wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL16 (60S ribosomal protein L10) (Laminin receptor homolog) (Protein QM) (Ribosomal protein L10) (Tumor suppressor QM) (P27635)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. Plays a role in the formation of actively translating ribosomes. May play a role in the embryonic brain development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6ZWV3}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL11
Sequence:
MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYIPSRGPLDKWRALHS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (D6REM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF
Protein: ATP-dependent clpX-like chaperone, mitochondrial (EC 3.6.4.10) (ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial) (Caseinolytic mitochondrial matrix peptidase chaperone subunit X) (O76031)
Organism: Homo sapiens (Human)
Function: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through up-regulation of heme biosynthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11003706}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:22841477}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Mitochondrial disaggregase
- ATP-dependent zinc metalloprotease YME1L1
- T-box transcription factor TBX22
- Lon protease homolog, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- GrpE protein homolog 1, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Lon protease homolog 2, peroxisomal
Sequence:
MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS
Protein: 7-keto 8-aminopelargonic acid transporter (KAPA transporter) (P53744)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transport into the cell of 7-keto 8-aminopelargonic acid.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Dethiobiotin synthetase
- Vitamin H transporter
- Biotin synthase, mitochondrial
- Uncharacterized protein YJR154W
- Transcription factor VHR1
- Putative aryl-alcohol dehydrogenase AAD10
Sequence:
MNRVGAVFLFVYERNFFLSIVPDRHRTEIRMSSSERSEVKFDKHFNWWSLLGIAFSLSCSWVGISASMAVGIASGGPLLIIYGLIIAAFFSLMCGISLGDFAAILPNSSGGSFWVLKMLEQESVTLKTPEYEDPSDDDEEVFLENYCQTFNVEVSSKFQKVSSMVVGLLNYFGAIFTTASICSSLSMSCIGIHKLLHPDYELKHWHVFVGYECINAVLTLFNIYSTPLPYISQFGLYTSLLSFAMTFIICIVSRSDNTVDPWPKASNIFGSFDNQTGWNSSGMAFVVGLVNPIWAFVGIDSATHMIDEVGYSKSRFLVPKVIITTIIVGFVTSFIYCVGLFFCITDQTAVVESILPIVEIFYQATGNRNLSVFLQCMCITTGFVSGIASGTWQSRILQSFGKSYAPFYKEGSLGNKSLKKLAVLTPGFKSPLYAHFLSQICVTIIGCIFMGSSTAFNAIITACITLLLMSYAVPSFIFLFVIKKEKFIHRIESDVNCVSRPNRRRMSMIPHIICILWTLFCLVFLSFPYTLPVTAGNMNYTSVVYAVVFCIISIVVFPTCI
Protein: Urotensin-2 (Urotensin II) (U-II) (UII) (Q9QZQ4)
Organism: Rattus norvegicus (Rat)
Function: Highly potent vasoconstrictor.
Subcellular location: Secreted.
Interaction partners:
- Urotensin-2 receptor
- Urotensin-2B
Sequence:
MDRVPFCCLLFVGLLNPLLSFPVTDTGEMSLQLPVLEENALRALEELERTALLQTLRQTVGTEAEGSLGQADPSAETPTPRGSLRKALTGQDSNTVLSRLLARTRKQRKQHGTAPECFWKYCI
Protein: Lipid III flippase (P0AAA7)
Organism: Escherichia coli (strain K12)
Function: Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (lipid III) from the inner to the outer leaflet of the cytoplasmic membrane during the assembly of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). Could also mediate the translocation of Und-PP-GlcNAc.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02024, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02024}.
Interaction partners:
- Probable ECA polymerase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- dTDP-fucosamine acetyltransferase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- ECA polysaccharide chain length modulation protein
- Glucose-1-phosphate thymidylyltransferase 2
- UDP-N-acetylglucosamine 2-epimerase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- dTDP-glucose 4,6-dehydratase 2
Sequence:
MSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRVVGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIGVLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMRKLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAIWLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYIVYFSLCCGVFLLWRRRA
Protein: Pleckstrin homology domain containing A7 (E9PL74)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVTAG
Protein: Serine/threonine-protein kinase pim-3 (EC 2.7.11.1) (Q86V86)
Organism: Homo sapiens (Human)
Function: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17876606}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
Sequence:
MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKAYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGATVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHSCGVVHRDIKDENLLVDLRSGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLLFRRRVSPECQQLIRWCLSLRPSERPSLDQIAAHPWMLGADGGVPESCDLRLCTLDPDDVASTTSSSESL
Protein: peptide chain release factor N(5)-glutamine methyltransferase (EC 2.1.1.297) (Q389Z0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
- Peptide chain release factor 1, putative
- Prokaryotic-type class I peptide chain release factors domain-containing protein
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MRRWLRNVRGGLLHPRAARLMVSCGKTHGLHMVSTVSRNTETEDEEIRDNESFPHQDDDDESVTEISEEMMRSLPKAPPKLRSAGSLLSTEEQEQLTRMIFKAHYAGEGMGENDRAMWYQSALEIHWLEEWAYEEFDGQTQRDVARRAVKKAVLQRVDLHKPLAYIIGHQPFYGCDIRCSPPLLCPRPETEMWTHWLVRTWLSKIPETTQPLRVLDMCCGTGCVGIAIAKHVPSAQVTAVDILDEAIGASEENAKLNGLEASRFCTLKSDMFESFLVSNSGSLTGEDTKLDLKKKEPAAEHAGSFDIIVSNPPYVLPDQYTDLPPGIKLWESKLALVGDEKREQQQYLYFQELSEFGSLLLKPKAMRNPALCAAPNIVIEVGLQAEQVASVMEKSKLWENVEIHLDYAQQMRWITASSSH
Protein: Cyclohexane-1-carbonyl-CoA dehydrogenase (ChCoA dehydrogenase) (EC 1.3.8.11) (Q2LQP0)
Organism: Syntrophus aciditrophicus (strain SB)
Function: Mediates the conversion of cyclohexane-1-carbonyl-CoA into cyclohex-1-ene-1-carbonyl-CoA in biosynthesis of cyclohexane-1-carboxylate, a by-product produced during fermentation of benzoate and crotonate to acetate.
Interaction partners:
- Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- 3-hydroxyacyl-CoA dehydrogenase
- Acetyl-CoA acetyltransferase
- Pyruvate:ferredoxin oxidoreductase
- Enoyl-CoA hydratase
Sequence:
MYINTETEDLKTAIDAIRKAVKDRIAPLAAEVDDSGVIKPEIYDLLWDLGLMTVTYPPEYGGSETNPGTLLCIGCEEIAKACASTALLLIIQAVGSFPLMHGGRKELLDRIAPRIVNNRELAGYLVSEPGAGSDVKAIRTKAVKDGNDWVINGTKCWATNGPIASFYSCLCRTKDDKGVQGYSFFLVERNTPGLSVGKIEHKMGMRGSQTSEVILEDVRVPAENLLGELNNGFKLAMKDFDMSRPAIAAQALGISEGAFAQMETYSRERYTFGKPLCEHGMITQIIADSAALIEAGRGLIYQAADLYDKGKKNTKLASMAKFFMGDAAVKITTDAIQVFGGYGYTHDYPVERMFRDAKLTQIFEGANQIQRIVVAREIRDEQSK
Protein: Guanylate cyclase activating protein 4 (Guanylate cyclase activator 1d) (Q6ZM98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Guanylate cyclase
- Guanylate cyclase
- Guanylate cyclase.
Sequence:
MGNNHASLDDILAEDMHHWYNKFMRESPSGLITLFELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIQDITRNRDIVPEEIVALIFEKIDVNGEGELTLEEFIEGAKEHPEIMDMLKILMDLTPVLLIIVEGRQK
Protein: O-fucosyltransferase 35 (O-FucT-35) (EC 2.4.1.-) (O-fucosyltransferase family protein) (Q94BY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGHHHDGGDGVPQHHVNSPRFSGPMTRRAQSFKRGGSAGSSSNNNNTHVGVSGGDGNNNNNTSSTLRVHHEIDLPLNSPRSEIVSGSSGSDPSGGFDSALNRKHQTYGQLRERVVKGLLRKPMGSVVSDFSLRERKKLGHWMFFAFCGVCLFLGVFKICATGWLGSAIDGAASDQDLSIPRVNLLDHSSHDYIYKDGGNDVDPTLVMVASDVVGDQNSVVEFSGVWAKPESGNFSRCIDSSRSRKKLGANTNGYLLINANGGLNQMRFGICDMVAVAKIMKATLVLPSLDHSSYWADDSGFKDLFDWQHFIEELKDDIHIVEMLPSELAGIEPFVKTPISWSKVGYYKKEVLPLLKQHIVMYLTHTDSRLANNDLPDSVQKLRCRVNYRALKYSAPIEELGNVLVSRMRQDRGPYLALHLRYEKDMLAFTGCSHSLTAEEDEELRQMRYEVSHWKEKEINGTERRLQGGCPLTPRETSLLLRALEFPSSSRIYLVAGEAYGNGSMDPLNTDFPNIFSHSILATKEELSPFNNHQNMLAGLDYIVALQSEVFLYTYDGNMAKAVQGHRRFEDFKKTINPDKMNFVKLVDALDEGRISWKKFSSKVKKLHKDRNGAPYNRESGEFPKLEESFYANPLPGCICENTEEEGLMRRT
Protein: E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Protein phosphatase 1 regulatory subunit 11) (T-complex testis expressed protein 5) (Tctex-5) (Q8K1L5)
Organism: Mus musculus (Mouse)
Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1 (By similarity).
Interaction partners:
- Protein phosphatase 1 regulatory subunit 7
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MAETGAGISETVTETTVTETTVTETTEPENQSLIMKLRKRKPEKKVEWSSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEDEEEGCSHKHCVRGHRKGRRPTTPAPTPTTPPQPPDPSQPPPGPMQH
Protein: Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC) (Q05AH6)
Organism: Mus musculus (Mouse)
Function: Negatively regulates the transcriptional activator activity of SPIN1 via inhibition of its histone methyl-binding ability. Represses the expression of a number of SPIN1-regulated genes and the SPIN1-mediated activation of the Wnt signaling pathway. Can also inhibit the histone methyl-binding abilities of SPIN2A, SPIN2B, SPIN3 and SPIN4 (By similarity). Positively regulates poly-ADP-ribosylation in response to DNA damage; acts by facilitating PARP1 ADP-ribosyltransferase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BUA3}. Chromosome {ECO:0000250|UniProtKB:Q9BUA3}. Note=Colocalizes with PARP1 to sites of DNA damage. {ECO:0000250|UniProtKB:Q9BUA3}.
Interaction partners:
- Spindlin-1
Sequence:
MALKAKGAAALDCFEVTLKCEEGDDDDEAVVVAVIPRPEPMLRVTQQEKTPPPRPNLLEAGVEGCEELKQQVSWEQEFLVGNSPGGSGRALCMVCGAEIRSPSADTARAHILEQHPHTLDLSPSEKSNILEAWSEGVALLQDIQADQPSLPSLESGQDGQPDPISNPDPVRMPAEIVVLLDSEDNPSLPKRLRPRGLRPLELPVTPVIEQGNKKPRGQRWKESPENEPARKKRSRHMTKILDPDPDPPSPESPTETFAAPAEVRHFTDGSFPPGFVLQLFSHTQLRTTDCKDSSKDSRAAEGLPQPQNPSSASPPGLRGTLDLQVIRVRMEEPPAVSLLQDWSKHPQGTKGVGTGDKPDWPTVLSESSATVKGQPKAGSGV
Protein: Photosystem I assembly factor PSA3, chloroplastic (Protein PHOTOSYSTEM I ASSEMBLY 3) (Protein PIGMENT DEFECTIVE 329) (Q9M3C6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor. Cooperates with PYG7 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit. Does not seem to be required for the expression of chloroplast genes encoding PSI subunits.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:28522455}. Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:B4FSG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:B4FSG1}. Note=Associates with the stromal face of the thylakoid membrane. {ECO:0000250|UniProtKB:B4FSG1}.
Interaction partners:
- Tetratricopeptide repeat domain-containing protein PYG7, chloroplastic
- Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic
- Carboxylesterase SOBER1
- Protein IQ-DOMAIN 31
- Ycf3-interacting protein 1, chloroplastic
- Probable carboxylesterase SOBER1-like
- F-box/kelch-repeat protein At5g39560
Sequence:
MVVVTHISTSFHQISPSFFHLRLRNPSTTSSSRPKLDGGFALSIRAYIEKPNSFSTFANKVIGSLPVIGLLARIISDEGGVGRDLVDFAEFRKRVGNKCTPDDSRAFYEFQQRRGKAGEPLYVLLCCWVAAVGAGLLKSEEILEGVTRVSISNDLEFEEQNFIALMTEARQRRAKLNIDAPTIPMELRVEKALEGIYACCFRRGLIEEEDEKLLKVMLIAVFPSVEKSEIERIIKEKATRVEEGGEEENVMAKRLPKEAIQMQMKDLEFLQQQNIES
Protein: UPF0648 protein C3H5.09c (Q6LA55)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protection of telomeres protein 1
- Protection of telomeres protein tpz1
Sequence:
MNPLFPFSLLNPSTMWSSSQNTSFVWVVIATGFLFHLVLFVLSYVLGWPFTNFGFFSVYGLRHTFRNGDSVFISYVALRLHRPSTSKPYLLRIVTKGLIYTPSLSSANDAQSAGKNENQRSRLVFKAKREEEKTEEKFCHAVYMSNLLRNVEQKWIQFLHKSWMKWLHISIQESQLTFPSVGTFELGSLSMEMRPETNNVVGYENPSDPELVSSCVICSIRLANLVYIDRRQSSQQITDYLDLSLQTYYSLDKSNVPDTILRLRSSIKVGVLYIDLDTPLFEHLLNSNSSGGNHSSSSSSSGKVHVMKDNVEAALLKLQEAQIQIGTLKLWKRNVTGCGATYILNGSDFGLNLILLNKKNPSHRMFFPVEACVHQILASALSFNVESITPGHSPHVLLNIPLVTITCLTSALAEYARDASDLHQLQNSILRVNSTLTSPSLDLRLELLHDVLSCFPKKHDSTSRKKPKFPYQYFPYMKFSVSLYEPALRFLIASKSDSDFPGMLVANLSSMFLDIKYSPSSEHIFEIESSLRLSSNKVFYHNPKNKKWLINTSDLITFSLGYICNNDHGSLNMFFRDFQIRIEEEEVINSLKKFIILTKIKSEQVGPRKPRTKLVEPLLFRIPKWLKHIQLEVHSLLLVITAIRPEISPEPRGINCSIDKIHSLYLNDKKSRSQGMRKFDLNLELLMIKSIIFKNGKSLNSHLFLQIPNINFIVSTILRDNTAISRFTTEINFLRCFASLLHNCCIFYAYRACSSLFGENKSHKRIEKTNTSPQEPGVVPEGWNFDFRLKNARVSIFLDDDVSLLLDCGGFTTLKKTEKKYAEMHAKFIQIHTKNSDVPTLWDRFLALGNVRYQLKDLSDLEKLHQVTCSYISIRIPHKFIPFILIESAINTVKAAIRVSAEPLTIDQQHDLAEEIKQPRVVPHIQIKSTKFKFEVDDDPFECRLGMNYRIGLTEQQMRIDRWNIFEERANLLRKAKDPSPKSASESSSFYQNGSDIDDNDSNSSNTSNHTTENANAQQRKLEDLNRSFEDFLGSRPTNNSSFLKNVSVDEDTAREKLMEYDSLSWISNIKRIREFRYHRLRIRRMTAWPESDALDKHILFKENIIPIPIRPPLVDISLLNFDFTLDKPSFPLEELPKFLNTVGRGQPLDYGYSIYFPMYIDWKMDEAKFLIRDYPLPLVYIPKLGRGQDKRISSWHLKSNMVITEQQATLAAIRDVSVKVIPADLTKEGIPYVVNVTRTVSPIKTFSKTEIDVNSSLPTFLLWCNSYQPALSDMTRIMDTFTKMPIDPSEKLGFWDKIRLVAHSQIRLRWLEDGDVFLSLKGSRDPYVILGEGAGFQFCWSGNVSWDIGCDENPANFMIVDSDKFYLTIPDFPRQINGILEGKPLPTKSTKRSYTTFGVLKDLRCRKVIAKLVGKVRWRAGFVPERHCDEDCTVCNRKKACRLWNFKPHWQVITRIPQYCHDTHYGVYDAYRDFRSHYIHCSLALESPRYLDDANAFENVNSYNTIHLTPLVFSHFSSWWNLFSNNMSYPLRSGNLFPTLDSSPNKKFGRHLATFKYALELTPLFISHMYNYKTNKNWQDRTASATGLKARVDNFTIDLHQRSEKHEVKNKANLGRKHQEATSMKVHLAEIDFKTIDLRAISASFDEGALDNSDSIPANVLDEEEKECFSFKNVDGPANWVDIDDYHEADWLLPQQNEKCSIYPLAFSPRFTYYRHTKCHRRNEKNEKEIIPDTCRFGDEFTHRCLMPSRENPKAVQYELLQKRRKELEEFMSSEQERIGFLKSQLESNNDSEEVRQEYEELTKRIVTLSDHYRLLEYLLKDESSCSQASQCSENGQVDLSYASLSESVHAFNNRFVAHNVQVKWNNFIRNAVMSYVHEVERVRGFAYYMSQKAIVFLRDLEKRTESANDDFFGNYTEDDEDRENARHLLKFLLEDSKKRFWVKTSDADREHGSEEGNTNSISNNEYDIIQSYVFRFISPQIQLQCSSNPEKAVIISIQSLQIKILSVVDPIFPDNDINYLIERRFLCKVNESQFFISKKSDFEVVNASSLVLNEYGCEHNTVWPPWVPFETTFDFVLTPAAFSRFLHRVSFSVIYTKHNDLRLQETVHSTRAFFEDLDTHADTLTFDFPRVVFSTDSSQYYDIFTIITDLLLYKEPAQKQRNQRLEEIMLAADFSDLTGTSEVVRALQARVHRLLDLKLQHQLYDVTFGIYAHIAQQLFLQNELHRCGEELYYLIESIAAVQNRGIHQNKVRSNLSWFLMAKEVVWHLLEDNKKPFLDVRLQNATFRRIENSDASNFNTLEIEFMKGSNLAPGCQFENIICPYFNHEFSNEQLLQQKFIRIHWEVLEAVAGIQVIQHFEINLFPLSLQIEQELATKLFAYAFPNRNESDGFPHIYSRNHDKRKENGSQGEADNSNYSGSLMRRRTNDQEEDALATPSSSRRDSRSKRASLIDFTIDKCLDVDDEGRMELQSMLDRAGSNMLITYFKIPSVVLRLSYRGTGGLGLENITGFVFTVPTMEYRNEVCSYLDLAMKLKHDLIRTVVSHTGKLLVEKVKGNYHLKEHEREVSSELLNLQQLSAEHNRHADLESMVMARDDYINVQQPLAEENQEEGSPASAISRNHSTRSSLNSPRQFWAYHGSRSKKIADIVKRHIPPTINGKRSKNKGNEGSNARVDFYNDERYDPVKRELILGASNRRK
Protein: Sterile alpha motif domain-containing protein 9-like (SAM domain-containing protein 9-like) (Q8IVG5)
Organism: Homo sapiens (Human)
Function: May be involved in endosome fusion. Mediates down-regulation of growth factor signaling via internalization of growth factor receptors.
Subcellular location: Early endosome {ECO:0000250|UniProtKB:Q69Z37}. Mitochondrion {ECO:0000269|PubMed:35310830}.
Interaction partners:
- Interferon-induced protein 44
- Interferon-induced protein with tetratricopeptide repeats 3
- Epithelial-stromal interaction protein 1
- Signal transducer and activator of transcription 1-alpha/beta
- Probable ATP-dependent RNA helicase DDX60
- Protein mono-ADP-ribosyltransferase PARP9
- XIAP-associated factor 1
- Interferon-induced protein 44-like
- Interferon-induced protein with tetratricopeptide repeats 2
- Probable ATP-dependent RNA helicase DDX60-like
Sequence:
MSKQVSLPEMIKDWTKEHVKKWVNEDLKINEQYGQILLSEEVTGLVLQELTEKDLVEMGLPWGPALLIKRSYNKLNSKSPESDNHDPGQLDNSKPSKTEHQKNPKHTKKEEENSMSSNIDYDPREIRDIKQEESILMKENVLDEVANAKHKKKGKLKPEQLTCMPYPFDQFHDSHRYIEHYTLQPETGALNLIDPIHEFKALTNTETATEVDIKMKFSNEVFRFASACMNSRTNGTIHFGVKDKPHGEIVGVKITSKAAFIDHFNVMIKKYFEESEINEAKKCIREPRFVEVLLQNNTPSDRFVIEVDTIPKHSICNDKYFYIQMQICKDKIWKQNQNLSLFVREGASSRDILANSKQRDVDFKAFLQNLKSLVASRKEAEEEYGMKAMKKESEGLKLVKLLIGNRDSLDNSYYDWYILVTNKCHPNQIKHLDFLKEIKWFAVLEFDPESMINGVVKAYKESRVANLHFPNQYEDKTTNMWEKISTLNLYQQPSWIFCNGRSDLKSETYKPLEPHLWQRERASEVRKLILFLTDENIMTRGKFLVVFLLLSSVESPGDPLIETFWAFYQALKGMENMLCISVNSHIYQRWKDLLQTRMKMEDELTNHSISTLNIELVNSTILKLKSVTRSSRRFLPARGSSSVILEKKKEDVLTALEILCENECTETDIEKDKSKFLEFKKSKEEHFYRGGKVSWWNFYFSSENYSSDFVKRDSYEKLKDLIHCWAESPKPIFAKIINLYHHPGCGGTTLAMHVLWDLKKNFRCAVLKNKTTDFAEIAEQVINLVTYRAKSHQDYIPVLLLVDDFEEQENVYFLQNAIHSVLAEKDLRYEKTLVIILNCMRSRNPDESAKLADSIALNYQLSSKEQRAFGAKLKEIEKQHKNCENFYSFMIMKSNFDETYIENVVRNILKGQDVDSKEAQLISFLALLSSYVTDSTISVSQCEIFLGIIYTSTPWEPESLEDKMGTYSTLLIKTEVAEYGRYTGVRIIHPLIALYCLKELERSYHLDKCQIALNILEENLFYDSGIGRDKFQHDVQTLLLTRQRKVYGDETDTLFSPLMEALQNKDIEKVLSAGSRRFPQNAFICQALARHFYIKEKDFNTALDWARQAKMKAPKNSYISDTLGQVYKSEIKWWLDGNKNCRSITVNDLTHLLEAAEKASRAFKESQRQTDSKNYETENWSPQKSQRRYDMYNTACFLGEIEVGLYTIQILQLTPFFHKENELSKKHMVQFLSGKWTIPPDPRNECYLALSKFTSHLKNLQSDLKRCFDFFIDYMVLLKMRYTQKEIAEIMLSKKVSRCFRKYTELFCHLDPCLLQSKESQLLQEENCRKKLEALRADRFAGLLEYLNPNYKDATTMESIVNEYAFLLQQNSKKPMTNEKQNSILANIILSCLKPNSKLIQPLTTLKKQLREVLQFVGLSHQYPGPYFLACLLFWPENQELDQDSKLIEKYVSSLNRSFRGQYKRMCRSKQASTLFYLGKRKGLNSIVHKAKIEQYFDKAQNTNSLWHSGDVWKKNEVKDLLRRLTGQAEGKLISVEYGTEEKIKIPVISVYSGPLRSGRNIERVSFYLGFSIEGPLAYDIEVI
Protein: tRNA (32-2'-O)-methyltransferase regulator trm732 (O60081)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in the methylation of the 2'-O-ribose of nucleotides at position 32 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)) by SPAC4F10.03c.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA N
- rRNA methyltransferase 2, mitochondrial
- Putative tRNA pseudouridine synthase C16C4.06c
Sequence:
MDLSVIKAASLDLESLPSQPTVSSFQQLRETFIQSKSEDWYLKNGLFFRYYSFLKSSLENATLDGPSQVACLDTISVWLRRIFNACKQDPEISKYVWDTMELKFWTNLFSLPANKISIPGLTGVQVAVKDVFSKSLQLYLLVCPSEDIKNDFLLDSLKHALHWDRHAKVVCTAIQLLVKVTGAEAVFAFQPDFFEQSLKLLKDYSYAQAISSTILTVLTLRFKSLSEETEDREEVETKWMNIWCPIILYEFYGNDRQVQAGMSSFLIPSLLGVSPGITVKFLSRLQNYPNVSKDARDAACLYALKIAKDSKIIKNLDLVKEHAFVKTLFKHPDIKIQLACFRLIALCPNVSSPLSFEDFDCLESNIEFSFNVLDPDSRQILLKSMQDFFIRLRASCHSIARTMRSRHSDKVALSGLLDRAMQFLTSFISVCKKHLYPTCNYQQVLVSLSFLDTLISFGLDDNVESSSIREAQHDFPFSMVIIDRDLSRLMIDRLKDPYDDIRNLCLKILLSYKSLPGFISDSDAYFLFNHGLELLNAVRSHECDGGAKTIYLCNHFMEKSVPGSVLANTKVILNRLKSNIEHAKTSLLEAAVNCPLQGYLIQLTYIFQSLSPTIVKNDNESWKNIVMELIKASETIWGLIKDVLCDDSPEGNLPDGEGEGGIVSNLEDTPAQLILSYSWRSLKETSSLLTVLLTKCLSLFDEEFTPFTLNYYGELMMTWLWEIRHRGAFTSVYPCFIEYCSFLFECNKHEISELPDPWLHKNLSVIQEKSSFITRRSGGIPLSITAILVAGKDKREQLIEQTVISLISIAKQPVEQKNIAGQFDLPQVHAMNTLKTIFTEHRLSSVSVEYLEPAIALSIEGFSHELWPIRNCSVMLFTALINRAFGSKKPKDAVNLGNNKGLSTKMFFSKFPTLHDYLLRELEVSVASLSSNDQPSTGLYPILNMFSRLQYAQPYGNENEWTGLSQFEPLIFKCTASRICKVREIASLSLTCLLDCSKMTTFIVSQLKGVAGLQQNEIHGKLLTIRAVLSCFFSKLTLQQVQEFYEVVPLAFINCFLEFTSSKTSFYAKKLFLEVLNSYFMSNTDSNAKRLQQLRRMTMDYCKRMLLDRKANVTNVFNTIGLPIHQQMAATIFLENLKEFSVYCDAHSIGFLVSKLLHYEFYEVQLTTLRSIVDSPRKKIIVNNPEILQALIKLTPRNQWSQVRALALSLLSDSLNSTSYRLLGISCSDMVSNILSNECLPIKESFIVLLGSCIKQLKTENFLEYKVTFAKWVEILLSYSNEYQPFSSRKAALDSIIHFDLFNAESTAEAFSFEFYILYLLLGDFLNDDDEEIRSLAANHAYQVLGTSAQCVTEIWNLWKLRTKATFGGQHDFQHCINKRLILEDGCELASVQLDNALSRNCSLFERERQNLYYSDNQKLEDLLFYASYPNEKLKDWATDGINAILSRFEDVSRDGPLGKTSDPNVWFTIYKIIRIAEHVHLPLDRVHSLMNRIDGHPSFCQ
Protein: Synaptosomal-associated protein (Q9VH76)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
- Syntaxin-1A
- Protein Mo25
- Synaptobrevin
- Neuronal synaptobrevin, isoform J
- Alpha-soluble NSF attachment protein
- Synaptotagmin 1
- Syntaxin-4
- Vesicle-associated membrane protein 7
- Secretory 22, isoform B
- Syntaxin-5
Sequence:
MAAVENAEPRTELQELQFKSGQVADESLESTRRMLALMDESKEAGIRTLVALDDQGEQLDRIEEGMDRINADMREAEKNLSGMEKCCGICVLPWKKVNIKDDGESAWKANDDGKIVASQPQRVIDERERGGMGAPPQSGYVARITNDAREDEMDENLGQVNSMLGNLRNMALDMGSELENQNKQVDRINAKGDANNIRMDGVNKRANNLLKS