wanglab/gogpt-training-data huggingface dataset:
Protein: SET and MYND domain containing, class 4, member 1, isoform B (SET and MYND domain containing, class 4, member 1, isoform C) (A1Z7W1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SET and MYND domain containing, arthropod-specific, member 2
- AT24727p
- SET and MYND domain containing, arthropod-specific, member 4, isoform A
- SET and MYND domain containing, arthropod-specific, member 6
- GH11294p
- SET domain-containing protein SmydA-8, isoform A
- SET and MYND domain containing, arthropod-specific, member 9, isoform A
- Protein-lysine N-trimethyltransferase SMYD5
Sequence:
MERLARTFSQQNELITLNENYKDEFETFKSLASMPADILQIFQKLALDLLQDLEQPVDRKGCAERSKNLREEGNLMFKESASGSSKDSVLKACRLYSEAVFEAENAVEELSLAFANRGIALQEYGYYREAYDDCSNALECGYPERLRHKVIMRQAFCAWKLKKIASLEEHLDYLGQLQLKESFEQQLEDLKQKLELLKNQPREQETQGKVVDKSLGEILTDPGPRGRYMVAKEAISKGNVIFSERASCFVPLEQLLICQQCAATLMSAPIPCPNCHQRVVYCSRKCREAHSAIHKFECAAYRKDILRLLGISHLALRLLLTYIPYIRPHLQEMTSAKGMWEEIMNLSRKPEESENAPEYLRSLRMVSQLDQAIDEELNYHILCANLLQLYLKEHTDFYDQFHSLPASIEDWQLIISALILRFAGQLLANGHVGDALLGVGMEPKEFVMLQPELWQKPRHLKRGQLHNLSHSDPITAINLPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIFNCYTMDYRNSLKLQRSHPLKAIYKFECTCAKCTRTDPDQNYLSFHRYRCEKPNCRQEFLPDAKVQQNNLRWWLRCNAEKPITCTVCHELQHFAWYNEFLGLIGSSADSSKRQALFKAFDDLDKWLVDHHSLKRIMAEELVTACFYEIDGGTSLDEFEYEDLARIIRKQLEGIAAQCGDNSTEYIARMTYLWDIIAQKKCRTDRKELLEMKGKVDYLASEHREVFLNYYNDFIEQ
Protein: Serpin 28Db (Q9VLV3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serpin 85F
- LP21446p
- IP10416p
- BPTI/Kunitz inhibitor domain-containing protein
- BG642163, isoform A
Sequence:
MQGNNKIKYLVLLLIATSVLGKFKLNLLELVMDKAESNFIASPLCIEIGISMILMGAKGTTAEELRSVLDLPVDVTEMAKKYERIMSNFQKHNGLRFTNWLYVNETYEVRQDYNTLMKSTFMAEGKDPLSQRKASNSISFSIHRKSHKGMRTISNDHNLQINESAVLVNTVYYSGAWKTRFSKKDTKLKVFHGDHNKKVYVRMMSHVGRFRIADHSYGQIIEMPFDNSDLSMIIGLPLHNTYLSSIEKILRTLSESLVENNVHVELPKFKIKYQTELVESLKKLGIHLIFSNTSDLSGLLTNGTGAKINHVVHKSFIEINERGASTGEASDHAESIQKKTRASTSFKVNRPFVFLIRDKHTVYFRGRVVRLPNELHL
Protein: Large ribosomal subunit protein mL52 (39S ribosomal protein L52, mitochondrial) (L52mt) (MRP-L52) (P0C2B7)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11551941}.
Interaction partners:
- Large ribosomal subunit protein mL63
- Large ribosomal subunit protein mL55
- Large ribosomal subunit protein mL54
- Large ribosomal subunit protein mL64
- Small ribosomal subunit protein bS21m
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL51
Sequence:
MAALGMLLSTGVRRLHCGSAARAGSQWRLRQGLAANPSGYGPLTELPDWSYADGRPAPPMKGQLRRKAQREKFARRVVLLSQEMDAGLQAWQLRQQEKLQEEKRKQQNALKPKGVLLQNPGPSQ
Protein: Transcription regulatory protein SNF2 (EC 3.6.4.-) (ATP-dependent helicase SNF2) (Regulatory protein GAM1) (Regulatory protein SWI2) (SWI/SNF complex component SNF2) (Transcription factor TYE3) (P22082)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Catalytic component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus.
Interaction partners:
- SWI/SNF complex subunit SWI3
- SWI/SNF chromatin-remodeling complex subunit SWI1
- Transcription regulatory protein SNF11
- Actin-like protein ARP9
- Transcription regulatory protein SNF6
- Transcription regulatory protein SNF12
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Actin-related protein 7
- SWI/SNF global transcription activator complex subunit SWP82
- Regulator of Ty1 transposition protein 102
Sequence:
MNIPQRQFSNEEVNRCYLRWQHLRNEHGMNAPSVPEFIYLTKVLQFAAKQRQELQMQRQQQGISGSQQNIVPNSSDQAELPNNASSHISASASPHLAPNMQLNGNETFSTSAHQSPIMQTQMPLNSNGGNNMLPQRQSSVGSLNATNFSPTPANNGENAAEKPDNSNHNNLNLNNSELQPQNRSLQEHNIQDSNVMPGSQINSPMPQQAQMQQAQFQAQQAQQAQQAQQAQQAQARLQQGRRLPMTMFTAEQSELLKAQITSLKCLVNRKPIPFEFQAVIQKSINHPPDFKRMLLSLSEFARRRQPTDQNNQSNLNGGNNTQQPGTNSHYNNTNTDNVSGLTRNAPLDSKDENFASVSPAGPSSVHNAKNGTLDKNSQTVSGTPITQTESKKEENETISNVAKTAPNSNKTHTEQNNPPKPQKPVPLNVLQDQYKEGIKVVDIDDPDMMVDSFTMPNISHSNIDYQTLLANSDHAKFTIEPGVLPVGIDTHTATDIYQTLIALNLDTTVNDCLDKLLNDECTESTRENALYDYYALQLLPLQKAVRGHVLQFEWHQNSLLTNTHPNFLSKIRNINVQDALLTNQLYKNHELLKLERKKTEAVARLKSMNKSAINQYNRRQDKKNKRLKFGHRLIATHTNLERDEQKRAEKKAKERLQALKANDEEAYIKLLDQTKDTRITHLLRQTNAFLDSLTRAVKDQQKYTKEMIDSHIKEASEEVDDLSMVPKMKDEEYDDDDDNSNVDYYNVAHRIKEDIKKQPSILVGGTLKDYQIKGLQWMVSLFNNHLNGILADEMGLGKTIQTISLLTYLYEMKNIRGPYLVIVPLSTLSNWSSEFAKWAPTLRTISFKGSPNERKAKQAKIRAGEFDVVLTTFEYIIKERALLSKVKWVHMIIDEGHRMKNAQSKLSLTLNTHYHADYRLILTGTPLQNNLPELWALLNFVLPKIFNSVKSFDEWFNTPFANTGGQDKIELSEEETLLVIRRLHKVLRPFLLRRLKKDVEKELPDKVEKVVKCKMSALQQIMYQQMLKYRRLFIGDQNNKKMVGLRGFNNQIMQLKKICNHPFVFEEVEDQINPTRETNDDIWRVAGKFELLDRILPKLKATGHRVLIFFQMTQIMDIMEDFLRYINIKYLRLDGHTKSDERSELLRLFNAPDSEYLCFILSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNEVRILRLITTNSVEEVILERAYKKLDIDGKVIQAGKFDNKSTSEEQEALLRSLLDAEEERRKKRESGVEEEEELKDSEINEILARNDEEMAVLTRMDEDRSKKEEELGVKSRLLEKSELPDIYSRDIGAELKREESESAAVYNGRGARERKTATYNDNMSEEQWLRQFEVSDDEKNDKQARKQRTKKEDKSEAIDGNGEIKGENIDADNDGPRINNISAEDRADTDLAMNDDDFLSKKRKAGRPRGRPKKVKLEGSENSEPPALESSPVTGDNSPSEDFMDIPKPRTAGKTSVKSARTSTRGRGRGRGRGRGRGRGRGRPPKARNGLDYVRTPAAATSPIDIREKVAKQALDLYHFALNYENEAGRKLSDIFLSKPSKALYPDYYMIIKYPVAFDNINTHIETLAYNSLKETLQDFHLIFSNARIYNTEGSVVYEDSLELEKVVTKKYCEIMGDNSQLDFTEFDEQYGTRPLVLPPVVTSSVAESFTDEADSSMTEASV
Protein: Protein P8 (Protein VIII) (Q9XJR5)
Organism: Pseudoalteromonas phage PM2 (Bacteriophage PM2)
Subcellular location: Virion membrane {ECO:0000305|PubMed:12134022}; Single-pass membrane protein {ECO:0000305|PubMed:12134022}. Note=Part of the capsid inner membrane. {ECO:0000305}.
Interaction partners:
Sequence:
MLGALMGVAGGAPMGGASPMGGMPSIASSSSAETGQQTQSGNFTGGGINFGSNNNNQLLIVGAVVIGLFLVIKRK
Protein: Triacylglycerol lipase ptl3 (EC 3.1.1.3) (Q9Y827)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Lipid droplet {ECO:0000250|UniProtKB:Q12043}.
Interaction partners:
- Putative phospholipase A2
- Putative lipase atg15
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Putative phosphatidate cytidylyltransferase
- Triacylglycerol lipase ptl1
- Putative monoglyceride lipase
- Nuclear elongation and deformation protein 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Phospholipase D1
Sequence:
MSKNEIKLQMEYASSYETWLEAAEKLDVIEGKYQWREQKESDEYDYVLVESRLHELRRHRLSKNTRLLLGLLRNSVARDFANMDNSRLYNYAHSGTKKLIDEFIQEVLMCLTYLEETPDLSLDEKITEFSRLKLTTGNTALILSGGGTFGMTHIGVLQSLHEQGLVPKIICGSSAGAIVACAAAVRNKEEQEILLRQFHTGDLSVFTDPNAAPPSVIQSVKQYFTRGCVLDISHLERVMKLLIGDFTFQEAYDRSGYILNVTVSCGSLFEMPSLLNYITAPNVLVWSAVVATCSVPFLFKRATLWERDPLTREVSAFCVTDAPLWMDGSVDNDIPHAKLTELFHVNHFIVSQVNFHIVPFIMDPTSHNWVERCCKKAIDLAAQEVSLTFRLFAELGIFSVLFTKLQSVITQKYSGDITIIPRLNYREVNKVIKNPTPSFLLDAATRGKRGTWTKVPVTRNHCAIEILIAAAYTRLIKRSKSLK
Protein: 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5 (EC 2.4.1.152) (3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5) (EC 2.4.1.65) (Fucosyltransferase 5) (Fucosyltransferase V) (Fuc-TV) (FucT-V) (Galactoside 3-L-fucosyltransferase) (Q11128)
Organism: Homo sapiens (Human)
Function: Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosaccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens. Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate. Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an alpha (1,4) linkage. Preferentially catalyzes sialylated type 2 oligosaccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide acceptors. Lactose-based structures are also acceptor substrates.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 1
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- Beta-1,4-galactosyltransferase 4
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Beta-1,4-galactosyltransferase 2
- Alpha-
Sequence:
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPNGSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVIVHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFHWRETLRPRSFSWALAFCKACWKLQQESRYQTVRSIAAWFT
Protein: Spindlin-1 (Ovarian cancer-related protein) (Spindlin1) (Q9Y657)
Organism: Homo sapiens (Human)
Function: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway. Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes. May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption.
Subcellular location: Nucleus {ECO:0000269|PubMed:16098913, ECO:0000269|PubMed:29061846}. Nucleus, nucleolus {ECO:0000269|PubMed:21960006}.
Interaction partners:
- Spindlin interactor and repressor of chromatin-binding protein
- Histone H3.2
- Histone H3.3
- Histone H3.3C
- Histone H3.1
- Histone H3-7
- Histone H3.1t
- Threonylcarbamoyl-AMP synthase
- Spindlin-2B
- CGG triplet repeat-binding protein 1
Sequence:
MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS
Protein: Estrogen-related receptor alpha (Steroid hormone receptor ERR1) (Q6Q6F6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma, coactivator 1 alpha.
- Peroxisome proliferator-activated receptor gamma, coactivator 1 beta.
Sequence:
MSSRERRSDLYIKAEPSSPEGGGGGGGGRTSPGGASSDSSQSGGGGSRGEGAGRYSPPLYTPALRCHFKEEGADGAEEGSTGSGGGRCKYALSTLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGNIEYSCPASNECEITKRRRKACQACRFTKCLKVGMLKEGVRLDRVRGGRQKYKRRPEVENATYQSAPIPLRKEGEKGSSSIIVSHLLVAEPEKLFAMPDPLQPDTAQRTLTTLCDLADRELVVIIGWAKHIPGFLSLSLADQMSVLQSVWLEVLVLGVAYRSLGCEDEVVFAEDFVLDEEMSRVAGLTELNAAISQLARRFRALQLDREEFVMLKAIALTNSDSVYIEDMEAVQKLRDLLHQALLELEVQRRPDDPQRAGRLLLTLPLLRQTAGRALTTFYSIKTRGGVPMHKLFLEMLEAMMDSP
Protein: Chemerin-like receptor 1 (Chemokine-like receptor 1) (G-protein coupled receptor ChemR23) (G-protein coupled receptor DEZ) (Q99788)
Organism: Homo sapiens (Human)
Function: Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobilization, phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3, MAPK14/P38MAPK and PI3K leading to multifunctional effects, like reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B. Positively regulates adipogenesis and adipocyte metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15728234, ECO:0000269|PubMed:16863918, ECO:0000269|PubMed:27716822}; Multi-pass membrane protein {ECO:0000255}. Note=Internalizes efficiently in response to RARRES2. {ECO:0000269|PubMed:27716822}.
Interaction partners:
- Retinoic acid receptor responder protein 2
- Hematopoietic SH2 domain-containing protein
- Nicotinamide phosphoribosyltransferase
Sequence:
MRMEDEDYNTSISYGDEYPDYLDSIVVLEDLSPLEARVTRIFLVVVYSIVCFLGILGNGLVIIIATFKMKKTVNMVWFLNLAVADFLFNVFLPIHITYAAMDYHWVFGTAMCKISNFLLIHNMFTSVFLLTIISSDRCISVLLPVWSQNHRSVRLAYMACMVIWVLAFFLSSPSLVFRDTANLHGKISCFNNFSLSTPGSSSWPTHSQMDPVGYSRHMVVTVTRFLCGFLVPVLIITACYLTIVCKLQRNRLAKTKKPFKIIVTIIITFFLCWCPYHTLNLLELHHTAMPGSVFSLGLPLATALAIANSCMNPILYVFMGQDFKKFKVALFSRLVNALSEDTGHSSYPSHRSFTKMSSMNERTSMNERETGML
Protein: Maestro heat-like repeat family member 4 (G3X8W1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVVNKIKNMMVMEQGQVLDTICHFLEKENQLWEKPEVSFWNPSVEKLLEFLNLDPRKATDKAFFFHLYGMILRECPSVEKVQCHLASLLDLSHQHSRQREGIALAVGLASTKHLEEVWALLEHLGRTKFLQSVAATEDSQDEILKSSFLSATILLTRSLQAEYSSQRYKFTQTPELIQCLLGILQKEPNSLTNFLRQKIILVIIGLSNLRPRFKPLLKSQILKTCLQTVYMLPPAKDSRNDLFSVEQASDTTVLYKKTVRALDLLLQNFISENPSMDEVCFLLQHIEYWLMSDKIHERSRAVQSIYLLLQYVVDSLKLAKEAVPSLLGHQIGILILLWRDKDKITQQHSHFCVYLLMELVFQQKGKLVESAQWSKMKHFESNVFREWEMKLYHLVKVFKEDLTVAQHTQLILTLVHSLGSYNHLHSDLAAKLLLLICVEPGFRKEQIAELLQGLFQELPNIQSKSVQQAISQATLALGTQHIQEVVEVILSLCQPSERWILPLWKALAANYQVARDVITLLYIKLKLRPPRRLLQSTYRARLVSLMALGTIYELLYTKEYRNTVCWAFSGILLGLLTELYYLLEVGLVQGLFDYQEDDLGSKPLGPCRICLEALKGLFWTTEYWEVFADVKLIQGWELFGQLETFPKGVTLLARAMAHYNCEIKAVLGQALISLKSSEERDNIVGICIITEFLNSPDVSQHMSWKTMYNSLNLGLSSRNQMVRAMSLKGLGSTLMHPKKATLLRSKLMELLDNFLQPEFKDPAGLMKIMGHLLHCLSAQGIGIVSLKIAQHLLSLFTDERAAVREGAIFLFGDVIHYGGKKLRQSLKDVASQATVPLLFNMADPCQEVAMKARFTFLRCAILLKWEFRKELFGKLAWGQGLGAANDIFIYMLESNVGNYQQFLSQALTYLDSSHMTVKLAAMKFIGALLQDYFNDLCIYLRKKDVIFLKNCLEALRHDTDSRTRRFYLNYWNDAVELSYYVQD
Protein: Putative pyruvate decarboxylase C13A11.06 (EC 4.1.1.1) (Q09737)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Alcohol dehydrogenase
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Putative aldehyde dehydrogenase-like protein C922.07c
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Probable transketolase
- Pyruvate kinase
- Alcohol dehydrogenase 4
- Probable L-lactate dehydrogenase
- Putative S-
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Sequence:
MSGDILVGEYLFKRLEQLGVKSILGVPGDFNLALLDLIEKVGDEKFRWVGNTNELNGAYAADGYARVNGLSAIVTTFGVGELSAINGVAGSYAEHVPVVHIVGMPSTKVQDTGALLHHTLGDGDFRTFMDMFKKVSAYSIMIDNGNDAAEKIDEALSICYKKARPVYIGIPSDAGYFKASSSNLGKRLKLEEDTNDPAVEQEVINHISEMVVNAKKPVILIDACAVRHRVVPEVHELIKLTHFPTYVTPMGKSAIDETSQFFDGVYVGSISDPEVKDRIESTDLLLSIGALKSDFNTGSFSYHLSQKNAVEFHSDHMRIRYALYPNVAMKYILRKLLKVLDASMCHSKAAPTIGYNIKPKHAEGYSSNEITHCWFWPKFSEFLKPRDVLITETGTANFGVLDCRFPKDVTAISQVLWGSIGYSVGAMFGAVLAVHDSKEPDRRTILVVGDGSLQLTITEISTCIRHNLKPIIFIINNDGYTIERLIHGLHASYNEINTKWGYQQIPKFFGAAENHFRTYCVKTPTDVEKLFSDKEFANADVIQVVELVMPMLDAPRVLVEQAKLTSKINKQ
Protein: Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11) (Q99278)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 19
Sequence:
MQPPYIQERLKSLNDIETQLCSMLQEASQVTFIFGELKRGNESVKPQFENHVKQFYERLDKSTTQLRKEIQLLDENVGTRLLPINVNKKALGQDTEKMEEQLDLLSAILDPSKSK
Protein: INO80 complex subunit E (A0A0U1RP99)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MWSTETENFGRPCFFLSSCVQLLCDLSSPRSHWKQRSFRVFPQEGGRCDYAPRARRTLGVVVRFIRRCKVSGSGGVRGRADLGSGTLLRGVSPWRVMNGPADGEVDYKKKYRNLKRKLKFLIYEHECFQEELRKAQRKLLKVSRDKSFLLDRLLQYENVDEDSSDSDATASSDNSETEGTPKLSDTPAPKRKRSPPMGGVPSPSSLSLPPSTGFPLQTSGAPSPYLSSMSVGPPDCPVGGPLAFPARGSGASVGAALTPL
Protein: Cation-transporting P-type ATPase B (EC 7.2.2.-) (P9WPT9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Copper-exporting P-type ATPase
- Uncharacterized protein Rv0104
- Uncharacterized protein Rv2000
Sequence:
MAAPVVGDADLQSVRRIRLDVLGMSCAACASRVETKLNKIPGVRASVNFATRVATIDAVGMAADELCGVVEKAGYHAAPHTETTVLDKRTKDPDGAHARRLLRRLLVAAVLFVPLADLSTLFAIVPSARVPGWGYILTALAAPVVTWAAWPFHSVALRNARHRTTSMETLISVGIVAATAWSLSSVFGDQPPREGSGIWRAILNSDSIYLEVAAGVTVFVLAGRYFEARAKSKAGSALRALAELGAKNVAVLLPDGAELVIPASELKKRQRFVTRPGETIAADGVVVDGSAAIDMSAMTGEAKPVRAYPAASVVGGTVVMDGRLVIEATAVGADTQFAAMVRLVEQAQTQKARAQRLADHIAGVFVPVVFVIAGLAGAAWLVSGAGADRAFSVTLGVLVIACPCALGLATPTAMMVASGRGAQLGIFIKGYRALETIRSIDTVVFDKTGTLTVGQLAVSTVTMAGSGTSERDREEVLGLAAAVESASEHAMAAAIVAASPDPGPVNGFVAVAGCGVSGEVGGHHVEVGKPSWITRTTPCHDAALVSARLDGESRGETVVFVSVDGVVRAALTIADTLKDSAAAAVAALRSRGLRTILLTGDNRAAADAVAAQVGIDSAVADMLPEGKVDVIQRLREEGHTVAMVGDGINDGPALVGADLGLAIGRGTDVALGAADIILVRDDLNTVPQALDLARATMRTIRMNMIWAFGYNVAAIPIAAAGLLNPLIAGAAMAFSSFFVVSNSLRLRNFGAQ
Protein: Hemolysin expression-modulating protein Hha (P0ACE5)
Organism: Escherichia coli O157:H7
Function: Down-regulates hemolysin expression, in complex with H-NS, and can also stimulate transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli. Decreases biofilm formation (By similarity).
Interaction partners:
- Hha toxicity modulator TomB
- Hha toxicity modulator TomB
- DNA-binding protein H-NS
- DNA-binding protein H-NS
- DNA-binding protein StpA
- DNA-binding protein StpA
- Transcription regulator Ler
- UPF0259 membrane protein YciC
- Biofilm regulator
- DNA polymerase III subunit theta
Sequence:
MSEKPLTKTDYLMRLRRCQTIDTLERVIEKNKYELSDNELAVFYSAADHRLAELTMNKLYDKIPSSVWKFIR
Protein: Lysosome membrane protein 2-B (Lysosome membrane protein II-2) (LIMP II-2) (Q9BKJ9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis.
Subcellular location: Lysosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to membranes of endolysosomal vesicles and macropinosomes. {ECO:0000269|PubMed:11489884}.
Interaction partners:
- Oxidation resistance protein 1
Sequence:
MKHIGRIVSFPIGLVLIAVGIIIFVVVNRTIKDEFKKAAVVIPDNGAEEIVDPWVRFIGNEGDPNNVRTYTFMAYNLTNPIETMQGHLPKYQEVGPYSYNYIYERINANLYEDDEKLSFKLWKRYFPIVADGYRDPTKDTIYHFNLVYGAAVKQAGSEVALSVALTAAAMGKIITGLTDPSFKVKAGFAAAPTVTAGAFSNLLTAAGNDPATACGLWQTSTSSSTPLVPFSVPIIAGSPSDISQAQCQALFDPSNKFSLTDPTNVGVYLLNPAGSKAALLASPFGLTSVQADLIMKYQLALTSTFVPTTLVSRFAECSDPKTCTNNPLYFGLLQWAKNPSLLGQSVFAIPNSGVPAAPEFGIYTSSELSLTKAGSLFLNTSTINLITPTSIGTILVYGQKLKADPTSIPPALYAPFSSGEFDAIVKYTGYIMAAFVDGDIIKNQIFKDYQGGPIVKHTVHDFLFNSTDPLLKLMYPDTPSAWVSSPLDNIQDVKVANATLHTDEIYTGVGDIDLVSSPITFEGEEELNYNKKIKVSGSFAEQLPPSYLSKDPEAPVNVFTDEFARSLSFRKEVGGNFGGIPYYRYRINESNWEINPDYFQTIPYLLNLTSIKSGAPAYLSRPRLKGIDVGYYYKAGITDLINDDEDLDVFADYEPRSGKAIHGRYSLQVNTYIQGSDGTNSTLYNKYSAFRSDVVHPMFWGVNIIAATQEQIDILTKAYKVDSFRYAITVILIVVGGFLSLISGGLFVLDKIIDL
Protein: TATA-box binding protein associated factor 4 (A0A0G2K849)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 6
- TATA box binding protein
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 3
Sequence:
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPELRAAAAGALGNHVVSGSPAGAAGAGPAASAEGAPAAAPEPPPAGRARPAGGGPRRPGSSSPRRLLVPAGPAPAPAKLRPPPEASAGPCPVAAAAATAAAAAGPDPAAAAPPAGPGASKPGPPGPPGPGAAQTLNGSAAPPTAPHAAPAVSPVNNGPAPPPAAGSVIQAAPAPAAPSPPAAPAPAAPPPPAPPAPVAPARPPGHPAAPAPPVSPAAAAAAAAAAAQNGAAPAPAAASGGAAGLGQPGAGAQGAKAEAPKPGPGPGPGPAAAAAAAGVAGGGAAGGVLLGPAMPGALPGPAPGTPAGLAKGAAAATPSLPRTPAATTGAIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAHAQAQPQSTMAPRPATPTGAAPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPTTTLQRSPGVQPQLVLGGSAQPASLGTATAVQTGTPQRTVTGASTTSTAATETMENVKKCKSFLSTLIKLASSGKQSTETAANVKDLVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQQPPASQATTALTAVVLSSSVQRTAGKTAASVTSALQPPVISLTQPTQVGVGKQAPPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNQLQPVPVVKPTVLPGTKALSTVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDDTFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCAGPGSGAEGSGPGAAVPGGSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK
Protein: Lipoprotein (A0A0H3L6J6)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MKHFTAAVATVALSLALAGCSFNIKTDSAPTTSPTTTSPTTSTTTTSATTSAQAAGPNYTIADYIRDNHIQETPVHHGDPGSPTIDLPVPDDWRLLPESSRAPYGGIVYTQPADPNDPPTIVAILSKLTGDIDPAKVLQFAPGELKNLPGFQGSGDGSAATLGGFSAWQLGGSYSKNGKLRTVAQKTVVIPSQGAVFVLQLNADALDDETMTLMDAANVIDEQTTITP