wanglab/gogpt-training-data huggingface dataset:
Protein: Translation factor GUF1 homolog, chloroplastic (EC 3.6.5.-) (Elongation factor 4 homolog) (EF-4) (GTPase GUF1 homolog) (Ribosomal back-translocase) (Q9FNM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes chloroplast protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- DNA-directed RNA polymerase III subunit 1
- Large ribosomal subunit protein bL28c
- 50S ribosomal protein L33
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein uL1c
- 50S ribosomal protein L20
- Large ribosomal subunit protein bL20c
- Large ribosomal subunit protein uL18z
Sequence:
MAMASAMDLSSPPTFFLSGTSTSSPSLRRLSSISVSGFRRHSNRKLQILCQATAGTEPQSGLSVSGSKLAARSGQDRLLKVPISNIRNFSIIAHIDHGKSTLADKLLQVTGTVQNRDMKEQFLDNMDLERERGITIKLQAARMRYVYEDTPFCLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENNLEIIPVLNKIDLPGAEPEKVLREIEEVIGLDCSKAIFCSAKEGIGITEILDAIVQRIPAPLDTAGKPLRALIFDSYYDPYRGVIVYFRVIDGKVKKGDRIFFMASGKDYFADEVGVLSPNQIQVDELYAGEVGYIAASVRSVADARVGDTITHYSRKAESSLPGYEEATPMVFCGLFPVDADQFPDLRDALEKLQLNDAALKFEPETSSAMGFGFRCGFLGLLHMEIVQERLEREYNLNLITTAPSVVYRVNSVNGDTTLCSNPSRLPDPGQRKSVEEPYVKIELLTPKDYIGALMELAQERRGEFKEMKYIAENRASILYELPLAEMVGDFFDQLKSRTKGYASMEYSVIGYRESDLIKLDILINAEMVEPLSTIVHRDKAYSVGRALTQKLKELIPRQMFKVPIQACIGSKVIASEALSAIRKDVLAKCYGGDISRKKKLLKKQAAGKKRMKAIGRVDVPQEAFMAVLKLEREVL
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q382R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MESFGPLAVVSATILSVIAVFYIGIMGPSRYHRNGVVGWLYRGMVKLPHACVSCCCCRSGTSGGLFSCFMKTRCGRCFHYLMNERHWGLVILYIILVWPVEIAYLALVAMRLKASLLSKMVSWGLVLFSEVVYFAAVFSDPGTVTSRSEKDAQKRAFATAGGAKPQMKKGHEATRKGEERMQYRKFLLSPRAEEEQGQRYVVDGILYGKDSTRGCGVECPTCNVPRPSRSKHCRMCNRCVRRYDHHCPWINNDVAEGNHRWFLLFLLIHIIECIWGLWDLYTMVVQFLTAQGLWVSAIRFANGYTYRITNIHRLFAIATMHPLVLFLIIFAAPITVVLAVFWLQQMSFVVSNVTINDMNKIDTTIDFITTLPTATDVYEEAQNVRSVLENVAARPPRRLRALKRPSAEAIVVGSKKDKAYRKEVSKMLMSDLKGLFNRGVWNNLKEVMFPYS
Protein: BAG family molecular chaperone regulator 5 (BAG-5) (Bcl-2-associated athanogene 5) (Q8CI32)
Organism: Mus musculus (Mouse)
Function: Co-chaperone for HSP/HSP70 proteins. It functions as a nucleotide-exchange factor promoting the release of ADP from HSP70, thereby activating HSP70-mediated protein refolding (By similarity). Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding. Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity).
Subcellular location: Note=In cardiomyocytes, localized at specialized membrane contact sites between T-tubules and the sarcoplasmic reticulum, known as junctional membrane complexes. {ECO:0000269|PubMed:35044787}.
Interaction partners:
- Cyclin-G-associated kinase
- Heat shock 70 kDa protein 1B
- Heat shock cognate 71 kDa protein
- BAG family molecular chaperone regulator 2
- E3 ubiquitin-protein ligase CHIP
- Ras-related protein Rab-7L1
- BAG family molecular chaperone regulator 1
- Leucine-rich repeat serine/threonine-protein kinase 2
- Heat shock 70 kDa protein 4
- E3 ubiquitin-protein ligase parkin
Sequence:
MDMGNQHPSISRLQEIQREVKAIEPQVVGFSGLSDDKNYKRLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFKEAQALVKDKIVPFYSGGNCVTDEFEEGIQDIILRLTHVKTGGKVSLRKARYRTLTKICAVQEVIEDCMKKQPSLPLSEDVHPSVAKINSVMCEVNKARGTLIALLMGVDSSETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADSTHAFDLGQNHSIIKIENVLKRMREIKNELLQAQSPPELYLRAKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQILITYLDLKEALEKRKLFPCEEHPPHKAVWEILGNLSEILGEVLSFGGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVKLAQNILSYLDMKSDEWEY
Protein: Multiple inositol polyphosphate phosphatase 1 (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Q9VV72)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Has a role in embryonic tracheal development where it localizes to the leading edge of actively migrating branches. In these leading cells, enhances formation and/or maintenance of filopodia which may drive branch migration and elongation by cell-cell intercalation. The function in tracheal morphogenesis is dependent on its inositol polyphosphate phosphatase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26628373}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:26628373}. Apical cell membrane {ECO:0000269|PubMed:26628373}. Basolateral cell membrane {ECO:0000269|PubMed:26628373}. Cell projection, filopodium {ECO:0000269|PubMed:26628373}. Cell junction {ECO:0000269|PubMed:26628373}. Note=Has a dynamic localization pattern during tracheal development. During early tracheal invagination (embryonic stage 10), localizes mainly to the apical cell membrane. During the primary tracheal branching stage (embryonic stage 11), found mainly at the basolateral cell membrane. At later stages (embryonic stage 13-15), also localizes to cell-cell junctions and filopodia. {ECO:0000269|PubMed:26628373}.
Interaction partners:
- Kinase
- Multiple inositol polyphosphate phosphatase 1
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- Uncharacterized protein, isoform C
- Phosphoglycerate mutase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Phosphoglycerate mutase
- Kinase
- Phosphoglycerate mutase
Sequence:
MRLLILLLLPLVAIAQDDYCFSKDTSRLQTRQFSSKTAYQIVKGTDIDKQYLVPGCQPQKMWIFHRHGTRLPKKSMINKASRVAELRDLIINNYQVARTKPETDALCQTDLIAIKLWKWNSSITPDMEEYLTAQGYEDLRGTAKLYQRYYPTVLTANYNDTYYQFRHTDTQRTTESFKAFAEGLFGSQNAAHPVEIPKQDLLLRPYDYCSSFKNVNYKDEGSEYYKFHQSKLYNDTLADISTRLGFLYTLEEADIKLMYDMCRYEQAWNVDRNSVWCGAFLPEQITVFEYLEDLKYYYGSGYGFPENAHLNCRLVQDLLTHLSNPVSPHVVAHFGHSTGLLTLLTALGIQKDDIKLRADNYDSLTSRRWKSSLIDPFAANFVAVKYDCPADLDREKVVFFLNQQAVQLDWCSVGLCKWSDVLEKYKTIADADCGEYYCRTGGAPSLGSGVGGLLATTLAAMLVYLMH
Protein: ATPase E1 (AtE1) (Q0WRA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tetratricopeptide repeat
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- AT3G18790 protein
- Protein ABA AND ROS SENSITIVE 1
- Pre-mRNA-processing factor 19 homolog 1
- Pre-mRNA-processing factor 19 homolog 2
- AT4g21110/F7J7_50
- Transcriptional regulator ATRX
- rhamnogalacturonan endolyase
- SNW/SKI-interacting protein
Sequence:
MAAVQQQQAMQKNTLYVGGLADEVNESILHAAFIPFGDIKDVKTPLDQANQKHRSFGFVTFLEREDASAAMDNMDGAELYGRVLTVNYALPEKIKGGEQGWAAHPLWADADTWFERQQQEKEILKMQAENKAAMETAEELHRKKLAEDRQGEMEEDTDTKNDPMARAEADALSHGDA
Protein: Cuticle collagen dpy-10 (Protein dumpy-10) (P35800)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment.
Interaction partners:
- Homeobox protein unc-4
- Basement membrane proteoglycan
- Protein unc-119
- Cuticle collagen dpy-2
- Nematode cuticle collagen N-terminal domain-containing protein
- Endoprotease bli-4
- Tubulin beta-2 chain
- C-mannosyltransferase dpy-19
Sequence:
MKNNAKEDYRTFSLTTNYSRQMIYRCVTGLQIGFSLFSFIIVCVALPIMYNHVQNTITYVDREMAYCEVRFLYFYCIKFFSTLQRSNDEAALELQYGKMRMTGNRTARGAYGSGASHGFRPTAYGDEITGAPLETECPGCCIPGPPGPRGSSGTPGKPGLPGNAGKPGMPGTTPNQTCPLNQVREPPPCRPCPKGPPGIKGWPGFPGDVGPPGPPGLKGIDGEDGAPGETGPTGPPGYRGGPGAPGDKGPTPEGDLKEGPPGDEGPPGPIGAPGMPGLPGRNGLTGGQGERGWPGVSGESGEPGYPGPEGPMGGQGPPGEPGVCVCQNVDSILLINPGPQPRIRADDYNSDDGYGGSRGGGDRAGYQGYGRK
Protein: tRNA endonuclease vms1 (EC 3.1.-.-) (O74977)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000250|UniProtKB:Q04311}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q04311}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q04311}.
Interaction partners:
- Cell division cycle protein 48
- Ribosome quality control complex subunit 2
- Nuclear protein localization protein 4
- Ribosome quality control complex subunit 1
- RQC trigger complex subunit RQT4 homolog
- Probable mitochondrial import receptor subunit tom70
- ATPase family gene 2 protein
- Eukaryotic translation initiation factor 6
- Mitochondrial import protein 1
- Probable mitochondrial import receptor subunit tom40
Sequence:
MGDISKHNIFSLPEDILAKLELREEYSVEEKTDSANLSNQGDIVDSTQKNISSCVNCQIDNLHTLDERKSHIKSDWHRFNTKRKITKLPPVSQDEFESIIEDLPESLSGSESETNSESEEDNFQIEKAFKQSLNIGKVDSADENNNQRTNSPLTWFQLSNASAEVPTYIGVYKHMFSGNNHITKDLLVQQQNHNRQKPLQLAMFMVGGGHFAAMIASNEFNPRDPHVPKVLAQKTIHRYTTRRKQGGSQGAADNTKGNIHSAGSGLRRYNEQALIKDIQQVFKDWGKLLETCDLIFVRAIGSSNRSIFFSQPGALISPKDPKLRVFPFTTKRATHSELLRCYKELVTPKISHVDSISIKAQEEERKRQAEIEKEIRQSRLQEEERKKKKLAKYTEVIISNLKASNIEAFLEYLRSNDLSINFQFYPKNVHLHTSTPLHYAVTQKNAKLVAKLLRNGADPAMLNGNGKTPFEISTGNKEVKDEFLIARHELGESFFDWEAAKVGAPQSREQIQKQRQKAKTKLENQRRDKERQEELRRKEAMQKIEEQSKRDYDKLHGEGHSLGINNVRKVDELQSLSPEMRMRIEREKRAAAAMKRMQTK
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit H (Phosphatidylinositol-glycan biosynthesis class H protein) (PIG-H) (Q14442)
Organism: Homo sapiens (Human)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI alpha-1,2-mannosyltransferase 3
- Protein preY, mitochondrial
- GPI ethanolamine phosphate transferase 2, catalytic subunit
Sequence:
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCENSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVKDIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAHQKATSTSP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q95U75)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MELRQTHLANKDLDGATEDDSIVELRRRDAQATPLPRIAVSALPTLQPHPTPKERQKPPMPRLLSTEDDAGVSFALGSIEKHIHNVEESFKQQQQNQQSQSSMDVMKLEIKRKQSKRYGETENLLRPGISDMSSENDFQYLGGRRAGELDDSNELMLSEFQRGSDGRNSIGAYSKNSAAAANGANAVKAKLARTASDTKNNDTVLAMRATFKQKQHLQDEKQPAVWRPAGTGPTPAARSSSSTTSTSGSASRGGSSSSVVDGVAPSKLTATTISASKRREENLRQFEALLAQKSSHRHGASGASGTGSNAASSKRRSDRPIVAPIPPYNSSRAEHVTSSTRHSVDPRSHSGHESRSGTASTHPPVGHHPTSRVPSVVANRSNVYSNNAAQGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIGKTEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGAETLRVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETKARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPTIADEAAKPRVLRFTWSMKTTSPLMPDQIMQKIREVLDQNNCDYEQRERFVLWCVHGDPNTDSLVQWEIEVCKLPRLSLNGVRFKRISGTSIGFKNIASRIAFDLKL
Protein: Vesicle-associated membrane protein 8 (VAMP-8) (Endobrevin) (Edb) (O70404)
Organism: Mus musculus (Mouse)
Function: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells. Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:27628032}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22118466}; Single-pass type IV membrane protein {ECO:0000305}. Zymogen granule membrane {ECO:0000269|PubMed:15363411}; Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells (By similarity). Midbody region during cytokinesis (By similarity). Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (PubMed:15363411). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9614193}.
Interaction partners:
- Syntaxin-8
- Vesicle transport through interaction with t-SNAREs homolog 1B
- Synaptosomal-associated protein 29
- Syntaxin-7
- Synaptosomal-associated protein 23
- Syntaxin-4
- Syntaxin-17
- Syntaxin-3
- Syntaxin-6
- BET1 homolog
Sequence:
MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT
Protein: Eukaryotic translation initiation factor 4E transporter (4E-T) (Dm4E-T) (eIF4E transporter) (Q8IH18)
Organism: Drosophila melanogaster (Fruit fly)
Function: eIF4E1-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (By similarity). Probably plays a role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (By similarity). Acts as a binding platform for multiple RNA-binding proteins. Required for the formation of P-bodies (By similarity).
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:24335285}. Cytoplasm {ECO:0000269|PubMed:24335285}. Nucleus {ECO:0000269|PubMed:24335285}. Note=Mainly localizes to processing bodies (P-bodies) (PubMed:24335285). Present at low level in other parts of the cytoplasm and in the nucleus (PubMed:24335285). {ECO:0000269|PubMed:24335285}.
Interaction partners:
- Eukaryotic translation initiation factor 4E1
- ATP-dependent RNA helicase me31b
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- Trailer hitch, isoform H
- eIF-4F 25 kDa subunit
- Eukaryotic translation initiation factor 4G1, isoform B
- Enhancer of mRNA-decapping protein 3
Sequence:
MDTSKISARYSKVDLLALRYEGKSRQRPQCSTRLELQTLGFWKINLNTAALTVSSAYSNQNKNRLSPEADNSSLICSNSSSISSRRAMRNRERANNYYQRFVPTDSLLISGEDKDKDALSHGQPYKLNIIDHRSISSSHLMPAFAKRRFVISKGSNSEESNEGINTCASKGKAASSPSRKGSELDTAETCLNFVQPDHDQCMSSSPTFSTSRQERRIGSGRLLPRSDNWDYKNEKTVEASIENEKETSPNGSGSTSSLNQHNQSQHRSRTFSGRLVERVPEVTDRRFQYDSKKSFDRQGINNRRISGKEPFSTQSRSKRGNSYLIHEEPEWFSAGPKSQLETIDLHGFEDLEKNEERSVTEDKNNQIQQLDKNLDAQASKDEASMRNSNDSLNFREVIPSDEKKHTDENVVTSIQNSTDLGHPNKNKPIQMQPSQNPESEFNFDAFLNMHPLDNSVLSNDETGKSDSKGTSRFSRWFRQKEAANNNEFPGFRESHAQEKRGIPSVKDLEAQMIKVDMRTDLINPIAGSLCQTVQMEKPIARDTEAFKKLLQQLGSQARQHHPCNDDCRTINLSNIANHVHLESKLHQKINDGHLQQPELSVNVPTMPTSSHVFLQKRLEIQHLIQRLHCGDVSHDFLEKELDNPSTPAATKDVIATVLNEYSHSKRNPVVTGDPNIFTQQSFLQPQSVHQHYSQELHSQNTANHTINQLISHGNSPTPLAFTPTSVLRKMTADKDTQSPSTYCQNPQYHVHQQNAKQVGTRENVLEPQLTATMAVQPRMILGGGNFAIGQNNQHLSPNMSQSRNQQVLKWTSGNMQMVHGKTFGRPILKGGLNSMPHSNSALPFTAHKIEMQPIHQPHLQQQQHRFKAVQSVESNLNTESVHQNITSPVGWHQLYMQHQQQHHHTRQQLSQRVIYGEMHRQSNPQMSPPVPGFSDSSDSGNVIKANSLTSPSYQRDERISSPTNQLAQWFSPELLAKASAGKLPLLNVNQALSLEEFERSIQHSSGVVHN
Protein: Internexin neuronal intermediate filament protein, alpha b (F1Q8F1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Neuropeptide FF-amide peptide precursor-like.
Sequence:
MSYGSDIYSASSYRKIFGDSTRFSASPSRLSSSRSGFKSQSVNRPNIPSSYKRSTRSGFPSSSLDSFDFTQSTVLNNEFKIIRTNEKEQMQGLNDRFAMFIEKVRNLEQHNKVLETELVTLRQRQTEPSRLAELYQQEIRELRSQLEELNAEKNQMMFERDSIEEDLQKLHEKFEEEMRMREEAEQTLRAFKKDVDNASMVRLDLEKKVESLLDEINFLRKVHEEEVAELMNMIQASQVSVEMEVAKPDLTSALKDIRGQYEAMASKNLQSAEEWYKSKFADLSEQANKSNEVIRASREELNEFRRQLQSKTIEIESLRGTNESLERQIHEMEDRHNAEIMGYQDSIGELENDLRTTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRISTGITYPTPASVSSYSYQSRLYSSTSMSSKKEVKDDDDKQQSGKPGKGSSQSDDSKKNDKIDSGDLNSTNQKN
Protein: Transcriptional adapter 2 (Q59WH0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B. Required for expression of many CAS5-dependent genes. Plays a key role in cell wall integrity, cell adhesion, hyphal development and pathogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Histone acetyltransferase GCN5
- Protein SPT3
- Histone acetyltransferase
- Histone acetyltransferase
- SGF29 C-terminal domain-containing protein
- Transcription initiation factor TFIID subunit 10
- SAGA histone acetyltransferase complex subunit
- Transcription and mRNA export factor SUS1
- Transcription initiation factor TFIID subunit 6
Sequence:
MDSRTKLFHCDVCSSDCTNRIRIQCAICTDYDLCVPCFAAGLTTGDHKPWHDYQIIEQNTYPIFDRDWGADEELLLIQGCETSGLGNWADIADHIGNRSKEEVAEHYFKIYLESKDYPLPEMNKDFTDVSPLQFLEERKERLEKRKNIPLPPPRGKPVASVPLCHEIQGYMPGRLEFDHEAENEAEIPIKDMVFDPEDSANDIDLKLTILDIYNSRLTTRAERKRVMILNHLLDYRKNIGSDKRKSKEEKDLLKKINAFIRILTPEDFESFSRDLLTELKCRMKIQQLQTWRRNGITTLEDGAKFEKDKVIRAAHYQRMGNGTGSGRHSQTPGLTNGNSFNGNGHRNKFSPQPEFRSKSTTARAPLDISHAADFELLSAEEKQLCATLRILPKPYLAIKNQLMREAVKNNGVLKKKDARQALKIDVNKASKIYEFFVHMGWCSQG
Protein: Heterogeneous nuclear ribonucleoprotein A0 (B5X9N1)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MDNSSQLCKLFVGGLNVDTDDDGLRKHFEQYGQLTDCVVVVNKQLQRSRCFGFVTYSSAEEADAAMAARPHVVDGTNVELKRAVAREDAGKPEALAKVKKIFIGGLKDDIEDEHLNEYFSQFGEIEKAEVIAEKETGKKRGFGFVHFTDNDSADKAVVLKFHNINGHKVEVKKALTKQEMQATGRGGRGGRGMRGGQNSVLGHLAKCGHCETKSFKKTSNQTGRKITSQNLICTSSSCYRTRSIAKFIYHLCSKMRACSCR
Protein: NADPH-dependent aldose reductase GRE3 (AR) (EC 1.1.1.21) (Genes de respuesta a estres protein 3) (NADPH-dependent aldo-keto reductase GRE3) (Xylose reductase) (EC 1.1.1.-) (P38715)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)-lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- D-xylulose reductase
- Sorbitol dehydrogenase 2
- Sorbitol dehydrogenase 1
- Xylulose kinase
- Transaldolase
- Transketolase 1
- Transaldolase NQM1
- Glyoxalase I
- Transketolase 2
- Ribulose-phosphate 3-epimerase
Sequence:
MSSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA
Protein: Two-component response regulator ORR3 (Type A response regulator 3) (OsRR3) (Q4GZK8)
Organism: Oryza sativa subsp. indica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Interaction partners:
Sequence:
MSTKTVPEPEPHVLAVDDSIVDRTVISRLLRSSKYRVTTVDSGKRALEVLSLDRNVHMIITDYCMPEMTGFDLLKRVKESAELKEIPVVLMSSENSPTRIRRCLEEGAEDFLIKPVRPSDVSRLCNRVIMK
Protein: Adenosylhomocysteinase (AdoHcyase) (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (P83783)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-synthase
- S-adenosylmethionine-homocysteine S-methyltransferase
- S-adenosylmethionine synthase
- cystathionine gamma-synthase
- Cystathionine beta-lyase
- cystathionine gamma-lyase
- Cysteine synthase 1
- Cysteine synthase
- Homocysteine/cysteine synthase
Sequence:
MSSAPATNYKVADISLAAFGRKDIELSENEMPGLMYIRKKYGPSQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIFSTQDHAAAAIAAAGVPVFAWKGETEEEYQWCIEQQLFAFKDGKKLNLILDDGGDLTSLVHEKYPEMLEDCYGLSEETTTGVHHLYKSLRDGKLKVPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAIVAGFGDVGKGCAMALHGMGARVIVTEIDPINALQAAVSGYQVAPMDEVASIGQIFVTTTGCRDIITGKHFEQMPEDAIVCNIGHFDIEIDVAWLKANAESVVNIKPQVDRYLMKNGRHVILLADGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFNADNKEFREKFPEFAKTGPFDVGVHLLPKVLDETVARCHLDHLGAKLTTLTETQAEYLGIPEEGPYKADIYRY