALGAAVRLHLELGQPAAAAALCLELAAALRAVGQPAAAAGHFQRAAQLHLPLMPLAALQALGDAASCQLLARDYTGALALFTRMQRLAREHGGHPVQQLELLPQPPSGPQPPLSGPQPRPVLGSTLPLPQPPDHAPGSVAPSPGTLGAFADVLVRCEVSRVLLLLLLQPPPAKLLPEHAQTLEKYSWEAFDGHGQDTSGQLPEELFLLLQSLVMAAQEKDTEGIKKLQVEMWPLLTAEQNHLLHLVLQETISPSGQGV
Protein: High mobility group nucleosome-binding domain-containing protein 3 (A0A087WZE9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPKRKSPENTEGKDGSKVTKQEPTRRSARLSAKPAPPKPEPKPRKTSAKKEPGAKISRGAKGKKEEKQEAGKEGTAPSENGETKAEEIHISRSTVNVSTSRGTPPSTLSVKGQIETVRAQKTESVDNEGE
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (P9WID1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Pyruvate kinase
- Fructose-bisphosphate aldolase
- Ribulose-phosphate 3-epimerase
- Transketolase
- ATP-dependent 6-phosphofructokinase
Sequence:
MSVANLKDLLAEGVSGRGVLVRSDLNVPLDEDGTITDAGRIIASAPTLKALLDADAKVVVAAHLGRPKDGPDPTLSLAPVAVALGEQLGRHVQLAGDVVGADALARAEGLTGGDILLLENIRFDKRETSKNDDDRRALAKQLVELVGTGGVFVSDGFGVVHRKQASVYDIATLLPHYAGTLVADEMRVLEQLTSSTQRPYAVVLGGSKVSDKLGVIESLATKADSIVIGGGMCFTFLAAQGFSVGTSLLEDDMIEVCRGLLETYHDVLRLPVDLVVTEKFAADSPPQTVDVGAVPNGLMGLDIGPGSIKRFSTLLSNAGTIFWNGPMGVFEFPAYAAGTRGVAEAIVAATGKGAFSVVGGGDSAAAVRAMNIPEGAFSHISTGGGASLEYLEGKTLPGIEVLSREQPTGGVL
Protein: Roa1p (A0A1D8PCM6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKEGASVLSISSENQVGVKVRNLTVSVKSQQQKTTKHTEDQEAQYEQGTSKILNNLSFDIECGQLVAIMGGSGSGKTTLLNTLSQRTNINNKNLGFSGSVTYETSSSNKHIKHAYLLQTDIFLPGLTVWETLSTQADLRLPSHVTKQEKIELIEYILDVLELSHLKNTYVASFSSNASTLSGGEQRRVSLAIQMLSKPAILFLDEPTTGLDTSSSLKLVHVLKKLASPEYGITIILSIHQPRPEIGQLFDKICLLTRGGRLVYFGNLANAEMYFNNLNFLGRDSDDHSKHILEYIMDLSVKDTTSVEKEQQTVERINKLVQTWSNNHQFQQQQEENRSSKESHQFKKNLTLFSKPKTDKISFWQEVNVLTKRTFKLTFRDYKRLLVFNVGIVIIGVTVGWMFYRPKHDLAGIRSLTSTLYVAMEIMGFVPMYFEIERLWETDGVFFYREYSENQVSIPGFLISRRLGKLFLEDLPMSLLFSIITFFMWGLRLGDGSHFGIYFVVVFLIELCCMGTAMFSFAIAPSYPISALLINLIYQIQNSACGYFVNAATMPVYVKWTKYLAYFWYAFGALTNNQFSGWHGKCPYNDINDPRCQEFSGDYQIKILGFPVGWVGAPIGYLVLWTVGFFVLSGILFYFKQHDVSMAKTKKNTIGEGEEDHEALHQKKTEREQDYITDKHDLEININNIHLDVTTSNLFGQTKSTKTLLDNVTASFQANKVNVIMGPSGSGKTTLLNYLSNRLSRNSKFIASGSIRLNGIQKISRDQLSKISAYVTQHDSSLIEQLTVRETLYYQAKLRLPLDQHKFIPTIINKLIRQTGLVDCADTLIGSEYVKGISGGEKRRVSIAIQLLSRPKVLFLDEPTSGLDSSTAETILTLLGELAKENNTTIILTIHQPSEQLFYKFGSLLLLGRGGKVIYDGTSVGIVEYLESLGYNNPEGHNIADYILDLISRGMNEDKMQSERRVAELISYWQANSIKKLCSTATFSQEIIDLPQYYYQRLPIFITFPTIFRRQLLTSYRAKDVVINRAGQTIFLAIVHTLYFTPLRNTQEGISNRLGLVQEVLNLYFAGLINNITLYPFERNLFYQEYRDGIYGVTEFGLSYLINELPTEVIPCFFFAALIVFACGLPRTPQMFFAMFGTGFVSINCGESLGIFVNSIFTHMGVATNVLSTFVSLAIFMGGTMSLHMPGFFKGINFISPMKYAVAICANLGFKNQSFKCNSEAADCLLTTGEDVLSYYNMKQNLGPMVGGLIGCLVIYRVVAILSIYVRVKWF
Protein: Mediator of RNA polymerase II transcription subunit 9 (Mediator complex subunit 9) (Q8VCS6)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 22
Sequence:
MASSGVAGGRQAEDTLQPPPELLPESKPPPPPQPLPVAALPPPAAPRPQSPAGAKEENYSFLPLVHNVIKCMDKDSPDLHQDLNALKTKFQELRKLIGTMPGIHVSPEQQQQQLHSLREQVRTKNELLQKYKSLCMFEIPKD
Protein: CX3CL1-binding protein 2 (Gametocyte exported protein 7) (PfGEXP07) (Q8IEJ0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage and probably at the ring/trophozoite stages, plays a role in Maurer's cleft formation and/or morphology. Also, involved in the loading of the virulence factor EMP1 into the Maurer's cleft membrane. By binding to host chemokine CX3CL1, mediates the cytoadherence of host erythrocytes infected with parasite mature forms (late trophozoite and schizont) to endothelial cells, which sequesters them away from the circulation and thus prevents their elimination by the host spleen.
Subcellular location: Host cell membrane {ECO:0000269|PubMed:27653778}; Multi-pass membrane protein {ECO:0000255}. Note=At the ring and trophozoite stages, localizes to Maurer's clefts, specifically in the central region of the cleft (PubMed:24983235, PubMed:32184257). Localizes to the cell membrane of host erythrocyte infected with parasite mature forms (late trophozoite and schizont) (PubMed:27653778). {ECO:0000269|PubMed:24983235, ECO:0000269|PubMed:27653778, ECO:0000269|PubMed:32184257}.
Interaction partners:
Sequence:
MSFCYVRTISIALFLFIFLFLNNGNFKNNFYRKDNKYSSIKIRSFRSLAENQKVETEQSTPAKPEPTEFVNNDIHQNKNTFKKLKNNEKKKEILEEKMKDFVKLYVNKSSGECQRYRLQQHLKNYSSSNEYKKFMNKFVKFLKVHNDLNALKSQLHFNNVRAATIIFIAGFLSIFAILLTISAVAATSKFTNNMLAIAGVGALGSALSLPGMALLFVPAMLYVLNRKNEITNHYSERIIKQVSNF
Protein: Transposon Tn7 transposition protein TnsB (P13989)
Organism: Escherichia coli
Function: Sequence-specific, DNA-binding protein required for Tn7 transposition. Recognizes sequences necessary for recombination at both left and right ends of Tn7 and, together with TnsA, forms the transposase. TnsB executes the 5'-DNA strand breakage and joining reactions.
Interaction partners:
Sequence:
MWQINEVVLFDNDPYRILAIEDGQVVWMQISADKGVPQARAELLLMQYLDEGRLVRTDDPYVHLDLEEPSVDSVSFQKREEDYRKILPIINSKDRFDPKVRSELVEHVVQEHKVTKATVYKLLRRYWQRGQTPNALIPDYKNSGAPGERRSATGTAKIGRAREYGKGEGTKVTPEIERLFRLTIEKHLLNQKGTKTTVAYRRFVDLFAQYFPRIPQEDYPTLRQFRYFYDREYPKAQRLKSRVKAGVYKKDVRPLSSTATSQALGPGSRYEIDATIADIYLVDHHDRQKIIGRPTLYIVIDVFSRMITGFYIGFENPSYVVAMQAFVNACSDKTAICAQHDIEISSSDWPCVGLPDVLLADRGELMSHQVEALVSSFNVRVESAPPRRGDAKGIVESTFRTLQAEFKSFAPGIVEGSRIKSHGETDYRLDASLSVFEFTQIILRTILFRNNHLVMDKYDRDADFPTDLPSIPVQLWQWGMQHRTGSLRAVEQEQLRVALLPRRKVSISSFGVNLWGLYYSGSEILREGWLQRSTDIARPQHLEAAYDPVLVDTIYLFPQVGSRVFWRCNLTERSRQFKGLSFWEVWDIQAQEKHNKANAKQDELTKRRELEAFIQQTIQKANKLTPSTTEPKSTRIKQIKTNKKEAVTSERKKRAEHLKPSSSGDEAKVIPFNAVEADDQEDYSLPTYVPELFQDPPEKDES
Protein: Glutaredoxin-2, mitochondrial (Q6AXW1)
Organism: Rattus norvegicus (Rat)
Function: Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release (By similarity).
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250}.
Interaction partners:
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin, mitochondrial
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Thioredoxin
Sequence:
MSWYRAASVGRRLVASGRILAGRRGAAGAAGSGMGNSTSSFWGKSATTPVNQIQETISNNCVVIFSKSSCSYCSMAKKIFHDMNVNYKVVELDMVEYGSQFQEALYKMTGERTVPRIFVNGIFIGGAADTHRLHKEGKLLPLVHQCYLNKSKRKDVE