wanglab/gogpt-training-data huggingface dataset:
Protein: pullulanase (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase) (L0C9D3)
Organism: Bacillus sp. CICIM 263
Interaction partners:
Sequence:
MVQGIHDEVGFIVRTDSWEKDGGDRFINVQSGNDEVWVKAGDEHTYTSPPDGEYKDFPAFERVKVKLHYFRYDGNYEGWNLWTWPEGKDGKRVDFTAEDDFGKVAEFELENQEGMKRAGFIVRKSMEGNDWAGREFGDRFITKFDENGNAEIWIVQGTESIYYNPDYIEKDPKIVNASMDTFNQITLETNFPFQWRDWKSIINIDNADIKEVVPYDGNEESNVTNKVKVVTEDKLDFRQSYKISAVSFGEAEVKIGEIVRSKEFDDAFYYDGKLGNQYTKNKTSFRLWAPTASEASIVLYDSWDDQTAEELPLKRGEKGTWTTVLKGDQNGLIYNYKVKIGGEWTEAADPYVRAVTVNGDRGVVMDLDSTNPKQWNKQKPELKNPEDSIIYEVHVRDLSIHEDSGIMHKGKFLGAAEKSTINSKGEKTGLNHIKDLGVTHVQFLPIYDYRTVDETKLDEPQYNWGYDPKNYNVPEGSYSTDPYDPAARITELKTMIQAYHDEQLRVVMDVVYNHVFAVNESSFHKLVPGYYFRYNEDGTLANGTGVGNDTASERKMVQKFIVDSVAYWAEEYNLDGFRFDLMGIHDTETMNKVRKELDTIDPTIIIIGEGWDLNTPLAAEKKANQKNAEDMPGIGHFNDGIRDGLKGSVFDELDKGFVNGKQGMESFVQQGIAAGLDYPDEMATYKDPEQAVTYAEAHDNHTLWDKLELTNPDAEEEFKKKMHKLASSIILTSQGVSFVHAGQEFMRTKYGDHNSYKSPDSINQLDWDRRTEFSGEVDYFKGLIKLRKHYKSFRMTTAEDIQSKLHFIDAPDNTVAYRLDAKGLKDRAKEIVVIHNANTEPAKISLPGKGPWHLLADGKQAGIRTLKIYQSKTIEVPAQTSFILKR
Protein: Glycerol-3-phosphate acyltransferase 4, isoform D (EC 2.3.1.15) (A0A0B4LGJ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
- BcDNA.GH07066
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- glycerol kinase
- Glycerol-3-phosphate dehydrogenase
Sequence:
MIAVLLDIFWIPIGGFLSFLIFISAINKSIGVRKAYVNLLLRIFEYGRVSIETASKENQHIQNPKTDDKQGVQLVDDADSKEGTNGATLITRDAVLLPQPQEPAPEKPVSSTKDEINFDFEKCLDYVKSGVEAIIEDDVTSRFEAEELKSWNMLTRTNRHYEFISWKITSIWVFGFFIRYVILMPLRVLVCFVGVLFAVLSSSIVACLPFRFVRLSLASLSFKITFRLISSSMSSFIKFHNKQYKPTVSGFCVANHTSPLDVAILSTDCTYSLVVWLTVCTAAVGYLKDGPFKRDLVHKVLGMCFGVLSSAISAVITYHNEDNRPSSGICVANHTSPIDVLVLMCDSTYSLIGQRHGGFLGVLQRALARASPHIWFERGEAKDRHLVAERLKQHVSDPNNPPILIFPEGTCINNTSVMQFKKGSFEVGGVIYPVAIKYDPRFGDAFWNSAKYSMMQYLYMMMTSWAIVCDVWYLPPMYRQEGESAIDFANRVKSVIAKQGGLIDLVWDGQLKRMKPKKEWREIQQVEFANRLKSDST
Protein: T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) (Chaperonin containing T-complex polypeptide 1 subunit 2) (P78371)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20080638}.
Interaction partners:
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta-2
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- Cell division cycle protein 20 homolog
- MOB-like protein phocein
Sequence:
MASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
Protein: SKP1-interacting partner 15 (F-box only protein 3) (O49279)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- F-box/LRR-repeat/kelch-repeat protein At1g09650
- U11/U12 small nuclear ribonucleoprotein 25 kDa protein
- Putative F-box only protein 11
- F-box protein At3g17320
- Phosphatidylinositol/phosphatidylcholine transfer protein SFH11
- F-box only protein 13
- F-box/kelch-repeat protein At5g48990
- F-box/kelch-repeat protein At5g42360
- Putative F-box/FBD/LRR-repeat protein At5g44960
- F-box/kelch-repeat protein At5g48980
Sequence:
MESSPVNCLPPDSLHQIFSSLPIRDIMICRSVCKFFNQLLTSQCFIEIISTRPPLNLLALRPPHHHHSHRHSGNGHATNIRPYIHVYDPEQNQWFRFNLDFLPFRSPQPVASSSGLIYLWGDSIDLAESSKSLVACNPLTRQFKVLPQLGSAWSRHGTVLVDSVNRVMVLTELAALYYSGTVVANQWLKFSSNLPSKPRSPVLMSSSVFALCDVGSPWRSQWKLFSCKLTNLTITHTNWVCLEKHEWGDIFDIIKRPRLLRGNGDSKLLMIGGLKSTFSLNPACSTILILRLDLESLEWEEAGRMPLEMYRGFQESSKFKVFGGGDRVYFSAKRMGKLAMWDCWQGWRWIEGVPGYADGLCRGFVFDAKLTLMP
Protein: Integrin subunit alpha D (A0A0G2K4L8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MTLKFLLVTVLTLCHGFNLDTENPMTFQENARGFGQSVIQLGETRVVVAAPQEVKAVNQTGALYQCDYSTNRCDPIPLQVPPEAVNMSLGLSLAATTVPPQLLACGPTVHQNCKENTYVNGLCYLFGSNLLRKPQQFPEALRGCPQQESDIAFLIDGSGSINSIDFQKMKEFVSTVMDQFQKSKTLFSLMQYSDEFRTHFTFNDFKRNPDPKSHVRPIRQLNGRTKTASGIRKVVRELFQKINGARDNAAKILVVITDGEKFGDPLNYEDVIPEAEEAGIIRYVIGVGNAFHKPQSRRELDTIASKPAGDHVFQVDNFEALNTIRNQLQEKIFAIEGTQTGSTSSFEHEMSQEGFSAAITSNGPLLGSVGSFDWAGGAFLYPSKDKATFINTTRIDSDMNDAYLGYASAVISRNRVQSLVLGAPRYQHIGLVVMFKQNFGAWEPHTDIKGSQIGSYFGASLCSVDMDADGNTNLILIGAPHHYEKTRGGQVSVCPLPRGRARWQCEAILHGDQGHPWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQGAVYIFHGASVASISTPHSQRIAGARFSPGLQYFGQSLSGGKDLTMDGLMDLAVGAQGRLLLIRAQPVLRLEATMEFSPKNLARSVFACQEEVVKNKDAGEVRVCLHVRKNTKDRLREGDIQSTVTYDLALDPGRSVVRAFFDETKNGILRRIRVFGLTQKCETLKLILPDCVDNSVSPIILRLNYTLVGEPLRSSRDLRPVLAMEAQRIFTAMFPFEKNCGNDTICQDDLSITVSSIRVNTLVVGDSRDFDVSVTLRNDGEDSYGTKVTCYYPSGLSYRKVSASQNQFSKKPWRVIAEPSSSEGQGVLKSTIWDINHPIFPANSEVTFNVTFDVDSDASLGNKLLLKVVVTSENNVSRTDKTESQLELPVKYAIYMVVTSGESSIKYLNFTASEMTSKVIQHQYQFNNLGQRSFPVSVVFWIPVQINKVTIWDPPQVTFSQNLSSVCRTEQKSPSHSKFQDELERTPVLNCSVAVCKRIQCDIPSFNSKEIFNVTLQGNLLFDWYIETSHDHLLLVSTAEILFNDSAFALLPGQETFVKAQTETKVEPYKVHNPVPLIVGSSVGGLVLLALITAGLYKLGFFKRQYKDMMNEAAPQDGPPQ
Protein: Calcineurin-like phosphoesterase domain-containing protein (O33337)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTWKGSGQETVGAEPTLWAISDLHTGHLGNKPVAESLYPSSPDDWLIVAGDVAERTDEIRWSLDLLRRRFAKVIWVPGNHELWTTNRDPMQIFGRARYDYLVNMCDEMGVVTPEHPFPVWTERGGPATIVPMFLLYDYSFLPEGANSKAEGVAIAKERNVVATDEFLLSPEPYPTRDAWCHERVAATRARLEQLDWMQPTVLVNHFPLLRQPCDALFYPEFSLWCGTTKTADWHTRYNAVCSVYGHLHIPRTTWYDGVRFEEVSVGYPREWRRRKPYSWLRQVLPDPQYAPGYLNDFGGHFVITPEMRTQAAQFRERLRQRQSR
Protein: Uncharacterized protein C23D3.16 (C6Y4A8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C29A10.17
- Uncharacterized protein C1778.05c
- Uncharacterized protein tam1
- GTP-binding protein gtr1
- Folliculin-like protein bhd1
- Putative aminopeptidase C13A11.05
- Protein sat1
- Guanine nucleotide exchange factor subunit ric1
Sequence:
MDSQLSENLLKCVNETYRGAMLVRNGLPIATAGDVNAEEQRVICEWNSNAVSEVLHLHDSNTKILIATKESCVLGLIYRNT
Protein: Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (dPABP2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1) (Protein rox2) (Q7KNF2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity). Plays a role in the positive regulation of alpha-1,3 fucosylation, possibly by cooperating with swm which regulates nuclear export of fucosyltransferase FucTA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10481015}. Cytoplasm {ECO:0000269|PubMed:10481015}. Note=Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. Mostly found in the nucleus in the germarium. From egg chamber formation onwards, expressed in both the nuclei and cytoplasm of nurse cells and the oocyte. At stage 10, abundant in the nuclei of nurse cells, oocyte and follicle cells and in the cytoplasm of nurse cells. Uniformly distributed in the cytoplasm of early embryos then progressively localizes to nuclei during the pre-blastoderm and syncytial blastoderm stages. After cellularization, localizes mainly to the nucleus and remains nuclear in later embryonic and larval stages. During mitosis, expression levels are reduced in prophase nuclei and expression is localized to the cytoplasm during metaphase. Localizes to nuclear speckles.
Interaction partners:
- polynucleotide adenylyltransferase
- Cleavage stimulation factor 64 kD subunit
- Polyadenylate-binding protein
- Nuclear cap-binding protein subunit 2
- LD40489p
- Nuclear cap-binding protein subunit 1
- Dosage compensation regulator mle
- Zinc finger CCCH domain-containing protein 3
- Splicing factor U2AF 50 kDa subunit
- LD29830p
Sequence:
MADEDITLNEDQLLESLEETNGEQETEIATEVEEEGSMQIDPELEAIKARVKEMEEEAEKIKQMQSEVDKQMAGGSTTGLATVPLSLEEKQEIDTRSVYVGNVDYGASAEELEAHFHGCGTINRVTILCNKADGHPKGFAYIEFGSKEFVETALAMNETLFRGRQIKVMSKRTNRPGLSTTNRFARGSFRGRGARVSRACCHSTFRGARRAMGYRGRANYYAPY
Protein: Protein O-mannosyltransferase 1 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 1) (dPOMT1) (Protein rotated abdomen) (Q9VTK2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Rt/POMT1 and tw/POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16219785}; Multi-pass membrane protein {ECO:0000269|PubMed:16219785}.
Interaction partners:
- Protein O-mannosyl-transferase 2
- Dystroglycan 1
- FI03527p
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- EGF domain-specific O-linked N-acetylglucosamine transferase
- GPI mannosyltransferase 2
Sequence:
MSATYTNTITQRRKTAKVRQQQQHQWTGSDLSGESNERLHFRSRSTNSMQQHTAISNSPSPLCCNGARALTMLNCCVDVNCHLNAPLRGSVNRHTTPTPTPTATPTPVATPKQASPSPTSDRSRSLSRSPSPSRSRSLSCQKQIDKNSAGAASAEERKTANASSQPFTVNLRIDLFSWTLFLLAFGTRFYKLATPPHIVFDELHYGKYISMYMRNIFFFDQHPPLGKQLIAGLVSLAGYDGNYTFTRIGEPYSPEMPIFWFRFLPAMCGSLLAPAVYNLLLEAKLSRWSSALGGLLVVLDNSLLTQSRFVLMESMLLLATTVGIACLLRFQRSRLGSLEWFFTGTAAAVCLGAAGTVKYVGFLALGLAFYLLCRHLWQLLYDAGLTDRQLWMHAISRLLIFVGIPLAVYLGVFYIHFKTLHRAGPHDSIMTSAFQASLDGGLASITKGQPLAVVHGSQITLRHTHGRTCWLHSHAAVYPVRYPDKRGSSHQQQVTCYSFKDVNNWWLVKRPTKENLVVGDEPDIIRHGEIIQLVHGITSRALNSHDVAAAMTPQCQEVSCYIDYEIKMAGELLWRVEILNRDSEGDIWHAIKSEVRLVHVSTEASLKFSGRQLPEWGFNQHEVVADREKAIHEDAIWNVEEHRYTQTEDHRERERQMLTAEMIPTKRTRISFWAKLLELQSKMLFQTKSVPNHMYSSMPHEWPLMDKGIAYWLDSQSSAQIYLLGNILLWYTATMGILVYAGLLAFYAMRRQRLCFDISEQEWQRFVLAGDTFFMGYVMHYIPYFCVDRTLFLHNYLPAFVFKLLLLCFVVEHLDYLLRRFCTGRGVHLVRLYRLMLILWLVGVLSIFSKFIPFSYGARKMTLNEVRSLRWKDTWDFVLHKNHHLY
Protein: Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Kinase from chicken homolog B) (hKFC-B) (MARK Kinase) (MARKK) (Prostate-derived sterile 20-like kinase 2) (PSK-2) (PSK2) (Prostate-derived STE20-like kinase 2) (Thousand and one amino acid protein kinase 1) (TAOK1) (hTAOK1) (Q7L7X3)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. Plays an essential role in the regulation of neuronal development in the central nervous system. Also plays a role in the regulation of neuronal migration to the cortical plate (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:13679851}.
Interaction partners:
- Serine/threonine-protein kinase TAO3
- Serine/threonine-protein kinase TAO2
- Dual specificity mitogen-activated protein kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 6
- Protein S100-A8
- Cell division cycle protein 20 homolog
- Serine/threonine-protein kinase PLK1
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Serine/threonine-protein kinase 25
- Nuclear migration protein nudC
Sequence:
MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHIFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGVGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDVSDDKSELDMMEGDHTVMSNSSVIHLKPEEENYREEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMSNEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASGWSHNPTGGPGPHWGHPMGGPPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSMGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT
Protein: Sulfurtransferase 18 (F4JZ39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSQSISSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDILVGCQSGARSLKATTELVAAVSGYKKVRNVGGGYLAWVDHSFPINTEEEEPSAN
Protein: Serine--glyoxylate aminotransferase (EC 2.6.1.45) (Alanine--glyoxylate aminotransferase) (AGT) (EC 2.6.1.44) (Asparagine aminotransferase) (EC 2.6.1.-) (Serine--pyruvate aminotransferase) (EC 2.6.1.51) (Q56YA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates, including asparagine. Functions exclusively as a catabolic enzyme in Asn metabolism. Involved in root development during seedling establishment after seed germination by regulating serine homeostasis and acetate conversion.
Subcellular location: Peroxisome {ECO:0000269|PubMed:11309139, ECO:0000269|PubMed:24505423}.
Interaction partners:
- Glycerate dehydrogenase HPR, peroxisomal
- Peroxisome biogenesis protein 5
- Glycolate oxidase 2
- Glutamate--glyoxylate aminotransferase 1
- Serine hydroxymethyltransferase 1, mitochondrial
- Aminomethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Phosphoserine phosphatase, chloroplastic
- Glutamate--glyoxylate aminotransferase 2
Sequence:
MDYMYGPGRHHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNTLSPGDRIVSFLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDENHTIKAICIVHNETATGVTNDISAVRTLLDHYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKFYKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTQKEEWISNTVTAVMVPPHIDGSEIVRRAWQRYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYLQHHIPLIPSRI
Protein: Large ribosomal subunit protein uL10m (39S ribosomal protein L10, mitochondrial) (L10mt) (MRP-L10) (Q9VPL3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q7Z7H8}.
Interaction partners:
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL13m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL40
Sequence:
MATLIQRSLSLAKSSTPALQFLRFRGKINIQRPKAPHYERARVVAVTQPKYPELPKAKSCFKTRAERTQQQQENPYNEIIAREVRNWLDHSRLVAFFHLSSITADDIFRVRVQLHKQNLHLKSYGSKIIEQAVKNTRYEAIVPLFHSNHCIVFSPDPEKTAALLRIVRRVPQMVLLGGIVEETMLSRNQLVAYAQMPGLHAVQAQLVQTLSQAPGHLIQQLQAHQNSFVQVLDVHAKNQMNEETPKST
Protein: TNFAIP3-interacting protein 1 (A20-binding inhibitor of NF-kappa-B activation 1) (ABIN) (ABIN-1) (Nef-associated factor 1) (Naf1) (Virion-associated nuclear shuttling protein) (VAN) (mVAN) (Q9WUU8)
Organism: Mus musculus (Mouse)
Function: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating TAX1BP1 and A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG (By similarity). Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 1A
- TNFAIP3-interacting protein 2
- Tax1-binding protein 1 homolog
- Polyubiquitin-B
- Nuclear factor NF-kappa-B p105 subunit
- E3 ubiquitin-protein ligase RNF31
- NF-kappa-B essential modulator
- Ubiquitin carboxyl-terminal hydrolase CYLD
Sequence:
MEGRGPYRIYDPGGSTPLGEVSAAFERLVEENTRLKGKMQGIKMLGELLEESQMEASRLRQKAEELVKDSELSPPTSAPSLVSFDDLAELTGQDTKVQVHPATSTAATTTATATTGNSMEKPEPASKSPSNGASSDFEVVPTEEQNSPETGSHPTNMMDLGPPPPEDSNLKLHLQRLETTLSVCAEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHMEPHPEHVCGAYPYAYPPMPAMVPHHAYKDWSQIRYPPPPVPMEHPPPHPNSRLFHLPEYTWRPPCAGIRNQSSQVMDPPPDRPAEPESADNDCDGPQ
Protein: Metastasis associated 1 family member 3 (Metastasis associated 1 family, member 3, isoform CRA_a) (F6RRE2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLADKHAKEIEEESETTVEADLTDKQKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVARAVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLYRHSYDLSSAISVLVPLGGPVLCRDEMEEWSASEASLFEEALEKYGKDFNDIRQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPTYKPNPNQISTSNGKPGAVNGAVGTTFQPQNPLLGRACESCYATQSHQWYSWGPPNMQCRLCAICWLYWKKYGGLKMPTQSEEEKLSPSPTTEDPRVRSHVSRQAMQGMPVRNTGSPKSAVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSKSTRKPLACIIGYLEIHPAKKPNVIRSTPSLQTPTTKRMLTTPNHTSLSILGKRNYSHHNGLDELTCCVSD
Protein: Polycomb group protein ASXL1 (Additional sex combs-like protein 1) (Q8IXJ9)
Organism: Homo sapiens (Human)
Function: Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its ubiquitination and degradation by TRIP12, thereby inactivating the PR-DUB complex and regulating Polycomb silencing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Histone-lysine N-methyltransferase EZH2
- Polycomb protein SUZ12
- Forkhead box protein K1
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Methylcytosine dioxygenase TET2
- Histone-binding protein RBBP4
- Host cell factor 1
- E3 ubiquitin-protein ligase RING2
- Polycomb complex protein BMI-1
Sequence:
MKDKQKKKKERTWAEAARLVLENYSDAPMTPKQILQVIEAEGLKEMRSGTSPLACLNAMLHSNSRGGEGLFYKLPGRISLFTLKKDALQWSRHPATVEGEEPEDTADVESCGSNEASTVSGENDVSLDETSSNASCSTESQSRPLSNPRDSYRASSQANKQKKKTGVMLPRVVLTPLKVNGAHVESASGFSGCHADGESGSPSSSSSGSLALGSAAIRGQAEVTQDPAPLLRGFRKPATGQMKRNRGEEIDFETPGSILVNTNLRALINSRTFHALPSHFQQQLLFLLPEVDRQVGTDGLLRLSSSALNNEFFTHAAQSWRERLADGEFTHEMQVRIRQEMEKEKKVEQWKEKFFEDYYGQKLGLTKEESLQQNVGQEEAEIKSGLCVPGESVRIQRGPATRQRDGHFKKRSRPDLRTRARRNLYKKQESEQAGVAKDAKSVASDVPLYKDGEAKTDPAGLSSPHLPGTSSAAPDLEGPEFPVESVASRIQAEPDNLARASASPDRIPSLPQETVDQEPKDQKRKSFEQAASASFPEKKPRLEDRQSFRNTIESVHTEKPQPTKEEPKVPPIRIQLSRIKPPWVVKGQPTYQICPRIIPTTESSCRGWTGARTLADIKARALQVRGARGHHCHREAATTAIGGGGGPGGGGGGATDEGGGRGSSSGDGGEACGHPEPRGGPSTPGKCTSDLQRTQLLPPYPLNGEHTQAGTAMSRARREDLPSLRKEESCLLQRATVGLTDGLGDASQLPVAPTGDQPCQALPLLSSQTSVAERLVEQPQLHPDVRTECESGTTSWESDDEEQGPTVPADNGPIPSLVGDDTLEKGTGQALDSHPTMKDPVNVTPSSTPESSPTDCLQNRAFDDELGLGGSCPPMRESDTRQENLKTKALVSNSSLHWIPIPSNDEVVKQPKPESREHIPSVEPQVGEEWEKAAPTPPALPGDLTAEEGLDPLDSLTSLWTVPSRGGSDSNGSYCQQVDIEKLKINGDSEALSPHGESTDTASDFEGHLTEDSSEADTREAAVTKGSSVDKDEKPNWNQSAPLSKVNGDMRLVTRTDGMVAPQSWVSRVCAVRQKIPDSLLLASTEYQPRAVCLSMPGSSVEATNPLVMQLLQGSLPLEKVLPPAHDDSMSESPQVPLTKDQSHGSLRMGSLHGLGKNSGMVDGSSPSSLRALKEPLLPDSCETGTGLARIEATQAPGAPQKNCKAVPSFDSLHPVTNPITSSRKLEEMDSKEQFSSFSCEDQKEVRAMSQDSNSNAAPGKSPGDLTTSRTPRFSSPNVISFGPEQTGRALGDQSNVTGQGKKLFGSGNVAATLQRPRPADPMPLPAEIPPVFPSGKLGPSTNSMSGGVQTPREDWAPKPHAFVGSVKNEKTFVGGPLKANAENRKATGHSPLELVGHLEGMPFVMDLPFWKLPREPGKGLSEPLEPSSLPSQLSIKQAFYGKLSKLQLSSTSFNYSSSSPTFPKGLAGSVVQLSHKANFGASHSASLSLQMFTDSSTVESISLQCACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLVVR
Protein: Transaldolase (EC 2.2.1.2) (Q6FMY5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transketolase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase
- Fructose-1,6-bisphosphatase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 2
- 6-phosphofructokinase
- ATP-dependent 6-phosphofructokinase
Sequence:
MSTENGGNSTLENLRNAGTNVVTDTGEFELISKFKPRDSTTNPSLILAATKNPNYASLIDVAIDYAKAKGGTIEQQTNNAADRLLVEFGKRITDLIPGVVSTEVDARLSFDKKGTVDKALQIIKLYEENGVSKDRVLIKIASTWEGIQAARELEAQHGIHCNLTLLFNFTQAVACAEANVTLISPFIARVLDWYKANTKNDYNIENHPGVLFVKKTYNYYKKHGYKTIIMGASFRTLDEIRALAGLDNATLGIPLLENLQNSTEKIDRVLTPEGAQKDGVDMITLIDDEAKYRYEFNSDAMAVEKLADGIRTFAKDTNTLYSLLRTKLEKAN