wanglab/gogpt-training-data huggingface dataset:
Protein: Long-chain-fatty-acid--CoA ligase (E1JHE4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bardet-Biedl syndrome 9
- Bardet-Biedl syndrome 1
- Bardet-Biedl syndrome 8
- Delta
- BBSome complex member BBS4 homolog
Sequence:
MLFRKARRHFLPFYMFNGFLXQRNERYQRLRYNSSNIGHPRHELTHNSLLDNYANSNVIINIDNCALYSTNRPADRKSITDGSHDRQRRRRQRFLVIFRFFCATVAFGLAIACVIYTLHTMGWIFAVLVALVALLLTKPGWRWFYIAGATASRDLTALWAYIKLLRYTKRHERLNYTVADVFERNVQAHPDKVAVVSETQRWTFRQVNEHANKVANVLQAQGYKKGDVVALLLENRAEYVATWLGLSKIGVITPLINTNLRGPSLLHSITVAHCSALIYGEDFLEAVTDVAKDLPANLTLFQFNNENNNSETEKNIPQAKNLNALLTTASYEKPNKTQVNHHDKLVYIYTSGTTGLPKAAVISHSRYLFIAAGIHYTMGFQEEDIFYTPLPLYHTAGGIMCMGQSVLFGSTVSIRKKFSASNYFADCAKYNATIGQYIGEMARYILATKPSEYDQKHRVRLVFGNGLRPQIWPQFVQRFNIAKVGEFYGATEGNANIMNHDNTVGAIGFVSRILPKIYPISIIRADPDTGEPIRDRNGLCQLCAPNEPGVFIGKIVKGNPSREFLGYVDEKASAKKIVKDVFKHGDMAFISGDLLVADEKGYLYFKDRTGDTFRWKGENVSTSEVEAQVSNVAGYKDTVVYGVTIPHTEGRAGMAAIYDPERELDLDVFAASLAKVLPAYARPQIIRLLTKVDLTGTFKLRKVDLQKEGYDPNAIKDALYYQTSKGRYELLTPQVYDQVQRNEIRF
Protein: Fibrillarin (M0R299)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
VMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYR
Protein: Cytochrome P450 monooxygenase stcF (EC 1.14.-.-) (Cytochrome P450 60A2) (Sterigmatocystin biosynthesis cluster protein F) (Q12609)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
- Norsolorinic acid ketoreductase stcE
- Uncharacterized protein.
- Norsolorinic acid synthase stcA
Sequence:
MILPLILVLYLLSTAAYRLWLHPLRNYPGPCWWAVWRVPYLKGTIRGTIVRDIQRLHNQYGPVVRIAPDELSYITPEAAKPIYTSSPEFPKDPMHLPPFHNGAPGILAADYAHHRRYRRLLASAFSEKGLRAQQGMIQSHIDRLMTRLQGNCSSGSLDMTVWFNWATFDIIGDLAFGEPFGCLERMETNPWIASIQGNVKSIPILNALRRYRLDRLIEFLAPPRLLEMRRRNAQFTAEKVDRRLKHATTTRGDLWDSVLADPPDGEPPMSRAEMVSNASAIVLAGSETSATTLSGCLWLLLTNPEYLQQLTERIRARFSTATVIDAQTVTQIQGLQAVLDESLRLYPAVPMQSNRIVPPPGARLAGSWVPGGTSVAVQQFAACRSPTNFHRPDEFIPERWEKEGEFINDRREASQPFSIGPRNCIGRQLALAEMRLILVHLLWHFDIELDRRRMENMDWMAVQGIWILWDKKPLWVVLKNRST
Protein: 3beta-hydroxysteroid dehydrogenase dhs-16 (EC 1.1.1.-) (O16881)
Organism: Caenorhabditis elegans
Function: 3beta-hydroxysteroid dehydrogenase that converts 3beta-hydroxysteroids to 3-ketosteroids, an essential step in the production of dafachronic acids from cholesterol. Catalyzes the dehydrogenation of lathosterol (5alpha-cholest-7-en-3beta-ol) to lathosterone (5alpha-cholest-7-en-3-one), a step required for maximal biosynthesis of Delta(7)-dafachronic acid. Dafachronic acids act as ligands and bind directly to the nuclear hormone receptor (NHR) daf-12, suppressing dauer formation and inducing reproductive growth, they can also regulate C.elegans lifespan.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cholesterol 7-desaturase
- 3beta-hydroxysteroid dehydrogenase/Delta
- Sterol 4-C-methyltransferase strm-1
- 3-ketosteroid oxygenase
- Nuclear hormone receptor family member daf-12
- NADPH--cytochrome P450 reductase
- NPC intracellular cholesterol transporter 1 homolog 1
- NPC intracellular cholesterol transporter 1 homolog 2
Sequence:
MLELIYILPLLCFVYFLFRRFVLENFYVESSGKYVMITGCDSGFGRLLATSLLDKHVNVFAACFTQQGMASLHSEWKLKKGPKGQLYTLQLDVTSQASVDSAKSFVTKILKEQNSKLWGLVNNAGIFSIHGPDDWCSVDEYASSLNVNTLGAVRMCHAFVPLIKKSRGRIVTMGSTAGRLHGLYVAPYVTAKFAVEAYMDCLRLEMRPFGVSVHILEPGCFKTELLNNDAQRMRIQKIWNSLSVETKEEYGEDYRNDFERAWEAGVNVVANPNIGWVVDCYSHALFSWWPRLRYCPGWDAIFMFIPLSIFPTALQDWILAGLYKLNPGPSLTPAVLVKNKKRRSAIQWIQFLSQIAIIPLLYTIFFVKNTQKQTVETSTHHHNVTVSE
Protein: RNA polymerase-binding protein RbpA (Q9RKY0)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Binds to RNA polymerase (RNAP), stimulating transcription from principal, but not alternative sigma factor promoters. Stimulates transcription from several principal sigma factor HrdB (SigA)-dependent promoters but not from a SigR-dependent promoter. Stimulation occurs in the presence of the transcription initiation inhibitor rifampicin (Rif).
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- RNA polymerase-binding transcription factor CarD
- DNA-directed RNA polymerase subunit alpha
- RNA polymerase principal sigma factor HrdA
- RNA polymerase principal sigma factor HrdC
- RNA polymerase principal sigma factor HrdB
- RNA polymerase principal sigma factor HrdD
- Transcriptional regulator WhiB
Sequence:
MSERALRGTRLVVTSYETDRGIDLAPRQAVEYACEKGHRFEMPFSVEAEIPPEWECKVCGAQALLVDGDGPEEKKAKPARTHWDMLMERRTREELEEVLEERLAVLRSGAMNIAVHPRDSRKSA
Protein: GSKIP domain-containing protein (D9PTP1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLPRTPDLIFVNVTTLEAQPYCLELTLKGWRITSLRSDCMVGDFTRLELFTKYYDSLYLLMDDISPGYRERFSEKLVQRLKLIEAGEEDQVAPCASLQSPSLSTDSSSKESQYSSTESLPIVTPVSTPAIDPDFKPKFK
Protein: Thioredoxin domain-containing protein 15 (Q96J42)
Organism: Homo sapiens (Human)
Function: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Involved in ciliogenesis.
Subcellular location: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q6P6J9}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVPAAGRRPPRVMRLLGWWQVLLWVLGLPVRGVEVAEESGRLWSEEQPAHPLQVGAVYLGEEELLHDPMGQDRAAEEANAVLGLDTQGDHMVMLSVIPGEAEDKVSSEPSGVTCGAGGAEDSRCNVRESLFSLDGAGAHFPDREEEYYTEPEVAESDAAPTEDSNNTESLKSPKVNCEERNITGLENFTLKILNMSQDLMDFLNPNGSDCTLVLFYTPWCRFSASLAPHFNSLPRAFPALHFLALDASQHSSLSTRFGTVAVPNILLFQGAKPMARFNHTDRTLETLKIFIFNQTGIEAKKNVVVTQADQIGPLPSTLIKSVDWLLVFSLFFLISFIMYATIRTESIRWLIPGQEQEHVE
Protein: Acyl-CoA-binding protein (ACBP) (Diazepam-binding inhibitor) (DBI) (Endozepine) (EP) (P31786)
Organism: Mus musculus (Mouse)
Function: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07108}. Golgi apparatus {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}.
Interaction partners:
- Translocator protein
- Diazepam-binding inhibitor-like 5
- Apolipoprotein E
- Apolipoprotein A-I
- Apolipoprotein C-III
- Apolipoprotein A-V
- Apolipoprotein B-100
- Apolipoprotein A-II
- Clusterin
- Peroxisomal biogenesis factor 3
Sequence:
MSQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI
Protein: Palmitoyltransferase ZDHHC15 (EC 2.3.1.225) (Acyltransferase ZDHHC15) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15) (DHHC-15) (Q2TGJ4)
Organism: Rattus norvegicus (Rat)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Palmitoylates IGF2R and SORT1, promoting their partitioning to an endosomal membrane subdomain where they can interact with the retromer cargo-selective complex (By similarity). Thereby, regulates retrograde transport from endosomes to the Golgi apparatus of these lysosomal sorting receptors and plays a role in trafficking of lysosomal proteins (By similarity). In the nervous system, catalyzes the palmitoylation of DLG4/PSD95 and regulates its synaptic clustering and function in synaptogenesis. Could be involved in the differentiation of dopaminergic neurons and the development of the diencephalon (By similarity). Could also catalyze the palmitoylation of GAP43 (By similarity). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Could also palmitoylate FYN as shown in vitro (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:31189538}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density {ECO:0000269|PubMed:31189538}.
Interaction partners:
Sequence:
MRRGWKMALSGGLRCCRRVLSWVPVLVIVLVVLWSYYAYVFELCLVTVLSPAEKVIYLILYHAIFVFFAWTYWKSIFTLPQQPNQKFHLSYTDKERYKNEERPEVQKQMLVDMAKKLPVYTRTGNGAVRFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYKFFLQFLAYSVLYCLYIATTVFSYFIKYWRGELPSVRSKFHVLFLLFVACMFFVSLVILFGYHCWLVSRNKTTLEAFCTPVFTSGPEKNGFNLGFIKNIQQVFGDNKKFWLIPIGSSPGDGHSFPMRSMNESQNPLLANEEPWEDNEDESQDYPEGLSSLAVESET
Protein: Large ribosomal subunit protein uL3 (60S ribosomal protein L3) (H7C422)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
QMMNLLTGGQKLCADCHVLIWLCGVLWPSHRKFSAPRHGSLGFLPRKRSSRHRGKVKSFPKDDPSKPVHLTAFLGYKAGMTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDEDGKKQLEKDFSSMKKYCQVIRVIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRT
Protein: SET domain and MYND-type zinc finger protein 6 (EC 2.1.1.-) (O94256)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes to chromatin.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Histone-lysine N-methyltransferase set9
- Histone H4
- Protein arginine N-methyltransferase 2
- Lysine-specific histone demethylase 1
Sequence:
MDAPLIASVILPEFGKGTVATDNIPIGKIIIRKRVDILSLDSANLTRTCSTCTEEKVKTQRCAACKIIHYCSKGCQKADWPFHKLECKALQASKQNGILPSVCRLLIRLYLLWQKNPAIIEPMEGHQNEFQAVSSSWSDAELIASAASHYTQIYQAELFQKLFCRLAVNAMNLVTSSFDSLGMCLDTILCRLNHSCDPNCQIIFDGAIVQLVSKRDIKKDEQLFISYIDIRLPKSIRQKQLLKKYFFSCYCPRCENDHTTKETDGSKWMGRLRNSKSLMKNLAMARDLWSCGWKQTAFPWSNLLHHIKLGMLDESNFNGAFAALYLKSSADEFLDALHVVDEYQLLLLGKQVAMEVKHLMFPNDKPLEMEFPSSSQPQQTVPTNNSLFLLKNIPSFGGLHHCILGRYSISLDDFVLWLLDRAQRLQQAVRISHPSTTFCSNVENDIKEIFEVCKDYCMLHVQNNLKAFEEKLWAACKDFLVTY
Protein: Magnesium transporter NIPA3 (NIPA-like protein 1) (Non-imprinted in Prader-Willi/Angelman syndrome region protein 3 homolog) (Q8BMW7)
Organism: Mus musculus (Mouse)
Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+), Cu(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:32439805}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGVQLRLPPGEPCHEGYVLSLVCSNSSRASCEITNVSESLPYPVVYTNLNSSKTNFSISASVENKYNLYVGLVLAISSSVFIGSSFILKKKGLLQLADKGITRAGQGGHSYLKEWLWWAGLLSMGAGEAANFAAYAFAPATLVTPLGALSVLISAILSSYFLNERLNIHGKIGCILSVLGSTVMVIHAPQEGEVTSLHEMEMKLRDPGFVSFAVIISVISLVLILIVAPKKGQTNILVYIAICSLIGAFSVSSVKGLGIAIKELLERKPVYKDPLFFILLTMLALSVTTQINYLNKALDTFNTSLVTPIYYVFFTSMVVTCSAILFQEWYGMKAGDIIGTLSGFFTIINGIFLLHAFKNTNITWSELMSTAKKEALSPNGNQNSYVLLENADFSASGYDDDITLFSRTNDQSSHKL
Protein: ER protein translocation subcomplex subunit sec67 (O14085)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as non-essential component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec72 may be involved in signal peptide recognition for a defined subset of leader peptides, or may increase the efficiency of unusual or 'difficult' secretory precursors to the translocation pore, it may be that this protein binds charged leader peptides to the membrane until they engage the translocation apparatus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Translocation protein sec63
- Translocation protein sec66
- Translocation protein sec62
- Probable protein transport protein Sec61 subunit gamma
- Protein transport protein sec61 subunit beta
- Protein transport protein sec61 subunit alpha
- Uncharacterized protein C19G7.17
Sequence:
MVAKQESVVAPQVDVSKWSGKELELGKKVNEYAKSLATFKYPFFIPPPYPPAKPNMALSTQVNKMKQTANEAFKRKKYEEAKKLYGLALQLALNRCTWEPSILTREEASVMLCNRAAAEIALSQFPEALADANAALKIRNNYGKCYYRKAKALEAMHRIEEAKQVVRDGLILAEPVTRNELVALWASYTEKD
Protein: Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)] (H0YLH9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU363135}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363135}. Secreted {ECO:0000256|RuleBase:RU363135}.
Interaction partners:
Sequence:
XRQARMDYSFDTTAEDPWVRISDCIKNLFSPIMSENHGHMPLQPNASLNEEEGTQGHPDGTPPKLDTANGTPKVYKSADSSTVKKGPPVAPKPAWFRQSLKGLRNRASDPRGLPDPALSTQPAPASREHLGSHIRASSSSSSIRQRISSFETFGSSQLPDKGAQRLSLQPSSGEAAKPLGKHEEGRFSGLLGRGAAPTLVPQQPEQVLSSGSPAASEARDPGVSESPPPGRQPNQKTLPPGPDPLLRLLSTQAEESQGPVLKMPSQRARSFPLTRSQSCETKLLDEKTSKLYSISSQVSSAVMKSLLCLPSSISCAQTPCIPKEGASPTSSSNEDSAANGSAETSALDTGFSLNLSELREYTEGLTEAKEDDDGDHSSLQSGQSVISLLSSEELKKLIEEVKVLDEATLKQLDGIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGTTHHDALAILRQAREPRQAVIVTRKLTPEAMPDLNSSTDSAASASAASDVSVESTEATVCTVTLEKMSAGLGFSLEGGKGSLHGDKPLTINRIFKGVGCVWFFACSPVVGMWPGPQKASGHFLGYVVSHNSMSSS
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (R9UQ53)
Organism: Middle East respiratory syndrome-related coronavirus (MERS-CoV)
Subcellular location: Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00034689, ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000256|HAMAP-Rule:MF_04099}.
Interaction partners:
Sequence:
MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPHVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH
Protein: Transcriptional regulator Medusa (Q4X0J5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MSTFQKPPSAALLGKFVPSFFLEHCCSFGKCRQTDRLTLSDYDSARSLHNGASYSTYGQTPYVTATSLVPSPMADQASQISDCGPYLPNQEYASSYEESRSPMLGAESRQLPEVVSYNPQRGSEGTRVFVQIQCPHDLHSSPYATLYLVFGSKKCECLPHFLGLQGSSFQYALSVDTPPFLATGSPSLAVPLQIIIDNHQGGSVNTLQVGVYTYEQTSQDSPSDESRKRRIASYSENVAYRPIRRAAGQQGYEDGRATSYSPYLQPLPAMNGFLPPYQGNASPRVAPAQYSAGSSASHSSIRAPSPLTPAWSPSIVNVTSDSRAPAYAIAHSLRQHKSSSPARPANPTLIRTSTLQQANGLGHSQSFNPYAMYPSKAVLKLNGDLDSMAEGWTKEEREAKRRLVQFTRMQNGSTIHADFKPVSPDERAPNSICISCIYWEGKDECFVTSVDTIYLLESLVGVRFTVEEKNRIRRNLEGFRPLTVSKAKADSEDFFKVIMGFPAPKPRNIEKDVKVFPWKILSHALKKIIGKYSASYSSTAGALPTPISSTFAGNGAASDSGTEPYAAASPQSVSDAAPSSSYCHSIATPAYSPPTGSSGPHMTGTVELRAVLPAVTQPYHSMASGYAYPTVCQQQGQLSLTAPVSRPSWNPNSLAHQPSASAAPSYSYLAPLPYSLPDPSHGC
Protein: Transcription factor Dp (Q24318)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes. Can stimulate E2F-dependent transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor E2f1
- Transcription factor E2F2
- Retinoblastoma family protein
- RE32990p
- Lin-52, isoform A
- Protein lin-54 homolog
- LD07342p
- Chromatin assembly factor 1 p55 subunit
- LD06557p
- Myb protein
Sequence:
MAHSTGGTVKTDEVNFFFRNEHGQISKMLKPAQNKSEMEGGKPVAVVYATGSSARNSGSASGIGNVGRMGAFSQMGSQGQFIRLQDNGLSIPKTEAGTTYTTVSAQKTSGAGSGHYDLPLKGDRYVKFTPNPIKMKSKLHAIQSNSLHSMSASSSSVQRKRKPDKAGKGLRHFSMKVCEKVEEKGKTTYNEVADDLVSEEMKNNAYDNNCDQKNIRRRVYDALNVLMAINVISKDKKEIRWIGLPANSTETFLALEEENCQRRERIKQKNEMLREMIMQHVAFKGLVERNKRNESQGVVPSPNASIQLPFIIVNTHKSTKINCSVTNDKSEYIFKFDKTFEMHDDIEVLKRMGFLLGLDKGECTPENIERVKSWVPPNLAKYVEAYGTGKTGENMYESDDEDNEFNGYLESANESQGFAQHSAQHTTDGEFKLEMDDDELDDDID
Protein: Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC 2.4.1.144) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III) (GNT-III) (GlcNAc-T III) (N-acetylglucosaminyltransferase III) (Q09327)
Organism: Homo sapiens (Human)
Function: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate. Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation. In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (By similarity).
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
Sequence:
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQASPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKPGTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCESNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (U6DU97)
Organism: Neovison vison (American mink) (Mustela vison)
Interaction partners:
Sequence:
DFLVRESQGKQEYVLSVLWDGQPRHFIIQSADNLYRLEGDGFPSIPLLIDHLLRSQQPLTKKSGIVLNRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYNHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGSRLRMKTLLQMVGDAAAGMEYLES
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-I) (Aminoglycoside resistance protein) (Q15BH7)
Organism: Morganella morganii (Proteus morganii)
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including tobramycin and netilmicin and to a lesser extent to gentamicin and amikacin.
Interaction partners:
Sequence:
MDSSPLVRPVETTDSASWLSMRCELWPDGTCQEHQSEIAEFLSGKVARPAAVLIAVAPDGEALGFAELSIRPYAEECYSGNVAFLEGWYVVPSARRQGVGVALVKAAEHWARGRGCTEFASDTQLTNSASTSAHLAAGFTEVAQVRCFRKPL