wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear receptor subfamily 2, group E, member 3 (Zgc:103631) (Q5U3F3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSMVPFSSPTESSRSNSTDDSQDGKSPAPGKVLNTGLLCKVCSDTSSGKHYGIYACNGCSGFFKRSVRRRLIYRCQAGTGMCPVDKAHRNQCQACRLKKCLQAGMNKDAVQNERQPRSTAQVRLDALDVDKDKEHLATTLEPTSSSTCSVISRPLLGSSISSSISSTDGSQHSNSPKNGHRFMASLMTAETCAKLEPEDVDENIDVTSNEPERSSPMYGSALYPSREPESVYETSARLLFMSVKWAKNLPVFSHLPFRDQVILLEEAWSELFLLCAIQWSLPLDNCPLLSLPDLSPTGQGKGSPSASDVRVLQEVFSRFKPLQVDPTEFACLKAIVLFKPETRGLKDPEQVENLQDQSQVLLAQHIHTLYPSQVARFGRLLLLLPSLHFVSSERIEHLFFQRTIGNTPMEKLLCDMFKN
Protein: Transcription termination factor 1a, mitochondrial (Mitochondrial transcription termination factor 1a) (mTERF1a) (Q8CHZ9)
Organism: Mus musculus (Mouse)
Function: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15582606}.
Interaction partners:
- Transcription termination factor 3, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- Transcription termination factor 4, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial
Sequence:
MASRNIWCVRRNFLFDLRDWMLQYSAEVFLKSISFRPFSAECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKLFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKRDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEEKISASQIIENPRILDSSINTLKTRIRELSHAGYDLSTSSIALLSWSQRRYEAKLKRLCG
Protein: Zygote arrest protein 2.L (Protein A8) (Zygote arrest protein 2B) (K7SGN7)
Organism: Xenopus laevis (African clawed frog)
Function: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation. Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs, inhibiting their translation.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:C3VD30}.
Interaction partners:
Sequence:
MAGFMYAPYNVYQGYGGNFGQNPHVAQPLAKNKQAAWKSNKASEPTDYLDNFQRAQLKAILSQVNPNLTPRLRKANTKEIGVQVNPRVDTGVQCSLGPRTLRRPPPPPCSPVKAADCVRFTRPLAVYSPVVDRRLFSLPQGGRLPKKSPDSQSQPLKERAPSPEDKEREKVSEKEPDTKDELEKRPVPGTEEPGNEEQTKSAFQFLEQKYGYFHCKDCKTRWESAYVWCISGSNKVYFKQLCRKCQKGYNPYRVEAIQCQVCAKTRCSCPQKQRHIDLKRPHRQELCGRCKNKRLSCDNTYSYKYIV
Protein: Uncharacterized protein C17A5.05c (O13767)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSWRPTHSVRNAPYSMRDNYAQGVDVYYKKVGGTYRNLHFRGLRLLLLQCLSHFWDHDEKFKSHGLHVIDLACGSGEVSETVIEWEHLGRELGIHGGAFKVRKEISIRSIPPELPPFELIATDPFTLEAYTNRIGKPCLTLNFQDIADEKLPPSSAEDGIYDLVICSFALHLLTEPSKLFSTCYALSVQCRWLLVLGPHKKPELKPEWGWDAWNIDTWCPLGYGISHDYVLERVHARFFKSRNLIDG
Protein: Transcription initiation factor TFIID subunit 3 (140 kDa TATA box-binding protein-associated factor) (TBP-associated factor 3) (Transcription initiation factor TFIID 140 kDa subunit) (TAF(II)140) (TAF140) (TAFII-140) (TAFII140) (Q5HZG4)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (By similarity). TAF3 forms the TFIID-A module together with TAF5 and TBP (By similarity). Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The TAF3-TBPL2 complex replaces TFIID at specific promoters at an early stage in the differentiation process.
Subcellular location: Nucleus {ECO:0000269|PubMed:17704303}.
Interaction partners:
- Transcription initiation factor TFIID subunit 10
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 11
- TATA box-binding protein-like 2
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 13
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 5
Sequence:
MCESYSRSLLRVSVAQICQALGWDSVQLSACHLLTDVLQRYLQQLGRGCHRYSELYGRTDPILDDVGEAFQLMGVNLHELEDYIHNIEPVTFPHQIPSFPVSKNNVLQFPQPGSKDAEERKDYIPDYLPPIVSSQEEEEEEQVPTDGGTSAEAMQVPLEEDDEMEEEEVINDENFLGKRPLDSPEVEEMPSMKRPRLLSTKGDSLDVVLLEAREPLSSINPQKTPPVLSPVRVQDRADLAPPSPQPPMLAPFAKSQLPIAKPLETKSFTPKTKTKASSPGQKTKSPKAALSPARLGSPIRSPKTIPKEKKSPGRSKSPKSPKSPKIVAHVPQTPVRPETPNRTPSAMVVEKTVKETIPVMKPTQTPPEVVKLNIEMQPKKPVVTDKTIDDSIDAVIARACAEREPDPFEFSSGSESEGDTFTSPKRISGSECATPKASTSSNNFTKSLATPLPLSSGTSSSDNSWTMDASIDEVVRKAKLGAPSNMPPTFPYISSPSISPPTPEPLHKGYEEKAKLPSSVDVKKKLKKELKTKLKKKEKQRDRERERERNKERSKEKDKMREREKEKEAGKELKYPWRELMKDEDSDPYKFKIKEFEDIDAAKVRLKDGIVRREREKHKDKKKDRERSKREKDKRERERLKEKNREDKIKAPPTQLVLPPKEMALPLFSPSAVRVPAMLPAFSPMLPEKLFEEKEKPKEKERKKDKKEKKKKKEKEKEKEKKEREREKERREREKREKEKEKHKHEKIKVEPVIPAPSPVIPRLTLRVGAGQDKIVISKVVPAPEAKPAPSLNRPKTPPPAPVPIPVRVSPTPLQPPLLTQAAVCPALMPSPAPALSGIGSAKAPVRSVVTETVSTYVIRDEWGNQIWICPGCNKPDDGSPMIGCDDCDDWYHWPCVGIMAAPPEEMQWFCPKCANKIKKDKKHKKRKHRAH
Protein: ABC1 protein, putative (Q389Y6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein
Sequence:
MRDSKSKEVGLHPQLFTVLQTDHLFSYQFISESSLFFPCLWLGAPTLNEMTVNAITGSIGNVARGVAKVVSAVTGASCSGGVSSNVNAFASAVQRRTPTAKKPSPLPRELQTHLNGSNRAKMRTAVYRTVPSTRAARAAGFGTLFLRLGWDKLVGSEAGDKMLPVNSHMRIVETLCRMRGAVMKLGQMLSIQDDNTIPSNITSLFERVRDSAYAMPPKQLEQTLAKEYNDKNWRQELFKEFITEPIAAASIGQVHRAAVSDQDTGEKVAVAVKVQYPGVAQSIDSDVANLRMLMSLNILPPGMFVDNILDELQQELKTECSYSKEAEKQLRYAELLQQSPELKEVFVVPKVYKSLSTDRVLVTQMLSGVSIDKLASLVGMQDVKDYVARSMLHLTLTELFQWRFMQTDPNYSNFLFCPQTNKIGLIDFGAAREYNQEFVKDYLDVVAAAARRDRQTVIEKSIKLGFLKGNEMKEMLNAHAESVLLLGLPFNNRDVPFDFSKENLPSRIQGYVPTIVRLRLCPPPTPIYSLHRRLSGAILLSTKLKATVPSGELFWNIYDELTSV
Protein: Probable mannosyltransferase KTR2 (EC 2.4.1.-) (P33550)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in N-linked glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
Sequence:
MQICKVFLTQVKKLLFVSLLFCLIAQTCWLALVPYQRQLSLDSYFFRRSREVSSRYDFTRRRHMNQTLKLSSNTYNDEPLNKTKGIKNQRENATLLMLVRNWELSGALRSMRSLEDRFNKNYQYDWTFLNDVPFDQEFIEATTAMASGRTQYALIPAEDWNRPSWINETLFEEALQLMEEKNILYGGSKSYRNMCRFNSGFFFRQKILDPYDFYFRVEPDVEYFCDFPYDPFKVMRQNNKKYGFVITMYEYEDTIPSLWEAVEEYLEETESADIDMESNAFGFVSNFDFIGKSFGVIDSNSGYNLCHFWTNFEIGDLNFFRSEKYIRFFEYLDSKGGFYYERWGDAPVHSIAASLLLKKDEIIHFDELGYKHMPFGTCPSAYYLRLQQRCLCDSNHPDNIDLNVISCLRRWWKDGSGKYFLKHDS
Protein: Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) (Q19842)
Organism: Caenorhabditis elegans
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P05165}.
Interaction partners:
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Ethylmalonyl-CoA decarboxylase
- Acyl-coenzyme A oxidase acox-1.1
- Acyl-coenzyme A oxidase acox-3
- Acyl-coenzyme A oxidase acox-1.2
- Acyl-coenzyme A oxidase acox-1.4
Sequence:
MLRAASSIRAVANRGLATAAVARPGVPLDEREGKEIYTTVGIDYNEPKFDKILIANRGEIACRVIKTARAMGIKTVAVHSDVDSNSLHVKMADEAVCVGEAPTAKSYLRADRILQAVEDTGAQAVHPGYGFLSENTKFAAELEKAGAKFIGPNSKAILDMGDKIHSKKIATAARVSMIPGYDGEIADEDMCVKVSRDIGYPVMIKASAGGGGKGMRVAWNDKQAREGYRLSKQEAASSFGDDRMLVEKFIDNPRHIEMQVLCDKHGNALWLNERECSIQRRNQKVIEEAPSSFVPPEMRRKMGEQAVQLAKAVGYDSAGTVEFLVDSQRNFYFLEMNTRLQVEHPITECITGIDIVQQMLRVSYGHPLPITQEQVPLNGWAFESRVYAEDPYKGFGLPSVGRLSRYVEPKHVDGVRCDSGIREGSEISIYYDPLICKLVTHGDNREQALNRMQEALDNYVIRGVTHNIPLLRDIVQEKRFRTGDITTKYLPEVYPEGFQGTSLSPKEQDVVIAFASALNARKLARANQFLNQNKQRSTHVASFSKTYKFVSSLPVKEGERPTEHAVEVEFVEGSANKAQVRIGGKTVTISGDLNLSHPVNSIEVDGEHITTQIVGKRAGEITVLYKGTPFKVKVLPEQAVKYLQYMKEKAKVDLSTVVLSPMPGAIKNVNVKPGDMVSEGQELVVMEAMKMQNSLHAGKTGRVKAVNVKVGATVDEGEVLVELE
Protein: Glutathione peroxidase (C8VJD9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glutathione reductase
- Superoxide dismutase
- PAPA-1-like conserved region protein
- Chromatin modification-related protein eaf3
- Thioredoxin reductase, putative
- superoxide dismutase
- Catalase B
- Oxidoreductin
- Superoxide dismutase
- Superoxide dismutase
Sequence:
MPFTYCGLVPRLLSFRSSSSSTRQVRLRIPIQKTTASPGRISGATISSSFASRTSACILHFPSHRTLLQRQQPHLRPSQSTARYRFSTMASATTFYDFEPVDKKGEAYPLNQLKGKVILVVNTASKCGFTPQFKGLETLYQSIKAKRPDDFVILGFPCNQFGGQDPGSNDQIQEFCQLNYGVTFPVLGKTEVNGDNANPLWTWLKESQPGLLGLKRIKWNFEKFLISADGKVVGRWASTTKPEGLESRILEEIEKAEKQGLLASKAMQPEAAGTDGETAKLA
Protein: Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2) (HA synthase 2) (O35776)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By similarity). This is one of three isoenzymes responsible for cellular hyaluronan synthesis and it is particularly responsible for the synthesis of high molecular mass hyaluronan (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Lysosome {ECO:0000250|UniProtKB:Q92819}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane and either back to endosomes and lysosomes, or out into extracellular vesicles. Post-translational modifications control HAS2 trafficking. {ECO:0000250|UniProtKB:Q92819}.
Interaction partners:
- CD44 antigen
- Hyaluronidase-1
- Hyaluronidase-2
- UDP-glucose 6-dehydrogenase
- TNF alpha-induced protein 6.
- Hyaluronidase
- Hyaluronidase
- Factor VII-activating protease
- Hyaluronidase.
Sequence:
MHCERFLCVLRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSVTYIWKNNFHERGPGETEESHKESSQHVTQLVLSNKSICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLIYACYWVVLLTLYVVLINKCGRRKKGQQYDMVLDV
Protein: Protein DSE2 (Daughter-specific expression protein 2) (P38844)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pseudohyphal growth, cell wall metabolism and required for the separation of the mother and daughter cells.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:11935221}. Membrane {ECO:0000269|PubMed:11935221}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11935221}. Note=GPI-anchored cell wall protein (GPI-CWP).
Interaction partners:
- Endochitinase
- Probable secreted beta-glucosidase SUN4
- Probable family 17 glucosidase SCW11
- Protein DSE1
- Protein EGT2
- Glucan endo-1,3-beta-D-glucosidase 1
- Antagonist of mitotic exit network protein 1
- Protein DSE3
- Metallothionein expression activator
- Probable family 17 glucosidase SCW4
Sequence:
MKFNFSTIFNILFFLFTLIEANSNGETVKLITSDGIVYSYAVYTKTLAPARVVVKTISYTTTRVYPITLANSVVSSTTEKITEVSTVSASEQVSATQTNSLVSTSTVSTISPTISSGSSTSSSSTYDIESSQSIESSGTSSATAEPSASSGFRLTSSSAFVSSTAPFSSQLSSSSSSETSSSSFSTSSSSAPLSLTSSSSSSSSFATIITLAPSSSKSGNSQLTLASSSSTSAVESSQTGSTIARTTSTLVPSSSVDTTSRATTSMPLESSSTQSISVSSSDGTCYVFYDDDDYYSTVYLTNPSQSVDAATTITSTNTIYATVTI
Protein: Protein tramtrack, alpha isoform (Repressor protein fushi tarazu) (Tramtrack p88) (P42282)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform alpha is required to repress genes that promote the R7 cell fate. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. May bind to the region 5'-AGGG[CT]GG-3'. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein phyllopod
- Transcription initiation factor IIA subunit 1
- BIP1 protein
- E3 ubiquitin-protein ligase sina
- Maternal gene required for meiosis, isoform H
- Cullin 3, isoform F
- Ubiquitin-conjugating enzyme E2-17 kDa
- Transcription activator GAGA
- Ets DNA-binding protein pokkuri
- FI20028p1
Sequence:
MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSVTPTKATPELSQRLFGSSSTTISATAPGGSSTGPSETISLLEISDERESAPVHLPTILGLKIRAINTTTPAQQGSPQTPTKSKPKIRQATGSNNSNSLLKQQLRGGAKDPEVPPATRITGAVTPNAALNAEEQSKEMPKKNQDEVNACIGLHSLANAAEQQAAQVASTGNLHHQLLLHMAANNSMLNTTDYYQQQQQESPSSAGQFMDDDLELLSLNDQQDKSDEPDHEMVTLADENAGLPGYQGNEAEATPAQEDSPAAETATAPPPAPRSGKKGAKRPIQRRRVRRKAQSTLDDQAEHLTEMSVRGLDLFRYASVVEGVYRCTECAKENMQKTFKNKYSFQRHAFLYHEGKHRKVFPCPVCSKEFSRPDKMKNHLKMTHENFTPPKDIGAFSPLKYLISAAAAGDMHATIYQQQQDHYHRQLAEQLEQQNASFDSRDSSLILPDVKMEHAEDQDAEQEAELSDGGYDASNPAAAAAAMLSLQQDVIIKDEIQISPSPSPTPPASCAVAEGKSLALASTAQTAT
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (P57717)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Subcellular location: Nucleus.
Interaction partners:
- Aromatase
- G-protein coupled estrogen receptor 1
- Progesterone receptor.
- Nuclear receptor coactivator 3
- Estrogen receptor 2b
- Nuclear receptor corepressor 2
- ATPase family AAA domain-containing 2.
- Vitellogenin 1
- Transcription factor Jun
- Cellular tumor antigen p53
Sequence:
MYPKEEHSAGGISSSVNYLDGAYEYPNPTQTFGTSSPAEPASVGYYPAPPDPHEEHLQTLGGGSSSPLMFAPSSPQLSPYLSHHGGHHTTPHQVSYYLDSSSSTVYRSSVVSSQQAAVGLCEELCSATDRQELYTGSRAAGGFDSGKETRFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYVCPATNQCTIDRNRRKSCQACRLRKCYEVGMMKGGIRKDRGGRSVRRERRRSSNEDRDKSSSDQCSRAGVRTTGPQDKRKKRSGGVVSTLCMSPDQVLLLLLGAEPPAVCSRQKHSRPYTEITMMSLLTNMADKELVHMIAWAKKVPGFQDLSLHDQVQLLESSWLEVLMIGLIWRSIHSPGKLIFAQDLILDRSEGECVEGMAEIFDMLLATVARFRSLKLKLEEFVCLKAIILINSGAFSFCSSPVEPLMDNFMVQCMLDNITDALIYCISKSGASLQLQSRRQAQLLLLLSHIRHMSNKGMEHLYRMKCKNRVPLYDLLLEMLDAQRFQSSGKVQRVWSQSEKNPPSTPTTSSSSSNNSPRGGAAAIQSNGACHSHSPDP
Protein: TBC1 domain family member 23 (Q7SXV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Putative Rab GTPase-activating protein which plays a role in vesicular trafficking. Involved in endosome-to-Golgi trafficking. Acts as a bridging protein by binding simultaneously to golgins, located at the trans-Golgi, and to the WASH complex, located on endosome-derived vesicles (By similarity). Plays a role in brain development. May act as a general inhibitor of innate immunity signaling (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9NUY8}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9NUY8}.
Interaction partners:
- Cell division cycle 16 homolog
- Protein FAM91A1
- Uncharacterized protein.
- Si:dkey-34l15.1
- cAMP-responsive element-binding protein 1b.
- Ras-related protein Rab-30
- TBC1 domain family, member 14.
Sequence:
MADAVGEVLEGSWNQDLADALDSAVCDLNSDQDGVIQVRDLSPPQRAKLWMIALNVSGKGDSLSSWDGVLDLPEQTLIHSRSQQLIDELGIPVEEGRDLVSDVESVITFYCKSRNVTFTPDLSWPHILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKGRPFHLFRLLLQYHEPEFCSFLDTKKITPDSYAINWLGSLFSSHCLPEVTQALWDVYLQQADPFLIFFLMLIILVNAKDNILIQEGDNKEEIIKMLEQSPSLLEAEDIEDLFSLAQYYNSKTPLSLRKENHNLFGSSLVALKEEDMDLSQALCLPVSVPEILQANQLQPEGVRFFVVDCRPAEQYNAGHLSTAFHLDSDLMLHNPSELALSVKSLLEAQKQSLESGSVASGEHLCFMGSGREEEDMYMNMVLAHFLQKNKEFVSIAKGGFMALQQHLADINVEGPDNVYVHWIVSTSGSHSSLSSADGELNSTDGKGVKSLVNKMTFALKSKSVNVKEKVISFIENTSTPVERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSISDDDRKEIVNIQTWINKPDVKHHIPCNEVKETGHMFPSHLLITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKFGNNNAAGVEIVAVERYLIPNAGDATKVIKQQIMKVLDALESS
Protein: Glycerophosphodiester phosphodiesterase domain-containing 5b (Glycerophosphodiester phosphodiesterase domain-containing protein 5 isoform X2) (A0A2R8Q763)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVKHQPLQVYERQLCLSCLTGIYGCRWKRYQRSHDDTTKWECLWSLILFFTFSLLLVWFYFWWEAHNDYSEFNWFLYNRSGEWSDGTVPILATTAAGFTYIAFLMILALCHVAVGQQLNLHWVHKIGVTVALLTTIIGVISVTQMWGEEWDVVWISLQATGPFLHIGALAAVTALAWLMAGQVARAEKTRFQAMVLLLYLSVLLTLYFIPLSISSPCIMERGSLKAAPAIIGHQGAPMLAPENTLLSFNRALQRNVSGLETDVTISLDGVPFLMRDRTLRRTTNVRRVFPERQYEDASLFNWTDLSTLNAGQWFLKDDPFWTVQYMSTTERWSVGNQTVCSLEQMLKLAAKYKSSALFTVHRPPVNHPHHHDWVNLTLDTVLGSGIPQGQVMWTVDSNREMVRKVAPGFQQTSMQKLPFDTLHHNGISRLLLRYNQASEQDVRLYKENNISVSLYTVNEPWLYSLLWCSGVPSVSSEAPQVLRKLHYPLWLMTPDEYCLIWISTDLISFAVVLGIFIFQKWRMSGMRSYNPEQIMLSAAVRRSSRDVNIMKEKLIFSEVSNGVNGDEAYSENGFNYYTN
Protein: Adiponectin receptor protein (Q9VCY8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Adiponectin receptor. In insulin-producing cells, regulates insulin secretion and controls glucose and lipid metabolism.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GTP cyclohydrolase 1
Sequence:
MDSATNLLEQQGSAADVSGGSHPAEVEVTTQARATFGMDAEGHATGEAVTTTTATLRREGSDEDIFEQVQMILRKRRGWGPEDSLSPNDLDILEYDDELVEEDDAGCPLPSTPEDTQLIEAEMTEVLKAGVLSDEIDLGALAHNAAEQAEEFVRKVWEASWKVCHYKNLPKWLQDNDFLHRGHRPPLPSFRACFKSIFRVHTETGNIWTHLLGCIAFIGVALYFISRPSVEIQTQEKIVFGAFFIGAIVCLGFSFAFHTLSCHSVEMGRLFSKLDYCGIALLIMGSFVPWLYYGFYCHYQPKVIYLSVVSILGILSIVVSLWDKFSEPALRPLRAGVFMSFGLSGVIPAIHYSIMEGWFSQMSRASLGWLILMGLLYILGALLYALRVPERWFPGKFDIWGQSHQIFHILVIAAAFVHYHGISEMAMYRVMYSECTVPIEPITF
Protein: Found in neurons, isoform A (Found in neurons, isoform B) (Found in neurons, isoform C) (Found in neurons, isoform E) (Found in neurons, isoform G) (Found in neurons, isoform H) (Putative RNA binding protein) (RT06063p1) (Q9VYI0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein elav
- LD31543p
Sequence:
MTNAMDIVKNGSANGSVDGSNDESRTNLIVNYLPQTMTQEEMRSLFSSIGELESCKLVRDKVSGNLVLPASLTALNPALQQGQSLGYGFVNYVRAEDAEKAVNTLNGLRLQNKVIKVSYARPSSESIKGANLYVSGLPKNLSQPDLEGMFASFGKIITSRILCDNISGLSKGVGFIRFDQRNEAERAIQELNGKTPKGYAEPITVKFANNPSNSAKAQIAPPLTAYLTPQAAAATRRLAGALPSAGRIRYSPLAGDLLANSILPGNAMTGSGWCIFVYNLAPETEENVLWQLFGPFGAVQSVKVIRDLQTSKCKGFGFVTMTNYDEAVVAIQSLNGYTLGNRVLQVSFKTNKTKTT
Protein: Aromatic and large neutral amino acid transporter 5-3 (Apicomplexan amino acid transporter 5-3) (TgApiAT5-3) (Major facilitator superfamily domain-containing protein) (A0A7J6K338)
Organism: Toxoplasma gondii
Function: L-tyrosine transporter that is essential for parasite survival and virulence. May also act as an aromatic and large neutral amino acid transporter. Does not cotransport other charged ions. Involved in amino acid homeostasis by facilitating the net uptake of L-tyrosine and maintaining intracellular pools of aromatic and large neutral amino acids through exchange.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30742695}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MESTEATMVERKAESPSSGDRARSIELAHQPTGAGASLSSFEVGGAKQGVNKAQDSAVNKGAANTPPRVAFGLSRYVVLVAYCLYCLLSGPSFMNWTTIADSLYKSGAFEWECKPGEIDTSVLPHEPKCPEQEVSVNHLFTVASCSYFVFAMLGGIMLDFAGPKFGALTGLACLITGWTLFGFSSESFRAYVPAMVFMGAGIDMAFFPCLCGANLFPGMVATIIAVYGSFRSISFIVGLSLRTIYINVEGATFRGVMLGYVGAGLGFCLLVALFIIPRRAWPAPDEAPSASAEQDVEAGADALAQKGEKNLTAIQSMKRDFLSLSFLPLFPYFVLVLITILFFAPSAKRLIPSAYEANQIISIFSFVPCIILGGIADRLGIVPVMMICNTCGLLSWILMLIPGIPCFAASQYIVSILISIQMSFLVSQVYCYVTEIFYPENLGKMIGFLCSVGGIISLVTDPMRKYSVDNGFYTMTVLCLIFALINEGLLLFMYVRKRKVPKVL
Protein: B-cell CLL/lymphoma 6, member B (Zinc finger protein), isoform CRA_a (cDNA FLJ16548 fis, clone PLACE7000410, highly similar to B-cell CLL/lymphoma 6 member B protein) (cDNA FLJ77637) (cDNA FLJ77701, highly similar to Homo sapiens B-cell CLL/lymphoma 6, member B (zinc finger protein)(BCL6B), mRNA) (A8KA13)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSPAAPEGALGYVREFTRHSSDVLGNLNELRLRGILTDVTLLVGGQPLRAHKAVLIACSGFFYSIFRGRAGVGVDVLSLPGGPEARGFAPLLDFMYTSRLRLSPATAPAVLAAATYLQMEHVVQACHRFIQASYEPLGISLRPLEAEPPTPPTAPPPGSPRRSEGHPDPPTESRSCSQGPPSPASPDPKACNWKKYKYIVLNSQASQAGSLVGERSSGQPCPQARLPSGDEASSSSSSSSSSSSEEGPIPGPQSRLSPTAATVQFKCGAPASTPYLLTSQAQDTSGSPSERARPLPGSEFFSCQNCEAVAGCSSGLDSLVPGDEDKPYKCQLCRSSFRYKGNLASHRTVHTGEKPYHCSICGARFNRPANLKTHSRIHSGEKPYKCETCGSRFVQVAHLRAHVLIHTGEKPYPCPTCGTRFRHLQTLKSHVRIHTGEKPYHCDPCGLHFRHKSQLRLHLRQKHGAATNTKVHYHILGGP
Protein: HMG-box transcription factor 1 (H7C4S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
QMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSSSKSEPAFPHHHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKGSNKEWQDVEDFARAEGCDNEEDLQMGIHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEVHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGPGGQDFARSGFSKNCGSPGSSQLSSNSLYAKAVKNHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNR