wanglab/gogpt-training-data huggingface dataset:
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein YwlC) (tRNA threonylcarbamoyladenosine biosynthesis protein YwlC) (P39153)
Organism: Bacillus subtilis (strain 168)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- Release factor glutamine methyltransferase
- Dephospho-CoA kinase
- Uncharacterized protein YwcI
- Ribosomal RNA large subunit methyltransferase H-methyltransferase)
- Uncharacterized protein YwlB
- Uncharacterized protein YycS
- Protein-arginine-phosphatase
Sequence:
MKTKRWFVDVTDELSTNDPQIAQAAALLRENEVVAFPTETVYGLGANAKNTDAVKKIYEAKGRPSDNPLIVHIADISQLEDLTGPAPEKAKTLMKRFWPGALTLILPCKPDALSPRVTAGLETVAIRMPDHPLALALIRESGLPIAAPSANLSGKPSPTKAEHVAHDLDGRIAGIVDGGPTGIGVESTVLSCADDIPVLLRPGGITKEQIEAVIGPIHVDKGLSDQNEKPISPGMKYTHYAPTAPLAICEGSPERIQHLIQEYQQGGRRVGVLTTEEKAGVYSADYVKSCGRRAQLETVAAGLYDALRSFDENKVDFIIAESFPDTGVGLAIMNRLMKAAGGRVIR
Protein: IMPACT family member YigZ (P27862)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Xaa-Pro dipeptidase
- Trk system potassium uptake protein TrkH
- Protoporphyrinogen IX dehydrogenase [quinone]
Sequence:
MESWLIPAAPVTVVEEIKKSRFITMLAHTDGVEAAKAFVESVRAEHPDARHHCVAWVAGAPDDSQQLGFSDDGEPAGTAGKPMLAQLMGSGVGEITAVVVRYYGGILLGTGGLVKAYGGGVNQALRQLTTQRKTPLTEYTLQCEYHQLTGIEALLGQCDGKIINSDYQAFVLLRVALPAAKVAEFSAKLADFSRGSLQLLAIEE
Protein: Flotillin-like protein 3 (Nodulin-like protein 3) (Q9LV90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane, caveola {ECO:0000250}.
Interaction partners:
- Hypersensitive-induced response protein 4
- Prohibitin-2, mitochondrial
- Prohibitin-4, mitochondrial
- Hypersensitive-induced response protein 2
- Prohibitin-1, mitochondrial
- Transmembrane protein
- Prohibitin-6, mitochondrial
- NDR1/HIN1-like protein 3
- Hypersensitive-induced response protein 3
- Prohibitin-3, mitochondrial
Sequence:
MSYRVAKASQYLAITGGGITDIKLAKKSWVFPWQSCTVFDVSPVNYTFEVQAMSSEKLPFVIPAVFTIGPRVDDPHALLLYAMLMSQHDKHSNHVNELVQGVIEGETRVLVASMTMEEVFKGTKEFKKEVFDKVQLELNQFGLVIYNANVKQLVDVPGHEYFSYLGQKTQMEAANQAKIDVAEAKMKGEVGAKERTGLTIQNAAKIDAESKIISTQRLGEGTKEEIKVKTEVKVFQNEKEALVAKADAALAIQKAALSQNSRVAEVEAAKAVALREAELQTKVEKMNALTRTEKLKAEFLSKASVEYETKVQEANWELYNKQKQAEAVLYEKQKQAEATKAAADAAFYSKQKDAEGLVAMADAQGTYLKTLLGAVNNDYSAMRDFLMINNGIYQDIAKTNAVAIRDLQPKISVWNHGGAEQGMNGGGKATMNDIAGLYKMLPPVLDTVYEQTGMQPPAWIGTLRGAEPKQSLHAQQHRG
Protein: Putative RNA-binding protein 15B (RNA-binding motif protein 15B) (Q6PHZ5)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex. Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist. Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation. Inhibits pre-mRNA splicing. Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus speckle {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NDT2}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000250|UniProtKB:Q8NDT2}.
Interaction partners:
- N
- Zinc finger CCCH domain-containing protein 13
- N
- Protein virilizer homolog
- Pre-mRNA-splicing regulator WTAP
- RNA-binding protein 15
- E3 ubiquitin-protein ligase Hakai
- RNA N
- YTH domain-containing family protein 1
- YTH domain-containing protein 1
Sequence:
MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGTKHPVPARARDKPRGSGGGGGHRDGRAAGDANHRASGGRSSGAPGGGGRTGKASGDPGAGGASPRASPLPPPPPPPGAEPAGPGSTAAPEYKTLLISSLSPALPAEHLEDRLFHQFKRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGSSRRSSSSSAAASTPPPGPPAPADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYQAVCEEDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGRVIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGGPDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLRVRDRTPPHLLYSDRDRTFLEGDWTSLSKSSDRRNSLEGYSRSVRSRSGERWGGDGDRSIAKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGGGQQSERGSDRTPERSRKENHSSEGTKESGSNSLSNSRHGAEERSHHHHHHEAPDSSHGKKTRESERNHRTTEAEPKTLEEPKHETKKLKTLSEYAQTLQLGWNGLLVLKNSCFPTSMHILEGDQGVISGLLKDHPSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLAIQSTPSGPGAEGMPVVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDNTGMLYAFPPCDFSQQYLQSALRTLGKLEEEHMVIVIVRDTA
Protein: Mannitol dehydrogenase 2 (EC 1.1.1.67) (P0CX09)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway.
Interaction partners:
Sequence:
MTKSDETTATSLNAKTLKSFESTLPIPTYPREGVKQGIVHLGVGAFHRSHLAVFMHRLMQEHHLKDWSICGVGLMKADALMRDAMKAQDCLYTLVERGIKDTNAYIVGSITAYMYAPDDPRAVIEKMANPDTHIVSLTVTENGYYHSEATNSLMTDAPEIINDLNHPEKPDTLYGYLYEALLLRYKRGLTPFTIMSCDNMPQNGVTVKTMLVAFAKLKKDEKFAAWIEDKVTSPNSMVDRVTPRCTDKERKYVADTWGIKDQCPVVAEPFIQWVLEDNFSDGRPPWELVGVQVVKDVDSYELMKLRLLNGGHSAMGYLGYLAGYTYIHEVVNDPTINKYIRVLMREEVIPLLPKVPGVDFEEYTASVLERFSNPAIQDTVARICLMGSGKMPKYVLPSIYEQLRKPDGKYKLLAVCVAGWFRYLTGVDMNGKPFEIEDPMAPTLKAAAVKGGKDPHELLNIEVLFSPEIRDNKEFVAQLTHSLETVYDKGPIAAIKEILDQV
Protein: Insulin gene enhancer protein isl-2b (Islet-2B) (Insulin gene enhancer protein isl-3) (Islet-3) (P53407)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Binds to one of the cis-acting domain of the insulin gene enhancer. May be involved in the regional specification of the myotome and also in target recognition by the caudal primary neuron.
Subcellular location: Nucleus.
Interaction partners:
- POU domain, class 4, transcription factor 3
- ELAV-like protein
- Transcription factor atoh7
Sequence:
MVDIIFSSSFLDDMGDHSKKKSGLAMCVGCGSQIHDQYILRVSPDLEWHAACLKCVECNQYLDETCTCFVRDGKTYCKRDYVRLFGIKCAKCTLGFSSSDLVMRARDSVYHIECFRCSVCSRQLLPGDEFSVRDEELLCRADHGLALERGPGGSPLSPGNIHTRGLHMAADPVSVRQTPHRNHVHKQSEKTTRVRTVLNEKQLHTLRTCYNANPRPDALMKEQLVEMTGLSPRVIRVWFQNKRCKDKKRSILMKQLQQQHGDKTNLQGMTGTALVAGSPIRHNPSVPGHPVDVQAYQPPWKALSEFALQSDLDQPAFQQLVSFSESGSLGNSSGSDVTSLSSQLPDTPNSMVPSPVET
Protein: Uncharacterized protein (Q38A40)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLTSHRISCLQQMEKQLRRLVRGEPILKDARNGSHGVSVADSNFKRTHIALKNKLLFRRVPITLSLLERSLLPIIRMESSSSRKVTGSNNAHPPKELEVNEEVTVSASSATLVGYETTQKSHLVPQQSMSAVAKIPLEGRQRHNKRSILTHSEAMFRLFSSLHYLESERRKLYLHHTDRLKLKLTEAEAAVRAAGGRQGKTGPSRREAIGAVRGVNEDISILKDSLLARSYLSARLWRFLLRKELWTAAIEDSRTSERKEVPTVLILLLSLQRMSFGILQDVTQGHHLNACSPRFVVSLPSRSRRCNQEEIHSAEHETGDEGATSQSVHEERCETSEAPEDDSMITLMCGTLPLTAPESVQAKKRREISAGSTGMKKTSRNFVGSCRPYPRKLRWLPPRSCDALSLVVDSLALCSAVLTELNIKNIIIQWGQVVELFEVLTVVQSTASLLLAVGGTGDEEEVTKMHSVLRNLEDAMIAVGGSARQTILMEEYEVLSSLSSVCAIRLLLALDGLQLLPMCESSSQRLIMQLLSRIFPQLSTGTQSALLQKSRQTSLFAFATRGHRLKLFSNCGNKSAVTAALESIRSRARLQQRQMQAALRSKYLEEVNTQSISELARNVSVHSLVAALSLFARTVQDARRQVYETQGRLLTASLFLIESILTAVTFSSPRGGDGIIHHKDLAPLLLALTPLWSLAYERCKLLRDVSNVRHNKCLPGKGAGSPLAKSEVVMVRYATDVVFNAVNVALVQRVELVENDSPPHNAVDGMEVISPSNVAAIVTALGSWCDISPNGKGISFVATTAALLKRLLLSDVKMWQELRLLSDPRREAFARALTEVMGSVGAMDSSVTEVLASIG
Protein: Aspergillopepsin-1 (EC 3.4.23.18) (Aspartic protease pepA) (Aspergillopepsin I) (Aspergillopeptidase A) (A2R3L3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q12567}.
Interaction partners:
Sequence:
MVVFSKTAALVLGLSSAVSAAPAPTRKGFTINQIARPANKTRTINLPGMYARSLAKFGGTVPQSVKEAASKGSAVTTPQNNDEEYLTPVTVGKSTLHLDFDTGSADLWVFSDELPSSEQTGHDLYTPSSSATKLSGYTWDISYGDGSSASGDVYRDTVTVGGVTTNKQAVEAASKISSEFVQNTANDGLLGLAFSSINTVQPKAQTTFFDTVKSQLDSPLFAVQLKHDAPGVYDFGYIDDSKYTGSITYTDADSSQGYWGFSTDGYSIGDGSSSSSGFSAIADTGTTLILLDDEIVSAYYEQVSGAQESEEAGGYVFSCSTNPPDFTVVIGDYKAVVPGKYINYAPISTGSSTCFGGIQSNSGLGLSILGDVFLKSQYVVFNSEGPKLGFAAQA
Protein: Alpha-2-macroglobulin (Alpha-2-M) (Q7SIH1)
Organism: Bos taurus (Bovine)
Function: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Vitamin K-dependent protein C
- Haptoglobin
- Alpha-1-antiproteinase
- Endoplasmic reticulum chaperone BiP
- Albumin
- Serotransferrin
- Ceruloplasmin
- Transthyretin
- Apolipoprotein A-II
- Apolipoprotein A-I
Sequence:
MGKNKLLYPSLTLLLLLLLPTDASVSGKPQYMVLVPSLLHTETPEKGCLLLSHLNETVTVSASLESVRENRSLFTDVVAEKDLFHCVSFTLPRSPTSQEVMFLTIQVKGPTQEFKKRTTVLVKNEESLVFVQTDKPIYKPEQTVKFRIVLLDESFHPLNELVPLVYVEDPKGNRIAQWQNLEVENGLQQLTFPLSSEPFQGSYKVVVQKGSGGTAEHPFTVEEFVLPKFEVQVRMPKIITILEEEVQVSVCGLYTYGKPVPGRVTMNMCRKYRNPSNCYGEESNAVCEKFSGELNNEGCFSQQVNTKIFQLKRQEFEMKIEVEAKIQEEGTEVELTGKGATEITTTITKLSFVTVDSNLRRGIPFTGKVLLVDGKGVPMPNKVIFITANEANHNSNTTTDEHGLAQFSITTTKIKGTSLSIRVKYKDHSPCYGYQWLSEEHQDAYHSANLVFSRSNSFVYLEPLPRELPCGKTQTVQAHYVLKGQVLKDLKELVFYYLIMAKGGIVRSGTHTLPVEQGDMQGHFSMSVPVESDIAPVARLLIYAILPDGEVVGDSARYEIEHCLANKVGLNFSPGQSFPASQAHLRVTASPQSLCALRAVDQSVLLMRPEAELSAATVYNLLPVKDLSSFPSSVNQQEEDNEDCISHDNVYINGIMYFPVSNTNEKDMYSFLQDMGLKAFTNSKIHKPKICPQPEEHRIQHHTLLASPVRAEMGRNRDFVHFDDTSEPPTETVRKYFPETWIWDLVVVSSSGVHEVEVTVPDTITEWKAGALCLSRDTGLGLSPTASLRVFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPEKEQETYCICGNGRQTVSWAVTPKSLGNVNFTVSAEAVESQELCGSEVPVVPEHGRKDTIIKPLLVEPEGLEKEVIFNSLLCPSVDFVFLGAEDGGQVLRHFPPAAATDTAADAHDPARPGAKVSESLSLKLPPNVVEESARASFSVLGDILGSAMRNTQNLLQMPYGCGEQNMARFAPNIYVLDYLNETQQLTAELKSKAILYLNTGYQRQLLYKHFDGSYSTFGEHRGNSEGNTWLTAFVLKSFAQARGYIFIDEAHITEALTWLAQKQKSNGCFRSTGTLLNNAIKGGVDDEVTLSAYITIALLEMPLPVTHPVVRNALFCLDSAWKSAKEGSQGSHVYTKALLAYAFALAGNQERRTEVLTSLYEEAVKEDNTIHWTRPQKPRLLTEDIYQPRAPSAEVEMTAYVILAHVTAQPAPNPEDLKRATSIVKWISKQQNCQGGFSSTQDTVVALHALSRYGAATFTSARKAAQVTIQSSGTFSTKFQVENSNRLLLQQVSLPEVPGEYSMSVTGEGCVYLQTSLKYNILPKKDEFPFALEVQTLPQTCDGPKAHTSFQISLSVSYIGSRPASNMAIVDVKMVSGFIPLKPTVKMLERSNVSRTEVSNNHVLIYLDKVTNETLTLTFTVLQDIPVRDLKPAIVKVYDYYETDEFAVAEYSAPCSKDIGNA
Protein: ADP-ribosylation factor 4 (P51644)
Organism: Xenopus laevis (African clawed frog)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P18085}.
Interaction partners:
Sequence:
MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEAAEELQKMLQEDELRDAVLLVFANKQDLPNAMAISEMTDKLTLQTLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR
Protein: Jabba, isoform E (Jabba, isoform G) (B7YZK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQETKTVATAKDQNQRDHIDEEEVIELHESRSFYDRVREQAERFASTRVGQFVIERADKALAMIEDTAKWSLPQDKSSAPLERPLPWAPFLMLIVLLRLTRIWLSVGALMIGNGPISPTDMVYFIQTRRRKLRAIRVHGLKVMRRRQQEVSYGSGKGMTQKLNQWFSRAMCRPGVQQDSSSRRVFVRHSEQGLSNFVVKRPREEDCNADADLTIDQMLAKYANENSEDDSDFVPNEEEEEEESSSSSGESESESGSSEGISSGEVDEVVSQPKQKSAGAVVENGVHKAEEKENDKGKLNITTTSNGNNDKEQADVAAAQPDEEWKSSPGHMSAAVMNTRLYNNTAAAGSPTCFNTSLGTQALLKRASIQSVLAHSTPTTEMRDQPIEEANNSVPQTPETEKTQPQTPKEVHNQNQQQNQQQRQRNHPHQRYRGRNRR
Protein: Uncharacterized protein (Q38A38)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRFPHSNVGLVIGLVSLLLQLHRVMVITEAAAINSFTVILVNDRNSAALREAPTGTTMQIPPYVVRLSADWTVIENPQWNEVSSEENDSEGRLLHCRLPLPQDENTVQTQVKHYIQLQEHRTAVRIWHWLEGMMNRDGCIFGDGEGPITGVSEWYLFCVRGAVRKVNKTTVAVLYGNRTSQKLQQTVRRLVHRARWSSQGSERSKSFKRWTSRIGEYKANVTWPRWNVERQLWELIYPTRRECRAWEADAAAFGESPERYIRNESHRWSDSRSFTLPRNKEVWETVVRLYCQQNQGDRHVLDWSITEVLQTCTHEVLLRSPAVCEWSQVLQNFHVNPIPCIPI
Protein: Cornifin-B (Small proline-rich protein 1B) (SPR1 B) (SPR1B) (Q62267)
Organism: Mus musculus (Mouse)
Function: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MSSHQQKQPCTAPPQLHEQQVKQPCQPPPPEPCVSQVKTPCDTKVPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKVPEPCLPKAPEPCQPIVPEPCPSTVTPILAQQKTKQK
Protein: NF-kappaB repressing factor (A3F769)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKILQMAEGIDIGEMPSYDLVLSKPSKGQKRHLSTCDGQNPPKKQAGSKFHARPRFEPVHFVASSSKDERQEDPYGPQTKEVNEQTHFASMPRDIYQDYTQDSFSIQDGNSQYCDSSGFILTKDQPVTANMYFDSGNPAPSTTSQQANSQSTPEPSPSQTFPESVVAEKQYFIEKLTATIWKNLSNPEMTSGSDKINYTYMLTRCIQACKTNPEYIYAPLKEIPPADIPKNKKLLTDGYACEVRCQNIYLTTGYAGSKNGSRDRATELAVKLLQKRIEVRVVRRKFKHTFGEDLVVCQIGMSSYEFPPALKPPEDLVVLGKDASGQPIFNASAKHWTNFVITENANDAIGILNNSASFNKMSIEYKYEMMPNRTWRCRVFLQDHCLAEGYGTKKTSKHAAADEALKILQKTQPTYPSVKSSQCHTGSSPRGSGKKKDIKDLVVYENSSNPVCTLNDTAQFNRMTVEYVYERMTGLRWKCKVILESEVIAEAVGVKKTVKYEAAGEAVKTLKKTQPTVINNLKKGAVEDVISRNEIQGRSAEEAYKQQIKEDNIGNQLLRKMGWTGGGLGKSGEGIREPISVKEQHKREGLGLDVERVNKIAKRDIEQIIRNYARSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGRKRRKEDLLDQLKQEGQVGHYELVMPQAN
Protein: Uncharacterized protein (Q4GYB0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTEELVQRVVQMQMTSPHFAEYCVAHVTDSKHKFLFDATDSEERRLYCALLQRMRGGFISDESRECAGATAAGTERQRQRHRHRMLTLWQSLSHYFTSAGAAGATTFCSRVAASAAVVYGPHMPHMFRNIKDLAAFVEMVDAAPRGEEHQRAIVQFMRGRLPMTEVFLHVMLQLCDGYVYEAWCMQAQKPVEEMCMRGGKNQKEEEGGSAYGMASRRKDAASWSTNYTAPSDIMVDEAALQKGGTVIFLANMLMAEHETFGRPLRYGAVFEHYILRMVQLLARYAMDGSEALAFVRETVEVWTEGNVFAPATLQDMRDAVGIKANANNHR
Protein: Non-structural maintenance of chromosomes element 1 homolog (Non-SMC element 1 homolog) (EC 2.3.2.27) (Q9D720)
Organism: Mus musculus (Mouse)
Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WV22}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}.
Interaction partners:
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 4
- Non-structural maintenance of chromosomes element 3 homolog
- EP300-interacting inhibitor of differentiation 3
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1B
- Small ubiquitin-related modifier 3
- Structural maintenance of chromosomes protein 1A
Sequence:
MQGSTRRAGAMTDVHRRFLQLLMTHGVLEEWEVRRLQNHCYQVHDRNATVDKLEDFINNINSVLESLYIEIKKGVTEDDGRPIYALVNLATTSVSKMATDFAENELDLFRKALELIVDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQSKWLIEKEGEFTLHGRAILEMEQFIRESYPDSVKMCNICHGLLIQGQSCETCGIRMHLPCVAKYFQSIPEPHCPHCNDYWPHDIPEVYNPEKEREAGISKSSRKSLRTRQH
Protein: Small nuclear ribonucleoprotein Sm D1 (snRNP core protein D1) (Q8JHH1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365054}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein polypeptide F.
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- Elongation factor Tu GTP-binding domain-containing 2.
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein Sm D3.
- Chloride channel, nucleotide-sensitive, 1A.
- Small nuclear ribonucleoprotein polypeptide A'
- Splicing factor 3B subunit 2
Sequence:
MKLVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKNREPTQLESLSIRGNNIRYFILPDSLPLDTLLVDIEPKVKSKKREAVAGRGRGRGRGRGRGRGRGRGGPRR
Protein: Protein MALE DISCOVERER 2 (AtMDIS2) (Probable LRR receptor-like serine/threonine-protein kinase MRH1) (EC 2.7.11.1) (Protein MORPHOGENESIS OF ROOT HAIR 1) (C0LGQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the pollen tube perception of the female signal by binding an unidentified female attractant. May be involved in the regulation of root hairs development.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:26863186}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Kinesin-like protein KIN-UC
- Potassium channel AKT2/3
- Adenine nucleotide alpha hydrolases-like superfamily protein
- Type I inositol polyphosphate 5-phosphatase 5
- Protein LURE 1.6
- COBRA-like protein 9
- Receptor-like kinase
- Myosin-1
- Glycerophosphodiester phosphodiesterase GDPDL3
- MDIS1-interacting receptor like kinase 1
Sequence:
MMGCGFHFPWFFFLIIGLQAPLSLSLTSQGSALLKFRARVNSDPHGTLANWNVSGINDLCYWSGVTCVDGKVQILDLSGYSLEGTLAPELSQLSDLRSLILSRNHFSGGIPKEYGSFENLEVLDLRENDLSGQIPPELSNGLSLKHLLLSGNKFSDDMRIKIVRLQSSYEVRLKKSPKLSPLAVLGCINRKLGHCVSRNRIIQVKKVEAIVFRIKATSRRFLKAFPSFLEETDIYKRRELLEETSNLAAEPAPSAPSPSPGIITEASPRSSGSFPAVTNAKKRRPPLVPPVPSPDKGSTSPDISKNQPQDNKQSKGSKHVWLYVVIAVASFVGLLIIVAVIFFCRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIETFDGYTVYKGTLSSGVEIAVASTAIAESKEWTRAMEMAYRRKIDTLSRINHKNFVNLIGYCEEDDPFNRMMVFEYAPNGTLFEHLHDKETEHLDWSARMRIIMGTAYCLQHMHGMNPPMAHTDFNSSEIYLTDDYAAKVSEIPFNLEARLNPKKHVSGDLEQTSLLLPPEPEANVHSFGVLMLEIISGKLSFSDEYGSIEQWASKYLEKDDLGEMIDPSLKTFKEEELEVICDVIRECLKTEQRQRPSMKDVAEQLKQVINITPEKATPRSSPLWWAELEILSSEAT
Protein: Protein cornichon homolog 4 (Q84W04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Polyubiquitin 3
- Protein trichome birefringence-like 18
Sequence:
MGDIWTWLISFFFLIALVGIIVYQLVCLADLEFDYINPYDSASRINSVVLPEFIVQGVLCVFYLLTGHWFMTLLCLPYLYYNFHLYSKRQHLVDVTEIFNLLNWEKKKRLFKLAYIVLNLFLTIFWMIYSALDDYED
Protein: Polycomb group protein FIE1 (Protein FERTILIZATION-INDEPENDENT ENDOSPERM 1) (OsFIE1) (WD40 repeat-containing protein 154) (OsWD40-154) (Q6ZJW8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They act via the methylation of histones, rendering chromatin heritably changed in its expressibility. Together with EZ1 and CLF forms a complex that is involved in gene transcriptional repression by trimethylation on histone H3 'Lys-27' (H3K27me3) of target genes. Involved in the regulation of embryo and seed endosperm development. FIE1-containing PcG complex in seed endosperm regulates the expression of various transcription factors by trimethylation on histone H3 'Lys-27' (H3K27me3) of target genes. Involved in the overall expression regulation of nutrient metabolism genes, such as prolamin synthesis and seed storage protein synthesis genes. Can regulate valine, leucine and isoleucine metabolism-related genes.
Interaction partners:
- Polycomb group protein EMF2B
- Histone-lysine N-methyltransferase CLF
- Histone-lysine N-methyltransferase EZ1
- Polycomb group protein EMF2A
- Probable lysine-specific demethylase SE14
- Histone-binding protein MSI1
- Os06g0275250 protein
- Os02g0708600 protein
- Os02g0708500 protein
- Os03g0640201 protein
Sequence:
MGPTSRNHKSSQKDVAPNEAKPPRYPQRNRSITASASASAFASPAVANSRVAKERPSSSTAGEGEPQETVLKLPSIPTLPARMAKLVPLEGLGCEAAVGSLTPSREREYKVTNKHTEGRRPVYAIVFNFLDVRYYDIFATACGPRLSTYRCLMNGKFALLQSYLDDDMNESFFTVSWACDIDGNPLLVAAGSTGIIRVINCATEKIYKSLVGHGGSVNEIKSQPSNPSLIISASKDESIKLWNVQTGILILVFGGVGGHRHEVLGVDFHTSDIYRFLSCGMDNTVRIWSMKEFWEYVEKSYSWTDATSKFPTKFVQFPVLCAEIHSNYVDCTKWLGDFVLSKSVENEILLWESITKEENPGEGHIDVLQKYPVPECNIWFMKFSCDFHHNQLAIGNRDGKVYVWKVQTSPPVLIARLNNPQVKSAIRQTAVSFDGSTILACTEDGNIWRWDEVDHPTAPVPSKKQK
Protein: EH domain containing 1 (EH-domain containing 1, isoform CRA_a) (A0A024R571)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004159}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004159}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004159}.
Interaction partners:
Sequence:
MEQPGTAASPVSGSMFSWVSKDARRKKEPELFQTVAEGLRQLYAQKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCAQLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNKADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISPGDFPSLRKMQELLQTQDFSKFQALKPKLLDTVDDMLANDIARLMVMVRQEESLMPSQVVKGGAFDGTMNGPFGHGYGEGAGEGIDDVEWVVGKDKPTYDEIFYTLSPVNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGHELPADLPPHLVPPSKRRHE
Protein: Alkyl/aryl-sulfatase BDS1 (EC 3.1.6.-) (Bacterially-derived sulfatase 1) (Q08347)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alkyl/aryl-sulfatase. Enables the use of SDS and 4-nitrocatechol as sulfur source.
Interaction partners:
- Putative uncharacterized transporter YOL163W
- Dihydroorotate dehydrogenase
- Putative uncharacterized transporter YOL162W
- Uncharacterized protein YOL160W
Sequence:
MIGAFKRNRGSSQSFAKECQPSTLKANLEVAKELPFSDRRDFEDATQGYIGSLSDEQIIGPDGGVVWCMKSYGFLEPETPANTVNPSLWRQAQLNAIHGLFKITDNVYQVRGLDISNMTIIEGNTSLIIIDTLFTTETAQESLKLYYRHRPQKPVRTVIYTHSHSDHYGGVKGIVKEADVKSGEVQIIAPVGFMESVVAENILAGNAMHRRSQYQFGMLLSPSVKGHVDCGIGKAASHGTVTLIAPTIIIEEPVEERTIDGVDFVFQLAPGSEAPSEMLIYMPQQRVLNMAEDVTHHMHNLYALRGVEVRDGNQWAKYIDAARVAFGSKTDVLIAQHHWPTTGQMRINELLKKQRDMYKFIHDQTLRLLNQGYTSRDIAETLRMPSSLEQEWSTRGYYGTLSHNVKAVYQKYLGWYDANPANLNPLPPVAYAKKAVEYMGGADAVLARAYKDFQKGEFRWVASVVNQLVFADPNNHQARELCADALEQLGYQAEASTWRNAYLVGAMELRQGVPKRRSTGKRNNIAVLNNEMFFDFLAVRLNATKAEGKIIVSNWCFINSNERFVITLENCALTYIQGWQTDADATITLKRTTFEALLANEITMVDFLRSKEVEIEGNRLRIEELLKLFDDFDQSFPVVEPMGGST