wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear factor of activated T-cells 5 (NF-AT5) (T-cell transcription factor NFAT5) (D3ZGB1)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes. Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3'. Mediates the transcriptional response to hypertonicity. Positively regulates the transcription of LCN2 and S100A4 genes; optimal transactivation of these genes requires the presence of DDX5/DDX17. Also involved in the DNA damage response by preventing formation of R-loops; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23233732}. Cytoplasm {ECO:0000269|PubMed:23233732}. Chromosome {ECO:0000250|UniProtKB:O94916}. Note=Nuclear distribution increases under hypertonic conditions (By similarity). Recruited to sites of R-loop-associated DNA damage following poly-ADP-ribosylation by PARP1 (By similarity). {ECO:0000250|UniProtKB:O94916, ECO:0000250|UniProtKB:Q9WV30}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Transcription factor GATA-4
- Signal transducer and activator of transcription 3
- Forkhead box P3
- Transcription factor Jun
- Calmodulin-like protein 3
- Calmodulin-1
- Stromal interaction molecule 1
- Calmodulin-like protein 4
- GATA-binding protein 3.
Sequence:
MPSDFISLLSADLDLESPKSLYSRDSLKLHPSQNFHRAGLLEESVYDLLPKELQLPPPRETSAASMSQTSGGEAGSPPPAVVAADASSAPSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTGNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLDSQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKEVDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCTQPAGVPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVGIYVVTNAGRSHDVQPFTYTPDPAAGALSVNVKKEISSPARPCSFEEALKAMKTTGCNVDKVTILPNALITPLISSSMIKTEDVTPMEVTSEKRSSPIFQTTKTVGSTQQTLETISNIAGNASFSSPSSSHLSPENENQQQLQPKAYNPETLTTIQTQDISQPGTFPAVSASSQLPSSDALLQQAAQFQTRDAQSRDTMQSDSVVNLSQLTEAPQQQQSPLQEQAQIPSNIFPSPNSVSQLQSTIQQLQAGSFTGSTASGSNGSVDLVQQVLEAQQQLSSVLFSTPDGNENVQEQLNADIFQVSQIQNSVSPGMFSSTESAVHTRPDNLLPGRADSVHQQTENTLSSQQQQQQQQQQQQQQQVIESSAAMVMEMQQSICQAAAQIQSELFPSAASANGSLQQSPVYQQPSHMMSALPTSEDMQMQCELFSSPPAVSGNETSTTTTPQVATPGSTMFQPPNSGDGEETGAQAKQIQSSVFQTMVQMQHSGDSQPQVNLFSSTKNIMSVQSNGTQQQGNSLFQQGSEMLSLQSGSFLQQSSHSQAQLFHPQNPIADAQSLSQETQGPMFHSANPIVHSQTSTASSEQLQPSMFHSQSTIAVLQGSSVPQDQQSPNIYLSQSSISNLQTNTVAQEEQISFFSAQNSISPLQSTSNTEQQAAFQQQPPISHIQTPLLSQEQAQPSQQGLFQPQVALGSLPANPMPQNQQGPIFQTQRPIVGMQSNSPSQEQQQQQQQQQQQQQQQQQQSILFSNQNAMATMASQKQPPPNMIFSPNQNPMASQEQQNQSIFHQQSNMAPMNQEQQPMQFQNQPTVSSLQNPGPTPSESPQTSLFHSSPQIQLVQGSPSSQEQQVTLFLSPASMSALQTSINQPDMQQSPLYSPQNNIPGIQGSTSSPQPQAALFHNTTGGTINQLQNSPGSSQQTSGMFLFGIQNNCSQLLTSGPATLPEQLMAINQPGQPQNEGQSSVTTLLSQQMPESAPLASSVNNSQNMEKIDLLVSLQSQGNNLTGSF
Protein: Arylsulfatase B (ASB) (EC 3.1.6.12) (N-acetylgalactosamine-4-sulfatase) (G4S) (P50429)
Organism: Mus musculus (Mouse)
Function: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (By similarity). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:19536613}. Cell surface {ECO:0000269|PubMed:19536613}.
Interaction partners:
- Alpha-L-iduronidase
- Arylsulfatase A
- Arylsulfatase G
- Hyaluronidase-1
- Hyaluronidase-2
- Hyaluronidase
- Hyaluronidase-4
- Hyaluronidase PH-20
- Hyaluronidase-5
- Hyaluronidase-3
Sequence:
MGKLSPCTGRSRPGGPGPQLPLLLLLLQLLLLLLSPARASGATQPPHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSCVPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGTRCALDLRDGEEPAKEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYGFIQDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNIDQDFFDGLPCPGKNMTPAKDDSFPLEHSAFNTSIHAGIRYKNWKLLTGHPGCGYWFPPPSQSNVSEIPPVGPPTKTLWLFDINQDPEERHDVSREHPHIVQNLLSRLQYYHEHSVPSHFPPLDPRCDPKSTGVWSPWM
Protein: S-adenosylmethionine permease SAM3 (S-adenosylmethionine metabolism protein 3) (Q08986)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity S-adenosylmethionine permease, required for utilization of S-adenosylmethionine as a sulfur source.
Subcellular location: Membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Homocysteine S-methyltransferase 2
- Urea active transporter
- S-adenosylmethionine synthase 1
- S-adenosylmethionine synthase 2
Sequence:
MDILKRGNESDKFTKIETESTTIPNDSDRSGSLIRRMKDSFKQSNLHVIPEDLENSEQTEQEKIQWKLASQPYQKVLSQRHLTMIAIGGTLGTGLFIGLGYSLASGPAALLIGFLLVGTSMFCVVQSAAELSCQFPVSGSYATHVSRFIDESVGFTVATNYALAWLISFPSELIGCALTISYWNQTVNPAVWVAIFYVFIMVLNLFGVRGFAETEFALSIIKVIAIFIFIIIGIVLIAGGGPNSTGYIGAKYWHDPGAFAKPVFKNLCNTFVSAAFSFGGSELVLLTSTESKNISAISRAAKGTFWRIAIFYITTVVIIGCLVPYNDPRLLSGSNSEDVSASPFVIALSNTGSMGAKVSNFMNVVILVAVVSVCNSCVYASSRLIQALGASGQLPSVCSYMDRKGRPLVGIGISGAFGLLGFLVASKKEDEVFTWLFALCSISSFFTWFCICMSQIRFRMALKAQGRSNDEIAYKSILGVYGGILGCVLNALLIAGEIYVSAAPVGSPSSAEAFFEYCLSIPIMIVVYFAHRFYRRDWKHFYIKRSEIDLDTGCSVENLELFKAQKEAEEQLIASKPFYYKIYRFWC
Protein: GH08757p (Julius seizure, isoform C) (Q32KC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRLDGALEPRPRQGAATIKGRQPLRRETREPCETQQQQPADEDDEATDAECLTTNSSSSSSSTSSTSSNNCQANLVCNPKRTTSATPTPRKTTGGRGNTRHTILMAPNVGHQRKSLGLRLPMKQGRSRRRMMGAEWGWERLNGLLLCLISVIALLPPLTLGDDGDNFFAVNAFSAGPETTTPEFDYASRGQKKFGDKCDNTLECGFPGSICDPKKKSCQCTEDLPVTNHYDKCGKEAAVNESCFFNEQCEMRYFQTECRDGRCICRFEMSPIWGKDGSVECKGRQDKRGPETYIDPAMIGVLVGMALMFVIICVVLRLFSQARWRENRTIFNTPNPRLMNVSLLRDSKLLHGQERRGSRMSVRAPSRQPSMASLRPHSPNPSLGKTGRMIRSKSNTRSSDSRVSDVSTCSRLLEHPSAASQHNLVHSHFLPYVPTTTASTATATNAIATYAASATPSPTPTPPPSAGHQLPMGHANATSTTSTANTTTTTTTYVSPAGIAPACGRTNKF
Protein: Serpentine Receptor, class BC (Class B-like) (O61938)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptor daf-37
- Serpentine receptor class gamma
- Serpentine receptor class gamma
- G-protein coupled receptor daf-38
- Guanine nucleotide-binding protein alpha-3 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
- Serpentine receptor class r-10
Sequence:
MSAITITCNSLSILFPIITCSINCYLIYSIFYSKRITWKSEFSLIYTRFAIDIVYTFFVPHNKIYYVLRQISDIFVMKNLTFYLVWPTIPLGAIRATLVLLITLDRVVASFFPIFYHNHRRRIPILAVISCVITFGLSDHIVLFEYCKYTVDVPLACDNFNCVINQCFFNYWSLRDQVQYFIIGVLSVLLCFRLFIWNNYVAIHANQVLSRATRIALLDSVIIFSFSIIPSFIFELLPTLSFASVGPWTIVFKHAGFMIESLIVCRLLFSEKVGRLVRRSTVITTY
Protein: Lipopolysaccharide export system protein LptC (P0ADV9)
Organism: Escherichia coli (strain K12)
Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015}.
Interaction partners:
- Lipopolysaccharide export system permease protein LptG
- Lipopolysaccharide export system protein LptA
- Lipopolysaccharide export system ATP-binding protein LptB
- Lipopolysaccharide export system permease protein LptF
- LPS-assembly protein LptD
- LPS-assembly lipoprotein LptE
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
- Inner membrane protein YrbG
- Arabinose 5-phosphate isomerase KdsD
- Intermembrane phospholipid transport system binding protein MlaC
Sequence:
MSKARRWVIIVLSLAVLVMIGINMAEKDDTAQVVVNNNDPTYKSEHTDTLVYNPEGALSYRLIAQHVEYYSDQAVSWFTQPVLTTFDKDKIPTWSVKADKAKLTNDRMLYLYGHVEVNALVPDSQLRRITTDNAQINLVTQDVTSEDLVTLYGTTFNSSGLKMRGNLRSKNAELIEKVRTSYEIQNKQTQP
Protein: NF-kappa-B inhibitor-like protein 1 (Inhibitor of kappa B-like protein) (I-kappa-B-like protein) (IkappaBL) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 1) (O88995)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with CACTIN in the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSNPSPQAPEEEASTSVCRPQSCSMASASRRHRRERRFRRYLSAGRLVRAQALLQRHPGLDVDAGQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGPDAYTDFFLPLLSRCPSAMGIKNKDGETPGQILGWGPPWDSAEEEEDEEVSKEREWRQKLQGELEDEWQEVIGRFEDDASRDTQEPESFSAWSERLAREHAQKQRQQLEAEGSCRPPRAEGSSHSWRQHEEEQRLFRERARAKEKELCESRARRAQEAQRDKGPEPPRAGPRAEHPRGAERGSLWRFGDVPWPCPGGGDPEAMAAALVARGPPLEEQGALKRYLRVQQVRWHPDRFLQRFRSQIETWELGRVMGAVTALSQALNRHAEALK
Protein: BCL2 associated transcription factor 1 (E9PKI6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRSNSRSHSSRSKSRSQSSSRSRSRSHSRKKRYSSRSRSRTYSRSRSRDRMYSRDYRRDYRNNRGMRRPYGYRGRGRGYYQGGGGRYHRGGYRPVWNRRHSRSPRRGRSRSRSPKRRSVSSQRSRSRSRRSYRSSRSPRSSSSRSSSPYSKSPVSKRRGSQEKQTKKAEGEPQEESPLKSKSQEEPKDTFEHDPSESIDEFNKSSATSGDIWPGLSAYDNSPRSPHSPSPIATPPSQSSSCSDAPMLSTVHSAKNTPSQHSHSIQHSPERSGSGSVGNGSSRYSPSQNSPIHHIPSRRSPAKTIAPQNAPRDESRGRSSFYPDGGDQETAKTGKFLKRFTDEESRVFLLDRGNTRDKEASKEKGSEKGRAEGEWEDQEALDYFSDKESGKQKFNDSEGDDTEETEDYRQFRKSVLADQGKSFATASHRNTEEEGLKYKSKVSLKGNRESDGFREEKNYKLKETGYVVERPSTTKDKHKEEDKNSERITVKKETQSPEQVKSEKLKDLFDYSPPLHKNLDAREKSTFREESPLRIKMIASDSHRPEVKLKMAPVPLDDSNRPASLTKDRLLASTLVHSVKKEQEFRSIFDHIKLPQASKSTSESFIQHIVSLVHHVKEQYFKSAAMTLNERFTSYQKATEEHSTRQKSPEIHRRIDISPSTLRKHTRLAGEERVFKEENQKGDKKLRCDSADLRHDIDRRRKERSKERGDSKGSRESSGSRKQEKTPKDYKEYKSYKDDSKNVFVFYTAYGG
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVH8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MRSIVLVSLLAFTQAYLKLDFEKTPKISDELTKRADNDSFIAPLLNGGELYTVQIAVGTPPQNLTVQLDTGSSDLWFVSASNPYCKNNKKFAPKKQDLMPITSDDGFPTSPNQVPKALRNINCNKYGFFNASGSSTYSRNDTNFSLSYGDETFASGPWGTDTISLNGVKVENVTFGLASFSNSTNPVFGIGLPGDESTYAMFSEDTNGTTNTQYSNFPLQLKQQGKIDKVAYSIYLNSTKSKQGSILFGAVDHSKYSGPLYTLPIVNRFGHLVENPYELEVTLSGLGLQRATSNITLFDQLLPALLDTGTTYTYMPSSVAQYLANQTNGVIDKKTSLIKLAKCPSKKSNDTIVFNFSGAQIKIKMVDFVEKHKGKCYLPCVSQESSFFLLGDSFMRHVYTVFDLDDKEISIAQANFNSTKEDIEEISSTVPSAVKAPQYYSSYVDFPTEISVTGDIFAPQATEFVPKPNNTNNKTNFTQDLLDIENMLLRRHYENRATTLSTSLPIFLIALSAVTALFL
Protein: Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 2) (DPRP-2) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9) (Q86TI2)
Organism: Homo sapiens (Human)
Function: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8. Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation. The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition.
Subcellular location: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:24562348}.
Interaction partners:
- Caspase recruitment domain-containing protein 8
- NACHT, LRR and PYD domains-containing protein 1
- Prolyl endopeptidase
- Dipeptidyl peptidase 2
- Transcription factor Dp family member 3
Sequence:
MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFKCPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVRLTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL
Protein: Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Legumaturain) (P13284)
Organism: Homo sapiens (Human)
Function: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:3136170}. Lysosome {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:3136170}.
Interaction partners:
- Glycophorin-C
- WD repeat-containing protein 90
- HLA class II histocompatibility antigen, DM alpha chain
Sequence:
MTLSPLLLFLPPLLLLLDVPTAAVQASPLQALDFFGNGPPVNYKTGNLYLRGPLKKSNAPLVNVTLYYEALCGGCRAFLIRELFPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACVLDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDRGMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGKKPDVCPSSTSSLRSVCFK
Protein: YTH domain-containing family protein 1 (DF1) (Dermatomyositis associated with cancer putative autoantigen 1) (DACA-1) (Q9BYJ9)
Organism: Homo sapiens (Human)
Function: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) shares m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs (By similarity). Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts (By similarity). Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells (By similarity). In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation (By similarity). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation. The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32492408}. Cytoplasm, P-body {ECO:0000269|PubMed:32492408}. Cytoplasm, Stress granule {ECO:0000269|PubMed:32451507}.
Interaction partners:
- Elongation factor 2
- N
- YTH domain-containing family protein 3
- RNA demethylase ALKBH5
- N
- Insulin-like growth factor 2 mRNA-binding protein 1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Pre-mRNA-splicing regulator WTAP
- Eukaryotic translation initiation factor 3 subunit B
- Heterogeneous nuclear ribonucleoproteins A2/B1
Sequence:
MSATSVDTQRTKGQDNKVQNGSLHQKDTVHDNDFEPYLTGQSNQSNSYPSMSDPYLSSYYPPSIGFPYSLNEAPWSTAGDPPIPYLTTYGQLSNGDHHFMHDAVFGQPGGLGNNIYQHRFNFFPENPAFSAWGTSGSQGQQTQSSAYGSSYTYPPSSLGGTVVDGQPGFHSDTLSKAPGMNSLEQGMVGLKIGDVSSSAVKTVGSVVSSVALTGVLSGNGGTNVNMPVSKPTSWAAIASKPAKPQPKMKTKSGPVMGGGLPPPPIKHNMDIGTWDNKGPVPKAPVPQQAPSPQAAPQPQQVAQPLPAQPPALAQPQYQSPQQPPQTRWVAPRNRNAAFGQSGGAGSDSNSPGNVQPNSAPSVESHPVLEKLKAAHSYNPKEFEWNLKSGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDSAFRCMSSKGPVYLLFSVNGSGHFCGVAEMKSPVDYGTSAGVWSQDKWKGKFDVQWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIISSYKHTTSIFDDFAHYEKRQEEEEVVRKERQSRNKQ
Protein: Tobamovirus multiplication protein 1 (AtTOM1) (Q9FEG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the efficient intracellular multiplication of tobamoviruses, probably being a membrane anchor promoting the formation of the replication complex.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10944200, ECO:0000269|PubMed:12514140}; Multi-pass membrane protein {ECO:0000269|PubMed:10944200, ECO:0000269|PubMed:12514140}.
Interaction partners:
- Tobamovirus multiplication protein 2A
- Tobamovirus multiplication protein 2B
- ADP-ribosylation factor-like protein 8b
- Ferric reduction oxidase 2
- Nicotianamine synthase 1
- Nicotianamine synthase 2
- Nicotianamine synthase 3
- Nicotianamine synthase
- Metal-nicotianamine transporter YSL1
- Probable nicotianamine synthase 4
Sequence:
MTDSGLMMPAEIAGILTTAITSWWDDVNESTQWQDGIFFALCGAYALVSAVALVQLIRIQMRVPEYGWTTQKVFHLMNFVVNGVRAVLFGFHMQVFLVHPKALCWVLLDLPGLLFFSAYTLLVLFWAEIYHQARSLPTDKLRITYISVNVAVYLAQIGIWAYIWVHDNSTVELVGKIFIAVVSFIAALGFLLYGGRLFFMLRRFPIESKGRRKKLHEVGSVTAICFTCFLIRCVVVAVSAFDKDLTLDVLDHPVLNLIYYMVVEVLPSALVLFILRKLPPKRVSAQYHPIQ
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FIM7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- non-specific serine/threonine protein kinase
- cAMP-dependent protein kinase
- Mitogen-activated protein kinase HOG1
- cAMP-dependent protein kinase
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Transcription factor
- Serine/threonine-protein kinase SCH9
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MTDAMIQEELASYLSDADRKTESPDTSFINSPSQTIPTENSSITNLKGFYNADIGNQLNQDALHSILENLEQSRCTRPVNLQHSLSSSSMNEEEVMTKPEFINPVLLSSATLPKLPSSLSPTTSAQHDSEADGTEVVLPSNNSNLQKAHNNLFMDSSLGNDYDNEVVDFFDVFGERDSLILNDDDADDEQDHDHDQDYDQDQDNFDDSAILSGSRRVSKLLSPTSLQTDRRASLTQTVELASSNPQTKHANAHEEIDANASDISKTLNEYSLDFHSASKLTKYRNRRQSVHGPVGSGVTKRKPSLESPLTSPTRTLQALSNANNQYRLTNNAGALNSMLLWEDAVLSDDDDLNEGEDRRNMFIASPASSGLFLNGNEDAALEVVEPSLNVSPVFNPKSLSILDAKNIELSSSKSSTTPVKEFATPMSSRTSVGSLAPSIASNSTTSIRRRRRSAVTPMSSRSSQSLSRRNKSVSVELPDGAKPFQCADCDKAFRRSEHLKRHVRSVHSTERPFPCMFCEKKFSRSDNLSQHLKTHKRHGDF
Protein: Putative D-/L-hydantoinase subunit A (EC 3.5.2.-) (Hydantoin utilization protein A) (Q01262)
Organism: Pseudomonas sp. (strain NS671)
Function: Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. HyuA and HyuB are both required for the conversion of D- and L-5-substituted hydantoins to corresponding N-carbamoyl-D- and N-carbamoyl-L-amino acids, respectively.
Interaction partners:
Sequence:
MKLFGVDVGGTFTDIIFSDTETRVTAIHKVPTTLDDPSTGVVQGILELCDRQYIDRTAIDHVFHGTTIATNAILEYDGAKTGMITTEGYRDIIHIGRHQRPQNYSIMQEIPWQDRPLVQRRHRLAIAERMGPVKGQVITPVQEDQVRGAVATLKERGVDSIIVNFLFSYTNPEHEQRVKEIIEEEYPEAFVTISSEVSPQFREFERFTTASINGFVGPKVKNYIQNLEQSLKDSGISAELHIMCSNGGVATPKTVSEKPVNTLLSGPAAGILGGAWAGELTNRQKLITFDVGGTSADIGIITDSGYGESSARDTWIAGYPVMVPMIDIHTIGAGGGSIAHIDEGGAFKVGPRSAGSRPGPACYGHGGLKPTVSDANVVLGRIDEHNFLGGEMKIYTNAAYKVIDELAGQLDLSRERTAEGVLQIMNNNMANAIREKTIQKGEDPREFSLVAFGGAGPLHAVEVAQILNIPEVIIPLYPGINSATGLLTTDLKYDVIKTEFMMSTNMDFSGLNEDLAGLETQLINQLKEDGVSKQDIRILRSADCRYAGQGYELRVDLPDVFLDEETIVDALNNFHESHKAEYGHNFTDSPIEFVNIRVTGTGYMPKIEKQAIHHEYQLEDALLKTGDATFNIDGSLVKVEINFYQREKIPVGAEFNGPCIVLQKDTTTVIPPNCTAYIEEYGNMIIKVGV
Protein: KCNQ potassium channel, isoform C (B7YZR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDPDNDIYAFYDIRGYKGKCRPGRPNSERILQPRMSLLGKPLNYNRGTRRDVRYRRLQSRLYNFLERPRGLHAIFYHVMVFLMVFTCLALSVFSTIKEYEEDAVYILFRMEILVVIWFTMEFGARLWSSGCRSRYQGCLGRLKFVKRPFCIIDIVTILASIVVLGMGTSGQVFATSALRGLRFFQILRMVRMDRRGGTWKLLGSVVYAHRQELITTMYIGFLGLIFASFLVYMWEKDVNDKFSNFAQALWWGVITLCTVGYGDMVPITWQGKLIASCCALLGISFFALPAGILGSGFALKVQQQQRQKHMIRRRQPAATLIQAVWRCYAADEHSVSVATWNIHRVALPSPPASRASSSFKHNTSFVARLPTIRRHKSQTIQTPGGGDGGGVSKPPGSSRASTRYTRTIRDINASVENLDEEDEPRCTQLTNRHKTAIRFIRKLKYFVARRKFKEALKPYDVKDVMEQYAAGHVDLLGRVKMLHLRLDQILGKQGSKAKDVYASKISLASRVVKVERQVADIEEKLDILIKAYMEDRDRFLALPLPAKPKIHSISPSHKPLHHAHNLAMIDVWKRTAALSVHPEQVTTTPLLNPSAPDSSELRSLTATQTPTTTTDAIATQTPMPPHVQHTATNTKYKHPKTCSLHRSTSEPYSKQEQRITIPDEGADSLDSSAKPTPPDSSSN
Protein: Zinc finger protein 280C (Suppressor of hairy wing homolog 3) (Zinc finger protein 633) (Q8ND82)
Organism: Homo sapiens (Human)
Function: May function as a transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDDDKPFQPKNISKMAELFMECEEEELEPWQKKVEETQDEDDDELIFVGEISSSKPAISNILNRGHSSSSSKGIKSEPHSPGIPEIFRTASQRCRDPPSNPVAASPRFHLVSKSSQSSVTVENASKPDFTKNSQVGSDNSSILLFDSTQESLPPSQDIPAIFREGMKNTSYVLKHPSTSKVNSVTPKKPKTSEDVPQINPSTSLPLIGSPPVTSSQVMLSKGTNTSSPYDAGADYLRACPKCNVQFNLLDPLKYHMKHCCPDMITKFLGVIVKSERPCDEDKTDSETGKLIMLVNEFYYGRHEGVTEKEPKTYTTFKCFSCSKVLKNNIRFMNHMKHHLELEKQNNESWENHTTCQHCYRQYPTPFQLQCHIESTHTPHEFSTICKICELSFETEHILLQHMKDTHKPGEMPYVCQVCQFRSSTFSDVEAHFRAAHENTKNLLCPFCLKVSKMATPYMNHYMKHQKKGVHRCPKCRLQFLTSKEKAEHKAQHRTFIKPKELEGLPPGAKVTIRASLGPLQSKLPTAPFGCAPGTSFLQVTPPTSQNTTARNPRKSNASRSKTSKLHATTSTASKVNTSKPRGRIAKSKAKPSYKQKRQRNRKNKMSLALKNIRCRRGIHKCIECHSKIKDFASHFSIYIHCSFCKYNTNCNKAFVNHMMSSHSNHPGKRFCIFKKHSGTLRGITLVCLKCDFLADSSGLDRMAKHLSQRKTHTCQVIIENVSKSTSTSEPTTGCSLK