wanglab/gogpt-training-data huggingface dataset:
Protein: Chorismate synthase (CS) (EC 4.2.3.5) (5-enolpyruvylshikimate-3-phosphate phospholyase) (P0A2Y6)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Interaction partners:
Sequence:
MRYLTAGESHGPRLTAIIEGIPAGLPLTAEDINEDLRRRQGGYGRGGRMKIENDQVVFTSGVRHGKTTGAPITMDVINKDHQKWLDIMSAEDIEDRLKSKRKITHPRPGHADLVGGIKYRFDDLRNSLERSSARETTMRVAVGAVAKRLLAELDMEIANHVVVFGGKEIDVPENLTVAEIKQRAAQSEVSIVNQEREQEIKDYIDQIKRDGDTIGGVVETVVGGVPVGLGSYVQWDRKLDARLAQAVVSINAFKGVEFGLGFEAGYRKGSQVMDEILWSKEDGYTRRTNNLGGFEGGMTNGQPIVVRGVMKPIPTLYKPLMSVDIETHEPYKATVERSDPTALPAAGMVMEAVVATVLAQEILEKFSSDNLEELKEAVAKHRDYTKNY
Protein: CTD kinase subunit beta (CTDK-I subunit beta) (CTD kinase 38 kDa subunit) (CTD kinase subunit 2) (P46962)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK3, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15520468}.
Interaction partners:
- CTD kinase subunit gamma
- CTD kinase subunit alpha
- Serine/threonine-protein kinase BUR1
- DNA-directed RNA polymerase II subunit RPB1
- Protein BUR2
- RNA polymerase II holoenzyme cyclin-like subunit
- Serine/threonine-protein kinase KIN28
- Cyclin CCL1
- Transcription elongation factor SPT5
- RNA polymerase-associated protein LEO1
Sequence:
MPSTFESQLFFSRPFLSKRQIQRAQKNTISDYRNYNQKKLAVFKFLSDLCVQLKFPRKTLETAVYFYQRYHLFNRFETEVCYTVATSCLTLGCKEVETIKKTNDICTLSLRLRNVVKINTDILENFKKRVFQIELRILESCSFDYRVNNYVHIDEYVIKIGRELSFDYKLCNLAWVIAYDALKLETILVIPQHSIALAILKIAYELLDNKNWSSKRYSLFETDEKSVNEAYFDIVNFYINSFDMCDLQRHLPADLLPIGVERFMELKKNAGPESGLPQIPDHLLNADPYITITRDNNVQERRYVLSLELINGESSINSSTRHA
Protein: UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C) (Q9A4F3)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
Interaction partners:
- UvrABC system protein B
- UvrABC system protein A
- Transcription-repair-coupling factor
- DNA 3'-5' helicase
- LexA repressor
- Recombination protein RecR
Sequence:
MTDTPSASDAEAPLRQAAPLWGAALIKDEVTRLPDAPGVYRMIGEADEVLYVGKAKSLKKRVVQYAQGRFHTNRIANMVDATRAMEFITTRTEADALLLEINLIKQLKPRFNVLLRDDKSFPEIVIRRDHDAPQLRKHRGAHTIKGDYFGPFASAWAVNRTLNTLQKAFLLRSCSDSVYDSRDRPCMLYQIKRCAAPCTGLIGKDDYQALVDQAEAFLRGKSRAVMATMAKAMEEAAEELEFERAARLRDRIRALSAVAQETQINPETVEEADVVALHVEGGQACVQVFFFRAGQNWGNRAYFPRITGAADDPEDETVTEEQRIITAFLGQFYDDKPIPRLILANVQPAESELLSEAFALKSGRKVEIAVPKRGEKADLVQHVLTNAREALGRKMAEGSAQTKLLAGVAEAFKLDAPPERIEVYDNSHIQGANAVGGMIVAGPEGFMKGQYRKFNIKSTELTPGDDYGMMKEVLRRRFARLVKEEEEGDDANRPDLVLVDGGQGQLDAAIEIMADLGVDDIAVVGVAKGPDRDAGLERFFIPGQTPFMLEPKSPVLYYLQRLRDEAHRFAIGAHRTRRSMDLKKNPLDEIEGVGPGRKKALLHAFGSAKGVGRASVEDLVKVDGVSQALAERIFGFFRKG
Protein: Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein) (TRP14) (T1SH39)
Organism: Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus)
Function: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide (By similarity). May function as an antioxidant involved in response to viral infection.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BRA2}.
Interaction partners:
Sequence:
MAHYEEVNVRGYDEFCQAVSERKGKDIFAYFSGDKDASGKSWCPDCVTAEPIVRGQMSHLPEGSVFIYCQVGERAYWKDSTNAFKKTLKLSGVPTLLRYGTPQKLVEEECFKADLVRMMFTED
Protein: Tryptophan synthase alpha chain (EC 4.2.1.20) (Q72EU7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Interaction partners:
- indole-3-glycerol-phosphate synthase
- Tryptophan synthase beta chain
- Tryptophan synthase beta chain
- Anthranilate phosphoribosyltransferase
- Anthranilate synthase, glutamine amidotransferase component
- Anthranilate synthase, component I
- N-
- Para-aminobenzoate/anthranilate synthase glutamine amidotransferase
- Para-aminobenzoate synthase, component I
- Serine hydroxymethyltransferase
Sequence:
MSASRLERRIREAQAAGRPALIPFLTAGFPTKERFWDELEALDAAGADIIEVGVPFSDPVADGPVVAAASQRALESGVTLRWIMDGLAARKGRLRAGLVLMGYLNPFMQYGFERFVSDAADAGVAGCIIPDLPLDEDADLRALLAARDMDLIALVGPNTGEGRMREYAAVASGYVYVVSVMGTTGVRDGLPVEVADTLARARQCFSIPVALGFGISRPAQLEGLSHPPDAVIFGSALLRHLDAGGDAASFMKAWAER
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (F8WD24)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPCCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR
Protein: Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) (Protein deglutamylase CCP2) (Q5U5Z8)
Organism: Homo sapiens (Human)
Function: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CDK2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23085998}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23085998}. Note=Colocalizes with gamma-tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. {ECO:0000269|PubMed:23085998}.
Interaction partners:
- Myeloblastin
Sequence:
MFPALETHLKQTIPDPYEDFMYRHLQYYGYFKAQRGSLPNSATHQHVRKNNPQCLLNGSLGEKDDLIPDTLQKEKLLWPISLSSAVHRQIEAINRDFHSCLGWMQWRGLSSLQPPPPRFKDSPASAFRVAGITDSHMLSLPHLRSRQLLYDELDEVNPRLREPQELFSILSTKRPLQAPRWPIECEVIKENIHHIEWAPPQPEYFYQPKGNEKVPEIVGEKKGTVVYQLDSVPIEGSYFTSSRVGGKRGIVKELAVTLQGPEDNTLLFESRFESGNLQKAVRVDTYEYELTLRTDLYTNKHTQWFYFRVQNTRKDATYRFTIVNLLKPKSLYTVGMKPLLYSQLDANTRNIGWRREGNEIKYYKNNTDDGQQPFYCLTWTIQFPYDQDTCFFAHFYPYTYTDLQCYLLSVANNPIQSQFCKLQTLCRSLAGNTVYLLTITNPSQTPQEAAAKKAVVLSARVHPGESNGSWVMKGFLDFILSNSPDAQLLRDIFVFKVLPMLNPDGVIVGNYRCSLAGRDLNRHYKTILKESFPCIWYTRNMIKRLLEEREVLLYCDFHGHSRKNNIFLYGCNNNNRKYWLHERVFPLMLCKNAPDKFSFHSCNFKVQKCKEGTGRVVMWRMGILNSYTMESTFGGSTLGNKRDTHFTIEDLKSLGYHVCDTLLDFCDPDQMKFTQCLAELKELLRQEIHKKFHELGQDVDLEGSWSDISLSDIESSTSGSDSSLSDGLPVHLANIADELTQKKKMFKKKKKKSLQTRKQRNEQYQKKNLMQKLKLTEDTSEKAGFASTLQKQPTFFKNSENSSFLPMKNENPRLNETNLNRRDKDTPLDPSMATLILPKNKGRMQNKKPGFTVSCSPKRTINSSQEPAPGMKPNWPRSRYPATKRGCAAMAAYPSLHIYTYP
Protein: Extracellular ligand-binding receptor (Q13AY2)
Organism: Rhodopseudomonas palustris (strain BisB5)
Interaction partners:
- Inner-membrane translocator
- Inner-membrane translocator
- ABC transporter related
- ABC transporter related
- ABC transporter related
- ABC transporter related
- Inner-membrane translocator
- Inner-membrane translocator
- Inner-membrane translocator
Sequence:
MNRFLTTCLAAAFGLGLAVQAKAAEPIKIGSVLSVTGPAAFLGDPELKTLQLYVEKINQEGGLLGRPVQLIHYDDGSDATKANSFGKRLIEDDKVDVLIGGTTTGSTMSMAPLVDRAGIPFISLAGGVVIVEPVKKWMFKTPHTDRMAAERVFGDMKKRNLTKVALLSETSGFGQSGKKESEAAAARLGITLVANETYGPKDTDMSPQLTNIRSTAGVQALFIFGLGQGPAIANKNAKMLGLSLPIYHAHGVASEEFIKLSDGAAEGIRLPAAALLVASKLPDNDPQKPIALGYAKAYTDRYKEEVSTFGGHAYDALMIMVSAIKRAGDTDKNKVRDAIEQTKDHIGADGKFNMSPTDHMGLDLSAFRILEVRNGDWVLVD
Protein: Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) (P0DTA4)
Organism: Sus scrofa (Pig)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then tranfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate. Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:13752080}.
Interaction partners:
- Propionyl-CoA carboxylase beta chain, mitochondrial
- methylcrotonoyl-CoA carboxylase
- Methylmalonyl-CoA epimerase.
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Ethylmalonyl-CoA decarboxylase
- Acyl-coenzyme A oxidase
- Acyl-CoA synthetase short-chain family member 3, mitochondrial
- Uncharacterized protein
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MAGLWVGGSVLVAAGRRGSRSPRPLMRSVALWTLKHVPQYSRQRLLVSRSLCLAGYDSNEKTFDKILIANRGEIACRVIKTCKKMGIKTVAVHSDVDASSVHVTMADEAVCVGPAPTSKSYLNMDAIMEAVRTTRAQAVHPGYGFLSENKEFAKCLAAEGVIFIGPDTHAIQAMGDKIESKLLAKKAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDSETRRAMGEQAVALAKAVNYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHRQADIPINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSNRMEALKRMENALDNYVIRGVTHNIALLREVIINSRFVEGDINTKFLSDVYPDGFKGHKLTEDERNQLLAIASSLFVASQLRAQRFQEPENSRVPIIKPQVANWELSIRLHDEVHTVTASNSGPTFSVEVDGSKLNVTSTWNLASPLLSVSIDGTQRTIQCLSRDAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKAAEDTSSILHSPMPGVVVAVSVKPGDLVAEGQEICVIEAMKMQNSMTAGKTGKVKSVHCKAGDTVGEGDLLVELE
Protein: Adenylate kinase 3 (AK 3) (EC 2.7.4.3) (ATP-AMP transphosphorylase 3) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase 3) (AMK3) (Q9FK35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18162585}.
Interaction partners:
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Adenosine kinase 1
- Adenosine kinase 2
- AMP deaminase
- Thiamine pyrophosphokinase 1
- At5g66005
- Thiamine pyrophosphokinase 2
- Alkaline-phosphatase-like family protein
- Small ribosomal subunit biogenesis GTPase RsgA 1, mitochondrial
Sequence:
MATSSAASVDMEDIQTVDLMSELLRRMKCASKPDKRLVFIGPPGSGKGTQSPVIKDEFCLCHLSTGDMLRAAVAAKTPLGVKAKEAMDKGELVSDDLVVGIMDEAMNRPKCQKGFILDGFPRTVTQAEKLDEMLNRRGAQIDKVLNFAIDDSVLEERITGRWIHPSSGRSYHTKFAPPKVPGVDDLTGEPLIQRKDDNADVLRSRLDAFHKQTQPVIDYYAKKENLVNIPAEKAPEEVTKVVKKVVST
Protein: E3 SUMO-protein ligase NSE2 (E3 SUMO-protein transferase NSE2) (Non-structural maintenance of chromosomes element 2 homolog) (Q008Y9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDFVSDFSDGRKIKKLLEQSVEQSVEHAVNVVHMKIKHQSLNKAMNQVKNSSATIEEFEEVWKERSKAVEQKRINVKNLDEFKNFVKAVESAAGQAGAEVNDQANGTAYDEDLIMEDSGSEVFSFYDPWSKALIKNPMRNKMCGHIYDRDSVMPIIMDRIGIRCPVLGCANLCYIQPDHLVQDANVQQKIQQSMSNAIVDVTASEEDEE
Protein: Phosphodiesterase (EC 3.1.4.-) (B1AWC8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLHVNDLPPPRRHSWICFDVENGPSPGRSPLDPQAGSSSGLVLHAAFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVRNNFTLLTNLHGAPNKRSPAASQAPVSRVSLQEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRPLTCIMYAIFQERDLLKTFKISSDTFVTYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFQNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSPPLDERSRDCQGLMEKFQFELTLEEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLEETDIDIATEDKSPIDT
Protein: Probable purine permease 18 (AtPUP18) (Q9C508)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- At5g54141/$At5g54141
- General transcription factor 2-related zinc finger protein
- Small ribosomal subunit protein uS15c
- non-specific serine/threonine protein kinase
- Probable S-adenosylmethionine-dependent methyltransferase At5g37970
- Probable inactive receptor kinase At3g02880
- HAT dimerization domain-containing protein
- Cyclase-like protein 1
- Uncharacterized TPR repeat-containing protein At1g05150
- NADPH-dependent diflavin oxidoreductase 1
Sequence:
MEMTEASKQTTAEGSANPEPDQILSPRRSLELKQKKWWISVSLCIFLVLLGDSLVMLLLNFFYVQDNREDSDQDLQYRGTWLQALVQNAAFPLLIPLFFIFPSPKQNQETTNTRFLSFRLILLYISLGVLVAAHSKLFALGKLYANFGVFTLISATQLIFTAIFAAIINRFKFTRWIILSIIGSILIYVFGSPEFGGEPDENEEFYSIQAWLTFAASVAFALSLCLFQLCFEKVLVKTKRYGNKKVFRMVIEMQICVSFVATVVCLVGLFASGENKELQGDSHRFKKGETYYVLSLIGLALSWQVWAVGLMGLVLYVSGVFGDVVHMCTSPLVALFVVLAFDFMDDEFSWPRIGTLIATVVALGSYFYTLHKRNKKKMVELYQTENNIDV
Protein: ATP-dependent DNA helicase (EC 5.6.2.4) (Q55A06)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU364117}.
Interaction partners:
- DNA helicase
- RecQ-like DNA helicase BLM
- DNA topoisomerase 3
- DNA mismatch repair protein Mlh1
- Probable serine/threonine-protein kinase atr1
- Double-strand break repair protein
- Replication protein A subunit
- RecQ-mediated genome instability protein 1
- ATP-dependent DNA helicase ku70
- BRCT domain-containing protein
Sequence:
MDNRPMNKLISRSIFNKTNERSTLSLFQSLNYYYKRDFTSEINKTNNNFDNCQNNEEGYNVINNNKKNKNNSNNNNVEYNENDNSNNNNNNNKNEINNNEIDFDWSMKAKKKIKKSVLTGEDRLDKKTKDLKYLNSIGLLVKLKSTTISNNEISDNSNNNNLKDKENDEIETIALIDEDNEISTIKKKKKIKTNKNSYDDDNIDNESNDYTTTIIQNEDHNTFSSTTTTTRGSIKNKRNKSLKKEEIQKQHEENQDNNHDKISIEYDENELKKTYNLDENGDNIVEMSPAFKNNNLLIKKSKNKKTKQSNIDIDNDNDNVDNYIDNDDDDETIDKPKKSKSKSTTKSKKINVKKQDDENEEEEEDEDEEKEFKSIEISKLKKKKKEIKDGEYLNIKNVYKEWLESPIVIKLSNDDSCFTNSKIKINPKSFTIKSDDDDDGNGNGNGNGNDNDKNNLKLKREWHELVETCNRDIFGNKEFRNLQIEAINSILHDRDTFVSLPTGGGKSLCFQIPSIVDHRGVTFVISPLLALMQDQVHKLKSLGIPAESINSSGSQRENRDVLDQLLNGETCKLKLIYITPERLAQSEFLHLLDQLYDQGRLRRLVVDEAHCISEWGHSFRPKYRLISTFRDRFPSVPISAFTASATPNVEIDIKNSLKMVNPITINSSFLRPNLLYQVRQKQSDEESLLKDIYNFISFKYPNSTGIIYCATVRECEIVADYLSERGLSSNFYHAKLSNTQRSKLQKDWTNGEFKIVCTTIAFGMGIDKGDTRFVIHHSMPQSMESYYQQTGRAGRDGKHSDCLLFYNKSDLMRFKHIISLNQPKDPFNAFSNYNGVGIGDIGGEHLILDNDGNYISNYSSDESQYMDTIKNKIQQTSTKLEMLDSVASFCSTQSKCRRVTLLNYFGENSKSCGNMCDICISNSNSNSNNRSKAKQNQIDYSERIYNRNSYSISSFKNKKKKSHVSYDNDNDVD
Protein: Uncharacterized protein (Q38BW0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MERVTLSAPFNGRRLLSNESLVESQEARKGGLSSNKFPGRGRSVEPPLQSQDKDPTIKKPTALVMAPLGNTGLALPRLPTVPVPNVRRRIFKRPSLHIPVGTLEPVINLRQLKKVGEQVGRRHGEHTLSRNTEVGTEWKTGSGVGELANAKKSLRPRTALESPTAARRRAQSETIADPFTIRREGCVSLGLSQGLKSGSVLAHTLSSMRPRSTVVDGLVCSSLRQQEQPEGVFASECGGIMGYGATATTNALFSSSNSPNKITDETSGMCMSDSFSGGSSSGDGSDIEDLDDEGNSRPHSCFGDRIVISVSSGNNRGGRYFTHESKIRDISRRVAYNNFLDEEDIPVVSTRSLVRRPNGTRVTMKEGIKEDGIPSTTQ
Protein: Nucleolin 2 (Protein NUCLEOLIN LIKE 2) (AtNUC-L2) (Protein PARALLEL LIKE 1) (AtPARLL1) (Q1PEP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-rRNA processing and ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17108323, ECO:0000269|PubMed:27792779}.
Interaction partners:
- Protein THALLO
- M phase phosphoprotein 10
- Protein NUCLEOLAR FACTOR 1
- MATH domain and coiled-coil domain-containing protein At3g29580
- F-box/LRR-repeat protein At3g59250
- F-box/kelch-repeat protein At3g44120
- Putative F-box protein At1g64540
- U-box domain-containing protein 54
- Putative pumilio homolog 8, chloroplastic
- rRNA 2'-O-methyltransferase fibrillarin 2
Sequence:
MGKSSKKSVTEVETPASMTKPLKKGKRDAEEDLDMQVTKKQKKELIDVVQKEKAEKTVPKKVESSSSDASDSDEEEKTKETPSKLKDESSSEEEDDSSSDEEIAPAKKRPEPIKKAKVESSSSDDDSTSDEETAPVKKQPAVLEKAKVESSSSDDDSSSDEETVPVKKQPAVLEKAKIESSSSDDDSSSDEETVPMKKQTAVLEKAKAESSSSDDGSSSDEEPTPAKKEPIVVKKDSSDESSSDEETPVVKKKPTTVVKDAKAESSSSEEESSSDDEPTPAKKPTVVKNAKPAAKDSSSSEEDSDEEESDDEKPPTKKAKVSSKTSKQESSSDESSDESDKEESKDEKVTPKKKDSDVEMVDAEQKSNAKQPKTPTNQTQGGSKTLFAGNLSYQIARSDIENFFKEAGEVVDVRLSSFDDGSFKGYGHIEFASPEEAQKALEMNGKLLLGRDVRLDLANERGTPRNSNPGRKGEGSQSRTIYVRGFSSSLGEDEIKKELRSHFSKCGEVTRVHVPTDRETGASRGFAYIDLTSGFDEALQLSGSEIGGGNIHVEESRPRDSDEGRSSNRAPARGAPRGRHSDRAPRGGRFSDRAPRGRHSDRGAPRGRFSTRGRGPSKPSVMESSKGTKTVFNDEE
Protein: Neurobeachin-like protein 2 (Q6ZNJ1)
Organism: Homo sapiens (Human)
Function: Probably involved in thrombopoiesis. Plays a role in the development or secretion of alpha-granules, that contain several growth factors important for platelet biogenesis.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21765412}.
Interaction partners:
- Spermatogenesis-defective protein 39 homolog
Sequence:
MAASERLYELWLLYYAQKDLGYLQQWLKAFVGAFKKSISLSSLEPRRPEEAGAEVPLLPLDELHVLAEQLHQADLEQALLLLKLFIILCRNLENIEAGRGQVLVPRVLALLTKLVAELKGCPPPQGRGTQLENVALHALLLCEGLFDPYQTWRRQRSGEVISSKEKSKYKFPPAALPQEFSAFFQESLQNADHLPPILLLRLIHLFCAVLAGGKENGQMAVSDGSVKGLLSVVRGWSRGPAPDPCLVPLALEALVGAVHVLHASRAPPRGPELRALLESYFHVLNADWPAGLSSGPEEALVTLRVSMLDAIPMMLACEDRPVLQATFLSNNCFEHLTRLIQNSKLYLQSRAPPEGDSDLATRLLTEPDVQKVLDQDTDAIAVHVVRVLTCIMSDSPSAKEVFKERIGYPHLQEVLQSHGPPTHRLLQELLNMAVEGDHSMCPPPPIRNEQPVLVLAQWLPSLPTAELRLFLAQRLRWLCDSCPASRATCVQAGLVGCLLETLSTGLALEARCQEQLLALLQALGRVSIRPMELRHLLRPRPGLDSEPGGAEAGKARHAGAVIRTLSGMARHQGPARALRYFDLTPSMAGIMVPPVQRWPGPGFTFHAWLCLHPMDTAPTPAPTRPLQRKQLYSFFTSSGSGFEAFFTAAGTLVVAVCTRKEYLTMSLPEVSFADSAWHCVAIVHVPGRRPFSQNLVHVYKDGHLVKTAPLRCPSLSEPFSSCCIGSAGYRTTTTTTGLPTPPVPATLAYTHPALTRSQSVPASTGLGWGSGLVAPLQEGSIDSTLAGTQDTRWGSPTSLEGELGAVAIFHEALQATALRTLCTLGPNETAPFKPEGELHELSTRLLLHYSPQACKNNICLDLSPSHGLDGRLTGHRVETWDVKDVVNCVGGMGALLPLLERVAAQPKEAEAGPAETHDLVGPELTSGHNTQGLVLPLGKSSEERMERNAVAAFLLMLRNFLQGHMVNQESLVQCQGPAIIGALLRKVPSWAMDMNVLMSAQLLMEQVAAEGSGPLLYLLYQHLLFNFHLWTLSDFAVRLGHIQYMSSIVREHRQKLRKKYGVQFILDALRTHYSPQRERPLAADDLRTVQTSLLGLAREFLVRSLSADDVQVTQTMLSFLAATGDDGQAVGALDLLLALLHGSLVQESLAVFLLEPGNLEVLLALLVRPGSLPLLPDRVCKILRRLQQNERLPERSRQRLRLRECGLQGLVACLPEGTVSPQLCQGLYKLFLGADCLNLSDLLAVVQLSLQADLSVRLDICRQLFHLIYGQPDVVRLLARQAGWQDVLTRLYVLEAATAGSPPPSSPESPTSPKPAPPKPPTESPAEPSDVFLPSEAPCPDPDGFYHALSPFCTPFDLGLERSSVGSGNTAGGGGSSGTLTPASQPGTPSPLDGPRPFPAAPGRHSSSLSNVLEDGSLPEPTISGDDTSNTSNPQQTSEEELCNLLTNVLFSVTWRGVEGSDEAAWRERGQVFSVLTQLGASATLVRPPDCIKRSLLEMMLESALTDIKEAPVGVLASLTQQALWLLRLLQDFLCAEGHGNQELWSEKLFEGVCSLLDRLGAWPHLANGTADLREMAQIGLRLVLGYILLEDPQLHAQAYVRLHMLLQTAVPARREEACYVLSKLEAALGRVLNTSSLESATDEAGSPLAAAAAAAAAERCSWLVPLVRTLLDRAYEPLGLQWGLPSLPPTNGSPTFFEDFQAFCATPEWRHFIDKQVQPTMSQFEMDTYAKSHDLMSGFWNACYDMLMSSGQRRQWERAQSRRAFQELVLEPAQRRARLEGLRYTAVLKQQATQHSMALLHWGALWRQLASPCGAWALRDTPIPRWKLSSAETYSRMRLKLVPNHHFDPHLEASALRDNLGEVPLTPTEEASLPLAVTKEAKVSTPPELLQEDQLGEDELAELETPMEAAELDEQREKLVLSAECQLVTVVAVVPGLLEVTTQNVYFYDGSTERVETEEGIGYDFRRPLAQLREVHLRRFNLRRSALELFFIDQANYFLNFPCKVGTTPVSSPSQTPRPQPGPIPPHTQVRNQVYSWLLRLRPPSQGYLSSRSPQEMLRASGLTQKWVQREISNFEYLMQLNTIAGRTYNDLSQYPVFPWVLQDYVSPTLDLSNPAVFRDLSKPIGVVNPKHAQLVREKYESFEDPAGTIDKFHYGTHYSNAAGVMHYLIRVEPFTSLHVQLQSGRFDCSDRQFHSVAAAWQARLESPADVKELIPEFFYFPDFLENQNGFDLGCLQLTNEKVGDVVLPPWASSPEDFIQQHRQALESEYVSAHLHEWIDLIFGYKQRGPAAEEALNVFYYCTYEGAVDLDHVTDERERKALEGIISNFGQTPCQLLKEPHPTRLSAEEAAHRLARLDTNSPSIFQHLDELKAFFAEVVSDGVPLVLALVPHRQPHSFITQGSPDLLVTVSASGLLGTHSWLPYDRNISNYFSFSKDPTMGSHKTQRLLSGPWVPGSGVSGQALAVAPDGKLLFSGGHWDGSLRVTALPRGKLLSQLSCHLDVVTCLALDTCGIYLISGSRDTTCMVWRLLHQGGLSVGLAPKPVQVLYGHGAAVSCVAISTELDMAVSGSEDGTVIIHTVRRGQFVAALRPLGATFPGPIFHLALGSEGQIVVQSSAWERPGAQVTYSLHLYSVNGKLRASLPLAEQPTALTVTEDFVLLGTAQCALHILQLNTLLPAAPPLPMKVAIRSVAVTKERSHVLVGLEDGKLIVVVAGQPSEVRSSQFARKLWRSSRRISQVSSGETEYNPTEAR
Protein: Peroxisomal membrane protein PEX14 (Peroxin-14) (Q4QBZ9)
Organism: Leishmania major
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271, ECO:0000256|RuleBase:RU367032}.
Interaction partners:
- Putative peroxisome targeting signal 1 receptor
- Peroxin-13
- Peroxin-7
- Peroxin 19
- Peroxin-12
- Peroxisomal ATPase PEX6
- propanoyl-CoA C-acyltransferase
- Putative sterol carrier protein
- RING-type E3 ubiquitin transferase
- AAA+ ATPase domain-containing protein
Sequence:
MAAEVPSQPQAALEAPLPEPEQPSLSELDADTTVQSAIRFLQDPRVRCSPVESQIRFLKGKGVSDGQIKYALAKVGRTVTAEKIASVRAPLANAAPTGATATAYATPLSAQLKTARQNAPVAMTPGPQYTQMLFPHSPPPPQVERQTKTVDWRDVVIGAGAAMLAGFSAYKLFNRYSPYEFRRKSDKKPRLYRGSSSRPRPANIASSGSETDASSTPQRGCVLPLPPPPPMAAAAEPSVSAASPAALTEEVKRLQTELDEAKEALANERKKCADLAVSAAKIRADKQQLSRANDRLTQQIDGLKKDIESLEGKKSSAVGEATQTAAEGAVAAVPAPPSTYFPSVTTEGEQARNSAEVTSVTSASAPNSDVMPVLPVVPSPEATAIAAAAPAMPDPITEAAQAAPASVAAVAPAPESPPAVFAASTPYVDAAAPVATVTEVAAPLLSIGSAEPPKAGDGTPMSTG
Protein: RAB guanine nucleotide exchange factor 1 (E9PFK9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASSYHEVVSRKKMSLKSERRGIHVDQSDLLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGSKKEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEGMHYKRDLSIEEQSECAQDFYHNVAERMQTRGKVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALRWVTPQMLCVPVNEDIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQEAESWSPDACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAREVQDIVEKYPLEIKPPNQPLAAIDSENVENDKLPPPLQPQVYAG
Protein: Multiple C2 domain and transmembrane region protein 10 (O64492)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 16 kDa phloem protein 2
Sequence:
MTEAKTGTGNERLVVEIVGAHNLMPKDGEDSSSPFVEVQFENQRLRTKVKPKDLNPIWNEKLVFHVIDVNDLRHKALEINVYNEKRSSNSRNFLGKVRVLGSSVGREGESVVQLYTLEKRSLFSSVRGEISVKHYMTTTAENGENVRRVNRSGGSKKSKKVQNVSSSMAIQQQQQQQQQQISLHNHNRGNQQQSQQNGQGQRMLPFYPHQSEIKPLVITALPSPMPGPGPRPIVYSNGSSEFSLKETKPCLGGTSNGLGGLSSHKDKTSSTYDLVEQMQYLYVNIVKAKDLSVLGEVVSEVKLGNYRGVTKKVSSNSSNPEWNQVFVFSKERIQSSVVELFVKEGNKDEYTGRVLFDLSEIPTRVPPDSPLAPQWYKIENRNGGRGNGELMVSVWFGTQADEAFAEAWHSKAGNVHIEELSSIKSKVYLSPKLWYLRISVIEAQDVAIMDKGSSLMRFPELSAKLQVGSQILRTAIASAIPTKSFSNPYWNEDLMFVVAEPFEDCVTVVVEDRLNGGAIGGQNDVAVGRVQIPISAVERRTGDTLVGSRWFSLDNGNNNNRFGSRIHLRLSLDGGYHVLDEATMYNSDVRPTAKELWKPQVGLLEIGILSATGLMPMKVRDGKCGGIADSYCVAKYGPKWVRTRTVVDSLCPKWNEQYTWEVYDPCTVVTVGVFDNARVNENNNSRDVRIGKVRIRLSTLETGRVYTHSYPLIVLHPSGVKKTGELHLAVRLSCGNAVNMLHMYALPLLPKMHYTQPLGVHMLERLRYQTLNAVAARLSRAEPPLGREVVEYMLDHDFHVWSMRRSKANFFRLVNVISGLVAVAKLVEVMRSWSKPVYSTVFVLAFLFMVLFPELLLPCLLLYTAAVGVWRFRRRSRYPPHMDARISHAETVFPDELDEEFDTFPTSRGFDVVRMRYDRVRSIAGRVQTVVGDMASQGERVQALLSWRDPRATFLFLMFCLLAAVGFYTVPVKLTVAISGLYYLRPPRFRRKLPSRGLSFFRRLPSRADSLL