wanglab/gogpt-training-data huggingface dataset:
Protein: Branchpoint-bridging protein (Splicing factor 1) (Zinc finger protein bpb1) (O74555)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-u2af23 complex has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Splicing factor U2AF 59 kDa subunit
- Pre-mRNA-processing ATP-dependent RNA helicase prp11
- Splicing factor U2AF 23 kDa subunit
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor sap114
- Pre-mRNA-splicing factor sap62
- Pre-mRNA-splicing factor sap61
- Pre-mRNA-processing protein prp40
- U2 snRNP component prp10
- U1 small nuclear ribonucleoprotein 70 kDa homolog
Sequence:
MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHRRFDCPERINHTMNIVCRHCGSIGHIARDCPVRDQQPPMADSTADREYQSLMQELGGGSAISNGNGEPQKSIEFSESGAASPQAGHPPPWAAASTSVSSSTSSPAPWAKPASSAAPSNPAPWQQPAAPQSAPALSMNPSSLPPWQQPTQQSAVQPSNLVPSQNAPFIPGTSAPLPPTTFAPPGVPLPPIPGAPGMPNLNMSQPPMVPPGMALPPGMPAPFPGYPAVPAMPGIPGATAPPGAPGSYNTSESSNLNAPPGVSMPNGYSNR
Protein: Interleukin-36 beta (Interleukin-1 family member 8) (IL-1F8) (Q9D6Z6)
Organism: Mus musculus (Mouse)
Function: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Stimulates production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes. Induces expression of a number of antimicrobial peptides including beta-defensin 4 and beta-defensin 103 as well as a number of matrix metalloproteases (By similarity). Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Induces the production of pro-inflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23, and activates p38 MAPK phosphorylation in BMDCs. Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by T-helper 1 (Th1) cells, cultured CD4(+) T-cells and splenocytes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NZH7}. Secreted {ECO:0000269|PubMed:19717513}. Note=Secreted upon LPS treatment followed by ATP-induced activation of P2rx7. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (By similarity). {ECO:0000250|UniProtKB:Q9NZH7, ECO:0000269|PubMed:19717513}.
Interaction partners:
- Interleukin-1 receptor-like 2
- Interleukin-36 receptor antagonist protein
- Interleukin-1 receptor accessory protein
- Interleukin-36 alpha
- Interleukin-1 receptor type 1
Sequence:
MMAFPPQSCVHVLPPKSIQMWEPNHNTMHGSSQSPRNYRVHDSQQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDVKKGNLVFLGIKNRNLCFCCVEMEGKPTLQLKEVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIESEK
Protein: DNA topoisomerase 6 subunit B (AtTOP6B) (EC 5.6.2.2) (Protein BRASSINOSTEROID INSENSITIVE 3) (Protein ELONGATED HYPOCOTYL 6) (Protein ROOT HAIRLESS 3) (Q9C5V6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity. The B subunit binds ATP. Involved in cell-elongation processes.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03165}.
Interaction partners:
- DNA topoisomerase 6 subunit A
- Meiotic recombination protein SPO11-2
- Meiotic recombination protein SPO11-1
- DNA-binding protein BIN4
- DNA-binding protein RHL1
- DNA gyrase subunit A, chloroplastic/mitochondrial
- Probable nucleolar protein 5-1
- Transmembrane protein
- DNA topoisomerase 1 beta
Sequence:
MAGDDLVETKKGSSKNSKDSNESKLKQKSPAEFFAENKNIAGFDNPGKSLYTTVRELVENALDSAESISELPEVEVTIEEIVKSKFNSMIGLIDRERVDTQLYDDYETEKARGKRLAKEARASEIQAKNLASGKKNKEPGVSKVLKARGEASYYKVTCKDNGKGMPHDDIPNMFGRVLSGTKYGLKQTRGKFGLGAKMALIWSKMSTGLPIEISSSMKSQNYVTFCRLDIDIHRNIPHIHLHEKKGNKEKWHGAEIQVVIEGNWTTYRSKILHYMRQMAVITPYAQFLFRFISETPEKNVTIKFTRRTDVMPPIPIETKHHPSSVDLLLIKRLITDTSKKTLLQFLQNEFVNINKTLAARLIGEMGPDFGPSMAVKSVTSQQMVRIHQLFRQAKFDDPSGDCLSPAGEYNLRLGIIKELHPDMVATYSGSAQVFEGHPFIVEAGVSLGGRDVKQGINIFRFANRIPLLFEQGADVVTRTALKRINWNSYKINQTQDKIGVFVSIVSTKIPFKGTGKEYIGDDISEIATAVKSAIQQCCIQLKSKIVKRLQAREQQERKRSLSRYIPDATGAVYEVLKQMTEEHKTKRKRYGEEDIVMLDKVSKQIITKETLKEKLAEHVEQVDYEMALEYATQSGVSEEPRENIYLQHLDPNKSNFIDLHSPTFVFRLML
Protein: Lebercilin (Leber congenital amaurosis 5 protein homolog) (Q80ST9)
Organism: Mus musculus (Mouse)
Function: Involved in intraflagellar protein (IFT) transport in photoreceptor cilia.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17546029}. Cell projection, cilium {ECO:0000269|PubMed:21606596}. Note=Localized to the region between the outer and inner photoreceptor segments, corresponding to the photoreceptor connecting cilium (PubMed:17546029, PubMed:21606596). Colocalizes with IFT complex A and B proteins in the connecting cilium of photoreceptors (PubMed:21606596). {ECO:0000269|PubMed:17546029, ECO:0000269|PubMed:21606596}.
Interaction partners:
Sequence:
MGERARSPDIEQGKKGGKHPYSHYSSDLGSSPQSSGPSSPVNTTPCASTREKNPKRHLSDNQVHHPTVRKVSPKAVPSKKGIRVGFRSQSLNREPLRKDPDIVTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFTDQCTKGVQTAEDFELEDFPFTAQTVLCYENRWDEPEYLSSYLEYQDLNKHGSEMLSSVLGQEGKYDEDEDPCSAKQEARKPESEWAREELDKVKGKSALLGRAEKLALEAGRFPTENYQAQSVDKFEDEAERLKTEMLLAKLNEINKELQDPQNLGRAPLPLLPNFESKLHSPDRSTRPYSFPESLDRSFNGQHLQDLSFLTPRGEGGSPGPIRSPGQIRSPAPLDEFSFGSYVPSFGKTLGKSNPPSQKSSLLDFQSNSSESPSKDSLDLMSRKEKKATLMEQLFGPSASNTSVSSKSTDPHFPAASRGDMDPLHFLSGDRNSRVREPGDEEEDLFLREGRSFNPNRHRLKHASNKPTVTAVDSVDEDIEEVTLR
Protein: Probable CoA ligase CCL8 (HlCCL8) (EC 6.2.1.-) (M4IS90)
Organism: Humulus lupulus (European hop)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23300257}.
Interaction partners:
Sequence:
MHLNLKSLCSLTLISQAKTSNPFLSFSNCRPFSSLHSGSANLILMELLKEVAKEGSSASVGVAIRADQKSYSYKQLISSAQRICSLLCSTDLKASHKAGKQVTPALINGLSGHGHLGGARVGIVAKPSAEFVTGVLGTWLSGGVAVPLALSYPEAELLHVMTDSDISMILSTEDHQELMQKIAAKTAAQFSLIPPVPSSCSQEGAVDHLQTGDINTDSILHNTEISNENPALIVYTSGTTGKPKGVVHTHKSINAQVQTLAKAWEYTPADQFLHCLPLHHVHGLFNALFAPLYARSTVEFMPKFSVRGIWQRWRESYPTCETKVDDCITVFTGVPTMYTRLIQGYEAMDPELKEASASAAKQLRLMMCGSSALPIPVMQQWQTITGHRLLERYGMTEFVMAISNPLKGERKAGTVGKPFPGVEVRIVAEDENGSDTTGVGELCVRSPSLFKEYWRLPEVTKSSFTDDGFFKTGDAGKVDEDGYYVILGRTSADIMKVGGYKLSALEIESVLLEHPTVEECCVLGLPDKDYGEAVSAIIVPAAEAKKKGEEESKPAISLEELFSWAQHKLAPYKLPTRLFLWDSLPRNAMGKVNKKELKKKLTVEQGV
Protein: Phosphatase and actin regulator 1 (Q9C0D0)
Organism: Homo sapiens (Human)
Function: Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity. Involved in the regulation of cortical neuron migration and dendrite arborization (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Nucleus {ECO:0000250}. Note=Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import (By similarity). {ECO:0000250}.
Interaction partners:
- Myocardin-related transcription factor B
- Actin, alpha skeletal muscle
- Myocardin-related transcription factor A
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Myocardin
- A disintegrin and metalloproteinase with thrombospondin motifs 7
Sequence:
MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQARRATLLLPPTLMAASSEDDIDRRPIRRVRSKSDTPYLAEARISFNLGAAEEVERLAAMRSDSLVPGTHTPPIRRRSKFANLGRIFKPWKWRKKKSEKFKHTSAALERKISMRQSREELIKRGVLKEIYDKDGELSISNEEDSLENGQSLSSSQLSLPALSEMEPVPMPRDPCSYEVLQPSDIMDGPDPGAPVKLPCLPVKLSPPLPPKKVMICMPVGGPDLSLVSYTAQKSGQQGVAQHHHTVLPSQIQHQLQYGSHGQHLPSTTGSLPMHPSGCRMIDELNKTLAMTMQRLESSEQRVPCSTSYHSSGLHSGDGVTKAGPMGLPEIRQVPTVVIECDDNKENVPHESDYEDSSCLYTREEEEEEEDEDDDSSLYTSSLAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP
Protein: Ribose-phosphate pyrophosphokinase 4 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 4) (Q680A5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- FT-interacting protein 3
- 2-isopropylmalate synthase 1, chloroplastic
- Putative defensin-like protein 234
- Putative defensin-like protein 235
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
Sequence:
MSENAANNIMETKICTDAIVSELQKKKVHLFYCLECEELARNIAAESDHITLQSINWRSFADGFPNLFINNAHDIRGQHVAFLASFSSPAVIFEQISVIYLLPRLFVASFTLVLPFFPTGSFERMEEEGDVATAFTMARIVSNIPISRGGPTSVVIYDIHALQERFYFADQVLPLFETGIPLLTKRLQQLPETEKVIVAFPDDGAWKRFHKLLDHYPTVVCTKVREGDKRIVRLKEGNPAGCHVVIVDDLVQSGGTLIECQKVLAAHGAVKVSAYVTHGVFPKSSWERFTHKKNGLEEAFAYFWITDSCPQTVKAIGNKAPFEVLSLAGSIADALQI
Protein: Kir6.3 protein (Potassium inwardly rectifying channel subfamily J member 11,-like) (Potassium inwardly-rectifying channel, subfamily J, member 11, like) (Q5R205)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
- MAC-inhibitory protein
- ATP-binding cassette sub-family C member 9, member 9)
- ATP-binding cassette sub-family C member 8 isoform X1, member 8)
Sequence:
MLARKGLLPDGFLLTRLAEDAQPSRIRPKSQRARFITKSGSCNVAHKNIREQGRFLQDVFTTMVDLKWQHSLLIFTSAFLCSWMLFAMVWWLLAFAHGDLEPRDPNEPGPVPCVTSIHSFTSAFLFSIEVQVTIGFGGRMVTEECPLAIIVLIIQNILGLIINAIMLGCVFMKTAQANRRAETLIFSRNAVIAPRNGRPTLMFRVGDLRKSMIISANIQLQVIRRTVTAEGEVIPVCQLDIQVENPLRSNGIFLVSPLIISHTIDRGSPLYELSAQSMATEDLEIIVILEGVVETTGITMQARTSYIPEEILWGRRFVSIMTEEDGRYSVDYSKFGNTVPVRMPALSAKELDQTRGVQDSGPHEGKPQGWGLVRAGRGGYRRGGARACDDTAAKPWYVPAEKEEEKKGQKKTVKLEEIGREIEEETTEDMSD
Protein: Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) (P08179)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Interaction partners:
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylamine--glycine ligase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- N5-carboxyaminoimidazole ribonucleotide mutase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Bifunctional protein FolD
Sequence:
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPPQGYAADE
Protein: Down syndrome cell adhesion molecule 1, isoform AR (Q0E9L2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQFYITEAENEYVIKGNAAVVKCKIPSFVADFVQVEAWVDEEGMELWRNNATDAYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKVDMHDKMDFTIRSSNRSLNLFCKAQGFPMPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMALPKISPFNFGEESMSYGEFVNVQCTISGGDLPVNITWTLNNKPFEDYLEILTTKRGKRINELTIEAVSAKHAGNYSCIAENKAGVANHTAELKVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: LVV-hemorphin-7; Spinorphin] (P68871)
Organism: Homo sapiens (Human)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
- Hemoglobin subunit alpha
- Hemoglobin subunit zeta
- Haptoglobin
- Alpha-hemoglobin-stabilizing protein
- Hemoglobin subunit theta-1
- Haptoglobin-related protein
- Hemoglobin subunit mu
- Hemoglobin subunit delta
- BCL11 transcription factor A
- Krueppel-like factor 1
Sequence:
MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Protein: E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (RING finger protein 160) (RING-type E3 ubiquitin transferase listerin) (Zinc finger protein 294) (Zfp-294) (Q6A009)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (By similarity). Ubiquitination leads to Vcp/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O94822}.
Interaction partners:
- Ribosome quality control complex subunit NEMF
- Ribosome quality control complex subunit TCF25
- Ermin
- E3 ubiquitin-protein ligase ZNF598
- HBS1-like protein
- Transitional endoplasmic reticulum ATPase
- CCR4-NOT transcription complex subunit 4
- E3 ubiquitin-protein ligase UBR1
- ATP-binding cassette sub-family E member 1
- Large ribosomal subunit protein uL23
Sequence:
MGGKNKQRTKGNLRPSNSGRAAELLAKEQGTVPGFIGFGTSHSDLGYVPAVQGAEDIDSLVDSDFRMVLRKLSKKDVTTKLKAMQEFGIMCTERDTEAVKGVLPYWPRIFCKISLDHDRRVREATQQAFEKLILKVKKHLAPYLKSVMGYWLMAQCDTYPPAALAAKDAFEAAFPPSKQPEAIAFCKEEITTVLQDHLLKETPDTLSDPQTVPEEEREAKFHRVVTCSLLALKRLLCFLPNNELDSLEEKFKSLLSQNKFWKYGKHSVPQVRSAYFELVSALCQHVPQVMKEEAAKVSPSVLLSIDDSDPVVCPALWEAVLYTLTTIEDCWFHVNAKKSVFPKLMAMIREGGRGLAAVMYPYLLPFISKLPQSITEPKLDFFKNFLTSLVTGLSTERTKSSSSECSAVISAFFECLRFIMQQNLGEEEMVQMLINEQLIPFIDTVLKDSGLHHGPMFDHLADTLSSWEAKADAERDPGAVYNLENVLLSFWGRLSEICTEKIRQPEADVKSVLCVSSLVGVLQRPRSSLKLHRKKTAQVRFAINIPEAHKGDEKSMSSEGENSEGSDGGAQSPLSNTSSDLVSPLRKKPLEDLVCKLAEVSISFVNERKSEQHLQFLSTLLDSFSSVQVFNILLSDKQKNVVKAKPLEITKLAEKNPAVKFLYHKLIGWLNDSQKEDGGFLVDILYSALRCCDSGVERKEVLDDLTKEDLKWSSLLQVIEKACSSSDKHALVTPWLKGSILGEKLVALADCLCDKDLEATTSESHSSEQWSLLRLALSQHVKNDYLIGEVYVGRIIVKLHETLSKTKDLSEAANSDSSVSFVCDVVHSFFSSAGGGLLMPPSEDLLLTLFQLCAQSKERTHLPDFLICKLKNTLLSGVNLLVHQTASTYEQSTFLRLSVLWLKDQVQSSALDNTSLQVLLSAAGDLLGTLVESEDTSLLGVYIGSVMPSDSEWEKMRQALPVQWLHRPLLEGRLSLNYECFKTDFKEQDTKTLPNHLCTSSLLSKMILVAQKKKLVLEDNVLEKIIAELLYSLQWCEELDNAPSFLSGFCGILQKMNITYSNLSVLSETSSLLQLLFDRSRKNGTLWSLIIAKLILSRSISSDEVKPYYKRKESFFPLTEGSLHTIQSLCPFLSKEEKKEFSAQCIPAFLGWTKEDLCSINGAFGHLAIFNSCLQTRSIDDKQLLHGILKIITSWRKQHEDIFLFSCNLSEASPEVLGLNIEIMRFLSLFLKHCAYPLPLADSEWDFIMCSMLAWLETTSENQALYSVPLVQLFACVSFDLACDLCAFFDSITPDIVDNLPVNLISEWKEFFSKGIHSLLLPLLVNAIGENKDLSETSFQNAMLKPMCETLTYISKDQLLSHKLPARLVASQKTNLPEHLQTLLNTLTPLLLFRARPVQIAAYHMLCKLMPELPQHDQDNLRSYGDEEEEPALSPPAALMSLLSSQEELLENVLGCVPVGQIVTVKPLSEDFCYVLGYLLTWKLILTFFKAASSQLRALYSMYLRKTKSLNKLLYHLFRLMPENPTYGETAIEVSSKDPKTFFTEEVQLSIRETATLPYHIPHLACSVYHMTLKDLPAMVRLWWNSSEKRVFNIVDRFTSKYVSNVLSFQEISSVQTSTQLFNGMTVKARATTREVMATYTIEDIVIELIIQLPSNYPLGSITVESGKRIGVAVQQWRNWMLQLSTYLTHQNGSIMEGLALWKNNVDKRFEGVEDCMICFSVIHGFNYSLPKKACRTCKKKFHSACLYKWFTSSNKSTCPLCRETFF
Protein: RRM domain-containing protein (D5MCQ3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSVSSRRVPLPPTSQHRASSNFNTTPSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKVGSTSRHPSFQQFSSLGGPTAFLNGQHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKPMNPQ
Protein: Constitutive photomorphogenesis protein 10 (Q9LJD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of light signal transduction machinery. Involved in repression of photomorphogenesis in darkness by participating in the CDD complex, a complex probably required to regulate the activity of ubiquitin conjugating enzymes (E2s). Repression of photomorphogenesis is probably mediated by ubiquitination and subsequent degradation of photomorphogenesis-promoting factors such as HY5, HYH and LAF1. Although strongly related to ubiquitin-conjugating enzyme, it has no catalytic activity by itself due to the absence of the conserved Cys active site at position 120. It can however enhance the activity of E2 conjugating enzymes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11877375}.
Interaction partners:
- Light-mediated development protein DET1
- E3 ubiquitin-protein ligase COP1
- DNA damage-binding protein 1a
- Cullin-4
- DET1- and DDB1-associated protein 1
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- RING-box protein 1a
- Putative cullin-like protein 4
- Cullin-like protein 5
Sequence:
MMTPGGSGRLRPLPTAMYAGYSGTASSWVAKTSVSASGKRIQREMAELNIDPPPDCSAGPKGDNLYHWIATIIGPSGTPYEGGIFFLDIIFPSDYPFKPPKLVFKTRIYHCNVDTAGDLSVNILRDSWSPALTITKVLQAIRSIFLKPEPYSPALPVIARLYLTDREKHDEVAKEWTLRFAK
Protein: Pentatricopeptide repeat-containing protein 7, mitochondrial (O42910)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial RNA-binding protein required for the stability of the atp6 mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21727087}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 6
- Mitochondrial cox1 translation regulator ppr4
- Aspartate aminotransferase, mitochondrial
- Uncharacterized protein PB1E7.11c
- Pentatricopeptide repeat-containing protein 8
- Cytochrome b translation regulator cbp8
- ATP synthase subunit a
- Mitochondrial translation ATP-dependent RNA helicase mrh5
- Pentatricopeptide repeat-containing protein 2
- Small ribosomal subunit protein L51-b
Sequence:
MRNCVSPLLFAWTKHLRLREFKIPFPNRLVVRSLNQLSVHHEKVTGCRPRQASSDELHKYSKSASNEAFLSSFAENQLFHKCLPSSAGAVLSENDLMYIIRKVSEVYADNKTEKVTVPFDKHKNPFLIYVKKRFAECFDKNPDLCLIVYSKLEVETLAKITPIWINVAKKNKKEDFLVELCLRFLERFRSCNLTEQAILYQNFRENWWSNIKLPQNLKSLYVELCLVYHFHNSHLGMDSSTVSNLKRFCFSESLGHIFAPLRFQNQQLPLQHVYAFLFSIAYRDNQVDTAHFLYKQWSRAGMGPLPKDAFIKFVQLLSKNRNWVLMRDIVQLEEYNSYLLDHRIVSAFLKPLSEKGNYKDILSLISVWQHSVWRPSLAYLQVVYSFSMRALLVNRQYSSAFAFFWKIDPYIRNERLVSQMLQAASQLHYHDLILYVINTYYSGNIMKNLGNKDLICITQSSPPCNISGIKPGSLKLSPTTNTVLAKSICYWLNDAMALLFLLENQLNCKHSLFQRKSLIILLNGILNCPHSSYDLQFRAVSLLTGRIRLNVDFEVSVLASQLVFFVKHRDFKRTLITMKAISKLQKNFDVRIWNYWLVALIQQKLYSRAVKVYSKLICSSAVRNDTTRSLIRLIPKSYFKSYPLLKESETEKKTNSAL
Protein: Fibroblast growth factor (FGF) (A0A060Y7E5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- receptor protein-tyrosine kinase
- Fibroblast growth factor receptor 1
- receptor protein-tyrosine kinase
- Fibroblast growth factor receptor 2
- Serine-threonine/tyrosine-protein kinase catalytic domain-containing protein
- Ig-like domain-containing protein
- Protein kinase domain-containing protein
- Fibroblast growth factor receptor 2
- receptor protein-tyrosine kinase
- Fibroblast growth factor receptor 2
Sequence:
MATGEITTLPATPEDGGSGGFLPGNFKEPKRLYCKNGGYFLRINSNGSVDGIRDKNDPHNKLQLQATSVGEVVIKGVSANRYLAMNADGRLFGARRTTDECYFMERLESNNYNTYRSRKYPEMYVALKRTGQYKSGSKTGPGQKAILFLPMSARR
Protein: Transcriptional regulator, TetR family (Q9KR96)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Interaction partners:
- Succinate-semialdehyde dehydrogenase
Sequence:
MKLSEQKRLALIEAAKEEFTQFGFHAANMDRVCERAGTSKRTLYRHFTSKELLFIEVINLLVAQPHKVGFEYQSTRSLADQLHDYFAAKIDLLYRTIGLDVLRMIVGEFVRDPALTQQYLALMGTQDTALTAWLQAAIKDGKLIEKEVAPMATTLMNLFHGQFLWPQLLAAVELPDAKQQQIMMDEIIRVFVLSYGVSSPSHLSIELKP
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (Q57U08)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- intramembrane prenyl-peptidase Rce1
- CAAX prenyl protease
- Farnesyl pyrophosphate synthase
- squalene synthase
- RNA-editing complex protein MP42
- Peroxin 19
- Small GTPase, putative
- GTP binding protein
Sequence:
MSFVPPPASSTTHAQREVELTLLRFLEKYRPEVCDLWGTHSNIYLHADSNEKEEEMCTIDNEEGIVHSLNRESHEKYLKSRLVKLPEYAQRLYNAQPWMVYWTLQAAEMLGITEKLYEQISQDALGEFILSCLQEQPVEDEQKGCWGSEEGGKHGKGSMPQQCGNVYDFLRRCDADHTCAIGFSGGNYGQIPHLATSYAGVCSLCILECPEYLQALPRSAIKRWLLSLRCADGSFRMHIGGEADIRASYCVAVITTLLQLQDVDASSGDILREQEAQFVASCQTHEGGFACGRFASEAHGAYTQCGLAALILMKRPELCNYTALRGWLAARQLRFEGGFNGRTNKLVDSCYAHWVGASHVLLRVGESLAKITTCGETKRSLTSREMLLLDHAQLVDISNLHPESFEAWSQHEEEKQERASRVEAYLSATPLAASWSSSGVPNVLDDDAGDFYFNQRRLQLYILACCQNREEGGLMDKPNYPNDFYHTCYSLSGMSSAQNLQGMQVNRDGRDLSGNSFYAAAVSRGYIPGRRDSYGIVLPSDERSGVSSELHLSKNCLRPTNPIFNINQSKVLFALRTWGAKTFMC