wanglab/gogpt-training-data huggingface dataset:
Protein: Protein LTO1 homolog (Oral cancer-overexpressed protein 1) (Tumor-amplified and overexpressed sequence 1) (Q8WV07)
Organism: Homo sapiens (Human)
Function: The complex LTO1:YAE1 functions as a target specific adapter that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation. May play a role in the regulation of proline metabolism and ROS production.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P53846}.
Interaction partners:
- Protein YAE1 homolog
- ATP-binding cassette sub-family E member 1
- Fibroblast growth factor 19
- Fibroblast growth factor 3
- Fibroblast growth factor 4
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Liprin-alpha-1
- G1/S-specific cyclin-D1
Sequence:
MAGSQDIFDAIVMADERFHGEGYREGYEEGSSLGVMEGRQHGTLHGAKIGSEIGCYQGFAFAWKCLLHSCTTEKDSRKMKVLESLIGMIQKFPYDDPTYDKLHEDLDKIRGKFKQFCSLLNVQPDFKISAEGSGLSF
Protein: Spliceosome-associated protein 130 B (AtSAP130b) (SAP 130 B) (Pre-mRNA-splicing factor SF3b 130 kDa subunit B) (SF3b130 B) (P0DKL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (By similarity). Required for pollen and ovule development, especially during the transition from microspore to the bicellular stage in pollen development. Involved in the accumulation of QRT1 and QRT3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15393}.
Interaction partners:
- Nuclear protein-like
- Uncharacterized protein At3g23325
- At2g32600/T26B15.16
- Small nuclear ribonucleoprotein Sm D2
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- Splicing factor SF3a60 homolog
- Uncharacterized protein At4g14342
- Pliceosome associated protein-like protein
- Proline-rich spliceosome-associated
- Splicing factor 3B subunit 6-like protein
Sequence:
MYLYSLTLQQATGIVCAINGNFSGGKTQEIAVARGKILDLLRPDENGKIQTIHSVEVFGAIRSLAQFRLTGAQKDYIVVGSDSGRIVILEYNKEKNVFDKVHQETFGKSGCRRIVPGQYVAVDPKGRAVMIGACEKQKLVYVLNRDTTARLTISSPLEAHKSHTICYSLCGVDCGFDNPIFAAIELDYSEADQDPTGQAASEAQKHLTFYELDLGLNHVSRKWSNPVDNGANMLVTVPGGADGPSGVLVCAENFVIYMNQGHPDVRAVIPRRTDLPAERGVLVVSAAVHKQKTMFFFLIQTEYGDVFKVTLDHNGDHVSELKVKYFDTIPVASSICVLKLGFLFSASEFGNHGLYQFQAIGEEPDVESSSSNLMETEEGFQPVFFQPRRLKNLVRIDQVESLMPLMDMKVLNIFEEETPQIFSLCGRGPRSSLRILRPGLAITEMAVSQLPGQPSAVWTVKKNVSDEFDAYIVVSFTNATLVLSIGEQVEEVNDSGFLDTTPSLAVSLIGDDSLMQVHPNGIRHIREDGRINEWRTPGKRSIVKVGYNRLQVVIALSGGELIYFEADMTGQLMEVEKHEMSGDVACLDIAPVPEGRKRSRFLAVGSYDNTVRILSLDPDDCLQILSVQSVSSAPESLLFLEVQASIGGDDGADHPANLFLNSGLQNGVLFRTVVDMVTGQLSDSRSRFLGLKPPKLFSISVRGRSAMLCLSSRPWLGYIHRGHFHLTPLSYETLEFAAPFSSDQCAEGVVSVAGDALRIFMIDRLGETFNETVVPLRYTPRKFVLHPKRKLLVIIESDQGAFTAEEREAARKECFEAGGVGENGNGNADQMENGADDEDKEDPLSDEQYGYPKAESEKWVSCIRVLDPKTATTTCLLELQDNEAAYSVCTVNFHDKEYGTLLAVGTVKGMQFWPKKNLVAGFIHIYRFVEDGKSLELLHKTQVEGVPLALCQFQGRLLAGIGPVLRLYDLGKKRLLRKCENKLFPNTIISIQTYRDRIYVGDIQESFHYCKYRRDENQLYIFADDCVPRWLTASHHVDFDTMAGADKFGNVYFVRLPQDLSEEIEEDPTGGKIKWEQGKLNGAPNKVDEIVQFHVGDVVTCLQKASMIPGGSESIMYGTVMGSIGALHAFTSRDDVDFFSHLEMHMRQEYPPLCGRDHMAYRSAYFPVKDVIDGDLCEQFPTLPMDLQRKIADELDRTPAEILKKLEDARNKII
Protein: Calmodulin-3 (P0DP28)
Organism: Mus musculus (Mouse)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}.
Interaction partners:
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Actin-like protein 7A (Actin-like-7-alpha) (Testis-specific actin-2) (T-actin-2) (Q9QY84)
Organism: Mus musculus (Mouse)
Function: May play an important role in formation and fusion of Golgi-derived vesicles during acrosome biogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21278383}. Golgi apparatus {ECO:0000269|PubMed:21278383}. Cytoplasm {ECO:0000269|PubMed:12672658, ECO:0000269|PubMed:36734600}. Nucleus {ECO:0000269|PubMed:12672658, ECO:0000269|PubMed:21278383, ECO:0000269|PubMed:36734600}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:21278383}. Note=Detected at the Golgi apparatus during acrosome biogenesis (PubMed:21278383). Detected at the subacrosomal layer in round spermatids (PubMed:21278383). Detected in sperm head and tail (PubMed:21278383).
Interaction partners:
- Dynactin subunit 2
Sequence:
MSLDGVWAPQTANIGDGPAKKASDQASMQTQVLQTASLKDGPAKRAVWVRRDNAETEDPVKSTMSKDRPRLEVTKAVVVDLGTGFCKCGFAGLPKPTHKISTTVGKPYMETAKTGDNRKETFVGHELFNPDIHLKLVNPLRHGIIVDWDTVQDIWEYLFRQEMKIAPEEHAVLVSDPPLSPHTNREKYAEMLFETFNTPAMHIAYQSRLSMYSYGRTSGLVVEVGHGVSYVVPIYEGYPLPSITGRLDYAGSDLTTYLMNLMNNSGKHFSEDHLGIVEDIKTRCCFVALDPIEEKKIPAPEHEIHYTLPDGKEIRLGQERFLCSEMFFKPSLIKSMQLGLHTQTVSCLNKCDIALKRDLMGNILLCGGSTMLRGFPNRLQKELSSMCPNDTPQVNVLPERDTAVWTGGSILASLQGFQPLWVHRLEYEEHGPFFLYRRCF
Protein: Cyanide hydratase (CHT) (EC 4.2.1.66) (Cyanide-degrading nitrilase) (Formamide hydrolyase) (C8V9R7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants.
Interaction partners:
- Formamidase
Sequence:
MSPVLKKYKAAAVNAEPGWFDLEESVRRTIHWINEAGRNRCKLIAFPELWIPGYPYWMWKVNYQESLPLLKKYRENSLLSDSEEMRRIREAARANKIYVSLGYSEVDLASLYTTQVLISPAGNILNHRRKIRATHVERLVFGDGTGDTTESVVQTEIGRVGHLNCWENMNPFMKSYAASLGEQVHVAAWPLYPGKETLKYPDPYTNVAEANCDALANELPQLVTPAYAIETGTYTLAPWQTITEEGIKLNTPPGKPLEDPNIYNGHGRIFAPDGRNLVPHPAKDFQGLLYVDIDLDEIHLTKSLADFGGHYMRPDLIRLLVDGNRKDLVVSEDRINGGIKYTSTMDRVGLTKPLEAPKPTDQKE
Protein: L-lysine 4-hydroxylase (EC 1.14.11.-) (Alpha-ketoglutarate-dependent dioxygenase) (KDO2) (L-lysine hydroxylase) (C7PLM6)
Organism: Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM 2034)
Function: Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-lysine, leading to (4R)-4-hydroxy-L-lysine. Cannot use D-lysine or L-ornithine as substrate.
Interaction partners:
- Hypothetical protein
- PFAM: AMP-dependent synthetase and ligase
- KEGG: aha:AHA_4176 hypothetical protein.
- PFAM: Pyridoxal-dependent decarboxylase
- PFAM: IucA/IucC family protein
- KEGG: she:Shewmr4_1454 L-lysine 6-monooxygenase.
- PFAM: IucA/IucC family protein
- KEGG: sde:Sde_0569 hypothetical protein.
- Hypothetical protein
Sequence:
MRPLDVTPTISPGAQDLPRTMHFAAEPPLQPLIIDITEEEKLEITYIGKKLKRKYKSYDDPGFISMLHLNAYTLLPERIAKVLSNFGTDFSDQQYGAVVLRGLIEIGQDELGPTPRSWQETDHEKIMEYGFISSLLHGAVPSKPVEYFAQRKGGGLMHAIIPDENMSFTQTGSGSRTDLFVHTEDAFLHNAADFLSFLFLRNEERVPSTLYSIRSHGRPDAILQELFKPIYKCPKDANYASEEALGDDIRTSVLYGSRSAPFMRFDAAEQIYNEDANQDPEALHNLKRFWEEARKLIYNDFVPESGDLIFVNNHLCAHGRNAFLAGFREENGQLVKCERRLMLRMMSKTSLINIREVTHPENPYLIMEEHYGKVYSAHLANL
Protein: proline dehydrogenase (EC 1.5.5.2) (O50444)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- L-glutamate gamma-semialdehyde dehydrogenase
- Pyrroline-5-carboxylate reductase
- Conserved protein
- prolyl aminopeptidase
Sequence:
MAGWFAHTLRPAMLAAGRSDRLGRIVERSPLTRGVVRRFVPGDTLDDVVDIVTALRDSGRYLSIDYLGENVTDADDAAAAVRAYLGLLDVLGRRGDIACDGVRPLEVSLKLSALGQALDRDGQKIALDNARAICERAERVGAWVTVDAEDHTTTDSTLSISGDLRVDFPWLGTVVQAYLRRTLADCAELAAVGARVRLCKGAYDEPASVAYRDAAQVTDSYLRCLRVLTAGRGYPMVATHDPVIIAAVPGITRESGRSQGDFEYQMLYGVRDDEQRRLTGAGNHVRVYVPFGTRWYGYFLRRLAERPANLAFFLRALTDRRRARGCAER
Protein: Syntaxin-17 (Q9D0I4)
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. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:27628032}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z158}. Mitochondrion membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into membranes. Localizes to the completed autophagosome membrane upon cell starvation (By similarity). {ECO:0000250|UniProtKB:P56962}.
Interaction partners:
- Beclin 1-associated autophagy-related key regulator
- Vesicle-associated membrane protein 8
- Synaptosomal-associated protein 29
- Vesicle-associated membrane protein 7
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Synaptobrevin homolog YKT6
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 18 homolog
Sequence:
MSEDEEKVKLRRLEPAIQKFTKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREMEKLCLKVHKDDLVLLKRMIDPVKEAAATATAEFLQLHLESVEELKKQVNDEELLQPSLTRSTTVDGVLHTGEAEAASQSLTQIYALPEIPQDQNAAESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYKLAALPVAGALIGGVVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRRKQKMMEKLTSSCPDLPSQSDKKRS
Protein: Nucleoprotein (Protein N) (Nucleocapsid protein) (Q9IK92)
Organism: Nipah virus
Function: Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity).
Subcellular location: Virion. Host cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSDIFEEAASFRSYQSKLGRDGRASAATATLTTKIRIFVPATNSPELRWELTLFALDVIRSPSAAESMKVGAAFTLISMYSERPGALIRSLLNDPDIEAVIIDVGSMVNGIPVMERRGDKAQEEMEGLMRILKTARDSSKGKTPFVDSRAYGLRITDMSTLVSAVITIEAQIWILIAKAVTAPDTAEESETRRWAKYVQQKRVNPFFALTQQWLTEMRNLLSQSLSVRKFMVEILIEVKKGGSAKGRAVEIISDIGNYVEETGMAGFFATIRFGLETRYPALALNEFQSDLNTIKSLMLLYREIGPRAPYMVLLEESIQTKFAPGGYPLLWSFAMGVATTIDRSMGALNINRGYLEPMYFRLGQKSARHHAGGIDQNMANRLGLSSDQVAELAAAVQETSAGRQESNVQAREAKFAAGGVLIGGSDQDIDEGEEPIEQSGRQSVTFKREMSISSLANSVPSSSVSTSGGTRLTNSLLNLRSRLAAKAAKEAASSNATDDPAISNRTQGESEKKNNQDLKPAQNDLDFVRADV
Protein: Stretchin-MLCK (Q9NBB3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VLDDRVVQIEHLDGICELIINKPTINDNGIYVCTAKNKLGSQSTTHTVVVDTTHTSRRSSILSAIAMQEGGGGGESADAKAKGKKKKKEDEPEGGDGGYERRSRMPDPSPKQMLYFTVNLSNRYVAEGSKVKLQAVIGGPQPMIKWLKDDQNVTYGPNIRNMNRDSLAVLEFTNAKVEDSGTYSIVAQNESCKITTSAMLHVYETKVNTDVQPVFIRSLKETYHLNTNELILETAVRGQPTPAVQWFKDSIEIQSGGRFQIIEHQDGTCELIIDRPDNKDSGKYVVKAESRAGKMEISHYVLFEGQSHHIAENIHGVFHADKSLLRPKEVEKPVEKKPAPAPEPEWQA
Protein: Combgap, isoform C (A1Z9M4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYLLSTDGSLAVQKDVKGLTAGGKNNVVRRMFVVNDPSFPPGTQRVITAGGASTVVKKQDNNQQVLSLDKNCDILPGISVQVQKVIQGLEDNEDSQGEAPNLKLEPGTLELSPKTELQESMHFSETDATIKKERPYSCDECGKSFLLKHHLTTHARVHTGERPHICTHCGKSFAHKHCLNTHLLLHSTERPYQCQECKKSFTLKHHLLTHSRVHSRERPFVCQECGRAFPLKRHLVTHSKFHAGERPYVCEECGESFAQENHLIMHSRFHGSLNPFVCAECGASFPRKFQLVNHGRIHGKIPHSCTVCGKEFLQKRTLVSHMRRVHTGEQAHPCVSCGEGFLTKAELHQHVRTAHNGVNPNTSSATIIANQQLQQAHHHQAGQQTHPQTITVVSNPGNSTLLTVSTTDANGVARPQFVCRECGSAFNSREALALHLRLHTGDKSLMTDLCALTAALPGHFLSTASLNPGTVVTANPNLVGQSPVPVQIISSTGQVMSQTTLVQAANSTHPQAVVTAVPTMPVHGQQQHLQHVAQQQQQQQQQQQQQQQHVVSVAPANKPKSHFCASCGKGFAAKHGLMQHNRRHPNGGCTVRTHVCECGKAFFQKNHLMLHQRQHLETKPAISQQQVC
Protein: Fbxl18 protein (Q14BU8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSEEEAAAEAAGDTHLLGFSDEILLHILSHVPSTDLVLSVRRTCRKLAALCLDKSLVHTVLLQKDHQASEEKVKQLVKEIGREIQQLNMAGCYWLSGSTIEHVARCHSLVKVNLSGCHLTSLRLSKVLSALQHLRSLAIDVSPGFDASQLSSECKATLSRVQELKQTLFTPSYGVVPCCASLQKLLLYFEILDRTREGAVLSGQLMVGQSNVPHYQNLRVFYARLAPGYINQEVVRLYLAVLSDRTPENLHAFLISVPGSFAESGATKNLLDSMARNVALDALQLPKSWLNGSTLLQHMKFNNPFYFSFSRCTLSGGHLIQRLINGGKDLRSLASLNLSGCVHCLSADSLLRKAEDDID
Protein: Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2) (P18589)
Organism: Rattus norvegicus (Rat)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against vesicular stomatitis virus (VSV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2173790}.
Interaction partners:
Sequence:
MVLSTEENRSVDLVNLPSVPLPDGEAGVGENNKDSLNNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEVELSDPSEVEEAINTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVDIATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALLEDGKATVPCLAERLTMELISHICKSLPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFFLWSEEIERNFQKGSDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTVSEKNFSEFFNLHRTTKSKLEDIRLEQETEAEKSIRLHFQMEQIIYCQDQIYRKALQKVREEEAEEEERKHGKSRSSQSKNLQTSSMDEIFQHLNAYRQEAHNRISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEHSDTSEKRRFLKERLARLAQAQRRLAKFPG
Protein: Protein sds23/moc1 (Multicopy suppressor of overexpressed cyr1 protein 1) (Phosphoprotein at stationary phase 1 protein) (Q09826)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for normal DNA replication and for proper mitosis. Induces sexual development and ascus formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9242669}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9242669}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta
- 5'-AMP-activated protein kinase subunit gamma
- SNF1-like protein kinase ssp2
- Multifunctional tryptophan biosynthesis protein
- Transcriptional regulatory protein moc3
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
Sequence:
MPLSTQSSDSLSSAGRQSFGVNSVSDFLAQFPIPTNLPSNKWQDIPVTFLHDNEIALIDPETSMEEASSILIDRDLSALPIVAAKGSNEIATTFDYADLNSFLLMVVGFDDFNDGRFKKVAEDIRAGKVITAYEVAKLGKNKDDFITIPHTTSLGRLAEILSSGIRRVAVTNEQGELSFMASQRSIIRFLWNNIRAFPDLEPLMSRTIHSLDIGSTDITCISGDQKVAAALRQMNQTGIGSLAVVDAQFRLLGNISLVDVKYVTRSSSVYLLNKSCAHFLSVIKSEQGIRAGKDSAPAFNIYESSTFAFTLAKLVATQCHRLWLVQSPSCPPSPKNNAHLSPGSMGGVKVNQLLGVVSLTDIISVLYAHMKGTLPPAPHSAPSLRHGRRGSTSSHRSHSKASVDTQRR
Protein: Sin3A, isoform G (A0A0B4K765)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
- FI07430p
- Histone deacetylase HDAC1
- PHD finger protein 12
- BRMS1 transcriptional repressor
- Protein deacetylase HDAC6
- Inhibitor of growth protein
- Protein MBD-R2
- Chromatin assembly factor 1 p55 subunit
- Histone deacetylase complex subunit SAP30 homolog
- Lysine-specific demethylase 5
Sequence:
MMKRTRVDEVQFGTRPVPQTSGGVGVGVVGVTGGGPTSGGGGTATVGVNTTGVTIGTVVPSAHNATISGIGSIHHRILTPQHGGAQTIAYLPSTTPTATNLKTTTSIVDSTTAGGPVGAGAQVAVGVGSAAGGGGVVVSTGSTGTQTLQYTTSYSVASIQAGGTLKANTADGANTVQIHVTGGGAANNPASAQTVSSSSQTGTIRQRTISGTQTVATAVGNLATISQQQPVQQSPLGKAQTPPSSVVANSIPVGGTTPPQGQSGNATPRLKVEDALSYLDQVKYQYADQPQIYNNFLDIMKEFKSHCIDTPGVIERVSTLFKGHTELIYGFNMFLPPGYKIEIHSDALGCSVPVVSMPSPPGAPTSTGTVHMLTGNSSMSGAGHIAIKTTNAATLTPAAGAGAAAAAAAVAQIQSAGAVNLMTHGGASLTQTTIHALQQATPPQSQSPGGGHVHVSVTNSTAANAVVPGQPGISVSAHNVPQNYSRDRERATITPTGQVAGAAANVNASASIVVGGPPTPNSLSELSPHGGAGGGPGAGAAQHNLHHIQQAHQSILLGETGQQNQPVEFNHAITYVNKIKNRFQNQPAKYKKFLEILHDYQREQKVMKEGSLNQGKMLTEQEVYTQVAKLFGQDEDLLREFGQFLPDATNHQSGQYMSKSASVHNDHGKRPTATLSGGAHITMSSASPAPSGSPLHLGATTLPQIDKSAHAAAIGNLSAVNTSVSIKTYNNNQQQQNHVIGSGLNATRNDILFEKDYHAGLQQQAHQRGAGVGGHHHLAGTAAGANIGRPGVGASVMVSYDKEHRNNHHVQKYVGHAPNQNLTHGHNAKKSPSYGIPSVIGSMPHISDNSLDRSSPGISYATPPLPSGPHGQHNSGSATRRPGDDSLVGHYASGAPPAKRPKPYCRDVSFSEASSKCTISDAAFFDKVRKALRSPEVYDNFLRCLTLFNQEIVSKTELLGLVSPFLMKFPDLLRWFTDFLGPPSGQPAGGLIDGMPLAATQRQGGGSSNSSHDRGTSHQSAAEYVQDVDLSSCKRLGASYCALPQSTVPKKCSGRTALCREVLNDKWVSFPTWASEDSTFVTSRKTQFEETIYRNIHRTEDERFELDLVIEVNSATIRVLENLQKKMSRMSTEELSKFHLDDHLGGTSQTIHQRAIHRIYGDKSGEIITGMKKNPFVAVPIVLKRLKVKEEEWREAQKTFNKQWREQNEKYYLKSLDHQAINFKPNDMKALRSKSLFNEIETLYDERHDQEDDAMEPFGPHLVLPYKDKTILDDAANLLIHHVKRQTGIQKQEKQKIKQIIRQFVPDLFFAPRQPLSDDERDDAFPFLVDDNTKMDVDSPLGRTESSTRNAKSTPSESASPARSNASTSSVTPAGIKKETDDSKATTGSFAPASSATASSATPVDDATPSTSSAAAAASAASSSTVSGTEGKPKDDPLSSHKEEGAGSTSSGVATSPRQAQDTAGAGVDVEIKLEHPADFSNPKLLPPHAHGQREDESYTLFFANNNWYLFLRLHAILCDRLHVMYERARLLAIEEERCRVNRRESTATALRLKPKPEIQVEDYYPTFLDMLKNVLDGNMDSNTFEDTMREMFGIYAYISFTLDKVVSNAVRQLQYCVTERAALDCVELFATEQRRGCTGGFCRDAHKTFDREMSYQRKAESILNEENCFKVYIYKIDCRVTIELLDSEPEEVDKPAALKAQKFSKYVERLANPALGGGGNTGRSDSALGNDSVVDGSDIKTEADEDTAELRYREGGIGGAGKARFLVRNKRRSKLLEEQVRQLFEHRRNRIEQHGTAASLEPISVDSAISSNSTTGGGGSGTNNNNNNNNNNNSWGGKRLERLGAPQVGLAEQYAFNDRDEISTNISNGRCFVTSKNLKLLKYDAVRRAKKSHCRVTQAKYAHFQTYVNKWLQQHVSEQQQQNCVDWLLGKTADQINASGWGSASKTKTVQQKDTSKTPYRIYNRYRVVQSAVSGGLMSATAPTPDGSVPAVNSAPSGSVSTVNNVQGSAAVSSTSHSMCNSSILSADSTTNTNASAQQQQHCNSAAAATTPNAEALQQVRPMES
Protein: Beta-glucosidase 24 (AtBGLU24) (EC 3.2.1.21) (Q9LKR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Glycosyl hydrolase family protein
- Beta-D-glucan exohydrolase-like protein
- At3g47000
- Beta-D-glucan exohydrolase-like protein
- beta-glucosidase
- Glycosyl hydrolase family protein
- Glycosyl hydrolase family protein
- SKU5 similar 3
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Alpha-L-fucosidase 1
Sequence:
MVLQKLPLMSIGLLWLLIIVGPLVNADGPVCPPKPSDKLSRAHFPKGFLFGTATAAYQVEGAVNETCRGPSVWDIYCKKYPEKCNGDNGTQAVDFFYRYKEDIQLMKNLNTDSFRLSISWTRIFPHGREENGVSKSGVQFYHDLIDELKRNGIIPFVTVFHWDTPQTLENEYGGFLSAHIVKDFREYAEFVFKEYGGKVKHWITFNEPWVFAHAGYDVGKKAPGRCSPYAKDETVKGDCLGGRSGYEAYLVSHNLLNAHAEAVEAFRQCEKCKGGKIGIAHSPAWFEPHDFKDEQSGATIDRALDFIMGWHLDTTMFGDYPQTMKDIVGHRLPKFTTEQIAKLKNSADFVGINYYTSTFSKHLEKPNHAEPKFKQDSLVEWKNKNVNNITIGSKPETGPLPVYSTGFRKVLKYVKDKYANPEIIIMENGYGENLKENDSVENGTADYNRESYLKKHLWSMHKAICEDKVNVTGYFVWSLMDNFEWQDGFKNRFGLYYIDYKNNLTRHEKVSGKYYREFLSEGVRPSAIKKDEL
Protein: Hydroxycinnamoyl-CoA:piscidic acid hydroxycinnamoyltransferase (EC 2.3.1.-) (ArHCT1) (ArHPT1) (BAHD acyltransferase/hydroxycinnamoyltransferase) (BAHD-type hydroxycinnamoyltransferase) (Cimicifugic acid synthase) (D4NUX0)
Organism: Actaea racemosa (Black cohosh) (Cimicifuga racemosa)
Function: Catalyzes the formation of cimicifugic acids. Uses hydroxycinnamoyl-CoA thioesters as hydroxycinnamoyl donor substrates. Has a strict specificity for piscidic acid as an acceptor substrate as none of the various other acceptors tested including 4-hydroxyphenyllactic acid, malate, spermidine or tetrahydroxyhexanedioic acid are substrates. Donor substrates include 4-coumaroyl-CoA, caffeoyl-CoA, sinapoyl-CoA and feruloyl-CoA. No activity with cinnamoyl-CoA, isoferuloyl-CoA, 3,4-dimethoxycinnamoyl-CoA or 3,4-dihydroxybenzoyl-CoA as donors. In the reverse reaction with fukinolic acid and CoA as substrates, a formation of fukiic acid is evident. Hence, fukiic acid may also serve as an acceptor substrate. Involved in the biosynthesis of cimicifugic and possibly fukinolic acids.
Interaction partners:
Sequence:
MVCIKSSCVVKPSEPTPNVKLFLPESDQVKPWTHAPVFFVYQPEVDNSVSTSLENLKFSLSRALVPYYPLAGRLNGIGGGRFELHCNTMGAVIIEAESDARLEDFGDFRPTSETTKLAPYVDYAKDVSELPLLLVQLTRFKCGGIGIGIAMSHIVSDGKGAFGFITTWAKINRGEKGIIEPFHDRTAFYKGDPTAKPRCDHVELKGYPVLLGNKSAKEERAKETTTRMLNLSKNQVDKLKEKSNLGKPKDYVGREYSRFEAMSGHIWRCASKARRHENEQLTSLRITIDCRNRLRPPLPPRYSGNATMVTTSIAESGELLSNPLGLGFVCSVIRKCIDKVDDDYIKSATDFLISQDDLTPYRSGFHNVGSTEGVFLGNPNLAITSWVGLPINDVDFGWGKPIYMGPTALGYDGKLLIIPGKDDGSVIVPIRLQVAHIDDFEKFFYEDI
Protein: Ras-related protein Rab-17 (EC 3.6.5.2) (Q9H0T7)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post-endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development (By similarity). May also play a role in cell migration.
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:P35292}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P35292}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35292}. Note=May also localize at the basolateral and apical plasma membrane. In neurons, localizes to the cell body and dendritic shaft and spine. {ECO:0000250|UniProtKB:P35292}.
Interaction partners:
- Rab proteins geranylgeranyltransferase component A 1
- Rab proteins geranylgeranyltransferase component A 2
Sequence:
MAQAHRTPQPRAAPSQPRVFKLVLLGSGSVGKSSLALRYVKNDFKSILPTVGCAFFTKVVDVGATSLKLEIWDTAGQEKYHSVCHLYFRGANAALLVYDITRKDSFLKAQQWLKDLEEELHPGEVLVMLVGNKTDLSQEREVTFQEGKEFADSQKLLFMETSAKLNHQVSEVFNTVAQELLQRSDEEGQALRGDAAVALNKGPARQAKCCAH
Protein: Pygopus homolog 2 (Drosophila) (Pygopus homolog 2 isoform 1) (Q1L8T6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- B-cell CLL/lymphoma 9 protein isoform X1
- Lymphoid enhancer-binding factor 1
- Catenin beta-1
- HCLS1-associated protein X-1
- Aquaporin-10b
Sequence:
MAGQQQQGKRGKGSQMKSPEKKKRKSNSQGAAFSHLSEFAPPPTPMVDHLVASNPFDDDFGPPSRSAGGGGPGGATFLPSPGAGGGGYGGPGRMGGGMGFMGGPGGPGSGQPGRRPPFGPPTPNTGPHHPLGFGGMPGFGGGGGGGGGGGGGFPPGGPSQFNMPPNFSPPMHPGQGFNPMLSPGAMGGGPGGGGGPPHPRFGMPQQQPPHGQGGHPFNSPPLPGGPGPRGPPHGPMNPMGGMGGGMNMMGMGGGGGGGNMVGGHPGMPPQGQFPPPQDGPYPGSSPPVGEEGKNFGGPGGGPPVPSQQQPPNLNPSGPPSNNATPGPSPAPGHPQPGGGFPQDVPQPNPNTPGQPQSVPQPPNPNSSPTGPLNGPQPQAPNNQHPPPNSTGGPGPNTPSNQQQPTPPNSAPGSTPYSQQNNTPGGPMPNQPPNSNQNNLNNNSSGSNTPGSNPNPPSNSNSTPNTQSPLPSGPAPPSSGPGSGPPKLGGGMVFPCGLCMSEVHDDQEAILCEASCQRWFHRDCTGLTEPAYGLLTRESAAVWACDFCLKTKEIQAVYVRQGLGQLVAANDG