wanglab/gogpt-training-data huggingface dataset:
Protein: Fanconi anemia group D2 protein homolog (Protein FACD2) (Q8MYL1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Fanconi anemia group I protein homolog
- E3 ubiquitin-protein ligase Fancl
- DEAD-box ATP-dependent DNA helicase Fancm
- Breast cancer type 2 susceptibility protein homolog
- BcDNA.LD22910
- Crossover junction endonuclease MUS81
- Serine/threonine-protein kinase ATM
- DNA repair protein Rad51 homolog
- Rad51 recombinase D
- DNA excision repair protein ERCC-1
Sequence:
MYKQFKKRSKKPLNTIDENATIKVPRLAETTTNISVESSSGGSEENIPASQEHTQRFLSQHSVILAATLGRTQSSSRNIATLSRQPNNFFELVLVRAGVQLDQGDSLILACDHVPIVSKLREIFTSASSYTDKMETFKTGLNAAMAPGSKLVQKLLTGCTVDAAGEEQIYQSQNSMFMNFLMIDFMRDACVEVLLNKIEEVAKSDRVIMGKAAIPLPLLPLMLTQLRYLTASHKVEIYSRIEVIFNRATESAKLDIIANAELILDASMHDEFVELLNINYSSTEDLFHMTTVQTLGNLSLSDRTQAKLRVRILDFATSGQCSDAILPHLIRLLLNVLKIDTDDSVRDLIGSLRGIFNWRHTNETEKISASEDSKKSQLELFGFLELGLIRSKKFYQACQRSSASVPAAEFTSFDMILLLLLIHVNEDNSLYIENILRRRIKLEHITVSILEEIRQHYRHILEQHITTLMNILHDFMREKNRIVSDFAKSSYSILFKIFNSIQKNILKKLLELTCDKSSPHLTTMALELLRELQRKSAKDVQNCATLLIPMLDRISDLSLTQTRVAMDLLCHVAFPDPNLSPCLQLQEQVDMVVKKQLINSIDNIKKQGIIGCVQLIDAMARIANNGVDRDEFIASVENVDSLPDGRGKMAANLIIRTEASIGNSTESLALFFEELATVFNQRNEGTSGCELDNQFIAWACDLVTFRFQASFVTENVPETLKGIKLEYQLNINELDDTDANTESDVLNIGINISKLVLSPKVKACDSIYVLAPLFNYVRVLYKHRHQDSLESINALLGCAIVLPSFFEDDNYVSVFENFEAEQQKDILSIYFHTVNWMRVSISAFASQRDPPTRRRVLSRLGELIRIEQRMKPLLARAPVDFVAPPYQFLTNVKLSNQNQKRPGPKPAAKLNATLPEPDLTGNQPSIADFTIKVGQCKTVKTKTDFEQMYGPRERYRPMEVEIIMLLVEQKFVLNHQLEEEQMGEFLGLLELRFLLEDVVQKLEAAVLRHHDSYDADSFRPHLAKPEDFICDLLPCLHEVNNHLITLGEAIDNQLTEVSHVYSNLDLFKDQFCYIKSCFGLCVRLFALYFAWSEWSDKSQEQLLHKSLLKLQPKTQWKRLEKQSVPQLANLTFQYFLKYEKSVLNLSTAVHLHRLLCNLLKLGSLQSDASQPRFQQAEDLRILCGTLLRRKWFHYSGTLDKGGQCNIYLDELVKGFLKKSNAKSQTELLTELVKQCSILNTKDKALTSFPNFKKANFPLLFRGLCEVLIHSLSGQVSVDSRGDKLKLWESAVDLLNGLLSIVQQVEQPRNFGLFLKHSLLFLKLLLQHGMSALESIVREDPERLTRFLHELQKVTRFLHQLCCHSKSIKNTAIISYIPSLRETIETLVFRVKALLAANNCHSAFHMGNMINRDLHGDSIITPRSSFAGEENSDDELPADDTSVDETVLGDDMGITAVSVSTRPSDGSRRSKSSSRSKCF
Protein: Protein LST7 (Lethal with SEC thirteen protein 7) (P53237)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the nitrogen-regulated transport of amino acid permeases GAP1 and PUT4 from the Golgi to the cell surface.
Interaction partners:
- Protein LST4
- Proline utilization trans-activator
- GTP-binding protein GTR1
- GTP-binding protein GTR2
- Protein transport protein SEC13
- Mitotic check point protein BFA1
- Mitotic check point protein BUB2
- Target of rapamycin complex subunit LST8
- SEH-associated protein 4
- Nitrogen permease regulator 3
Sequence:
MSSTVISLAHFCDKHGPRIISVTQSAEKGTLGEELLVPDYPTESYCESCLLQFPEESTRSMRCFIEDVPFITTQYSSIRYQLLNSIIKRAFSEETMIYDNMPFIFFDDLRGLNLVIGFKLYDENARGNERRYCFILTVDSRSHDDSMKMLSEHWNFIIGGFDKMIAYIKNIHKSEFLGKNKTVENNLETLNNNAFIGSYLRANKSKFGRNLVSLTDDKFLFVRIHKWNSFLLHTVMNENKLP
Protein: ACD shelterin complex subunit and telomerase recruitment factor (R4GNJ5)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGSGRLVLRPWIRELILGSETPSSPRAGQLLEDAEAAVAGPSHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQVDRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSLGPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGTPALPGHMSSEESGTSISLLPALSLAAPDPGQRSSSQPSPAICSAPATLTPRSPHASRTPSSPLQSCTPSLSPRSHVPSPHQALVTRPQKPSLEFKEFVGLPCKNRPPFPRTGATRGAQEPCSVWYEYEPPCTSLCARVQAVRLPPQLMAWALHFLMDAQPGSEPTPM
Protein: Decoration protein (Capsid protein pb10) (Q6QGD6)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Decoration protein that binds asymmetrically to the center of each capsid protein hexamer after capsid expansion. Stabilizes the capsid and protects from DNA release.
Subcellular location: Virion {ECO:0000269|PubMed:16876823, ECO:0000269|PubMed:24198424}. Note=120 copies of the decoration protein are localized on the exterior of the capsid. {ECO:0000269|PubMed:16876823}.
Interaction partners:
Sequence:
MIDYSGLRTIFGEKLPESHIFFATVAAHKYVPSYAFLRRELGLSSAHTNRKVWKKFVEAYGKAIPPAPPAPPLTLSKDLTASMSVEEGAALTLSVTATGGTGPYTYAWTKDGSPIPDASGATYTKPTAAAEDAGSYKVTVTDSKQVSKDSTTCAVTVNPTVPGG
Protein: Probable rRNA-processing protein EBP2 (EBNA1-binding protein 2) (Nucleolar protein p40) (Q99848)
Organism: Homo sapiens (Human)
Function: Required for the processing of the 27S pre-rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19170763, ECO:0000269|PubMed:2879624}. Note=Associated with the nucleolus in an RNA-dependent manner.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Ribosome production factor 2 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Pescadillo homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- Protein MAK16 homolog
- Ribosome biogenesis protein WDR12
- WD repeat-containing protein 74
- Nucleolar complex protein 2 homolog
Sequence:
MDTPPLSDSESESDESLVTDRELQDAFSRGLLKPGLNVVLEGPKKAVNDVNGLKQCLAEFKRDLEWVERLDVTLGPVPEIGGSEAPAPQNKDQKAVDPEDDFQREMSFYRQAQAAVLAVLPRLHQLKVPTKRPTDYFAEMAKSDLQMQKIRQKLQTKQAAMERSEKAKQLRALRKYGKKVQTEVLQKRQQEKAHMMNAIKKYQKGFSDKLDFLEGDQKPLAQRKKAGAKGQQMRKGPSAKRRYKNQKFGFGGKKKGSKWNTRESYDDVSSFRAKTAHGRGLKRPGKKGSNKRPGKRTREKMKNRTH
Protein: X-box-binding protein 1 (Hepatocarcinogenesis-related transcription factor) (HTF) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form] (Q9R1S4)
Organism: Rattus norvegicus (Rat)
Function: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland. Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins. Modulates the cellular response to ER stress in a PIK3R-dependent manner. Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes. Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35426, ECO:0000250|UniProtKB:P17861}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P17861}. Note=Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner. Colocalizes in the nucleus with SIRT1. {ECO:0000250|UniProtKB:P17861}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000250|UniProtKB:P17861}. Cytoplasm {ECO:0000250|UniProtKB:P17861}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P17861}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Note=Shows no preferential localization to either the nucleus or the cytoplasm. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localizes predominantly at the endoplasmic reticulum membrane as a membrane-spanning protein; whereas may be only marginally localized on the cytosolic side of the ER membrane as a peripheral membrane. {ECO:0000250|UniProtKB:O35426, ECO:0000250|UniProtKB:P17861}.
Interaction partners:
- DNA damage-inducible transcript 3 protein
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Cyclic AMP-dependent transcription factor ATF-4
- Endoplasmic reticulum chaperone BiP
- TATA box binding protein
- Hypoxia-inducible factor 1-alpha
- TATA-box binding protein like 1
- TATA box-binding protein-like 2
- Endoplasmin
Sequence:
MVVVAAAPSAASAAPKVLLLSGQPASGGRALPLMVPGPRAAGSEASGTPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLQLENQLLREKTHGLVIENQELRTRLGMNALVTEEVSEAESKGNGVRLVAGSAESAALRLRAPLQQVQAQLSPPQNIFPWILTLLPLQILSLISFWAFWTSWTLSCFSNVLPQSLLIWRNSQRSTQKDLVPYQPPFLCQWGPHQPSWKPLMNSFVLTMYTPSL
Protein: FI18835p1 (Uncharacterized protein, isoform A) (Q9VCV9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEPAAQQQQSQNGKERSKSTEEKEVPREPALVLKDIDIKTELESLVKLLDGKIYKEEEVAMEELHQYLIEDDGSWALGDNFLIFVQRVLRDNQAFSPDTRIHLIRTLAYAALKDDVIIILHQDRRDHTLMNYAQDIDKQTPEEQQAWAMFMCNLFENLGPSEWLLYISEWEYNGQTISNIRVTTKVAVHCILSNCPQLKNIGSMILYNIAIKEVKTVVFDDIAVELAMAILQFFQSSPNEDQIFRTLRALVRFLEVSQDVPMIIQMIGPHPKQFAGKSERVDELIKIISRKVPA
Protein: Uncharacterized protein (Q381S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MAVVHKNFADYYNSLVSRVPTHHELLLRLCREETGERKAIEEQLSHALADLMHERGVMIAERKEIERNPTLKFEPSLTRLITLGMRQTNLELIRQRQQNPLVRQQPLIRAFPRAKYFTLLKEEEELRTWLSGVEHRLREKVEKECSHSWFLLVCLRQLVDHENEVRERIQQTEADQRVVIRRGVFRYAPPEFFRRQCVERTKGPVKEKTFEEEHLDSRAVVEAEELEEWKCMLRWLFDMYGVRLYSTSRCETAERYFIEEEEQKELWEKTLECTRESYGPYGKLTATIAWHGTSCTPLMRMLTCLPEKIREAAEAKAREANKYPPVHESSAESSRSVTPRQEVEEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQPAEEVAQETAAEQTDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQSAEQAEDATEQPAEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQPAEEVAQETAAEQTDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQSAEQAEDATEQPAEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQSAEQAEDTTEQPAEEVAQETAAEQTDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQSAEQAEDTTEQPGEQAEDTTEQPAEQAEDTTEQPAEEAEDTTEQPTEQAEDATEQPAEQAEDATEQPDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQSAEQAEDTTEQPGEQAEDTTEQPAEQAEDTTEQPAEEAEDTTEQPTEQAEDATEQPAEQAEDATEQPDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDTTEQPAEQAEDTTEQPAEEAEDTTEQPTEQAEDTTEQPAEEAEDATEQPGEQAEDTTEQPAEQAEDATEQPAEEVAQETAAEQTDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQPAEEVAQETAAEQTDEHEELDEADIPKEASTGSSPKKPASEDAGEQVAAEGVEDATEQPAEQAEDATEQPGEQAEDATEQPTGEGDA
Protein: Rab GTPase-activating protein eat-17 (RabGAP eat-17) (Abnormal pharyngeal pumping eat-17) (S6F527)
Organism: Caenorhabditis elegans
Function: Rab GTPase activating protein for the small GTPase rab-6.2. Required for grinder formation, which is the feeding organ that breaks down food.
Interaction partners:
- Ras-related protein rab-6.2
- Abnormal pharyngeal pumping eat-20
Sequence:
MVPSPALVGTPSVFPHHQSTSFFQETASFFNLDWERLWHSRSNSNSTSSPRNSPSQLSPPMAATAALRRSSDYGSADTECGEPCETGAPVSLNEVDLLAKMEQLNKSNEEDSRSVASKKTGSSESRKGAREHSPEEDEYFQEDLWSVWGELILNWEIEVKKRPNYIKDLVKRGIPQHFRMIAWQNLSNASVSSVHDLYSDYMRQSSVYEKVIQRDIPRTYPELDFFKDGERGQSLLFNVIKAYSVHDKEVGYCQGSAFIVGLLLLQMPEEEAFAVLVSLMENYRLRELYKPTMTDLGLCMFQLECLVQDQMPDLYTHFNNMGFDTSMYASSWFLTLFTTTMPLDIANRIMDCFLVEGMDFIFCISIAILQQARIELLRLDMEGMLKYFQREVRERYEFDADLLFTVANQVQLNAKRMKRLEKDYLTKRTKEQEEAVELRRLRTENRLLRQRIDYLEAESSALADRLVKGQVNLAQEAENYINIAHELNKLRDMNSDVHRKLEGAYETIRELSSARRDNIMDTGTQVDDTSMIEHIHSLQQELIEAHTRQADSENTLRDAKLRVSELEMANKRLLENEPSEDVAGLQEELISVKMREAESSLALKEMRQRLAELEQHWAKYVHVRAFDPSSASIEKESTSEAHSTQQQPSPPLTSARARLAKITASLIGGSTEETDNCISVRELEDQLMGVRIKEADTLAELKEMRQKVMELETQNHVCTNQLKRQDEEMKRVREDSEVLVKKRKELEDQLKDEKEKLDNKESEFNEGRINDRLKYSEAMQTIQDLQSSISQLELKKAEKWTQNQLRGSSVCDLDEESNSHGSICSNVDHLSLASDEMNALLADMTVRIPTLDDLAEEGSATETDELRPKELNDGNDTTDSGVQLSDSH
Protein: DNA replication licensing factor MCM4 (EC 3.6.4.12) (Q6NZV2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA helicase
- WD repeat and HMG-box DNA-binding protein 1
- Cell division cycle 7 homolog
- DNA replication licensing factor MCM7
- Chromatin licensing and DNA replication factor 1
- Cell division control protein
- DNA helicase
- DNA replication licensing factor MCM2
- CDC45 cell division cycle 45 homolog
- DNA replication complex GINS protein SLD5
Sequence:
MSSPSSQSRKRDPPTPASEDPLSPPSQRSRAHDTSTELQPMPTSPAQDASLFSSPMAPRSVLQSEIDASSPLMYGTPSSRVEGTPRSGIRGTPARQRADLGSVRKAPQVDMHSEPASGDAAVAGDQGAGQRLVIWGTDVNVGTCKEKFQRFLQQFTDPDSREEENAGLDLNEPLYMQKLDEISVVGEPVLNVNCTHIQTFDADLYRQLICYPQEVIPTFDMSVNELFFDRFPDSVLEHQIQVRPYSAIKTRNMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFRCQVCAFNTRVEVDRGRIAEPAVCRNCNTTHSMALVHNRSVFSDKQMIKLQESPEDMPAGQTPHTTVVYAHNDLVDKVQPGDRVNITGIYRAAPMRLNPRQSQVKSVYKTHIDAIHFRKTDEKRLHGLDEDGEQKLFTKERVALLKELAAKPDVYERLSSALAPSIYEHEDIKKGILLQLFGGTRKDFTQTGRGNFRAEVNILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMSDNTRSVLHEVMEQQTLSIAKAGIICQLNARTSILAAANPVESQWNPKKTTIENIQLPHTLLSRFDLIFLMLDPQDEAYDRRLAHHLVSLYYQSEEQIEEEHLDMAVLKDYIAFARTTVHPRLSEEASQALIEAYVDMRKIGSGRGMVSAYPRQLESLIRLAEAHAKVRFSGKVETIDVEEAKRLHREALKQSATDPRTGFVDISILTTGMSATARKRKEEVAQALKKLIQSKGKTPAMKYQQLFDDLRGQSEAAITKDMFDEALRLLADEDYLTVTGKTVRLL
Protein: Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (MMP-X1) (MT-MMP) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT1-MMP) (MT1MMP) (P53690)
Organism: Mus musculus (Mouse)
Function: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P50281}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P50281}. Melanosome {ECO:0000250|UniProtKB:P50281}. Cytoplasm {ECO:0000250|UniProtKB:P50281}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm. {ECO:0000250|UniProtKB:P50281}.
Interaction partners:
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- 72 kDa type IV collagenase
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 3
- Decorin
- CD44 antigen
Sequence:
MSPAPRPSRSLLLPLLTLGTALASLGWAQGSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADLATMMAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPAYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV
Protein: Malonyl-CoA:anthocyanidin 5-O-glucoside-6''-O-malonyltransferase (EC 2.3.1.-) (Anthocyanin 5-aromatic acyltransferase-like protein) (Anthocyanin 5-glucoside malonyltransferase) (At5MaT) (Q9LJB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the malonylation of the 5-O-glucose residue of anthocyanins, using malonyl-CoA as the malonyl donor. Acts only on anthocyanin substrates containing a 5-O-glucosyl moiety. Acts on the four native A.thaliana anthocyanins, A3, A7, and to a lesser extent, A6 and A10. Can also use the non-native anthocyanin compounds cyanin (cyanidin 3,5-diglucoside), malvin, pelargonidin 3,5-diglucoside, peonidin 3,5-diglucoside, cyanidin 3-coumaroylglucoside 5-glucoside, delphinidin 3-coumaroylrutinoside 5-glucoside and petunidin 3-coumaroylrutinoside 5-glucoside as substrates. Is the sole enzyme responsible for producing malonylated anthocyanin 5-O-glucosides in A.thaliana. Is not able to catalyze acyl transfer using acetyl-CoA, butyryl-CoA, hexanoyl-CoA, benzoyl-CoA, cinnamoyl-CoA, methylmalonyl-CoA, succinyl-CoA, p-coumaroyl-CoA or caffeoyl-CoA.
Interaction partners:
- UDP-glycosyltransferase 75C1
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Dihydroflavonol 4-reductase
- Glutathione S-transferase F12
- Flavonoid 3'-monooxygenase
- Serine carboxypeptidase-like 10
- Transcription factor TT8
- Leucoanthocyanidin dioxygenase
- NAC domain-containing protein 6
- Naringenin,2-oxoglutarate 3-dioxygenase
Sequence:
MVNFNSAVNILEVVQVSPPSSNSLTLPLTYFDLGWLKLHPVDRVLFYHVPELTRSSLISKLKSSLSATLLHYLPLAGRLVWDSIKTKPSIVYSPDDKDAVYLTVAESNGDLSHLSGDEPRPATEFHSLVPELPVSDESARVLAVQVTFFPNQGFSLGVTAHHAVLDGKTTAMFLKAWAHNCKQEQEALPHDLVPSLDRIIVQDPTGLETKLLNRWISASNNKPSLKLFPSKIIGSDILRVTYRLTREDIKKLRERVETESHAKQLRLSTFVITYAYVITCMVKMRGGDPTRFVCVGFASDFRSRLNPPLPPTFFGNCIVGSGDFDVKAEPILEEGEGKGFITAVETLTGWVNGLCPENIEKNMLLPFEAFKRMEPGRQMISVAGSTRLGIYGSDFGWGKPVKVEIVTIDKDASVSLSESGDGSGGVEVGVCLKKDDVERFGSLFSIGLE
Protein: 7-methyl-GTP pyrophosphatase (m(7)GTP pyrophosphatase) (EC 3.6.1.-) (P0A729)
Organism: Escherichia coli (strain K12)
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305}.
Interaction partners:
Sequence:
MPKLILASTSPWRRALLEKLQISFECAAPEVDETPRSDESPRQLVLRLAQEKAQSLASRYPDHLIIGSDQVCVLDGEITGKPLTEENARLQLRKASGNIVTFYTGLALFNSANGHLQTEVEPFDVHFRHLSEAEIDNYVRKEHPLHCAGSFKSEGFGITLFERLEGRDPNTLVGLPLIALCQMLRREGKNPLMG
Protein: White-opaque regulator 1 (Q5AP80)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Master transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. WOR1 Binds the intergenic regions upstream of the genes encoding three additional transcriptional regulators of white-opaque switching, CZF1, EFG1, and WOR2. Phenotypic switching from the white to the opaque phase is a necessary step for mating. Plays a role in cell adhesion and pseudohyphal growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:16950924}.
Interaction partners:
- Op4p
- Enhanced filamentous growth protein 1
- White-opaque regulator 3
- Zinc cluster transcription factor CZF1
- White-opaque regulator 2
- Predicted GPI-anchored protein 17
- Mating-type-like protein A1
- Adhesion and hyphal regulator 1
- Wor4p
- Wh11p
Sequence:
MSNSSIVPTYNGYIHNTRDALAVIQQVLDKQLEPVSRRPHERERGVLIVSGSVFVFIEQSSGIKRWTDGISWSPSRIQGRFLVYGELDKKNLIDKDKKKKKKRKFGPDDEYDHNVNEPDYTGGYGNHLHNDNRSHLNKNSRSGPMLLATGTGSITHTVIENKPSSSASMIHSNVIPASSSFLTDYRTSLGNGPMVSAAISQNGLVKKTITLTTTTKELHMEGKAEKQTIHLISYYSKQDIDSGKLQRPSESDLKHVQISPALWTMVQENSLGGKAPIDDEECFIVDGHNQYTNVSYIQQQQQQHQLQHQPLLHHSSSVAGSTTSIVNNSLSISNGGYGNNYSKNLSRSYNKYSNSQVSQLSYMLPPQTESSSTATIASGASVSVKREDDTNNGSNAPTGNENQYVNAINHSHTSSYGGQGYATDATGIATPAYNSYSQANTSINTSSQQQQQLQQGQYGQYVQYGVAPSTISGATSTNNNSGNAPNIPQDVYYSHYTGFVQPHYPQYHIATGNASDQYNTNAANHQYHSNNTTSSANNNSSSRTTGVGSKRKPSIVSNSTSGSVSGGNGNGNNYGYNSNSSTSTNRPPAVSTNTTSTTSGGSSFSGPSSNITTNSMSNNPWFNSSTNMAVNSSYITSSGGGNSHGGIGNNEYEPMPMTNNSASIPAYYQQHVPSHVGSAQQHQSQQQVAGVGAPHIIHNHPYLHPTYGQGSNSASTGDNSTPGGSSGSGSGGSGNNGAGGSSSVAATSGVTSSNTSGNIVTNGTLVAAGTDDAVGNSSGSYYTGT
Protein: Conserved oligomeric Golgi complex subunit 3 (COG complex subunit 3) (Component of oligomeric Golgi complex 3) (Q961G1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in ER-Golgi transport.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 5
- LD27967p
- Vacuolar protein sorting-associated protein 53 homolog
- RINT1-like protein
Sequence:
MDDVERIQSENENLRKIRNRLMQWESKTDPLAALSIQQEEHLDVLTNLWRDSGPSAPAPTTPTQVGPTDSSAAATSQSGDDIRLPAEGLQNTNEFLLWFADVSAEIEQRGDADYHKYLQQLEQRKAECSHMLDQIAGAMERLGALCDEYDFVSQKTSALNTASEQLIEEQERLQELSHEIQRRLHYFSQVELLNQRLQSPTLSVASEAFRECLNKIDECLNYIEENPKFKDAAAYNVKYRQCLAKASGLVRNYVTSVINQATEATLHPKNNMPDASAALKAPDAAFALYYGKYQTAAAKVKRVAQLIESRSEHSLDYAQLMADLQQHYLAQRASVMSPAVNLSIQNVKVAHKGDHCSLTRSACAFLVHVCQDEQRLFYQFFSTGAPHLTVYLEGLCTILYDTMRPFIIHINHLETLAEICSILRIEMLEEHVQQNPVALEAFATIAHQLLQDVQERLVFRAHLYLQSDIQNFNPSSGDLAYPEKLEMMESIALSLQEPAPLRRSDSRNSMVSSVSSAVETESVATAYTVKQMNSPADLHGMWYPTVRRTLVCLSRLYRCVDRPIFQGLSQEALKLCIQSVSHAAGKISANKTPIDGELFEIKHLLILREQIAPFRVDFTVKETSLDFSKVKTAAFGLLQKRKQLFSMGSNNALLEFLLEGTPQIKEHLLDSRKEVDRQLKSVCEKYIKDAVQMLVGPLITFLEKAQSLLAQSTPATPQSPESTKASYVLRQSPWASPQQISSIIQETQRLIKAKLAVLQRSMQLYLSNRDTEFIIFRPIRNNIIQSFVKLEQLLTTNGYSTDDMIITSCPSAEQVSILLSSASILAAEGVASFAAAARKISTSSSVEGSTVGRKLSAMSNKSELVEEPKVEEVAGQIEVVPAEVQPPAKIEEEEVTETQTQANSE
Protein: CTC-interacting domain 11 (F4IEC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAVVETGAAATAADAGGVVIQPPPSSPPSSMTSQDSGVSSDDQNHHSRIDQVLRHDQGLYSKIGSHVARSDGVDGGESFKRDMRELQELFSKLNPMAEEFVPPSLNKQGGNGVNGGFFTSAGSFFRNNGFAGTGNGGYGNENGGFRRKKSFGQGKRRMNARTSMAQREDVIRRTVYVSDLDQQVTEEQLAGLFVSCGQVVDCRICGDPNSVLRFAFIEFTDEEGAMTALNLSGTMLGFYPVKVLPSKTAIAPVNPTFLPRTEDEREMCARTIYCTNIDKKVTQSDVKIFFESFCGEVYRLRLLGDYQHSTRIAFVEFVMAESAIAALNCSGVVLGSLPIRSSFKDACSSEITEASNALILALQVFTYLMSPQYIYRCVVLKTALHRHVKMFVCISHLLFSKCNSGI
Protein: Tubulin gamma-1 chain (Gamma-1-tubulin) (P23257)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32066907}. Note=In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs). {ECO:0000269|PubMed:32066907}.
Interaction partners:
- Gamma-tubulin complex component 4 homolog
- Gamma-tubulin complex component 3
- Gamma-tubulin complex component 2 homolog
- Gamma-tubulin complex component
- Grip163
- Grip71
- GEO02508p1
- Gamma-tubulin complex component
- Testis-specific gamma-tubulin ring protein 91
- Spindle assembly abnormal 4
Sequence:
MPSEIITLQLGQCGNQIGFEFWKRLCLEHGISPSGVLEDFANDGLDRKDVFFYQADDDHYIPRAVLLDLEPRVINTIMGSVYSKLYNPENVYLSKHGGGAGNNWASGYSQGEKLQEEVFDIIDREADGSDSLEGFILCHSIAGGTGSGMGSFIMERLADRYPKKLIQTFSVFPNQDEISDVVVQPYNSMLTLKRLTTAADSVVVLDNTALNRIACDRLHIQNPSFSQINNLVSTIMSVSTTTLRYPSYMNNNLIGLTAPLIPTPQLHFLMTGYTPLTSDSDIHTQQLVNVRKTTVLDVMRRLLQPKNMMVSTGPDKSNHHCYISILNIIQGEVDPTQVHKSLQRIRDRKMAQFIPWGPTSIQVALSRSSPYVQSNHRVSGLMLANHTSICSLFERALNQYDKLRKRGAFLDQFRREDIFKDDLNELDESRETVDCLVQEYEAATREDYMQFSVKRGNGPVDSKSEDSRSVTSAGS