wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (O09009)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1. May be involved in limb formation and in neurogenesis (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Beta-1,3-N-acetylglucosaminyltransferase manic fringe
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- GDP-fucose protein O-fucosyltransferase 1
Sequence:
MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHWCPMKNRVEGAFQ
Protein: Cytochrome c oxidase VII, putative (Q57XX4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPRPFGVWAPATTLAEYRARIPGMSNFKLRWVFGARREVYYHPEALAHFKDHQQYKDAVDTVRAMRTSDKFFGEGVKLPHHPLIKMGVILSIHGYLTYCCLRYYYGTHVPANNPTWRKIVNKEWEEAINNSPWDHMSHVWQYSDQYASSIGEAAALGRRKFYIPA
Protein: D-aminoacyl-tRNA deacylase (DTD) (EC 3.1.1.96) (Gly-tRNA(Ala) deacylase) (O14274)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}.
Interaction partners:
- Uncharacterized protein C577.11
- N-acetyltransferase ats1
- Pre-mRNA-splicing factor 38
- Cytochrome b-c1 complex subunit 10
- V-type proton ATPase subunit D
- ADP-ribosylation factor-like protein alp41
- Pre-mRNA-splicing factor prp1
Sequence:
MKAVIQRVLNASVSVDDKIVSAIQQGYCILLGVGSDDTPEDVTKLSNKILKLKLFDNAEQPWKSTIADIQGEILCVSQFTLHARVNKGAKPDFHRSMKGPEAIELYEQVVKTLGESLGSDKIKKGVFGAMMNVQLVNNGPVTILYDTKE
Protein: Cleavage and polyadenylation specificity factor subunit 6 (Q9VSH4)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in pre-mRNA 3'-processing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 5
- YTH domain-containing protein 1
- Cleavage stimulation factor 64 kD subunit
- Pre-mRNA cleavage complex 2 protein Pcf11
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- LD24014p
- Factor interacting with poly
- Cleavage and polyadenylation specificity factor 73
Sequence:
MADVVLDLYAEDLDKDFAGQAQDEFGGDGVDLYDDIGGPTESAASGGGGGGTPSADGAAGPGSGEPGERNSGGPNGVYHQSSGSLTPTMNRRYQLYVGNLTWWTTDQDIANSLRDIGVSDLQEVKFFENRANGQSKGFSVISLGSESSLRAVLDQLPKKEMHGQAPVVTYPSKQALTQFESLQKTRPVPPPQQNGPPRGPAPPSMGGGPMPTGHPGGPQGGGPPGHPPRGMNSIMQPGQYRPQHMSQVPQVGGPNSGPPRMQPPMHPQGGLMGNQQPPPRYPSAQGQWPGQRPGGPRPGPPNGPPQRPMFQGGPMGMPVRGPAGPDWRRPPMHGGFPPQGPPRGLPPAPGPGGPHGAPAPHVNPAFFNQPGGPAQHPGMGGPPHGAPGPQPGMNMPPQQGMNMTPQHGPPPQFAQHGPRGPWPPPQGKPPGPFPDPQQMGPQLTEVEFEEVMSRNRTVSSSAIARAVSDAAAGEYSSAIETLVTAISLIKQSKVAHDERCKILISSLQDTLHGIEAKSYNRRERSRSRERSHRSRQRRERSTSRYRERSRERERDRDRERERDGGSYRERSRSRERERQAPDHYRDDSRSVRPRKSPEPVVAEAAEAPSSKRYYEDRERYRSSDRERRDRDRDRDRERERDRDRREEHRSRH
Protein: 32 kDa beta-galactoside-binding lectin (Galectin-1) (O44126)
Organism: Haemonchus contortus (Barber pole worm)
Function: Binds galactose. Exerts immunomodulatory effects on host peripheral blood mononuclear cells to down-regulate host immune response. Hemagglutinates human, dog, rabbit, chicken and mouse erythrocytes but does not hemagglutinate the erythrocytes of goat, its natural host.
Subcellular location: Membrane {ECO:0000269|PubMed:10599080}.
Interaction partners:
Sequence:
MVSQFLHWYEYNKPVPYRSLLQEKIEPGQTLIVKGSTIDESQRFTINLHSKSADFSGNDVPLHISVRFDEGKVVMNTFANGEWGKEERKSLPIKKGDSFDIRIRAHDDRFQIVIDQKEFKDYEHRLPLTSITHLSIDGDLYLNHVHWGGKYYPVPYESGIASGFPIDKTLLIFGTVEKKAKRFNINLLRRNGDIALHFNPRFDEKAVIRNALAANEWGNEEREGKMPFEKGVGFDLAIKNEAYAFQIFVNGERFTSFAHRQDPNDISGLQIQGDIELTGIQIQ
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (X1WET9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3, subunit F
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
Sequence:
MRDTENMEAEMEYDDEEEPSFSDPEDFDDDISDQELLGDVLRDKPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKITNEFYPDADGKTKGYIFLEYSAPSHAHEAVKNADGYKLDKQHTFRVNLFTDFDKYMSICDEWEAPEKQPFKDFGNLRHWMEDPDCRDQYSVIYDSGERTGIFANDVKEPIEVEERARWTETYVRWSPKGTYLATFHQRGIALWGGEKFKQIQRFSHQGVQLIDFSPCERYVVTFSPLMDTKDDPQAIIIWDVLTGQKKRGFHCESSAHWPIFKWSPDGKFFARMTQDMLSIYETPSMGLLEKKSLKINGIKDFSWSPGDNIIAFWVPEDKDIPARVTLMQFPSRNEMRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKDSIIAFAWEPNGSKFAVLHGESPRINSSFYHVKSNGKIDLIKMFDKQQANSIFWSPQGQFLVLAGLRSMNGALAFVDTSDCTMMNIAEHYMASDVEWDPTGRFVVTSVSWWSHKVDNAFWLWTFQGRLLQKNNKERFCQLLWRPRPPSLLTQEQIKLIKKDLKKYSKIFEQKDRLSQSKASKELVDKRRTMMEEYRKHRKRAMDMYQEQRPLRLELRGGVDTDELDSNVDDWEEETIEFFINEEIIPIGDL
Protein: Phosphate-specific transport system accessory protein PhoU (Pst system accessory protein PhoU) (Repressor protein PhoU) (Q83WB2)
Organism: Edwardsiella tarda
Function: Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. Encoded together with proteins of the phosphate-specific transport (Pst) system in the polycistronic pstSCAB-phoU operon. PhoU is essential for the repression of the Pho regulon at high phosphate conditions. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR-PhoB transitory complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0A9K7}.
Interaction partners:
- Phosphate transport system permease protein PstA
- Phosphate import ATP-binding protein PstB
- Phosphate transport system permease protein
- Phosphate-binding protein PstS
- Phosphate regulon sensor protein PhoR
- Signal peptidase I
- Phosphate regulon transcriptional regulatory protein PhoB
Sequence:
MDNLNLNKHTSGQFNAELEYIRTQVMSMGGLVEQQLTDAITAMHNQDADLARRVVEGDAKVNMMEIAIDEACVKIIAKRQPTASDLRLVMAIIKTISELERIGDVADKICRTALEKFSQQHQPLLVSLESLGQHTVQMLHDVLDAFARMDLNEAIRIYREDKKVDQEYEGIVRQLMTYMMEDSRTIPSVLTALFCARSIERIGDRCQNICEFIFYYVKGQDFRHIGGDDLEQLLTDHRRVDEA
Protein: Flavin-containing monooxygenase 3 (EC 1.14.13.148) (EC 1.14.13.32) (EC 1.14.13.8) (Dimethylaniline monooxygenase [N-oxide-forming] 3) (Dimethylaniline oxidase 3) (FMO II) (FMO form 2) (Hepatic flavin-containing monooxygenase 3) (FMO 3) (Trimethylamine monooxygenase) (P31513)
Organism: Homo sapiens (Human)
Function: Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds. Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 3A4)
- Cytochrome P450 2D6
- Cytochrome P450 2C9
- Cytochrome P450 2A6
- Cytochrome P450 1A2
Sequence:
MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFSNSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFATTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPGVFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFGTFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVKPNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPLLEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMNDINEKMEKKRKWFGKSETIQTDYIVYMDELSSFIGAKPNIPWLFLTDPKLAMEVYFGPCSPYQFRLVGPGQWPGARNAILTQWDRSLKPMQTRVVGRLQKPCFFFHWLKLFAIPILLIAVFLVLT
Protein: Urease accessory protein UreG (Q9RP19)
Organism: Sporosarcina pasteurii (Bacillus pasteurii)
Function: Facilitates the functional incorporation of the urease nickel metallocenter. Binds a maximum of 4 Ni(2+) and 2 Zn(2+) ions per homodimer. The affinity for Zn(2+) is 10-fold higher than that for Ni(2+). This process requires GTP hydrolysis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MKTIHLGIGGPVGSGKTTLVKTLSEALKEEYSIAVITNDIYTREDANFLINENILEKDRIIGVETGGCPHTAIREDASMNFEAIEELKNRFDDLEIILLESGGDNLSATFSPELVDAFIYVIDVSEGGDIPRKGGPGVTRSDFLMVNKTELAPYVGVDLDTMKNDTIKARNGRPFTFANIKTKKGLDEIIAWIKSDLLLEGKTNESASESK
Protein: Protein E6 (P06931)
Organism: Bovine papillomavirus type 1
Function: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase and modulates its activity. Protects host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MDLKPFARTNPFSGLDCLWCREPLTEVDAFRCMVKDFHVVIREGCRYGACTICLENCLATERRLWQGVPVTGEEAELLHGKTLDRLCIRCCYCGGKLTKNEKHRHVLFNEPFCKTRANIIRGRCYDCCRHGSRSKYP
Protein: Maintenance of ploidy protein mob1 (O94360)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in promoting the onset of septum formation during the latter stages of mitosis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10769201}. Note=Spindle pole body throughout mitosis, relocates to the medial ring during interphase.
Interaction partners:
- Serine/threonine-protein kinase sid2
- Septation initiation network scaffold protein cdc11
- Tyrosine-protein phosphatase CDC14 homolog
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein kinase ppk35
- Serine/threonine-protein kinase orb6
- Cell division control protein 7
- Septum-promoting GTP-binding protein 1
- Serine/threonine-protein kinase sid1
- Cell division control protein 16
Sequence:
MFGFSNKTAKTFRVRKTEAGTKHYQLRQYAEATLGSGSLMEAVKLPKGEDLNEWIAMNTMDFYTQINMLYGTITEFCTAASCPQMNAGPSYEYYWQDDKIYTKPTRMSAPDYINNLLDWTQEKLDDKKLFPTEIGVEFPKNFRKVIQQIFRRLFRIYAHIYCSHFHVMVAMELESYLNTSFKHFVFFCREFGLMDNKEYAPMQDLVDSMV
Protein: Protein tyrosine phosphatase, non-receptor type 3 (A0A096MJT2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTSRLRALGGRINNIRTSELPKEKTRSEVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPEVSPVSCIFE
Protein: Vomeronasal 2, receptor 82 (A0A3B2WD32)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLLSWLLIVWFLQMPTFTWIIATHICPTDTKHLIHSDGTVVIGAFFPILHNSRVSKIIDWRYFPMDSDDYFGINARNYQLVLAMLFAVNEINLNSHILPNTSLGLEIYNLPAIGRNIFRTVFSWLTGLSSVIPNYTCRKESKSAATLTGLSWKTSETIWTILDLYKFPQLHPFLKKIQVKNSVGDDVVLDWKRKADPEYDITNIWNFPTGLSLLVKVGTFVPSAPKGKQLSMSEYMINWPIGFTEVGVFLIEVNIICFWM
Protein: Paralemmin-1 (Paralemmin) (A0A087WWY4)
Organism: Homo sapiens (Human)
Subcellular location: Apicolateral cell membrane {ECO:0000256|ARBA:ARBA00037796}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037796}. Basolateral cell membrane {ECO:0000256|ARBA:ARBA00037871}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037871}. Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium membrane {ECO:0000256|ARBA:ARBA00004527}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004527}.
Interaction partners:
Sequence:
MNYKRVSNTPLRTVDGSPMMKAVVHAVDGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPTEAASREENQAGPEATTSDPQDLDMKKHRCKCCSIM
Protein: Chromophore lyase CRL, chloroplastic (EC 4.-.-.-) (Protein CONSTITUTIVE ACTIVATOR OF AAA-ATPase 33) (Protein CRUMPLED LEAF) (Q9FI46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins (By similarity). Required for plastid division, and involved in cell differentiation and regulation of the cell division plane. Maintenance of plastid homeostasis controls plant preconditioning to stress and stress acclimation.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:15086805}; Single-pass membrane protein {ECO:0000269|PubMed:15086805}.
Interaction partners:
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Cell division topological specificity factor homolog, chloroplastic
- Plastid division protein PDV2
- Dynamin-like protein ARC5
- Cell division protein FtsZ homolog 1, chloroplastic
- AAA-ATPase At3g28580
- Glycine--tRNA ligase, chloroplastic/mitochondrial 2
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- At3g63160
- Type IV inositol polyphosphate 5-phosphatase 11
Sequence:
MGTESGSDPESSSNGWSRARGLVVKTLVLIGGALLIKRLTKSTTRRDHARVVSRSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKELKCDVEVSSYAIRDAEEYKNFCDRPKDQRPLPEEVIGDIGEHLTTIHLNCCDRGKRCLYEGSTSPGGFPNSWNGASYCTSDLAVLKNNEIHLWDRGFDENRNQVWGPKEGPYEFKPATSSSINENLSALNILYQSSIDKPIQGSLILQD
Protein: Hopanoid transporter HpnN (B3QHB6)
Organism: Rhodopseudomonas palustris (strain TIE-1)
Function: Essential for hopanoid transport from the cytoplasmic to the outer membrane. Required for the C(35) hopanoid, bacteriohopanetetrol, to remain localized to the mother cell type.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:21873238}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLKSAIVSIVRASTRFAAFTVLIGVFLAVAAGFYTYQHFGINTDINHLISSDLDWRKRDIAFEKAFDQERLILAVVEAPTPEFANAAAAKLTAELSKNNINFDSVKRLGGGPFFDRSGLLFLPKDEVAKATGQFQQAVPLIEIMAGDPSIRGLTAALETGLVGLKRGELTLDATAKPFNTVAATVEDVLGKQQAFFSWRGLVNPEPLTDGDKRAFIEVKPILDFKALEPGKAATDAIRQAAVDLKIEQDFGARVRLTGPVPIANEEFATVKDGAVVNGIGTVVVVLLILWMALHSSKIIFAVAANLVIGLSITTAVGLMLVDSLNLLSIAFAVLFVGLGVDFGIQFSVRYRSERHKTGDLEKALVQAAEYSAVPLSLAAMSTTAGFLSFLPTSYKGISELGEIAGAGMAIAFFTSITVLPALLKLLNPAGEKEPLGYAFLAPVDHFLEKHRIAIIVGTIGVALAGLPLLYFMHFDFNPINLRSPKVESIATFLDLRKDPNTGANAVNVMAPNEQAAREIEAKLAKLPQVSRTISLDTFVPPDQPEKLKLIQAGAKVLEPALNPEQIDPPPSDQDNIASLKSSAEALRRAAGEATGPGADASRRLATALTKLAGADQAMREKAQDVFVRPLLLDFELLRNMLKAQPVTLDNLPADIVSSWKTKDGQIRVEVLPSGDPNDNDTLRKFAAAVLQAEPLATGGPVSILKSGDTIVASFIQAGLWALLSISILLWITLRRISDVALTLVPLLVAGAVTLEICVLIDLPLNFANIVALPLLLGVGVAFKIYYVTAWRSGRTNLLQSALTRAIFFSALTTATAFGSLWLSSHPGTASMGKLLALSLLTTLGAVLLFQPALMGKPRHIDESGDTDL
Protein: RE67695p (Visgun, isoform A) (Visgun, isoform B) (Q8I0D8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNRQAKFLILCLFVGLFSANLCEEVTTPAPADTTTQESKNTTTPPDTTTTVTPPSTSTTSTTTEKTTTTPPITTSTEKTTTSTTPASTTSSTTPASTTSSTTPATTTTTPGTTSTTTPSPNSTTTTPPPHTSTTPAPKPVPCGHFDGSSFIGGIVLTLGLLAIGLVAYKFYKARNERNYHTL
Protein: Non-specific lipid transfer protein GPI-anchored 12 (AtLTPG-12) (Protein LTP-GPI-ANCHORED 12) (Xylogen-like protein 13) (AtXYLP13) (AtXYP11) (Q9ZVC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable lipid transfer protein.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- Putative actin-5
- Ubiquinol oxidase 2, mitochondrial
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Actin-4
- Actin-12
- Isocitrate dehydrogenase regulatory subunit 1, mitochondrial
- Non-specific lipid transfer protein GPI-anchored 14
Sequence:
MLTTNTLAVLLLLFLSLCSGQSPPAPEPIAADGPSSPVNCLVSMLNVSDCFSYVQVGSNEIKPEAACCPELAGMVQSSPECVCNLYGGGASPRFGVKLDKQRAEQLSTICGVKAPSPSLCSVLGFPTISPAGSEDSSSGSEGSDKDKKNGAMTTKYCGVALNSLALLLLFTFLSLS
Protein: Terpene synthase 4 (EC 4.2.3.-) (Q75J90)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene (E)-nerolidol.
Interaction partners:
- Squalene synthase
Sequence:
MEEKIKFYFEIIDFQNQKFKIQEFTSKLIGLKEESFTTFKPIVYEKYLNWTQSIEESILKTNGTINKSIFEEIFSYCGYIGEFLEYEPFIVFLKFTTFGIILDDYIFEKINSLNMKLNEKEKLINSLIYYNNKNENKIGFEFWEIINEFQNFTHKESFQRIINANSLWIKSSIDSRNISNSPINSRCSFNEYFEKRSSDASGDFILTISMIGIMDNYIENSIIESKEFQTINYHAKSFFLLINDLYSFNREINENDLLNYIKILAIQLNSIQLSIDKTIELIIDHYLKFLSSIETILKLYQNDQSTYQLLKQVFQNSNKILSGIYFAHKKSKRYN
Protein: SIX homeobox 3 (A0A0G2K2C0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Paired box protein Pax-6
- Visual system homeobox 2
- Homeobox protein OTX2
- LIM/homeobox protein Lhx2
- Sonic hedgehog protein
Sequence:
MVHTGQSMVFRSPLDLYSSHFLLPNFADSHHCSLLLASSGGGSGAGGGGGAGGGGGGGGGNRAGGGGAGGAGGGGGGGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSILSVTSSDSECDV
Protein: Protein ecdysoneless homolog (Human suppressor of GCR two) (hSGT1) (O95905)
Organism: Homo sapiens (Human)
Function: Regulator of p53/TP53 stability and function. Inhibits MDM2-mediated degradation of p53/TP53 possibly by cooperating in part with TXNIP. May be involved transcriptional regulation. In vitro has intrinsic transactivation activity enhanced by EP300. May be a transcriptional activator required for the expression of glycolytic genes. Involved in regulation of cell cycle progression. Proposed to disrupt Rb-E2F binding leading to transcriptional activation of E2F proteins. The cell cycle -regulating function may depend on its RUVBL1-mediated association with the R2TP complex. May play a role in regulation of pre-mRNA splicing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}. Nucleus {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270, ECO:0000269|PubMed:33941617}. Note=Predominantly is located in the cytoplasm. {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}.
Interaction partners:
- Protein AAR2 homolog
- Pre-mRNA-processing-splicing factor 8
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Zinc finger HIT domain-containing protein 2
- U5 small nuclear ribonucleoprotein TSSC4
- U5 small nuclear ribonucleoprotein 40 kDa protein
- E2F-associated phosphoprotein
- PIH1 domain-containing protein 1
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MEETMKLATMEDTVEYCLFLIPDESRDSDKHKEILQKYIERIITRFAPMLVPYIWQNQPFNLKYKPGKGGVPAHMFGVTKFGDNIEDEWFIVYVIKQITKEFPELVARIEDNDGEFLLIEAADFLPKWLDPENSTNRVFFCHGELCIIPAPRKSGAESWLPTTPPTIPQALNIITAHSEKILASESIRAAVNRRIRGYPEKIQASLHRAHCFLPAGIVAVLKQRPRLVAAAVQAFYLRDPIDLRACRVFKTFLPETRIMTSVTFTKCLYAQLVQQRFVPDRRSGYRLPPPSDPQYRAHELGMKLAHGFEILCSKCSPHFSDCKKSLVTASPLWASFLESLKKNDYFKGLIEGSAQYRERLEMAENYFQLSVDWPESSLAMSPGEEILTLLQTIPFDIEDLKKEAANLPPEDDDQWLDLSPDQLDQLLQEAVGKKESESVSKEEKEQNYDLTEVSESMKAFISKVSTHKGAELPREPSEAPITFDADSFLNYFDKILGPRPNESDSDDLDDEDFECLDSDDDLDFETHEPGEEASLKGTLDNLKSYMAQMDQELAHTCISKSFTTRNQVEPVSQTTDNNSDEEDSGTGESVMAPVDVDLNLVSNILESYSSQAGLAGPASNLLQSMGVQLPDNTDHRPTSKPTKN
Protein: Cytochrome f (P0C387)
Organism: Oryza sativa (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MENRNTFSWVKEQMTRSISVSIMIYVITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVLRIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAPPDRISPELKEKIGNLSFQSYRPNKKNILVIGPVPGKKYSEIVFPILSPDPAMKKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATSTGVVRKILRKEKGGYEISIVDASDGRQVIDLIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFFASVILAQVFLVLKKKQFEKVQLYEMNF
Protein: Transketolase 2 (TK 2) (EC 2.2.1.1) (P33570)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase A
- Transaldolase B
- Glucose-6-phosphate isomerase
- Ribulose-phosphate 3-epimerase
- Fructose-bisphosphate aldolase class 1
- Fructose-1,6-bisphosphatase class 1
- ATP-dependent 6-phosphofructokinase isozyme 2
- Ribose-5-phosphate isomerase B
- Ribose-5-phosphate isomerase A
- Triosephosphate isomerase
Sequence:
MSRKDLANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWNDFLKHNPTDPTWYDRDRFILSNGHASMLLYSLLHLTGYDLPLEELKNFRQLHSKTPGHPEIGYTPGVETTTGPLGQGLANAVGLAIAERTLAAQFNQPDHEIVDHFTYVFMGDGCLMEGISHEVCSLAGTLGLGKLIGFYDHNGISIDGETEGWFTDDTAKRFEAYHWHVIHEIDGHDPQAVKEAILEAQSVKDKPSLIICRTVIGFGSPNKAGKEEAHGAPLGEEEVALARQKLGWHHPPFEIPKEIYHAWDAREKGEKAQQSWNEKFAAYKKAHPQLAEEFTRRMSGGLPKDWEKTTQKYINELQANPAKIATRKASQNTLNAYGPMLPELLGGSADLAPSNLTIWKGSVSLKEDPAGNYIHYGVREFGMTAIANGIAHHGGFVPYTATFLMFVEYARNAARMAALMKARQIMVYTHDSIGLGEDGPTHQAVEQLASLRLTPNFSTWRPCDQVEAAVGWKLAVERHNGPTALILSRQNLAQVERTPDQVKEIARGGYVLKDSGGKPDIILIATGSEMEITLQAAEKLAGEGRNVRVVSLPSTDIFDAQDEEYRESVLPSNVAARVAVEAGIADYWYKYVGLKGAIVGMTGYGESAPADKLFPFFGFTAENIVAKAHKVLGVKGA