wanglab/gogpt-training-data huggingface dataset:
Protein: Sal-like protein 4 (Zinc finger transcription factor 24hpf) (A0MWC1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQSKPQHINSDDPASTENGILHNSQSEEEGSDAKRRRSEETRVCEKCCAEFFDEAEFLEHERNCTKSQQVVIMKDGDGSEVPPEFSQRSPGDVLSDPCDQSTNSYSKHGAESDEMMEGEFMLNQDNPSNHDQEVSGSPGYVASSKLQDSNVTLESMAATKVAVTQHSSNSSSQKSPPPQPHQDTLLAIPMILEQLVSLQQQQLQQIQLTEQIRIQVAMVAPPSLHAAVGAVMDPLKALGAHLSQQLSAAAALIGKRTGSQSLSLEALKQAKLPQSATIPTSLPGGLGSIPLKPDLKGLPDLASRLPALLPQSPGVIGLQSPFNNLATSMDPSKKAKTKGPVVSEPPKNVSVEHSFKHKCKFCGKTFGNDSALQIHLRSHTGERPFKCNICGNRFTTKGNLKVHFQRHKEKYPHIKMNPHPVPEHLDNMPSNNGIPYGMSVPMEENGFSETKPVLGVPTTGPPAGPHPPVLQAFKPSFDIPAAGDPYSQRPSSSGSDGASISSGMFGQDIAGSDQSKDSPDAMVGLHHINGNSLTGENGSGTAKLQQMVDCLEKRTNDPNECVICHRVLSCQSSLKMHYRTHTGERPYKCKICGRAFSTKGNLKAHYGVHRANTPLKMQHSCPICHKKFTNAVVLQQHIRMHMGGQIPNTPLPENQFESPEALDSSMTEDKTIDSNGHEESMEEQDFELDNQEKLNYSTGPQPVTKDDQTFPGQPSMFTGITALENHMKNLTSALNLQRQSSTASESDSGLKDSPLGSGEVDYKNDRSPVVSDSVSFHSLSPIDGPPSNGPSKSPESTNLDDSVKSRPDTDAPQDFSENNGALDLTSSFTSKPIKEEPGLSFASGEYGSSQLPFMRVPPSLVKLEMQIPPETPMGAHGLYSSQLPQGAATPPASSSAPRRSTKQHLCNMCGKNFSSASALQIHERTHTGEKPFACSICGRAFTTKGNLKVHVGTHMWNNTARRGQRLSLDNPMALMAMGNEPKMMPDMLPPPKDLIPPPINFDPSMWNQYAAAFTNGLTMKTNEISVIQNGGIPLPGSLGGPLVGSTGGITKMESSQMGIPGTVAEMEKNGSESIAKFPHFMEEGKVN
Protein: FACT complex subunit Ssrp1 (Chorion-factor 5) (Facilitates chromatin transcription complex subunit Ssrp1) (Recombination signal sequence recognition protein) (Single-strand recognition protein) (dSSRP1) (Q05344)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to single-stranded DNA and RNA with highest affinity for nucleotides G and U. The FACT complex is required for expression of Hox genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:12934007, ECO:0000303|PubMed:10199952}. Chromosome {ECO:0000269|PubMed:12934007, ECO:0000303|PubMed:10199952}. Nucleus, nucleolus {ECO:0000269|PubMed:12934007}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000269|PubMed:12934007}.
Interaction partners:
- FACT complex subunit spt16
- RNA polymerase II-associated factor 1 homolog
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- Transcription elongation factor SPT6
- Hyrax
- DNA-directed RNA polymerase II subunit RPB3
- Ctr9, isoform A
- FI06213p
- Chromodomain-helicase-DNA-binding protein 1
Sequence:
MTDSLEYNDINAEVRGVLCSGRLKMTEQNIIFKNTKTGKVEQISAEDIDLINSQKFVGTWGLRVFTKGGVLHRFTGFRDSEHEKLGKFIKAAYSQEMVEKEMCVKGWNWGTARFMGSVLSFDKESKTIFEVPLSHVSQCVTGKNEVTLEFHQNDDAPVGLLEMRFHIPAVESAEEDPVDKFHQNVMSKASVISASGESIAIFREIQILTPRGRYDIKIFSTFFQLHGKTFDYKIPMDSVLRLFMLPHKDSRQMFFVLSLDPPIKQGQTRYHYLVLLFAPDEETTIELPFSEAELRDKYEGKLEKEISGPVYEVMGKVMKVLIGRKITGPGNFIGHSGTAAVGCSFKAAAGYLYPLERGFIYIHKPPLHIRFEEISSVNFARSGGSTRSFDFEVTLKNGTVHIFSSIEKEEYAKLFDYITQKKLHVSNMGKDKSGYKDVDFGDSDNENEPDAYLARLKAEAREKEEDDDDGDSDEESTDEDFKPNENESDVAEEYDSNVESDSDDDSDASGGGGDSDGAKKKKEKKSEKKEKKEKKHKEKERTKKPSKKKKDSGKPKRATTAFMLWLNDTRESIKRENPGIKVTEIAKKGGEMWKELKDKSKWEDAAAKDKQRYHDEMRNYKPEAGGDSDNEKGGKSSKKRKTEPSPSKKANTSGSGFKSKEYISDDDSTSSDDEKDNEPAKKKSKPPSDGDAKKKKAKSESEPEESEEDSNASDEDEEDEASD
Protein: Transcription activator of gluconeogenesis ERT1 (Ethanol regulator of translation 1) (P38140)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes like PCK1. Involved in restriction of Ty1 transposition.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein SIP4
Sequence:
MCTPDENDYKTSTDPDTSANTNHTLEKKKRKKRKNTNVACVNCSRLHVSCEAKRPCLRCISKGLTATCVDAPRKKSKYLAGIPNRELPMNIQPDLPPRKIMIPIYNNSSNSSLNVNNMGEQQKFTSPQHIVHKAKFLSNAADSEYSILSNIIYQDTLSNKIPIDILYSNTNSTSNSTIGNSSNNSPTGTNTSPEETEMEKIRQLYSEQRANIPPHPYPSSNQNVYSILLGPNSAKIVASQVNLFANHFPLVPVDSADNSLNFKRLLPRDPSEKSSQINWDSSINQYYLNSETVTFPELAIPLKRRKNHLVSVSLESCSPDAANIKSNVEWEHSLRYSTPMEIYTSINAPFSHTPGFHHLLVYLKHRFNQQDLVKMCRSIAEFRPIFIACSVTLTEEDMIFMEQCYQRTLLEYVKFIAQIGTPTCIWRRNGQISYVNEEFEILCGWTREELLNKMTFIVEIMDDESVRDYFKTLSKVAYRDFRGSEKMKVCRLLSPIKGKIIHCCCMWTLKRDVSGLPLMILGNFMPILN
Protein: Lovastatin nonaketide synthase, enoyl reductase component lovC (EC 2.3.1.161) (Lovastatin biosynthesis cluster protein C) (Trans-enoyl reductase lovC) (Q9Y7D0)
Organism: Aspergillus terreus
Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
Sequence:
MGDQPFIPPPQQTALTVNDHDEVTVWNAAPCPMLPRDQVYVRVEAVAINPSDTKMRGQFATPWAFLGTDYAGTVVAVGSDVTHIQVGDRVYGAQNEMCPRTPDQGAFSQYTVTRGRVWAKIPKGLSFEQAAALPAGISTAGLAMKLLGLPLPSPSADQPPTHSKPVYVLVYGGSTATATVTMQMLRLSGYIPIATCSPHNFDLAKSRGAEEVFDYRAPNLAQTIRTYTKNNLRYALDCITNVESTTFCFAAIGRAGGHYVSLNPFPEHAATRKMVTTDWTLGPTIFGEGSTWPAPYGRPGSEEERQFGEDLWRIAGQLVEDGRLVHHPLRVVQGGFDHIKQGMELVRKGELSGEKLVVRLEGP
Protein: Origin of replication complex subunit 1A (AtORC1a) (Origin recognition complex subunit 1a) (Q710E8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication (By similarity). H3K4me3 effector that regulates positively the transcription of a subset of genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P54789}.
Interaction partners:
- Origin of replication complex subunit 3
- Origin of replication complex subunit 5
- Origin of replication complex subunit 2
- DNA replication licensing factor MCM5
- Origin of replication complex subunit 6
- CDT1-like protein b
- DNA replication licensing factor MCM3
- CDT1-like protein a, chloroplastic
- Origin of replication complex subunit 4
- DNA replication licensing factor MCM4
Sequence:
MASSLSSKAKTFKSPTKTPTKMYRKSYLSPSSTSLTPPQTPETLTPLRRSSRHVSRKINLGNDPIDLPGKESVEEINLIRKPRKRTNDIVVAEKSKKKKIDPEVSFSPVSPIRSETKKTKKKKRVYYNKVEFDETEFEIGDDVYVKRTEDANPDEEEEEDPEIEDCQICFKSHTNTIMIECDDCLGGFHLNCLKPPLKEVPEGDWICQFCEVKKSGQTLVVVPKPPEGKKLARTMKEKLLSSDLWAARIEKLWKEVDDGVYWIRARWYMIPEETVLGRQRHNLKRELYLTNDFADIEMECVLRHCFVKCPKEFSKASNDGDDVFLCEYEYDVHWGSFKRVAELADGDEDSDQEWNGRKEEEIDYSDEEIEFDDEESVRGVSKSKRGGANSRKGRFFGLEKVGMKRIPEHVRCHKQSELEKAKATLLLATRPKSLPCRSKEMEEITAFIKGSISDDQCLGRCMYIHGVPGTGKTISVLSVMKNLKAEVEAGSVSPYCFVEINGLKLASPENIYSVIYEGLSGHRVGWKKALQSLNERFAEGKKIGKENEKPCILLIDELDVLVTRNQSVLYNILDWPTKPNSKLVVLGIANTMDLPEKLLPRISSRMGIQRLCFGPYNHRQLQEIISTRLEGINAFEKTAIEFASRKVAAISGDARRALEICRRAAEVADYRLKKSNISAKSQLVIMADVEVAIQEMFQAPHIQVMKSVSKLSRIFLTAMVHELYKTGMAETSFDRVATTVSSICLTNGEAFPGWDILLKIGCDLGECRIVLCEPGEKHRLQKLQLNFPSDDVAFALKDNKDLPWLANYL
Protein: Nitrite oxidoreductase subunit C (Q1PZD4)
Organism: Kuenenia stuttgartiensis
Interaction partners:
Sequence:
MKKFYRLLGSSSVALLGCLFLSVALCIAEEAEGVKGVAEEELTPAKEVLNVKYMQIDVPAHITVGALEGAFKNAEGVQVKLQKQDKAFPNGGGSVNSAEIKAIHDGITIYFQVIWDDATDNKQAIATQEFRDGAALMFPLGKITISPEEPFSPRMGDRQKPVNLWHWKADWEADLLATGGIEECPARYPNMHDDFSTNPHSVNYHKGVIQSAAELSGGYAAHNLLSLPRGRAVEDLNAEGFGTLTSQDHQDVDGCSKFENKKWTVVFCRSLNTGDPLDVQFVPGESTYFNMAVWNGDREDRNGQKNISIQWHPLSLERIAWQ
Protein: Exosome complex component MTR3 (mRNA transport regulator 3) (P48240)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. MTR3 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Subcellular location: Cytoplasm. Nucleus, nucleolus.
Interaction partners:
- Exosome complex component RRP4
- Exosome complex component CSL4
- Exosome complex exonuclease RRP6
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
- Superkiller protein 7
- Exosome complex component RRP46
- Exosome complex component RRP40
- Exosome complex component RRP45
- M-phase phosphoprotein 6 homolog
Sequence:
MNVQDRRRLLGPAAAKPMAFSNTTTHVPEKKSTDLTPKGNESEQELSLHTGFIENCNGSALVEARSLGHQTSLITAVYGPRSIRGSFTSQGTISIQLKNGLLEKYNTNELKEVSSFLMGIFNSVVNLSRYPKSGIDIFVYLTYDKDLTNNPQDDDSQSKMMSSQISSLIPHCITSITLALADAGIELVDMAGAGEANGTVVSFIKNGEEIVGFWKDDGDDEDLLECLDRCKEQYNRYRDLMISCLMNQET
Protein: HL01686p (Q8MSD6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQAMRESIDGMQQVYDATARKSYALDPHSVVTTSSTVSLLMKPTAAVGLTYAEVLSGQASPVSSGNESVTNSRPERDPSTTTTTTTTTATKTTARTTAATERNAFE
Protein: Tuberoinfundibular peptide of 39 residues (TIP39) (Parathyroid hormone 2) (Q91W27)
Organism: Mus musculus (Mouse)
Function: Plays a role as a potent and selective agonist of PTH2R resulting in adenyl cyclase activation and intracellular calcium levels elevation. Induces protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. May inhibit cell proliferation via its action of PTH2R activation. Neuropeptide which may also have a role in spermatogenesis. May activate nociceptors and nociceptive circuits.
Subcellular location: Secreted.
Interaction partners:
- Parathyroid hormone 2 receptor
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone
- Parathyroid hormone-related protein
Sequence:
METCQMSRSPRERLLLLLLLLLLVPWGTGPASGVALPLAGVFSLRAPGRAWAGLGSPLSRRSLALADDAAFRERARLLAALERRRWLDSYMQKLLLLDAP
Protein: Lycopene beta-cyclase (Q4W8B7)
Organism: Brevundimonas sp. NBRC 101024
Interaction partners:
Sequence:
MQAAAPDSSAPDLLLLGGGLANGLLALRLSQVRPELDVRIVEAADRLGGIHTWSFFEADLTPAQRAWIAPLIACRWPGYSVRFPAFERRLVTGYCSVTAERFAEAVTQALAGRIVTGAAVVSAGPTEAVLADGHRLTARAVIDGRGPTAAPDLALGFQKFVGLEVRLTAPHGLKEPIVMDACVDQSGGYRFLYVLPFDDRTLLIEDTRYTDGDDLDHDLFRTGVRDYAAQRGWVIETVLREEEGVLPVALDGDIAAHLKRLGPTALSGLRAGLFHPTTGYSLPDAVRLADHLAERIEAAPDGPALAQVIRRHARDVWAQRGFYRLLNRMLFRAARPDQRYRVLERFYRLPQPLIERFYAGETTLADKARILSGKPPVPIGAALTCLVERGRA
Protein: V-type proton ATPase subunit a2 (V-ATPase subunit a2) (V-type proton ATPase 95 kDa subunit a isoform 2) (V-ATPase 95 kDa isoform a2) (Vacuolar H(+)-ATPase subunit a isoform 2) (Vacuolar proton pump subunit a2) (Vacuolar proton translocating ATPase 95 kDa subunit a isoform 2) (Q9SJT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Involved in vacuolar nutrient storage (e.g. accumulation and storage of nitrate) and in tolerance to some toxic ions (e.g. zinc ions sequestration in vacuoles).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15653794, ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873, ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:18441211}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:15653794, ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873, ECO:0000269|PubMed:18441211}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit c''2
Sequence:
MAESHGGGGGCCPPMDLMRSEPMQLVQVIVPMESAHLTVSYLGDLGLVQFKDLNSEKSPFQRTYAAQIKRCGEMARKIRFFKEQMSKAGVTPKETLDRENDIDLDDVEVKLEELEAELVEINANNDKLQRSYNELVEYKLVLEKAGEFFASAHRSATAQQSEIETEQVGEDLLEAPLLQEEKSVDPTKQVKLGFLTGLVPREKSMVFERILFRATRGNIFIRQSVIEESVVDPNSGEKAEKNVFVVFYSGERAKSKILKICEAFGANRYPFSEDLGKQAQMMTEVSGRLSELKTTIGAGLDQRNILLETIGDKFEQWNLKIRKEKAIYHTLNMLSLDVTKKCLVGEGWSPVFAATEIQDALHRAAVDSNSQVGSIFQVLRTKEMPPTFFRTNKFTTAFQEIVDAYGVAKYQEANPSVFTIVTFPFLFAVMFGDWGHGICLLLATMYLILREKKLSSQKLGDIMEMAFGGRYVIFMMSLFSIYTGLIYNEFFSIPYPLFASSAYDCRDVSCSEATTIGLIKTRDTYPFGVDPVWHGTRSELPFLNSLKMKMSILIGVAQMNLGIIMSFFNAKFFKSAVNIWFQFVPQMIFLNCLFGYLSVLIIIKWCTGSQADLYHVMIYMFLSPMDDLGENQLFPNQKIVQLTFLFLALVSVPWMLLPKPFILKKQHEARHQGLSYAQLDETDESLQVETNGGGHGHEEFEFSEIFVHQLIHTIEFVLGAVSNTASYLRLWALSLAHSELSSVFYEKVLLMAWGFNNVFIWIVGILVFIFATVGVLLVMETLSAFLHALRLHWVEYQNKFYEGDGYKFAPFTFTLVGNEDE
Protein: HTH-type transcriptional regulator GalS (Mgl repressor and galactose ultrainduction factor) (P25748)
Organism: Escherichia coli (strain K12)
Function: Repressor of the mgl operon. Binds galactose and D-fucose as inducers. GalS binds to an operator DNA sequence within its own coding sequence (corresponding to residues 15 to 20).
Interaction partners:
- Galactose/methyl galactoside import ATP-binding protein MglA
- D-galactose/methyl-galactoside binding periplasmic protein MglB
- HTH-type transcriptional regulator GalR
- Galactose-proton symporter
Sequence:
MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFMPTLVRRHSVATRQNAAAITNSTNQAM
Protein: Sol1p (Q59ST9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SCF ubiquitin ligase complex subunit
Sequence:
MSSSNDTPSLFVTPQTPPRQQQRRKSNTGAISTPVASSVLLTPSTTTKKPTRTPVSQKRKQGVQLSPPQANKFPFTPITPQKSPCKTRKNLDLFTSNEKFGLLLPSPSTIGSGRCHNSFTQAPPPLFDLKKVNEFKVPKTPAKQIIDNSRTKESENEDDWEVMDIDEVAKIPRAKLRNPFIDTFEPTSPVTPEESTGDRINYDTHMELINSKTGKKRVVKLTKNQMKIKPKRLSFDNI
Protein: Mitogen-activated protein kinase 8 interacting protein 1 (E9PBB9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQLVLKMDSSPDNDSWLEDQWERWLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
Protein: Nurim (Nuclear envelope membrane protein) (Nuclear rim protein) (Q8VC65)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Delta
Sequence:
MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARHGWLAALQDRSILASLAWDLCLLLLFVVQHSLMATEAVKAWTSRYFGVLQRSLYVACTALALQLVMRYWETTPRGPVLWEARAEPWATWVPLLCFVLHVVSWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLSLKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLFTLYLGLAHGLDQQDLRYLRSQLQRKLHLLSRPQDGEAE
Protein: 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16) (O34002)
Organism: Antarctic bacterium DS2-3R
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.
Interaction partners:
Sequence:
MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGLYNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTAHIMEQVADNALIRPLSEYNGPEQRQVP
Protein: Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase) (mtKAS) (O94297)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Putative acyl carrier protein, mitochondrial
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Fatty acid synthase subunit alpha
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Uncharacterized acyltransferase C1851.02
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Putative fatty acid elongase 2
- Putative fatty acid elongase 1
- Cytosolic Fe-S cluster assembly factor nbp35
Sequence:
MKRVVITGLGAVTPLGNGVKTNWRNLIQGKSGIVSLKGFPEYEQIPSKVAGVIPRGKEKEEWNVLDYVDQGKLREVATFTQLALTSAAEALKDARWIDIDEQEKLATGVCFGTGIGNLDDALNENGVLNKAGIRKVSPRVISKILINMPAGYISQRYGFTALNHTTTTACAAGCHAIGDAFNFIKLGHADVIIAGGSESCINPLTVAGFSKARSLSTKFNDNPKAASRPFDANRDGFVIGEGSAALVLEELEHAKNRNAHIYAEIVGYGLASDSYHITAPNPNGDAAYYAMKRSLKQAGLSASQLDYINAHATSTKLGDVAESIAITRLLCDVNRNPEAFPVSSSKGSIGHLLGAAGAIESVYTVLTVQKGVLPPTLNFEYSDIPQQFQCDYVPNVAKESRINVALSNSFGFGGTNASLCFKKFLQ
Protein: Receptor for activated c kinase (Q8IBA0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein eS12
- 40S ribosomal protein S3
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S7
- 40S ribosomal protein S26
- 40S ribosomal protein S25
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S10, putative
- 40S ribosomal protein S23, putative
Sequence:
MMDNIKEAEISLRGVLEGGHSDWVTSVSTPTDPKLKTIVSASRDKKLIVWNINTDDDSGEIGTAKKSLTGHSQAINDVSISSDGLFALSGSWDHSVRLWDLSLGETIRSFIGHTSDVFSVSFSPDNRQIVSASRDKTIKLWNTLAQCKYTITDQQHTDWITCVRFSPSPNQAIIVSCGWDKLVKVWNLKNCDLNKNLEGHTGVLNTVTISPDGSLCASGGKDGVAKLWDVKEGKHLYSLETGSTINSLCFSPCDYWLCAATDRFIRIWNLESKLIISEIYPVKQSKIGVPWCTSLTWSANGQLLYCGSTDGNIYVYEVKKHSV
Protein: At5g15190 (Q8GW49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transmembrane emp24 domain-containing protein p24beta3
- Transmembrane emp24 domain-containing protein p24beta2
- Ethylene-responsive transcription factor SHINE 3
- Ethylene-responsive transcription factor SHINE 2
- Ethylene-responsive transcription factor WIN1
- Coatomer subunit delta
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase 2
Sequence:
MMTMGGREAESWPEMEAIARKMVEEVETESSGSSEAETESPRSVGRWITAKEKVHNQVLKIREEDLCVLVEDKVTNPEDRRYLRPRRFNLFLISRQNLPCSPLSGKGRSVNVVQTQ
Protein: AP-3 complex subunit beta (Q7YU20)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004145}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MGLDVEFGADPASGAAFFQSDGRKHDDLKQMLDSNKDGLKLEAMKRIIGMIARGRDASDLFPAVVKNVVSKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVSMIVPIVMLAIRDSAADLSPYVRKTAAHAIPKLYSLDADQKDELVMVIEKLLSDRTTLVVGSAVMAFDEVCPERVDLIHKNYRKLCNFLLDVDEWGQVIIINMLTRYARTQFVDPNADDEDLVNDGLGETPVSERFYDESSHSSSHSDDGSSDDEKKNKSSTNNKNNGGGNGSRTPSSPSNSYHIDVDHRLLLRQTKPLLQSRNASVVMAVAQLYHHVAPKNEVQLIAKALIRLLRSHKEVQSVVLNCIASMSTKRKAIFEPHLKSFFVRTSDPTHIKLLKLDILTNLASAGSISLILREFQTYISSSDRSFVAATIQAIGRCASSIKEVTETCLSGLVHLLSNHDEHVVAESVVVIKRLLQTKAAEHFEIITQMAKLIDYINVPAARAAIIWLIGEYNEKVPLIAPDVLRKMAKSFVDEQDVVKLQVLNLGVKLYLTNPEQTSLLCQYVFTLARYDPNYDVRDRARFLRQIIFPASGTSSVLSQHARQVFLASKPAPVPESKYRDGNNFQLGSLSHYLNMPAAGYKELPAFPVIPPDSSVRNIAGFMQDKLPGEDSPSGHSKDKSGREGGKEKGAGGEKGFLSESDDKSSAYSESGSSSGSGTSDSESDSDGSGSSDEEEEEVQKQQPTKVSSVKERLIDAGSNELAATSSPVKATINNNNNARGSSGTSDSEDSSAYSGSSSDDSASGSDNEVKKNETKTDTGTKPEKLKEKHEKQPEQTAVKSNLDLLLDLDDIPPIGPVMTPSLGGFLTPGKVMRISKLASLYNNSSIGTPMMAGQAAPLQPQHARNRVELVGPSHIEFKHKELLNKVSGHGLHLAYRFTRSPHLYSSSMCSIELQFQNRGEKEITAIRLGQTTLPAGMQLNEFAPITVLQPQQTASGVLGVDFNDSTHAVDLELLSSAGSSRLQLKPPVGELVRSVQIGESCHREERAKLRGMNEHQCELRGLRQDLIDVVALRQKVFESINVAHTHSSSSGQLHCFAGQTLSSKSLVLLTLDWKTEDALTLLVNCEKMVIGSMVLNELRNALQLSFAM
Protein: GH12888p (Q8T0R1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRATIEFEECLKDSPRFRQFVSKEESDIEHLEQRLEKIIKLCNVAVDSGKEYVKNQSAFAMSLWDLQQHFLDNKNAHNALGKLIHCFQEMNKFHTILLDQASRTVLKNLSVFVKDDINQVKDYKGHFLKVSEGYDNALIKNAQASKNRPQEMQEAANILSASKSCFQHTALDYVNYITLAQARKVPSILSTLLDYYQACVTYYHQGFDLCNDFDEFFKNISEDLNALRGDYQQLEKAMQNRHMSVNRYCDSNTNSTSNKIEGYLFKKKSKGFKTWCRRWFYLSDNQLVYRKRSNEDSFSVMEEDLRICSVRPVNEGDRRFCFEVISPTKSHILQADSADMLSLWISALQHSIGAAIQHDSTHHSRPQSTNAPNNSLPAKRRIHWEEFLKIPGNAYCCDCRSPEPRWASINLGITLCIECSGVHRSLGVHYSKVRSLTLDAWESENVKVMMELGNEVVNRIYEARIGDDCGLKKPTEQCEIGVREAWIKAKYVERRFVCGMPKPQELLASETAEVLSIDSGGVVEDGESGGSGIAKRATLSLGGTRKWAVKKLRRRQKQRSIPKTLSDDPSIYNTAKTGDELEDDDDDESINIPSMSLSISRDDLLVIGDDLALDRLETPGILGSDQESTDGESDAESPEELPFSQLDANQLLYMASVVHNLPVMCMAFALGADKMWKNPQDRQRSFLHQAVISGSVMACEFLLLNGAAIDAVDEMGYSALHISTAKGHIAQVYLLLKHKAAYDLSSSDGKKALDIAVDQENADIVTL