wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase complex subunit SAP130 (130 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p130) (Q8BIH0)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone deacetylase complex subunit SAP30
- Inhibitor of growth protein 2
- Paired amphipathic helix protein Sin3a
- SIN3-HDAC complex-associated factor
- AT-rich interactive domain-containing protein 4B
- Sin3 histone deacetylase corepressor complex component SDS3
- AT-rich interactive domain-containing protein 4A
- Paired amphipathic helix protein Sin3b
- Histone deacetylase 1
- Inhibitor of growth protein 1
Sequence:
MSSQQFPRLGTPSPGLSQPPSQIASSGSAGLINQVATVNDEAGRDADVGTREHVGPSSSLPPREEKQEPVVVRPYPQVQMLPAHHAVASATPVAVTAPPAHLTPAVPLSFSEGLMKPPPKPTMPSRPIAPAPPSTMSLPPKVPGQVTVTMESSIPQASAIPVATISGQQGHPSNLHHIMTTNVQMSIIRSNAPGPPLHIGASHLPRGAAAAAVMSSSKVTTVLRPTSQLPNAATAQPAVQHLIHQPIQSRPPVTTSSTIPPAVVATVSATRAQSPVITTTAAHAADSTLSRPTLSIQHPPSAAISIQRPAQSRDVTTRITLPSHPALGTPKQQLHTMAQKTIFSTGTPVAAATVAPILATNTLPSTTTAGSVSHTQAPTSTIVTMTMPSHSSHATAVTTSNIPVAKVVPQQITHTSPRIQPDYPPERSSLIPISGHRASPNPVAMETRNDNRPSVPVQFQYFLPTYPPSAYPLAAHTYTPITSSVSTIRQYPVSAQAPNSTITAQTGVGVASTVHLNPMQLMTVDASHARHIQGIQPAPISTQGIQPAPIGTSGIQPAPIGTPGIHSAAPINTQGLQPAAMANQQPQPEGKTSAVVLADGATIVANPISNPFSAAPAATTVVQTHSQSASTNTPAQGSSPRPSILRKKPATDGMAVRKTLLPPQPPDVATPRVESSMRSASGSPRPAGAKPKSEVHVSIATPVTVSLETISNQNAEQPTVAVPPTAQQPPPTIPSMIAAASPPSQPAIALSTIPGAVPVTPPITTIAATPTLSAPVGGTPSTVLGPPVPEIKVKEEAEPVDITRPVSTVPPLATNTVSPSLALLASNLSMPPSDLPPGASPRKKPRKQQHVISTEEGDMMETNSTDDEKSAAKSLLVKAEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYSDVRVKEEKKAMLQEIANQKGVSCRAQGWKVHLCAAQLLQLTNLEHDVYERLTNLQEGIIPKKKAATDDDLHRINELIQGNMQRCKLVMDQISEARDSMLKVLDHKDRVLKLLNKNGTVKKVSKLKRKEKV
Protein: Cyclin N-terminal domain-containing protein (G5EAX4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- cyclin-dependent kinase
- Cyclin dependent kinase inhibitor Pho81, putative
Sequence:
MDLNRTALQEFIAQPVSRDMVAYLAQQAALVIRCESHVTTTASTQTVHGQHTPPSTPPMDAADQQLPRLPSVEAFITSLVTRSQVQVPTLMTTLVYLARLRARLPPVAKGMRCTVHRIFVASLILAAKNLNDSSPKNKHWARYTVVKGYEGFSFSLPEINLMERQLLFLLDWDTRVTEADLFLHLEPFLAPIRHRLQQREAKMHQPREWHRFQASAELLACRLRRQKLEARLEARRRLPPSPQPSASLSSVSSSSSLQSDAAVSAPDSDRYQPYPPRRRPSNRSRHSVSPPSIQEIPGLSRTETVPTLCSRSSSVAPSTRSNTPASLRPSSSYNSMDQEIQVVDVSRSPGLSSGYVHLPSSTMMVPLPADVAMAKGDDIAVQQPSKKMRMSGHSGSSGFVARFLASATGTYMGHRMRPRV
Protein: Phosphatidylinositol 3-kinase catalytic subunit type 3 (EC 2.7.1.137) (F1MTL5)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MGEAEKFHYVYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFEIVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGRWKPMDVEDSLELLSSQYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQGSVSESVSNSGINSAEIDSSQIITSPLPPVSSPPSASKTKESSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Protein: NEDD4-binding protein 3 (N4BP3) (O15049)
Organism: Homo sapiens (Human)
Function: Plays a positive role in the antiviral innate immune signaling pathway. Mechanistically, interacts with MAVS and functions as a positive regulator to promote 'Lys-63'-linked polyubiquitination of MAVS and thus strengthens the interaction between MAVS and TRAF2. Also plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (By similarity).
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:11717310}. Cell projection, axon {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites. {ECO:0000250|UniProtKB:Q3LUD3}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
Sequence:
MATAPGPAGIAMGSVGSLLERQDFSPEELRAALAGSRGSRQPDGLLRKGLGQREFLSYLHLPKKDSKSTKNTKRAPRNEPADYATLYYREHSRAGDFSKTSLPERGRFDKCRIRPSVFKPTAGNGKGFLSMQSLASHKGQKLWRSNGSLHTLACHPPLSPGPRASQARAQLLHALSLDEGGPEPEPSLSDSSSGGSFGRSPGTGPSPFSSSLGHLNHLGGSLDRASQGPKEAGPPAVLSCLPEPPPPYEFSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALREPPTPWSPRLESSKI
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (Q92410)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Interaction partners:
- Trehalose-phosphatase
- Trehalose 6-phosphate synthase/phosphatase complex subunit
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen [starch] synthase
- Trehalase
- glycogenin glucosyltransferase
- Glycogenin glucosyltransferase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
Sequence:
MVQGKVLVVSNRIPVTIKRLDNGSYDYSMSSGGLVTALQGLKKTTEFQWYGWPGLEIPEDEQTKVNDELKSKFNCTAIFLSDTIADLHYNGFSNSILWPLFHYHPGEMNFDENAWAAYIEANKKFALEIVKQVNDDDMIWVHDYHLMLLPEMLRQEIGNKKKNIKIGFFLHTPFPSSEIYRILPVRKEILEGVLSCDLIGFHTYDYARHFISSVSRIVPNVSTLPNGIKYQGRSISIGAFPIGIDVDNFIDGLKKDSVVERIKQLKSKFKDVKVIVGVDRLDYIKGVPQKLHAFEVFLNENPEWIGKVVLVQVAVPSRGDVEEYQSLRSTVSELVGRINGEFGTVEFVPIHYLHKSIPFDELISLYNISDVCLVSSTRDGMNLVSYEYIACQQDRKGVLILSEFAGAAQSLNGALIVNPWNTEDLSEAIKESLTLPEEKREFNFKKLFTYISKYTSGFWGESFVKELYKCNPQKSLRD
Protein: Major latex homologue type2 (Major latex protein-like protein) (Major latex-like protein) (Polyketide cyclase/dehydrase and lipid transport superfamily protein) (Q96274)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- EPIDERMAL PATTERNING FACTOR-like protein 5
- Nuclear-pore anchor
- PLAT domain-containing protein 1
Sequence:
MAMSGKYVAEVPLKGSAEKHYRRWRSQNNLFPDAIGHHVQGVTVHDGDWDSHGSIKSWNYTLDGKPEVIKEKREIDDEKMALTFRGLEGHVMEKYKKYEVILQFIPKSNEGCVCKVTLIWENRNEDSPEPINYMKFVKSLVADMDDHILKGQNKA
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g07650 (EC 2.7.11.1) (C0LGE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Myosin-2
- Oligopeptide transporter 4
Sequence:
MIYLHRIYFIIVLFTLIFHGRLGFSDNNKLHEAEVRALKEIGKKLGKKDWDFNKDPCSGEGTWIVTTYTTKGFESNITCDCSFLPQNSSCHVIRIALKSQNLTGIVPPEFSKLRHLKVLDLSRNSLTGSIPKEWASMRLEDLSFMGNRLSGPFPKVLTRLTMLRNLSLEGNQFSGPIPPDIGQLVHLEKLHLPSNAFTGPLTEKLGLLKNLTDMRISDNNFTGPIPDFISNWTRILKLQMHGCGLDGPIPSSISSLTSLTDLRISDLGGKPSSFPPLKNLESIKTLILRKCKIIGPIPKYIGDLKKLKTLDLSFNLLSGEIPSSFENMKKADFIYLTGNKLTGGVPNYFVERNKNVDVSFNNFTDESSIPSHDCNRVTSNLVESFALGNKSHKGSTCFLQRMPCVHPKRYHLYKLYINCGGGEVKVDKEITYQADDEPKGASMYVLGANKRWALSSTGNFMDNDDDADEYTVQNTSRLSVNASSPSFGLYRTARVSPLSLTYYGICLGNGNYTVNLHFAEIIFTDDNTLYSLGKRLFDIYVQDQLVIKNFNIQEAARGSGKPIIKSFLVNVTDHTLKIGLRWAGKGTTGIPIRGVYGPMISAISVEPNFKPPVYYDTKDIILKVGVPVAAATLLLFIIVGVFWKKRRDKNDIDKELRGLDLQTGTFTLRQIKAATDNFDVTRKIGEGGFGSVYKGELSEGKLIAVKQLSAKSRQGNREFVNEIGMISALQHPNLVKLYGCCVEGNQLILVYEYLENNCLSRALFGKDESSRLKLDWSTRKKIFLGIAKGLTFLHEESRIKIVHRDIKASNVLLDKDLNAKISDFGLAKLNDDGNTHISTRIAGTIGYMAPEYAMRGYLTEKADVYSFGVVALEIVSGKSNTNFRPTEDFVYLLDWAYVLQERGSLLELVDPTLASDYSEEEAMLMLNVALMCTNASPTLRPTMSQVVSLIEGKTAMQELLSDPSFSTVNPKLKALRNHFWQNELSRSLSFSTSGPRTASANSLVDAEEKTGLLD
Protein: 8-demethyl-8-aminoriboflavin-5'-phosphate synthase (AFP synthase) (EC 2.6.1.114) (8-amino-flavin synthase) (K4REZ6)
Organism: Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
Function: Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin). Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined oxidation, decarboxylation and transamination reaction. The catalysis is initiated by an oxidation step in which the C-8 methyl group on the dimethylbenzene ring of FMN is converted to a formyl group to yield the 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) intermediate. In the presence of thiamine, the formyl group is oxidized into a carboxyl group to yield the 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate. Finally, in the presence of L-glutamate as an amino donor, decarboxylation and aminotransfer occur, resulting in production of 8-demethyl-8-aminoriboflavin-5'-phosphate. Addition of NAD (but not NADP) to the reaction increases the yield 1.7-fold. The reaction also proceeds without the addition of any electron acceptor, and it is possible that molecular oxygen serves this role.
Interaction partners:
Sequence:
MALKALILNTTLRRSPSRSQTQGLIDKAVPLYEKEGIETEVVRVIDHDIEQEYWDDYDDWNAGEKARREDEWPWLLEKIREADILVIATPITLNMCTSAAHVILEKLNLMDELNGDTKQFPLYNKVAGLLMCGNEDGAHHVAGTVLNNLGRLGYSVPPNAAAYWLGPAGTGPGYIEGKGDRHFHTNKLIRFMVANTSHLARMLQETPYTTDLEACAQAAREESDDVFAIRVNVNTPAIRYKRFQKLGEVKVEESQLG
Protein: Ubiquitin-like domain-containing protein (Q38A50)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDDKQAFFVRCIDGKTFKMVIRGDLGKLTVGKIRRYLKSYGVQDGMQLLFNGLSLADEQVGSDFGLCNGATLHLGPPSFSEPAVPQRTHGQGFSDEAAGSRTGDPTDTPHSSLSGDSRERNSKADSTHRDPCGGLSHADPARGTATYSGGRYNVDKGIPVTATSATKTNIDRIPSADLTSHSGFPVALEVENQQLREQVELLRREVADLRQKNKAPRATVLRQDLTSIEVLQSAKSNLQELAEELGVPLQFDTNFTCVVGDDESHTVLVTFDCVTERLYIYSTLLTQIPHDGEVRAKLYELLLEGSLLSREVCGGGIGISPQNGLVLLSTTIPLRHCNSSALKDIMPVFVETVARWRSLINELLN
Protein: AT3g20680/F3H11_7 (Plant/protein (DUF1995)) (Q9LHQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASSTLFKLNSQTFKALNPSPPSLSPPNSRIFHLHFSKSLSQQHSKLNHKSTTTRLFAPLCSSLPSPSSSSPPLSKEEAINQAKTCLLSCLIKPLNNPKLASPKLRKLKQPRFRLEIPILDDDSPSSLSQLAFSIFHDLPISRRGSNVKLLFLWPNPSFIDPAVKAFRSDSIHHIAMSPVSDSLKTALRSADVAIFMAPEKSQLEDVKTASEAFSTKPVVMINPRWLFEEEKSFGDGFIGSFEVIYAFTGLEVRGVFSKRKGVIFKCVRDGVVSGERWNVLVEEEEGNGTLKVVSQFNSRPSIEEVELVLYNLMAMNSPITKSAKFLSDLVSNITGKK
Protein: Small ribosomal subunit protein mS38 (Mitochondrial mRNA-processing protein cox24) (Q9P7H5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in the splicing of the mitochondrial mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P32344}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32344}; Matrix side {ECO:0000250|UniProtKB:P32344}.
Interaction partners:
- Tubulin-specific chaperone C
- Probable Rho-type GTPase-activating protein 3
- Probable Rho-type GTPase-activating protein 4
Sequence:
MLRRGALSTILKGLNGLSLRSPIPIWHVSASPEVGSKYNLPTVPTTSHVSYRQIAKANFFAGYRPLSANQICVPKVESKTQVSQSQDEEDQPQEYVLSLEDGYLYAQSFSASGSVTQTQPARISTQVWEQICDKLISITPLDLTSVKRKRKLKMNKHKFKKRLRRQRALRKRLGK
Protein: Probable ornithine decarboxylase (ODC) (EC 4.1.1.17) (Q54UF3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Interaction partners:
- Spermidine synthase
- Probable ornithine aminotransferase
- Uncharacterized cyclodeaminase
- Bifunctional protein argC
- S-adenosylmethionine decarboxylase proenzyme
- Arginase/agmatinase/formiminoglutamase family protein
- Tyrosine aminotransferase
- Multifunctional protein pyr1-3
- Cystathionine beta-synthase
Sequence:
MTGTKRNGEEVVNENNNNNVAEETNKKAKVDESSTETTESTSCSLLSRCEKLDIVRKELDVKPWDQGKVTIQELITSLLDKTDRDAFFVADVGVIIKQWQKWVKNLPNVKPYYAVKCNPTVGVLRVLDALGTNYDCASRTEIESVLNLGVDPSRIIYANPCKQISALKFARAHNVKLMTFDNLSELEKIEKFFPEAELVLRIAPDDSKSVMRFGSKFGVHIDDCNDLLEMAKEMNLKVVGVSFHVGSGCQSGDSYADALIMVKSVFDMAKKLNMELTLVDVGGGFTGSDDEKFNAFTKVIREKTAELFSPNVKIIAEPGRYFAAQSHTLAVTVISKRSIKQEDNRQHPRRTSNNMRQYNYYLADGVYGSFNNTKFDYAKVEPLLLKPSTKQPTPCTLFGPTCDSIDVVLKDTQIPELKIGDWLYFQDMGAYTIASSSSFNGFCPPPVYYYNSIPEEELKNL
Protein: PHD finger protein 21A (A0A8I6A676)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELQTLQEALKVEIQVHQKLVAQMKQDPQNADLKKQLHELQAKITALSEKQKRVVEQLRQNLIVKQEQPDKFQIQPLSQSENKLQTAQQQPLQPLQQQQQQQQQQQQQQQQQHAQQSAAPPSLTASQQVQATPPQPIKVPQFIPPPRLTPRPNFLPQVRPKPVAQNNIPIAPAPPPMLAAPQLIQRPVMLTKFTPTTLPTSQNSIHPVRVVNGQTATIAKTFPMAQLTSIVIATPGTRLAGPQTVQLSKPSLEKQTVKSHTEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSLGLVTHDHLEEIQSKRQERKRRTTANPVYSGAVFEPERKKSAVTYLNSTMHPGTRKRGRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTDGDIHEDFCSVCRKSGQLLMCDTCSRVYHLDCLEPPLKTIPKGMWICPRCQDQMLKKEEAIPWPGTLAIVHSYIAYKAAKEEEKQKLLKWSSDLKQEREELEQKVKELSSSISKCMEMKNTILARQKEMRSSLDKVKQLIRLIHGIDLSKPVDSEATVGALSNGPDCTPPANAASTPAPSPSSQSCTANCNQGEETK
Protein: Transcription factor tau subunit sfc7 (TFIIIC subunit sfc7) (Transcription factor C subunit 7) (A6X980)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q12415}.
Interaction partners:
- Transcription factor tau subunit sfc1
- Putative transcription factor tau subunit sfc9
- Transcription factor tau subunit sfc4
- Transcription factor tau subunit sfc6
- Transcription factor tau subunit sfc3
- Transcription factor IIIB 60 kDa subunit
- TATA-box-binding protein
- Putative RNA polymerase II transcriptional coactivator
- Transcription initiation factor IIF subunit beta
- Transcription factor TFIIIB component B''
Sequence:
MSSNSPSLETDVDDVENIVFQFQNSSLDFQSSDDFSILGIDQPHPIVRIGGMFFRGTWHQPIGTDIVVPSVNDSELSRDGLVLCKRRLMLEQIRLVPKNPSPSSSIHSPTQGEPENISEN
Protein: Aldehyde dehydrogenase family 2 member C4 (EC 1.2.1.3) (ALDH1a) (Protein REDUCED EPIDERMAL FLUORESCENCE 1) (Q56YU0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ferulic acid and sinapic acid biosynthesis by oxidation of conyferylaldehyde and sinapaldehyde, respectively. Can oxidize L-lactaldehyde. Possesses activity on acetaldehyde and glycolaldehyde in vitro.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Cytochrome P450 84A1
- Flavone 3'-O-methyltransferase 1
- F5F19.5 protein
- 4-coumarate--CoA ligase-like 1
- Cinnamoyl-CoA reductase 1
- 4-coumarate--CoA ligase 3
- 4-coumarate--CoA ligase-like 7
- 4-coumarate--CoA ligase-like 6
- Cinnamoyl-CoA reductase 2
- 4-coumarate--CoA ligase 4
Sequence:
MENGKCNGATTVKLPEIKFTKLFINGQFIDAASGKTFETIDPRNGEVIATIAEGDKEDVDLAVNAARYAFDHGPWPRMTGFERAKLINKFADLIEENIEELAKLDAVDGGKLFQLGKYADIPATAGHFRYNAGAADKIHGETLKMTRQSLFGYTLKEPIGVVGNIIPWNFPSIMFATKVAPAMAAGCTMVVKPAEQTSLSALFYAHLSKEAGIPDGVLNIVTGFGSTAGAAIASHMDVDKVSFTGSTDVGRKIMQAAAASNLKKVSLELGGKSPLLIFNDADIDKAADLALLGCFYNKGEICVASSRVFVQEGIYDKVVEKLVEKAKDWTVGDPFDSTARQGPQVDKRQFEKILSYIEHGKNEGATLLTGGKAIGDKGYFIQPTIFADVTEDMKIYQDEIFGPVMSLMKFKTVEEGIKCANNTKYGLAAGILSQDIDLINTVSRSIKAGIIWVNCYFGFDLDCPYGGYKMSGNCRESGMDALDNYLQTKSVVMPLHNSPWM
Protein: Syntaxin-18 (Q8VDS8)
Organism: Mus musculus (Mouse)
Function: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Vesicle-trafficking protein SEC22b
- Centromere/kinetochore protein zw10 homolog
- Vesicle transport protein USE1
- Vesicle transport protein SEC20
- RAD50-interacting protein 1
- Neuroblastoma amplified sequence
- Syntaxin-5
- Syntaxin-8
- Sec1 family domain-containing protein 1
- Syntaxin-17
Sequence:
MAVDITLLFRASVKTVKTRNKALGVAVGGGADGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTMSDYGRMTDTERDQIDQDAQIFIRTCSEAIHQLRTEAHKEIHSQQVKEHRTAVLDFVDDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPHTKRKDSTSEKAPQNASQDSEGKPAAEELPEKPLAESQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLVMCSFSLLFLDWYDS
Protein: Probable acid phosphatase SPBC4.06 (EC 3.1.3.2) (Q9USS6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1
- Low molecular weight phosphotyrosine protein phosphatase
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2
- Alkaline phosphatase
- Riboflavin synthase
- Thiamine-repressible acid phosphatase pho4
- Probable FAD synthase
- Acid phosphatase
- Thiamine-repressible acid phosphatase SPBC21H7.03c
Sequence:
MSQMSSASVKFPDSVPGVDYPKQLQLKYLQVIFRHGERAPVKERLGSAGIPKDWKLCNNARRFFAQIKGEKEWSVLGFERKVESPVDTSLAAPTSDNSPSGVCIHGELTDFGRVTTRTLGEYLRERYVKQLKFLPDELNNYADVYMRATPMVRALESLEHVFSGLYPESKRKMGLPVIFTRNWSDENLLPNENNCPRLVQLYEEFAERAAKLYDPLLAGRASEMMSQFMNGQPVRVVSSHPRLSGLLDTINAAIGSHVDFNPNLRDEQWLRDAETAVVEEWFGGYKVSKLMRQLGAGSLLNDLSMRMENFVVAEKNGSPYHRLALYGAHDVTIAAILASLDAFDYRWPPFTSHLEMELFEDTSSKSDSQNQSGDNKTTDLKLFSDESTDASNSAIVAASNSARDMSDWYVRITYNSTPVVMGACRGQGYKGNDTICPLSIFKDTVRALKPVEYHTMCKPVKK
Protein: KH RNA binding domain containing, signal transduction associated 3 (H0YAQ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKPTLRTRGVPAPAITRGRGGVTARPVGVVVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYGKKSGLTQDTR
Protein: Ninein homolog (Blastoderm-specific protein 25D) (P11929)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27053665, ECO:0000269|PubMed:27422905}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:27053665, ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32066907}. Cytoplasm {ECO:0000269|PubMed:30626718}. Note=During embryogenesis, localizes to the periphery of the centrosome where it partially overlaps with the pericentriolar region (PubMed:27053665, PubMed:27422905). Also localizes to pericentriolar region in larval brain neuroblasts (NBs) (PubMed:27053665). In dividing larval brain NBs and male germ stem cells (GSCs) asymmetrically localizes to centrosome pairs by preferentially accumulating at the younger, daughter centrosomes rather than the older, mother centrosomes (PubMed:27053665). In NBs daughter centrosomes it is only detected at interphase or during early mitosis (PubMed:27053665). However, it is symmetrically localized to centrosome pairs in embryos and ganglion mother cells in the developing brain (PubMed:27053665). In wing epithelial cells, localizes to non-centrosomal microtubule-organizing centers (ncMTOCs) at adherens junctions near the apical membrane (PubMed:27053665). In the fat body and myocytes of third-instar larvae, localizes to perinuclear ncMTOCs (PubMed:32066907). Enriched at the plus-ends of growing microtubules (MTs) (PubMed:27053665). Binds MTs, and with Dynein can move along MTs toward their minus-ends (PubMed:27422905). From stage 14 to stage 16 embryos, during which myonuclei split into two clusters and migrate toward muscle poles, broadly but weakly expressed in the cytoplasm and strongly enriched in cytoplasmic puncta of myotubes (PubMed:30626718). {ECO:0000269|PubMed:27053665, ECO:0000269|PubMed:27422905, ECO:0000269|PubMed:30626718, ECO:0000269|PubMed:32066907}.
Interaction partners:
Sequence:
MEVSADPYEQKLYQMFRSCETQCGLLDEKSLLKLCSLLELRDQGSALIASLGGSHQLGVSFGQFKEALLNFLGSEFDGNTSSGFIERSLVITDEPLNNTYIESPPESSDREVSPKLVVGTKKYGRRSRPQQGIYELSVTDSDNTDEDQLQQQQNQRSLNGCDELGVQVQRSSSQSDLPGSRRLRSVHTSGSKLKRCASLPARRKMNSNTTGATTSPTAAAKLKQLSIQSQAQHSSSVESLDTVTPQQLETISVHSIMEAWELASIPNTRNLLHVLGFDEEEEVNLQQLTKALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAYRQQHEENLKLRADNKAANQRVALLAVEVDERHASLEDNSKKQVQQLEQRHASMVREITLRMTNDRDHWTSMTGKLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQTSSSIGGTPEHSPLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSDASNSGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAYEDCEDYWQTKLSEERQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRLSPIDERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQEISSLQSEIEDLRQRLGESVEILTGACELTSESVAQLSAEAGKSPASSPISYLWLQSTIQEPAKSLADSKDEATASAIELLGGSPSHKTASRNNLTTSETSIFSTTPFESSQSGPSPTNSGNSNAYGANPGPAPISKPKRSQSPQQAAASEGEIADCETSSTASGKSFESNSKTSCLSHEKCSSPSALKEELKRLKFFELSLKEQIKDLSLQRDGLVMELQQLQEARPVLEKAYARTTHPTLQQRLNQLELRNRHLQNVIKQQQHYTESLMQQSWRQHQVELNDLHSRIETQGVLLADQTQRLQSADILVKDLYVENSHLTATVQRLEQQRARVNLIHQQQQQQRLVGGGLPGMP
Protein: trypsin (EC 3.4.21.4) (Q91036)
Organism: Gadus morhua (Atlantic cod)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
IKSLIFVLLLGAVFAEEDKIVGGYECTKHSQAHQVSLNSGYHFCGGSLVSKDWVVSAAHCYKSRIEVRLGEHHIRVNEGTEQYISSSSVIRHPNYSSYNINNDIMLIKLSKPATLNQYVQPVALPTECAADGTMCTVFGWGNTMSSVADGDKLQCLNLPILSHADCSNSYPGMITQSMFCAGYLEGGKDSCQGDSGGPVVCNGVLQGVVSWGYGCAESI