wanglab/gogpt-training-data huggingface dataset:
Protein: Pleckstrin homology-like domain family A member 1 (Proline- and glutamine-rich protein) (PQ-rich protein) (PQR protein) (Q9QZA1)
Organism: Rattus norvegicus (Rat)
Function: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. May be involved in translational regulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8WV24}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8WV24}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8WV24}. Note=Colocalizes with intracellular vesicles. {ECO:0000250|UniProtKB:Q8WV24}.
Interaction partners:
- Aurora kinase A
Sequence:
MRRTPAAERLSELGFPPRRGSQEPPFPLGVTRGWGGWPIEKRCEGPRPVPFSERSAEDGREQPAHGSGILWRVRTRLSLCRDPEPPPPPPPLCLLRVSLLCALRAGGRGSRWSEDSARLLLLPPAGASGSLKAERSSSTPYAGRMLESSGCKALKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQVQHQQQQQQQQQPGQGTAEPSQPSGPAVTSLEPPAKLKELHFSNMKTVDCVERKGKYMYFTVVMAEGKEIDFRCPQDQGWNAEITLQMVQYKNRQAILAVKSTRQKQQHLVQQQPPQTQQIQPQPQQPQIQPQPQPQIQPQPQPQPQPQPQPQQQPQPQQLHSYPHPHPHLYPHPHPHAHSHPHPHPHPHPHQLQHAHQPLHSQPQGHRLLRSTSNSA
Protein: Cobalt transport protein CbiN (Energy-coupling factor transporter probable substrate-capture protein CbiN) (ECF transporter S component CbiN) (Q05595)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cobalt import ATP-binding protein CbiO
- Cobalt transport protein CbiM
- Cobalt transport protein CbiQ
- Cobalt-precorrin-6A reductase
- Cobalt-precorrin-5A hydrolase
- Sirohydrochlorin cobaltochelatase
- Cobalt-precorrin-5B C
- Cobyric acid synthase
- Cobalt-precorrin-7 C
- Cobalt-precorrin-2 C
Sequence:
MKKTLMLLAMVVALVILPFFINHGGEYGGSDGEAESQIQAIAPQYKPWFQPLYEPASGEIESLLFTLQGSLGAAVIFYILGYCKGKQRRDDRA
Protein: Protein Rex (Rev homolog) (Rex-1) (p27Rex) (P0C206)
Organism: Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1)
Function: Rex escorts unspliced gag-pro-pol and singly spliced env mRNAs out of the nucleus of infected cells. These mRNAs carry a recognition sequence called Rex responsive element (RxRE or XRE) located at the 3' region of the long terminal repeat (LTR). This function is essential since most HTLV proteins are translated from unspliced or partially spliced pre-mRNAs that cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rex itself is translated from a fully spliced mRNA that probably readily exits the nucleus. Rex's nuclear localization signal (NLS) binds directly to KPNB1/importin beta-1 without previous binding to KPNA1/importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rex to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rex from KPNB1 and allows Rex's binding to the RRE in viral pre-mRNAs. Rex multimerizes on the RRE via cooperative assembly. This multimerization is critical for its full biological activity, since it may shield the viral RNA from being spliced or down-regulated, and probably exposes Rex's nuclear export signal (NES) to the surface. Rex can then form a complex with XPO1/CRM1, RANBP3 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rex/RRE/XPO1/RANBP3/RAN complex, so that Rex can return to the nucleus for a subsequent round of export (By similarity).
Subcellular location: [Isoform Rex]: Host nucleus, host nucleolus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform p21Rex]: Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPLRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPM
Protein: Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) (P20648)
Organism: Homo sapiens (Human)
Function: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (By similarity). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:24188822}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the apical canalicular membrane of parietal cells (PubMed:24188822). {ECO:0000269|PubMed:24188822}.
Interaction partners:
- Potassium-transporting ATPase subunit beta
- Inorganic pyrophosphatase
- Cytochrome P450 2C19
- Gastrin
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 116 kDa subunit a 3
- Inorganic pyrophosphatase 2, mitochondrial
- Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
- V-type proton ATPase 116 kDa subunit a 4
- Potassium-transporting ATPase alpha chain 2
Sequence:
MGKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTVQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFFRNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGVRCCPGSWWDQELYY
Protein: Transmembrane 9 superfamily member 2 (Endomembrane protein 8) (Transmembrane nine protein 2) (AtTMN2) (Q940S0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:P32802}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q940G0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRTPTTILLLVGAILFSGAGYVRSDASDHRYKEGDTVPLYANKVGPFHNPSETYRYFDLPFCIPEGVKEKKEALGEVLNGDRLVSAPYKLNFRDEKESEVYCNKKLSKEEVKQFRKAVEKDYYFQMYYDDLPIWGFIGKVDKDIKSDPSEFKYFLYKHIQFEILYNKDRVIEISARMDPHSLVDLTEDKEVDAEFMYTVKWKETETPFEKRMEKYSMSSSLPHHLEIHWFSIINSCVTVLLLTGFLATILMRVLKNDFMKYAQDEEAADDQEETGWKYIHGDVFRFPTHNSLFAASLGSGTQLFTLTIFIFMLALVGVFYPYNRGALFTALVVIYALTSGIAGYTSASFYCQLEGKSWVRNLLLTGCLFCGPLFLTFCFLNTVAITYTATAALPFGTIVVIVLIWTLVTSPLLVLGGIAGKNSKAEFQAPCRTTKYPREIPPLPWYRSAIPQMAMAGFLPFSAIYIELYYIFASVWGHRIYTIYSILFIVFIILIIVTAFITVALTYFQLAAEDHQWWWRSFLCGGSTGLFIYAYCLYYYYARSDMSGFMQTSFFFGYMACICYGFFLMLGTVGFRAALLFVRHIYRSIKCE
Protein: Ras-related protein Rab-8B (EC 3.6.5.2) (P70550)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250|UniProtKB:Q92930}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium (By similarity). Colocalizes with CDH1 in the basal compartment. {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-8A
- MICAL-like protein 2
- Rab-3A-interacting protein
- PEX5-related protein
- Optineurin
- Guanine nucleotide exchange factor for Rab-3A
- RILP-like protein 2
- Inositol polyphosphate 5-phosphatase OCRL
- Rab GDP dissociation inhibitor alpha
- Rab GDP dissociation inhibitor beta
Sequence:
MAKTYDYLFKLLLIGDSGVGKTCLLFRFSEDAFNTTFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIKNWIRNIEEHASSDVERMILGNKCDMNDKRQVSKERGEKLAIDYGIKFLETSAKSSTNVEEAFFTLARDIMTKLNRKMNDSNSSGAGGPVKITESRSKKTSFFRCSLL
Protein: Triacylglycerol lipase 2 (EC 3.1.1.3) (Lipase 2) (Neutral lipid hydrolase) (P54857)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial triacylglycerol (TAG) lipase with activity toward long-chain diacylglycerols (DAGs) and triacylglycerols (TAGs). Involved in mitochondrial lipid metabolism.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19959834}. Mitochondrion intermembrane space {ECO:0000269|PubMed:31483742}. Note=Imported into the IMS via the MIA40 disulfide relay system. {ECO:0000269|PubMed:31483742}.
Interaction partners:
- Triacylglycerol lipase 4
- Triacylglycerol lipase 3
- Triacylglycerol lipase 5
- Monoglyceride lipase
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Lipid phosphate phosphatase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Phosphatidic acid phosphohydrolase 1
- Phosphate metabolism protein 8
Sequence:
MKNDNKANDIIIDSVKVPDSYKPPKNPIVFCHGLSGFDKLILIPSVFHLTNLISNSIVHNMAENFMQDDEDKSDNKYTNLLEIEYWIGVKKFLQSKGCTVITTKVPGFGSIEERAMALDAQLQKEVKKIESKDKRHSLNLIAHSMGGLDCRYLICNIKNRNYDILSLTTISTPHRGSEMADYVVDLFENLNALRVSQKILPICFYQLTTAYMKYFNLVTPNSPKVSYFSYGCSFVPKWYNVFCTPWKIVYERSKGCPNDGLVTINSSKWGEYRGTLKDMDHLDVINWKNKLQDDWSKFFRTTTVGEKVDILNFYLKITDDLARKGF
Protein: Alpha-conotoxin PIC (C0HLM2)
Organism: Conus purpurascens (Purple cone)
Function: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits rodent (alpha-1-beta-1-delta-epsilon > alpha-1-beta-1-delta-gamma) and human (alpha-3-beta-1) nAChRs heterologously expressed in Xenopus oocytes, but has minimal effect on human alpha-7 nAChRs. Has no effect on the frequency of responses from the giant fiber (GF)-dorsal longitudinal and GF-tergo trochanteral muscle pathways in the D.melanogaster GF circuit. Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:28917942}.
Interaction partners:
Sequence:
SGCCKHPACGKNRC
Protein: Signal recognition particle 54 kDa protein (Q8IKX4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Signal recognition particle subunit SRP9
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72, putative
- Signal recognition particle receptor subunit alpha, putative
- Signal recognition particle 14 kDa protein
- 60S ribosomal protein L23
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L6, putative
- Small ribosomal subunit protein eS30
Sequence:
MVLTELGTQITNAFRKLQTSTLADDVVIEECLKEIIRALILSDINVSYLKDIKSNIKNNIEKNIDIYGNNKKKLVQKYVVEELIKLLEGKKEGYNPVKGKRNVILFVGLQGSGKTTTCTKYAHYYQKKGFKTALVCADTFRAGAFDQLKQNAAKVKIPFYGSYSEVDPVKIATDGVNAFLKDKYDLIIVDSSGRHKQENELFEEMIQVENSIQPEEIIFVIDSHIGQSCHDQAMAFKNSVSLGSIIITKIDGHAKGGGALSAVAATGCPITFIGTGEHVNDFEKFEAKSFVSRLLGLGDISGLVSTIKEVIDIDKQPELMNRLSKGKFVLRDMYDQFQNVFKMGSLSKVMSMIPGFGNNLISKGTEKEGIDKIKKFMVIMDSMTNEELDCIKPLNDSRCLRIVKGSGTRLQDIKELLEQFKFLQKMVVKMGKLGLRENNISNLMRNQKQFMSKMNNIMDPNMLKQLGGANNMVNILKEFTKMDDLGVSMANMMKQMGLKK
Protein: Cytochrome P450 26A1 (Q304P5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRNCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIHKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVTMQAFNREALQCYVPVIAEEVSGCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQAAEPDAGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSHHEDKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADSFTNKEEFNPDRFTSLHPEDTSRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARRCDWQLLNGPPTMKTSPPVYPVDNLPARFTHFQGDI
Protein: NAD-dependent protein deacetylase sir-2.1 (EC 2.3.1.286) (Protein sir-2.1) (Regulatory protein SIR2 homolog 1) (Q21921)
Organism: Caenorhabditis elegans
Function: NAD-dependent deacetylase (By similarity). Involved in metabolism, apoptosis, response to oxidative stress, response to DNA damage, and determination of lifespan. Required for a reduction of the 'Lys-16' acetylation of histone H4 (H4K16ac) on dosage-compensated X chromosomes in hermaphrodites. Plays a role in germ cell and somatic cell apoptosis in response to DNA damage. Functions upstream of daf-16/Forkhead box protein O in the Insulin/IGF-1-like signaling (IIS) mediated pathway, promoting daf-16 mediated transcriptional activation and increased lifespan. May also regulate lifespan independently of daf-16 by modulating the transcription of genes involved in the stress response of the endoplasmic reticulum (ER). Functions upstream of transcriptional coregulator hcf-1, perhaps acting independently of the IIS mediated pathway, to modulate lifespan and oxidative stress response. Acts upstream of the nicotinic acid metabolism pathway, which may be linked to the regulation of longevity. Plays a role in ascaroside-mediated longevity and stress resistance.
Subcellular location: Nucleus {ECO:0000269|PubMed:16280150, ECO:0000269|PubMed:16777605, ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:27650246}. Cytoplasm {ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:27650246}. Note=Translocates from the nucleus to the cytoplasm during apoptosis. {ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:27650246}.
Interaction partners:
- Forkhead box protein O
- Host cell factor homolog hcf-1
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide N-methyltransferase
- 14-3-3-like protein 2
- Purine nucleoside phosphorylase
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Nicotinamide N-methyltransferase-like
Sequence:
MSRDSGNDSEVAVTHGEVQEITEENPEIGSMHITQETDISDAPETNTDSSRQRTESTTSVSSESWQNNDEMMSNLRRAQRLLDDGATPLQIIQQIFPDFNASRIATMSENAHFAILSDLLERAPVRQKLTNYNSLADAVELFKTKKHILVLTGAGVSVSCGIPDFRSKDGIYARLRSEFPDLPDPTAMFDIRYFRENPAPFYNFAREIFPGQFVPSVSHRFIKELETSGRLLRNYTQNIDTLEHQTGIKRVVECHGSFSKCTCTRCGQKYDGNEIREEVLAMRVAHCKRCEGVIKPNIVFFGEDLGREFHQHVTEDKHKVDLIVVIGSSLKVRPVALIPHCVDKNVPQILINRESLPHYNADIELLGNCDDIIRDICFSLGGSFTELITSYDSIMEQQGKTKSQKPSQNKRQLISQEDFLNICMKEKRNDDSSDEPTLKKPRMSVADDSMDSEKNNFQEIQKHKSEDDDDTRNSDDILKKIKHPRLLSITEMLHDNKCVAISAHQTVFPGAECSFDLETLKLVRDVHHETHCESSCGSSCSSNADSEANQLSRAQSLDDFVLSDEDRKNTIHLDLQRADSCDGDFQYELSETIDPETFSHLCEEMRI
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (A0A2R8YDM2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQSKIWKLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
Protein: Nucleoporin Nup54 alpha-helical domain-containing protein (Q21295)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFARRGGITGIKAEDMPKNLPNLPDLPTTSASQAPAPATQNVSSPARRNLFGAPNDANRTLFTNSPASGTTSGTSGLFGTSSTTSGGLGGIGSTQQTAKSPVATRLAAFKSGTLGAGSLSGNTPTSFATPSALPGTNAPQSSFLSPANNLNVAPAAYRPPYSTFGGSTPFGAASTGTAAGSTLFGSSTAKPATGGFFGSSSGSTLGGLGATQQQQQPVVQQQQVIQQYHPFVKAVGDPKLFGNDNDGVVAKLNQVAAGLGVGKAPYKDGNQLLSFSMEGNLFERFVGIGYNRISERTDDEGFVTLVLRHPITNLNTEERRDKILEIIKAILGGGPNVEVRYAPGTSMRTLSDGCTEICIIAKEGGFVAGAIKLAQILNDAPKMTQLESQLQVDKTRVLPKVGMSKAQRDRYLETVPDGIDERIWRQAIKENPAPNKLLPVPVRGWEALRDRQKAQVGESKLFHEAINALGNRVEEANHEHADAVVKMEIIRNRHKTLSYRIVRVMLAQWIVSRYSRQIDTDEDVIEAKADTLLAQMNRHNQVKFYVDKFYEILESKPDKLQESMWKMFDMTIEDEHYARRVLTKFVNICSGLYESTHQQIESLEACRRALEG
Protein: Serine peptidase, putative serine peptidase, Clan SC, Family S9D (Q4GYA0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prolyl endopeptidase
- Ecotin-like protein 4
- Prolyl endopeptidase
- Ecotin-like protein 2
Sequence:
MAAFFGSLVKSFILPKPSPTYSADKHPGKLVHIPRVDWDTRKENGTFTYGLLLLDTAAKFIIIYAHTNAVDVAMVFETMSYVSKRTSTSVLLVEYTGYGIAYGETTERSMNEDVLSAYYYAVRHMRVPADRVVLMGCSIGTGPSAQVCALLQGEEEVPALLVLQSPFTSLKECANDMTPNVGSIVGYLGYDWFRTIDVVAQVRCPIIIHHGQCDDVVPFEHAQQLKRTIEEATPPGVVELHAEPNRGHNDLPTESANRFIDKKLRSFGQPRCLQPRCRPYHLVNPSIYEYLFCVKEQPIINMEELLKHWNETLSIGSFAYKREKLYVLLTASVSLFAMRCARAWQHYAGSRKRHYGNSYSASCNGSVGVVGGSGGNGDGSGSGAEELYCAKEDIIKRCLACWGSPLGAYLSVRGPPIRHKIFGVHLDVCVENVVASDGISNESGFRSCGGNPYFLKRDTGEAYLSVAELEFTHGLTRSVAAAMSTAPTLGGEEDEMDVFLQKNVVTRIQTQCERVVAFLDSNEWENMLEVLVRFGQRAPSFLSSKALQYYSECSSQARFGDSCGTGAACCGNDSGPAPRSEVMETIEDVDEWLRPWVVSPDTRMQLGTEVPWDYYLLKARLCVIEYTPLGPDTSWEEARRITDAWRVVKIIHDLFCSYSRRVLHPSFSAS
Protein: F-actin-capping protein subunit alpha (F4J7C4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADEEDELLETELSYDQKKEIAKWFFLNAPAGEINYVAKDLKAVLSDEEVYNEAAMEAFPVYNKTHMICLEMPSGAGDVIVSSYSEINENEYLDPRTAQVAIVDHVKQICTKVRPANDEELPSLYIEEYRYALDAEIQRYVSESYPKGMSAVNCVKGKDNEGPGSDFELVVIITAMRLSPQNFCNGSWRSVWNIDFQDESQVLDIKGKLQVGAHYFEEGNVELDAKKDFQDSTIFQSADDCAIAIANIIRHHETEYLASLEVAYSKLPDNTFKDLRRKLPVTRTLFPWQNTLQFSLTREVEKELGLGKISIISVVSCLSFGVMYTNRISKYDRYCSASRMKELKFGPKKSSVAGNRTRVSWVKARYPNRWTTTDMLLELLKN
Protein: Helix-loop-helix DNA-binding domain containing protein (Os12g0589000 protein) (Q2QMV9)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGGGLIADMSWTVFDLPSHSDESEMMAQLFSAFPIHGEEEGHEQLPWFDQSSNPCYYSCNASSTAYSNSNASSIPAPSEYEGYCFSDSNEALGVSSSIAPHDLSMVQVQGATEFLNVIPNHSLDSFGNGELGHEDLDSVSGTNKRKQSAEGEFDGQTRGSKCARKAEPKRAKKAKQTVEKDASVAIPNGSCSISDNDSSSSQEVADAGATSKGKSRAGRGAATDPQSLYARKRRERINERLKTLQNLVPNGTKVDISTMLEEAVHYVKFLQLQIKLLSSDEMWMYAPIAYNGMNIGLDLNIDT
Protein: Isoamyl acetate-hydrolyzing esterase 1 homolog (EC 3.1.-.-) (Q2TAA2)
Organism: Homo sapiens (Human)
Function: Probable lipase.
Interaction partners:
- GMP synthase
- Voltage-gated monoatomic cation channel TMEM109
- Glutamine synthetase
- Lengsin
- Glutamate dehydrogenase 1, mitochondrial
- Glutamyl-tRNA
- Delta-1-pyrroline-5-carboxylate synthase
- Glutamate dehydrogenase 2, mitochondrial
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Fatty acid desaturase 6
Sequence:
MALCEAAGCGSALLWPRLLLFGDSITQFSFQQGGWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGNSLDIPVAVTIFFGANDSALKDENPKQHIPLEEYAANLKSMVQYLKSVDIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQDFSSYLSDGLHLSPKGNEFLFSHLWPLIEKKVSSLPLLLPYWRDVAEAKPELSLLGDGDH
Protein: Aklanonic acid methyltransferase DauC (AAMT) (EC 2.1.1.288) (Q55214)
Organism: Streptomyces sp. (strain C5)
Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methyl esterification of aklanonic acid to yield aklanonic acid methyl ester.
Interaction partners:
Sequence:
MQDSSYKKQVTQAFDQSSSTYDRLGVEFFTPMGRRLVDISEPVTGERVLDIGCGRGACLFPAAEKVGSQGCVHGIDIAPGMIEEARKEATERGLRNISLMVMDAETPGFPARSFDLVMGSYSVIFLPDAVGALARYADILDHGGRIAFTSPVFRAGTFPFLPPEFTPLIPQALLEHLPEQWRPEALVRRFNSWLERAEDLVRTLEGCGYARLRQSTSRCG
Protein: Elongation factor Ts (EF-Ts) (Bacteriophage Q beta RNA-directed RNA polymerase subunit IV) (P0A6P1)
Organism: Escherichia coli (strain K12)
Function: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
Interaction partners:
- Elongation factor Tu 1
- Small ribosomal subunit protein uS2
- Elongation factor Tu 2
- Elongation factor G
- Small ribosomal subunit protein bS1
- Ribosome-recycling factor
- Large ribosomal subunit protein bL19
- Uridylate kinase
- Large ribosomal subunit protein uL1
- Trigger factor
Sequence:
MAEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKTVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS
Protein: IFNa1 (Interferon alpha 1) (Q6XQG7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MYTVQSWTCICLIICSMQSVCHCCDWIRHHYGHLSSEYLSLLDQMGGDITKQDAPVFFPTSLYRHIDDAEVEDQVRFLKETIYQITKLFDGNMKSVTWDKKKLDDFLNILERQLENLKSCVSPAMKPEKRLKRYFKKLNKNVLRKMNYSAQAWELIRKETKRHLQRLDILAAQMY